Proteostasis, oxidative stress and aging
The production of reactive species is an inevitable by-product of metabolism and thus, life itself. Since reactive species are able to damage cellular structures, especially proteins, as the most abundant macromolecule of mammalian cells, systems are necessary which regulate and preserve a functiona...
Saved in:
Published in | Redox biology Vol. 13; no. C; pp. 550 - 567 |
---|---|
Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
01.10.2017
Elsevier |
Subjects | |
Online Access | Get full text |
ISSN | 2213-2317 2213-2317 |
DOI | 10.1016/j.redox.2017.07.008 |
Cover
Abstract | The production of reactive species is an inevitable by-product of metabolism and thus, life itself. Since reactive species are able to damage cellular structures, especially proteins, as the most abundant macromolecule of mammalian cells, systems are necessary which regulate and preserve a functional cellular protein pool, in a process termed “proteostasis”. Not only the mammalian protein pool is subject of a constant turnover, organelles are also degraded and rebuild. The most important systems for these removal processes are the “ubiquitin-proteasomal system” (UPS), the central proteolytic machinery of mammalian cells, mainly responsible for proteostasis, as well as the “autophagy-lysosomal system”, which mediates the turnover of organelles and large aggregates.
Many age-related pathologies and the aging process itself are accompanied by a dysregulation of UPS, autophagy and the cross-talk between both systems. This review will describe the sources and effects of oxidative stress, preservation of cellular protein- and organelle-homeostasis and the effects of aging on proteostasis in mammalian cells.
[Display omitted] |
---|---|
AbstractList | The production of reactive species is an inevitable by-product of metabolism and thus, life itself. Since reactive species are able to damage cellular structures, especially proteins, as the most abundant macromolecule of mammalian cells, systems are necessary which regulate and preserve a functional cellular protein pool, in a process termed "proteostasis". Not only the mammalian protein pool is subject of a constant turnover, organelles are also degraded and rebuild. The most important systems for these removal processes are the "ubiquitin-proteasomal system" (UPS), the central proteolytic machinery of mammalian cells, mainly responsible for proteostasis, as well as the "autophagy-lysosomal system", which mediates the turnover of organelles and large aggregates. Many age-related pathologies and the aging process itself are accompanied by a dysregulation of UPS, autophagy and the cross-talk between both systems. This review will describe the sources and effects of oxidative stress, preservation of cellular protein- and organelle-homeostasis and the effects of aging on proteostasis in mammalian cells. The production of reactive species is an inevitable by-product of metabolism and thus, life itself. Since reactive species are able to damage cellular structures, especially proteins, as the most abundant macromolecule of mammalian cells, systems are necessary which regulate and preserve a functional cellular protein pool, in a process termed "proteostasis". Not only the mammalian protein pool is subject of a constant turnover, organelles are also degraded and rebuild. The most important systems for these removal processes are the "ubiquitin-proteasomal system" (UPS), the central proteolytic machinery of mammalian cells, mainly responsible for proteostasis, as well as the "autophagy-lysosomal system", which mediates the turnover of organelles and large aggregates. Many age-related pathologies and the aging process itself are accompanied by a dysregulation of UPS, autophagy and the cross-talk between both systems. This review will describe the sources and effects of oxidative stress, preservation of cellular protein- and organelle-homeostasis and the effects of aging on proteostasis in mammalian cells.The production of reactive species is an inevitable by-product of metabolism and thus, life itself. Since reactive species are able to damage cellular structures, especially proteins, as the most abundant macromolecule of mammalian cells, systems are necessary which regulate and preserve a functional cellular protein pool, in a process termed "proteostasis". Not only the mammalian protein pool is subject of a constant turnover, organelles are also degraded and rebuild. The most important systems for these removal processes are the "ubiquitin-proteasomal system" (UPS), the central proteolytic machinery of mammalian cells, mainly responsible for proteostasis, as well as the "autophagy-lysosomal system", which mediates the turnover of organelles and large aggregates. Many age-related pathologies and the aging process itself are accompanied by a dysregulation of UPS, autophagy and the cross-talk between both systems. This review will describe the sources and effects of oxidative stress, preservation of cellular protein- and organelle-homeostasis and the effects of aging on proteostasis in mammalian cells. The production of reactive species is an inevitable by-product of metabolism and thus, life itself. Since reactive species are able to damage cellular structures, especially proteins, as the most abundant macromolecule of mammalian cells, systems are necessary which regulate and preserve a functional cellular protein pool, in a process termed “proteostasis”. Not only the mammalian protein pool is subject of a constant turnover, organelles are also degraded and rebuild. The most important systems for these removal processes are the “ubiquitin-proteasomal system” (UPS), the central proteolytic machinery of mammalian cells, mainly responsible for proteostasis, as well as the “autophagy-lysosomal system”, which mediates the turnover of organelles and large aggregates. Many age-related pathologies and the aging process itself are accompanied by a dysregulation of UPS, autophagy and the cross-talk between both systems. This review will describe the sources and effects of oxidative stress, preservation of cellular protein- and organelle-homeostasis and the effects of aging on proteostasis in mammalian cells. fx1 The production of reactive species is an inevitable by-product of metabolism and thus, life itself. Since reactive species are able to damage cellular structures, especially proteins, as the most abundant macromolecule of mammalian cells, systems are necessary which regulate and preserve a functional cellular protein pool, in a process termed “proteostasis”. Not only the mammalian protein pool is subject of a constant turnover, organelles are also degraded and rebuild. The most important systems for these removal processes are the “ubiquitin-proteasomal system” (UPS), the central proteolytic machinery of mammalian cells, mainly responsible for proteostasis, as well as the “autophagy-lysosomal system”, which mediates the turnover of organelles and large aggregates. Many age-related pathologies and the aging process itself are accompanied by a dysregulation of UPS, autophagy and the cross-talk between both systems. This review will describe the sources and effects of oxidative stress, preservation of cellular protein- and organelle-homeostasis and the effects of aging on proteostasis in mammalian cells. [Display omitted] |
Author | Korovila, Ioanna Hugo, Martín Höhn, Annika Weber, Daniela Grune, Tilman Castro, José Pedro Jung, Tobias |
AuthorAffiliation | b German Center for Diabetes Research (DZD), 85764 Muenchen-Neuherberg, Germany d NutriAct – Competence Cluster Nutrition Research Berlin-Potsdam, 14558 Nuthetal, Germany a Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbruecke (DIfE), 14558 Nuthetal, Germany f Institute for Innovation and Health Research (I3S), Aging and Stress Group, R. Alfredo Allen, 4200-135 Porto, Portugal c German Center for Cardiovascular Research (DZHK), 10117 Berlin, Germany e Faculty of Medicine, Department of Biomedicine, University of Porto, 4200-319, Portugal |
AuthorAffiliation_xml | – name: e Faculty of Medicine, Department of Biomedicine, University of Porto, 4200-319, Portugal – name: f Institute for Innovation and Health Research (I3S), Aging and Stress Group, R. Alfredo Allen, 4200-135 Porto, Portugal – name: d NutriAct – Competence Cluster Nutrition Research Berlin-Potsdam, 14558 Nuthetal, Germany – name: a Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbruecke (DIfE), 14558 Nuthetal, Germany – name: b German Center for Diabetes Research (DZD), 85764 Muenchen-Neuherberg, Germany – name: c German Center for Cardiovascular Research (DZHK), 10117 Berlin, Germany |
Author_xml | – sequence: 1 givenname: Ioanna surname: Korovila fullname: Korovila, Ioanna organization: Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbruecke (DIfE), 14558 Nuthetal, Germany – sequence: 2 givenname: Martín surname: Hugo fullname: Hugo, Martín organization: Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbruecke (DIfE), 14558 Nuthetal, Germany – sequence: 3 givenname: José Pedro surname: Castro fullname: Castro, José Pedro organization: Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbruecke (DIfE), 14558 Nuthetal, Germany – sequence: 4 givenname: Daniela surname: Weber fullname: Weber, Daniela organization: Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbruecke (DIfE), 14558 Nuthetal, Germany – sequence: 5 givenname: Annika surname: Höhn fullname: Höhn, Annika organization: Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbruecke (DIfE), 14558 Nuthetal, Germany – sequence: 6 givenname: Tilman surname: Grune fullname: Grune, Tilman organization: Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbruecke (DIfE), 14558 Nuthetal, Germany – sequence: 7 givenname: Tobias surname: Jung fullname: Jung, Tobias email: tobias.jung@dife.de organization: Department of Molecular Toxicology, German Institute of Human Nutrition Potsdam-Rehbruecke (DIfE), 14558 Nuthetal, Germany |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/28763764$$D View this record in MEDLINE/PubMed |
BookMark | eNqNUU1vVCEUJaaNrbW_wMTMsgtnyueDWWjSNGqbNNGFrgkPLiOTNzACM7b_XmZebdouVHITCNxzDueeV-ggpggIvSF4RjDpzpezDC7dzigmcoZbYfUCHVNK2JQyIg8enY_QaSlL3JZSnBL8Eh1RJTsmO36Mzr7mVCGVakoo7ybpNjhTwxYmpWYoZWKim5hFiIvX6NCbocDp_X6Cvn_6-O3yanrz5fP15cXN1Aoq6tR4Ch1xmLGeUCsYkwrPGXeGMm87rxQm3jIvPZMglBdS9F3HiWRGECk5ZifoeuR1ySz1OoeVyXc6maD3FykvtMk12AG0FMAdbioUM06p73tQtrdWWmB-zkjj4iPXJq7N3S8zDA-EBOvdHPVS7-eod3PUuBVWDfZhhK03_QqchVizGZ785elLDD_0Im21EKxrDhvB2T1BTj83UKpehWJhGEyEtCmazKkQhMt969vHWg8ifxJqDfOxweZUSgavbagtorSTDsM_jLBn2P-z_35EQYt5GyDrYgNECy5ksLXlEP6K_w0DzM39 |
CitedBy_id | crossref_primary_10_1016_j_freeradbiomed_2018_08_037 crossref_primary_10_3390_ijms20092366 crossref_primary_10_3390_cells13211788 crossref_primary_10_3389_fmolb_2021_658742 crossref_primary_10_1016_j_arr_2020_101209 crossref_primary_10_1007_s11357_022_00698_x crossref_primary_10_1002_ctm2_1731 crossref_primary_10_1134_S0006297920100053 crossref_primary_10_18632_aging_205269 crossref_primary_10_3390_ijms19020610 crossref_primary_10_3390_biomedicines12081767 crossref_primary_10_3390_ijms20163896 crossref_primary_10_31832_smj_728050 crossref_primary_10_1016_j_arr_2020_101203 crossref_primary_10_1155_2022_1225578 crossref_primary_10_1007_s11356_021_16693_2 crossref_primary_10_1016_j_phymed_2021_153757 crossref_primary_10_1073_pnas_2101410118 crossref_primary_10_1155_2021_9932218 crossref_primary_10_3390_ijms24065508 crossref_primary_10_1016_j_btre_2024_e00833 crossref_primary_10_1016_j_biopha_2024_117090 crossref_primary_10_1016_j_abb_2020_108749 crossref_primary_10_1016_j_clnu_2023_11_007 crossref_primary_10_1016_j_jmb_2020_01_020 crossref_primary_10_1016_j_psj_2020_12_005 crossref_primary_10_1016_j_sjbs_2022_103363 crossref_primary_10_1111_nph_16365 crossref_primary_10_1038_s41598_020_64265_0 crossref_primary_10_3390_ijms19051495 crossref_primary_10_1016_j_exer_2023_109770 crossref_primary_10_1007_s11926_018_0724_6 crossref_primary_10_1155_2022_2249749 crossref_primary_10_1016_j_phytol_2023_01_001 crossref_primary_10_3390_antiox13030260 crossref_primary_10_1155_2021_5577498 crossref_primary_10_1038_s41392_023_01343_5 crossref_primary_10_1016_j_jbc_2023_104649 crossref_primary_10_1016_j_arr_2021_101456 crossref_primary_10_3934_agrfood_2024026 crossref_primary_10_1002_chem_202102344 crossref_primary_10_3390_biom15010113 crossref_primary_10_1007_s00114_019_1649_2 crossref_primary_10_7717_peerj_13715 crossref_primary_10_1096_fj_201701176R crossref_primary_10_1016_j_freeradbiomed_2020_02_014 crossref_primary_10_1007_s11357_024_01208_x crossref_primary_10_1039_C8FO02431F crossref_primary_10_1016_j_ijbiomac_2024_130726 crossref_primary_10_3389_pore_2024_1611623 crossref_primary_10_1186_s13024_023_00658_9 crossref_primary_10_3233_JAD_181052 crossref_primary_10_1016_j_mad_2023_111869 crossref_primary_10_1111_eci_14229 crossref_primary_10_3389_fgene_2024_1345459 crossref_primary_10_1051_medsci_2020221 crossref_primary_10_3390_biomedicines12122811 crossref_primary_10_3390_diagnostics14070764 crossref_primary_10_1016_j_mad_2021_111430 crossref_primary_10_1038_s41598_023_45045_y crossref_primary_10_1016_j_cbd_2021_100872 crossref_primary_10_3389_fnut_2024_1445080 crossref_primary_10_1111_acel_14344 crossref_primary_10_3390_antiox10030367 crossref_primary_10_1155_2020_8141307 crossref_primary_10_1016_j_bbrep_2024_101757 crossref_primary_10_1089_rej_2022_0052 crossref_primary_10_5483_BMBRep_2019_52_1_291 crossref_primary_10_3390_cells8111320 crossref_primary_10_3390_ijms20205148 crossref_primary_10_1016_j_neuint_2018_12_018 crossref_primary_10_1038_s41420_025_02295_1 crossref_primary_10_1074_jbc_RA118_002104 crossref_primary_10_1128_iai_00437_22 crossref_primary_10_1016_j_preteyeres_2020_100858 crossref_primary_10_1016_j_smim_2023_101838 crossref_primary_10_3390_ijms20143379 crossref_primary_10_1002_biot_201700652 crossref_primary_10_1016_j_freeradbiomed_2024_03_026 crossref_primary_10_1007_s10522_023_10050_1 crossref_primary_10_1007_s11357_019_00058_2 crossref_primary_10_3389_fcell_2021_637084 crossref_primary_10_3390_cells9051308 crossref_primary_10_1155_2020_5860356 crossref_primary_10_3390_cells11050829 crossref_primary_10_1016_j_brainres_2024_149202 crossref_primary_10_1007_s00266_023_03322_1 crossref_primary_10_3390_microorganisms10010014 crossref_primary_10_1007_s12035_021_02659_5 crossref_primary_10_1093_jambio_lxad065 crossref_primary_10_3389_fcell_2019_00143 crossref_primary_10_1016_j_abb_2022_109416 crossref_primary_10_1016_j_yjmcc_2019_12_009 crossref_primary_10_3390_molecules24152841 crossref_primary_10_3390_cells7120279 crossref_primary_10_1016_j_pestbp_2019_03_017 crossref_primary_10_1016_j_isci_2025_112118 crossref_primary_10_1002_mrd_70013 crossref_primary_10_1016_j_antiviral_2020_104989 crossref_primary_10_1016_j_cellsig_2018_10_019 crossref_primary_10_1111_acel_13481 crossref_primary_10_1016_j_ibmb_2022_103774 crossref_primary_10_1016_j_nbd_2024_106645 crossref_primary_10_31857_S0320972521030040 crossref_primary_10_3390_ijms24087221 crossref_primary_10_1002_bit_27899 crossref_primary_10_1080_19336934_2021_1911286 crossref_primary_10_3390_cimb46120872 crossref_primary_10_1093_femsyr_foy054 crossref_primary_10_1016_j_jhep_2020_10_034 crossref_primary_10_1155_2018_2450748 crossref_primary_10_3389_fmed_2022_837222 crossref_primary_10_1016_j_bbamcr_2021_119041 crossref_primary_10_1016_j_bbrc_2021_02_135 crossref_primary_10_1097_JTCCM_D_23_00016 crossref_primary_10_3389_fcvm_2019_00068 crossref_primary_10_3390_ijms23031174 crossref_primary_10_1089_rej_2022_0027 crossref_primary_10_1111_aos_16661 crossref_primary_10_3390_biology11070996 crossref_primary_10_3389_fphys_2021_701151 crossref_primary_10_1016_j_exger_2022_112011 crossref_primary_10_3389_fphar_2019_00020 crossref_primary_10_3390_ijms23010111 crossref_primary_10_1007_s12035_024_04430_y crossref_primary_10_1073_pnas_1912531117 crossref_primary_10_3390_antiox10030343 crossref_primary_10_3390_cells12020249 crossref_primary_10_3390_biom11030469 crossref_primary_10_1186_s13578_024_01260_2 crossref_primary_10_1080_15548627_2022_2128019 crossref_primary_10_3389_fphar_2024_1459909 crossref_primary_10_3390_biom11121789 crossref_primary_10_1016_j_mad_2023_111857 crossref_primary_10_1016_j_nbd_2023_106111 crossref_primary_10_3390_antiox10060952 crossref_primary_10_1089_ars_2020_8176 crossref_primary_10_1007_s11055_022_01219_1 crossref_primary_10_1021_acs_jproteome_2c00383 crossref_primary_10_3390_insects15120991 crossref_primary_10_1016_j_exger_2021_111552 crossref_primary_10_1016_j_chembiol_2021_04_003 crossref_primary_10_1021_acschemneuro_1c00099 crossref_primary_10_14336_AD_2024_0579 crossref_primary_10_3390_ijms21061976 crossref_primary_10_1111_resp_13303 crossref_primary_10_1111_acel_13065 crossref_primary_10_1111_jpi_12515 crossref_primary_10_1096_fj_202300978RR crossref_primary_10_1134_S0006297921030056 crossref_primary_10_3389_fnins_2020_00213 crossref_primary_10_3390_antiox10101535 crossref_primary_10_3390_ijms20010210 crossref_primary_10_2174_1573401318666220531111219 crossref_primary_10_1016_j_ecoenv_2021_112299 crossref_primary_10_1021_acsnano_3c09634 crossref_primary_10_1002_biof_1937 crossref_primary_10_1039_D3TB00984J crossref_primary_10_1016_j_rimpes_2022_100001 crossref_primary_10_1038_s41419_023_05744_w crossref_primary_10_3389_fnmol_2021_661993 crossref_primary_10_3390_ijms222312641 crossref_primary_10_1074_jbc_REV120_011743 crossref_primary_10_1016_j_metabol_2023_155585 crossref_primary_10_1016_j_exger_2018_10_018 crossref_primary_10_3390_antiox10040507 crossref_primary_10_1007_s10522_018_9775_3 crossref_primary_10_1021_acsomega_9b02375 crossref_primary_10_3233_JAD_221143 crossref_primary_10_3390_biology14030279 crossref_primary_10_1155_2018_9156285 crossref_primary_10_1093_jnen_nly024 crossref_primary_10_1111_febs_14927 crossref_primary_10_1039_D2RA04913A crossref_primary_10_1186_s12966_024_01654_y crossref_primary_10_3390_ijms25010513 crossref_primary_10_1016_j_mvr_2022_104380 crossref_primary_10_1186_s12014_022_09360_2 crossref_primary_10_3389_fcimb_2019_00435 crossref_primary_10_7554_eLife_70467 |
Cites_doi | 10.1016/S0047-6374(98)00152-3 10.1074/jbc.M111.277145 10.1172/JCI80514 10.1016/j.tcb.2010.03.007 10.1074/jbc.M008528200 10.1073/pnas.0908764107 10.1111/j.1471-4159.2008.05762.x 10.1093/emboj/21.11.2636 10.1021/jp410046w 10.1089/rej.2006.0513 10.1529/biophysj.104.049221 10.1128/MCB.23.23.8786-8794.2003 10.1080/15548627.2015.1034410 10.1016/S0021-9258(18)41681-X 10.1016/j.exer.2006.12.002 10.1073/pnas.96.11.6223 10.1016/j.jnutbio.2015.08.001 10.1016/j.freeradbiomed.2016.08.002 10.1016/j.redox.2017.01.017 10.1074/jbc.M709040200 10.1016/j.freeradbiomed.2014.10.774 10.1016/j.immuni.2009.10.009 10.1074/jbc.M413007200 10.1016/j.bbamcr.2013.05.026 10.1089/ars.2015.6494 10.7554/eLife.07545 10.1002/biof.1274 10.1016/j.freeradbiomed.2014.10.631 10.1016/j.cub.2014.06.004 10.1096/fj.14-252189 10.1146/annurev-biophys-083012-130417 10.1089/ars.2016.6815 10.1091/mbc.e11-08-0668 10.1006/abbi.1999.1657 10.1111/jpi.12189 10.1089/rej.2005.8.3 10.1038/ni.2060 10.1096/fj.00-0210com 10.1016/j.freeradbiomed.2014.11.013 10.1016/j.arr.2016.07.001 10.1016/j.freeradbiomed.2010.10.700 10.1006/jmbi.1999.2995 10.1038/cr.2013.168 10.1016/j.tcb.2015.03.002 10.18632/aging.100820 10.1016/j.phrs.2012.10.002 10.7554/eLife.01856 10.1006/abbi.2001.2663 10.1038/nsb0395-199 10.1016/j.cell.2012.12.016 10.1016/j.ajhg.2010.10.031 10.1016/j.molcel.2008.03.004 10.1111/j.1742-4658.2008.06441.x 10.1006/abbi.1996.0195 10.3389/fmicb.2015.00021 10.1074/jbc.M109.028902 10.1074/jbc.M110.129718 10.1074/jbc.M113.537175 10.1042/BST20150014 10.1007/s00018-011-0865-5 10.1073/pnas.93.26.15036 10.3389/fmicb.2012.00066 10.1016/j.cellsig.2010.06.004 10.1016/j.febslet.2009.12.047 10.1016/j.redox.2012.10.001 10.3390/cells5020024 10.1128/MCB.01204-10 10.1016/B978-0-12-397863-9.00003-1 10.1007/s00018-010-0565-6 10.1016/j.molcel.2010.09.012 10.1016/j.febslet.2006.06.029 10.1038/cr.2013.153 10.1016/j.freeradbiomed.2016.10.492 10.1006/abbi.2001.2332 10.1016/j.bbapap.2004.08.010 10.1186/1753-6561-5-S2-S4 10.1016/S0092-8674(94)90462-6 10.1242/jcs.093567 10.1016/j.freeradbiomed.2005.11.023 10.1016/j.redox.2013.01.004 10.1016/S0969-2126(02)00748-7 10.1016/B978-0-12-397863-9.00007-9 10.1042/bse0550119 10.1016/j.freeradbiomed.2012.08.591 10.1002/stem.1764 10.3389/fnmol.2014.00072 10.1016/j.cell.2010.08.002 10.1016/j.bcp.2012.11.016 10.1073/pnas.94.14.7156 10.1262/jrd.2012-096 10.1159/000351323 10.1016/S0047-6374(98)00011-6 10.1016/j.bbamcr.2008.01.002 10.1002/eji.201444902 10.1038/cr.2015.107 10.1016/S0891-5849(01)00480-4 10.1080/10715760600918142 10.1007/s00018-008-8291-z 10.1016/j.ceb.2016.01.006 10.4161/auto.28448 10.1016/j.devcel.2010.12.003 10.1016/j.freeradbiomed.2015.12.031 10.1016/j.cub.2016.08.008 10.1042/bse0550001 10.1128/MCB.01227-08 10.1016/j.tibs.2013.06.003 10.1038/80992 10.1016/j.mam.2009.04.001 10.1091/mbc.e07-11-1155 10.1073/pnas.1222244110 10.1016/j.redox.2013.12.008 10.1016/0092-8674(86)90807-X 10.1006/abbi.2000.2036 10.1016/j.febslet.2004.11.003 10.1073/pnas.0707025105 10.3109/10409238.2016.1172554 10.1016/j.molcel.2010.02.029 10.1016/j.biocel.2016.08.008 10.1080/15548627.2015.1017186 10.1111/j.1398-9995.2011.02551.x 10.1038/ncb2324 10.1016/j.redox.2013.12.029 10.1038/nrm3565 10.1038/nature11315 10.1016/j.freeradbiomed.2009.12.010 10.1074/jbc.M109.031575 10.3390/cancers2021354 10.1080/13813450701531235 10.1128/MCB.02070-07 10.1038/srep38299 10.1007/978-1-4020-6051-9_6 10.1111/nyas.12953 10.1016/j.bbamcr.2013.08.012 10.3390/ijms160817193 10.1016/j.abb.2003.10.010 10.4161/auto.26448 10.1006/bbrc.1996.0039 10.1016/j.redox.2013.01.006 10.1016/j.freeradbiomed.2012.05.039 10.1242/jcs.001073 10.1016/j.ymeth.2014.12.005 10.1016/j.redox.2016.10.015 10.1038/nrm2673 10.1074/jbc.M301048200 10.1080/15548627.2016.1147671 10.1038/nm.1851 10.1080/15548627.2015.1127464 10.1016/j.mam.2016.04.007 10.1111/j.1469-7793.2001.0001j.x 10.1002/eji.201445272 10.1042/BJ20070082 10.1038/360597a0 10.1016/S0531-5565(00)00137-6 10.1080/15384101.2016.1181876 10.1016/j.abb.2008.12.007 10.1042/bse0550079 10.1089/ars.2010.3766 10.1016/0891-5849(89)90028-2 10.1038/scientificamerican0563-64 10.1101/pdb.prot086272 10.1016/j.freeradbiomed.2011.03.031 10.1016/0891-5849(96)00175-X 10.4049/jimmunol.1300802 10.1038/nrn2499 10.1002/pro.2415 10.1089/ars.2011.4123 10.1101/cshperspect.a000158 10.1074/jbc.M116.736744 10.3389/fcell.2014.00068 10.1126/science.1141915 10.1016/j.tibs.2015.05.001 10.1146/annurev.pharmtox.051208.165340 10.1096/fj.00-0209com 10.1084/jem.181.4.1459 10.1080/15257770802138558 10.1016/j.bcp.2008.07.017 10.1074/jbc.M513737200 10.1038/nrm3270 10.1093/gbe/evv068 10.1016/j.abb.2012.04.018 10.1016/j.redox.2013.12.003 10.1016/j.arr.2016.04.010 10.1016/j.biochi.2011.03.004 10.1016/j.freeradbiomed.2010.12.011 10.1172/JCI73946 10.1007/s00204-015-1579-5 10.1073/pnas.1106015108 10.1128/MCB.01266-09 10.1074/jbc.M110.212027 10.1038/ncb1975 10.1096/fj.03-0177fje |
ContentType | Journal Article |
Copyright | 2017 The Authors Copyright © 2017 The Authors. Published by Elsevier B.V. All rights reserved. 2017 The Authors 2017 |
Copyright_xml | – notice: 2017 The Authors – notice: Copyright © 2017 The Authors. Published by Elsevier B.V. All rights reserved. – notice: 2017 The Authors 2017 |
DBID | 6I. AAFTH AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8 5PM ADTOC UNPAY DOA |
DOI | 10.1016/j.redox.2017.07.008 |
DatabaseName | ScienceDirect Open Access Titles Elsevier:ScienceDirect:Open Access CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic PubMed Central (Full Participant titles) Unpaywall for CDI: Periodical Content Unpaywall DOAJ Directory of Open Access Journals |
DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic |
DatabaseTitleList | MEDLINE MEDLINE - Academic |
Database_xml | – sequence: 1 dbid: DOA name: DOAJ Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 2 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 3 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database – sequence: 4 dbid: UNPAY name: Unpaywall url: https://proxy.k.utb.cz/login?url=https://unpaywall.org/ sourceTypes: Open Access Repository |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Biology |
EISSN | 2213-2317 |
EndPage | 567 |
ExternalDocumentID | oai_doaj_org_article_75e4d02c5203422fbbe8cbcc7ce3f931 10.1016/j.redox.2017.07.008 PMC5536880 28763764 10_1016_j_redox_2017_07_008 S2213231716304694 |
Genre | Journal Article Review |
GroupedDBID | 0R~ 0SF 457 53G 5VS 6I. AACTN AAEDT AAEDW AAFTH AAIKJ AALRI AAXUO ABGSF ABMAC ACGFS ADBBV ADEZE ADRAZ ADUVX AENEX AEXQZ AFTJW AGHFR AITUG ALMA_UNASSIGNED_HOLDINGS AMRAJ AOIJS BAWUL BCNDV DIK EBS EJD FDB GROUPED_DOAJ HYE HZ~ IPNFZ IXB M48 MO0 M~E NCXOZ O-L O9- OK1 RIG ROL RPM SSZ AAYWO AAYXX ACVFH ADCNI ADVLN AEUPX AFJKZ AFPUW AIGII AKBMS AKRWK AKYEP APXCP CITATION CGR CUY CVF ECM EIF NPM 7X8 5PM ADTOC UNPAY |
ID | FETCH-LOGICAL-c525t-af2e61d033b12c533780934da23fc6f8801fc3f7f37e58f575b664173a5177403 |
IEDL.DBID | IXB |
ISSN | 2213-2317 |
IngestDate | Wed Aug 27 01:25:46 EDT 2025 Wed Oct 01 15:30:00 EDT 2025 Tue Sep 30 16:43:00 EDT 2025 Fri Jul 11 15:46:36 EDT 2025 Wed Feb 19 02:41:49 EST 2025 Thu Apr 24 22:54:24 EDT 2025 Tue Jul 01 00:47:00 EDT 2025 Thu Jul 20 20:15:28 EDT 2023 |
IsDoiOpenAccess | true |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | C |
Keywords | Redox shift Oxidative stress Autophagy Lysosome Proteasome |
Language | English |
License | This is an open access article under the CC BY-NC-ND license. Copyright © 2017 The Authors. Published by Elsevier B.V. All rights reserved. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). cc-by-nc-nd |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c525t-af2e61d033b12c533780934da23fc6f8801fc3f7f37e58f575b664173a5177403 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 ObjectType-Review-3 content type line 23 |
OpenAccessLink | https://www.sciencedirect.com/science/article/pii/S2213231716304694 |
PMID | 28763764 |
PQID | 1925514780 |
PQPubID | 23479 |
PageCount | 18 |
ParticipantIDs | doaj_primary_oai_doaj_org_article_75e4d02c5203422fbbe8cbcc7ce3f931 unpaywall_primary_10_1016_j_redox_2017_07_008 pubmedcentral_primary_oai_pubmedcentral_nih_gov_5536880 proquest_miscellaneous_1925514780 pubmed_primary_28763764 crossref_citationtrail_10_1016_j_redox_2017_07_008 crossref_primary_10_1016_j_redox_2017_07_008 elsevier_sciencedirect_doi_10_1016_j_redox_2017_07_008 |
ProviderPackageCode | CITATION AAYXX |
PublicationCentury | 2000 |
PublicationDate | 2017-10-01 |
PublicationDateYYYYMMDD | 2017-10-01 |
PublicationDate_xml | – month: 10 year: 2017 text: 2017-10-01 day: 01 |
PublicationDecade | 2010 |
PublicationPlace | Netherlands |
PublicationPlace_xml | – name: Netherlands |
PublicationTitle | Redox biology |
PublicationTitleAlternate | Redox Biol |
PublicationYear | 2017 |
Publisher | Elsevier B.V Elsevier |
Publisher_xml | – name: Elsevier B.V – name: Elsevier |
References | Tai, Schuman (bib42) 2008; 9 Johnston-Carey, Pomatto, Davies (bib70) 2015; 51 Bandyopadhyay, Kaushik, Varticovski, Cuervo (bib122) 2008; 28 Sahu, Kaushik, Clement, Cannizzo, Scharf, Follenzi, Potolicchio, Nieves, Cuervo, Santambrogio (bib123) 2011; 20 Pacifici, Salo, Davies (bib28) 1989; 7 De Duve (bib103) 1963; 208 Chondrogianni, Tzavelas, Pemberton, Nezis, Rivett, Gonos (bib186) 2005; 280 Gavilan, Castano, Torres, Portavella, Caballero, Jimenez, Garcia-Martinez, Parrado, Vitorica, Ruano (bib75) 2009; 108 Stadtman, Van Remmen, Richardson, Wehr, Levine (bib8) 2005; 1703 Feng, He, Yao, Klionsky (bib104) 2014; 24 Konig, Ott, Hugo, Jung, Bulteau, Grune, Hohn (bib168) 2017; 11 Kiffin, Kaushik, Zeng, Bandyopadhyay, Zhang, Massey, Martinez-Vicente, Cuervo (bib181) 2007; 120 Catalgol, Wendt, Grimm, Breusing, Ozer, Grune (bib159) 2010; 48 Sautin, Johnson (bib1) 2008; 27 Poole (bib14) 2015; 80 Diaz-Villanueva, Diaz-Molina, Garcia-Gonzalez (bib57) 2015; 16 Hohn, Sittig, Jung, Grimm, Grune (bib160) 2012; 53 Husom, Peters, Kolling, Fugere, Thompson, Ferrington (bib171) 2004; 421 Klionsky, Eskelinen, Deretic (bib115) 2014; 10 Ulbricht, Gehlert, Leciejewski, Schiffer, Bloch, Hohfeld (bib125) 2015; 11 Kaushik, Massey, Mizushima, Cuervo (bib183) 2008; 19 Urbe, Liu, Hayes, Heride, Rigden, Clague (bib54) 2012; 23 Valko, Jomova, Rhodes, Kuca, Musilek (bib3) 2016; 90 Cascio, Call, Petre, Walz, Goldberg (bib38) 2002; 21 Israel (bib140) 2010; 2 Lapierre, Kumsta, Sandri, Ballabio, Hansen (bib196) 2015; 11 Schafer, Buettner (bib2) 2001; 30 Stadtman (bib9) 2006; 40 Di Cola (bib64) 1992; 41 Morozova, Clement, Kaushik, Stiller, Arias, Ahmad, Rauch, Chatterjee, Melis, Scharf, Gestwicki, Cuervo, Zuiderweg, Santambrogio (bib117) 2016; 291 Jonsson, Lowther (bib10) 2007; 44 Ullrich, Reinheckel, Sitte, Hass, Grune, Davies (bib155) 1999; 96 Korolchuk, Menzies, Rubinsztein (bib184) 2010; 584 Bauckman, Owusu-Boaitey, Mysorekar (bib110) 2015; 75 Reeg, Jung, Castro, Davies, Henze, Grune (bib30) 2016; 99 Stratford, Chondrogianni, Trougakos, Gonos, Rivett (bib76) 2006; 580 Esclatine, Chaumorcel, Codogno (bib105) 2009; 335 Tsukamoto, Hara, Yamamoto, Ohta, Wada, Ishida, Kito, Nishikawa, Minami, Sato, Kokubo (bib99) 2013; 59 Cuervo, Wong (bib119) 2014; 24 Kim, You, Lee, Ahn, Seong, Hwang (bib147) 2010; 22 Stewart, Koss, Bathina, Perciavalle, Bisanz, Opferman (bib49) 2010; 30 Wardyn, Ponsford, Sanderson (bib139) 2015; 43 Suzuki, Kodera, Saito, Fujimoto, Momozono, Hayashi, Kamata, Shichiri (bib7) 2016; 6 Bulteau, Szweda, Friguet (bib167) 2002; 397 Demasi, Shringarpure, Davies (bib86) 2001; 389 Fort, Kajava, Delsuc, Coux (bib83) 2015; 7 Luciani, Kesmir, Mishto, Or-Guil, de Boer (bib33) 2005; 88 van Deventer, Neefjes (bib69) 2010; 142 Jung, Hohn, Catalgol, Grune (bib178) 2009; 483 Murakami, Matsufuji, Kameji, Hayashi, Igarashi, Tamura, Tanaka, Ichihara (bib51) 1992; 360 Tsvetkov, Myers, Eliav, Adamovich, Hagai, Adler, Navon, Shaul (bib40) 2014; 289 Mauro, Leow, Anso, Rocha, Thotakura, Tornatore, Moretti, De Smaele, Beg, Tergaonkar, Chandel, Franzoso (bib142) 2011; 13 Hayashi, Goto (bib173) 1998; 102 Kravtsova-Ivantsiv, Ciechanover (bib48) 2012; 125 Baraibar, Friguet (bib163) 2012; 109 Mailloux, Willmore (bib16) 2014; 2 Murata, Sasaki, Kishimoto, Niwa, Hayashi, Takahama, Tanaka (bib81) 2007; 316 Hohn, Grune (bib89) 2014; 2 Kapeta, Chondrogianni, Gonos (bib137) 2010; 285 Konig, Besoke, Stuetz, Malarski, Jahreis, Grune, Hohn (bib102) 2016; 42 Wenzel, Baumeister (bib27) 1995; 2 Kuehn, Dahlmann (bib65) 1996; 329 Jager, Groll, Huber, Wolf, Heinemeyer (bib24) 1999; 291 Demasi, Netto, Silva, Hand, de Oliveira, Bicev, Gozzo, Barros, Leme, Ohara (bib166) 2013; 2 Bryan, Olayanju, Goldring, Park (bib129) 2013; 85 Li, Yang, Mao (bib100) 2011; 68 Chondrogianni, Petropoulos, Franceschi, Friguet, Gonos (bib190) 2000; 35 Li, Li, Bao (bib118) 2012; 69 Jung, Catalgol, Grune (bib17) 2009; 30 Hulpke, Tampe (bib61) 2013; 38 Merker, Sitte, Grune (bib156) 2000; 375 Clague, Heride, Urbe (bib41) 2015; 25 Handy, Loscalzo (bib13) 2012; 16 Groll, Bajorek, Kohler, Moroder, Rubin, Huber, Glickman, Finley (bib26) 2000; 7 Hohn, Konig, Jung (bib39) 2016; 25 Sitte, Merker, Von Zglinicki, Grune, Davies (bib175) 2000; 14 Schwartz, Ciechanover (bib52) 2009; 49 Agarwal, Xing, Demartino, Mizrachi, Hernandez, Sousa, Martinez, dos Santos, Garg (bib71) 2010; 87 Seah, de Magalhaes Filho, Petrashen, Henderson, Laguer, Gonzalez, Dillin, Hansen, Lapierre (bib195) 2016; 12 Yuan, Pan, Shen (bib124) 2016 Chondrogianni, Georgila, Kourtis, Tavernarakis, Gonos (bib185) 2015; 29 Xilouri, Stefanis (bib116) 2016 Merker, Ullrich, Schmidt, Sitte, Grune (bib157) 2003; 17 Zhou, Dewille (bib50) 2007; 405 Zmijewski, Banerjee, Abraham (bib87) 2009; 284 Cheong, Klionsky (bib111) 2015; 25 Pickering, Linder, Zhang, Forman, Davies (bib77) 2012; 287 Jung, Hohn, Grune (bib92) 2014; 2 Hohn, Jung, Grimm, Catalgol, Weber, Grune (bib161) 2011; 50 Gallagher, Chan (bib112) 2013; 55 Madeo, Zimmermann, Maiuri, Kroemer (bib193) 2015; 125 La Penna, Hureau, Andreussi, Faller (bib4) 2013; 117 Rock, Gramm, Rothstein, Clark, Stein, Dick, Hwang, Goldberg (bib5) 1994; 78 Radhakrishnan, Lee, Young, Beskow, Chan, Deshaies (bib153) 2010; 38 Ott, Konig, Hohn, Jung, Grune (bib182) 2016; 101 Steffen, Seeger, Koch, Kruger (bib154) 2010; 40 Kapphahn, Bigelow, Ferrington (bib177) 2007; 84 Aizawa, Kawahara, Tanaka, Yokosawa (bib37) 1996; 218 Tonoki, Kuranaga, Tomioka, Hamazaki, Murata, Tanaka, Miura (bib189) 2009; 29 Settembre, Fraldi, Medina, Ballabio (bib96) 2013; 14 Piao, Amaravadi (bib97) 2016; 1371 Rom, Reznick (bib144) 2016; 98 Zanker, Chen (bib62) 2014; 44 Levine, Mosoni, Berlett, Stadtman (bib19) 1996; 93 Ferrington, Gregerson (bib66) 2012; 109 Hohn, Grune (bib169) 2013; 1 Kastle, Grune (bib199) 2011; 93 Pickering, Linder, Zhang, Forman, Davies (bib135) 2012; 287 Kwak, Wakabayashi, Greenlaw, Yamamoto, Kensler (bib136) 2003; 23 Szabo, Kovacs, Grune, Haczku, Virag (bib91) 2011; 66 Sen, Baltimore (bib141) 1986; 47 Unno, Mizushima, Morimoto, Tomisugi, Tanaka, Yasuoka, Tsukihara (bib197) 2002; 10 Mony, Benjamin, O'Rourke (bib98) 2016; 12 Hoshi, Heinemann (bib6) 2001; 531 Davies (bib95) 2016; 49 Jang, Wang, Kim, Lalli, Kosik (bib138) 2014; 32 Radhakrishnan, den Besten, Deshaies (bib150) 2014; 3 Mao, Liu, Li, Luo (bib58) 2008; 65 Jadhav, Wooten, Wooten (bib126) 2011; 5 Huang, Li, Su, Kong (bib130) 2015; 26 Vangala, Sotzny, Kruger, Deshaies, Radhakrishnan (bib151) 2016; 26 Sitte, Merker, Von Zglinicki, Davies, Grune (bib174) 2000; 14 Theodore, Kawai, Yang, Kleshchenko, Reddy, Villalta, Arinze (bib131) 2008; 283 Arendt, Hochstrasser (bib23) 1997; 94 Ashizawa, Higashi, Masuda, Ohga, Taira, Fujimuro (bib46) 2012; 3 Rabl, Smith, Yu, Chang, Goldberg, Cheng (bib32) 2008; 30 Huber, Teis (bib114) 2016; 39 Hetz (bib152) 2012; 13 Xing, Jameson, Hogquist (bib80) 2013; 110 Jung, Engels, Kaiser, Poppek, Grune (bib21) 2006; 40 Metzger, Pruneda, Klevit, Weissman (bib45) 2014; 1843 Schultz, Abdel-Mageed, Mondal (bib148) 2010; 2 Schmidt, Finley (bib164) 2014; 1843 Carroll, Hewitt, Korolchuk (bib179) 2013; 55 Ferrington, Kapphahn (bib165) 2004; 578 Kim, Kim, Fang, Russell, Kim, Fan, Liu, Zhong, Guan (bib113) 2013; 152 Phadwal (bib127) 2015; 2015 Kalinina, Chernov, Novichkova (bib15) 2014; 79 Pickering, Lehr, Miller (bib74) 2015; 125 Ott, Konig, Hohn, Jung, Grune (bib170) 2016; 10 Li, Khor, Xu, Shen, Jeong, Yu, Kong (bib132) 2008; 76 Yun, Stanhill, Yang, Zhang, Haynes, Xu, Neubert, Mor, Philips, Ron (bib187) 2008; 105 Vilchez, Morantte, Liu, Douglas, Merkwirth, Rodrigues, Manning, Dillin (bib188) 2012; 489 Zhao, Ulrich (bib47) 2010; 107 Lemasters (bib108) 2005; 8 Ben-Neriah, Karin (bib146) 2011; 12 Chondrogianni, Stratford, Trougakos, Friguet, Rivett, Gonos (bib176) 2003; 278 Huh, Kim, Jeong, Park, Kim, Huh, Kim, Woo, Rhee, Lee, Ha (bib12) 2012; 16 Liepe, Holzhutter, Bellavista, Kloetzel, Stumpf, Mishto (bib85) 2015; 4 Levine, Berlett, Moskovitz, Mosoni, Stadtman (bib18) 1999; 107 Mishto, Liepe, Textoris-Taube, Keller, Henklein, Weberruss, Dahlmann, Enenkel, Voigt, Kuckelkorn, Stumpf, Kloetzel (bib60) 2014; 44 Radhakrishnan, Lee, Young, Beskow, Chan, Deshaies (bib149) 2010; 38 Wehmer, Sakata (bib35) 2016; 79 Karademir, Bozaykut, Kartal Ozer (bib31) 2014; 75 Jung, Grune (bib22) 2013; 1 Wolberger (bib53) 2014; 23 Vriend, Reiter (bib56) 2015; 58 Kansanen, Kuosmanen, Leinonen, Levonen (bib128) 2013; 1 Lilienbaum (bib20) 2013; 4 Schulman, Harper (bib43) 2009; 10 Pickering, Davies (bib94) 2012; 523 Desvergne, Ugarte, Petropoulos, Friguet (bib55) 2014; 75 Kunimoto, Kimura, Uede, Okuda, Aoyagi, Furukawa, Kanazawa (bib72) 2013; 227 Yin (bib162) 1996; 21 Ullrich, Reinheckel, Sitte, Hass, Grune, Davies (bib90) 1999; 96 McCarthy, Weinberg (bib68) 2015; 6 Henderson, Erales, Hoyt, Coffino (bib84) 2011; 286 Kaushik, Cuervo (bib120) 2012; 66 Rada, Rojo, Chowdhry, McMahon, Hayes, Cuadrado (bib134) 2011; 31 Perkins, Nelson, Parsonage, Poole, Karplus (bib11) 2015; 40 Caniard, Ballweg, Lukas, Yildirim, Eickelberg, Meiners (bib67) 2015; 7 Shang, Taylor (bib93) 2011; 51 Stoka, Turk, Turk (bib101) 2016 Orlowski, Wilk (bib25) 2000; 383 Eisenberg, Knauer, Schauer, Buttner, Ruckenstuhl, Carmona-Gutierrez, Ring, Schroeder, Magnes, Antonacci, Fussi, Deszcz, Hartl, Schraml, Criollo, Megalou, Weiskopf, Laun, Heeren, Breitenbach, Grubeck-Loebenstein, Herker, Fahrenkrog, Frohlich, Sinner, Tavernarakis, Minois, Kroemer, Madeo (bib194) 2009; 11 Svenning, Johansen (bib107) 2013; 55 Kastle, Reeg, Rogowska-Wrzesinska, Grune (bib198) 2012; 53 Ristic, Tsou, Todi (bib44) 2014; 7 Katsiki, Chondrogianni, Chinou, Rivett, Gonos (bib191) 2007; 10 Papaevgeniou, Sakellari, Jha, Tavernarakis, Holmberg, Gonos, Chondrogianni (bib192) 2016; 25 Bedford, Paine, Sheppard, Mayer, Roelofs (bib36) 2010; 20 Shaik, Schiavi, Ventura (bib109) 2016; 15 Sha, Goldberg (bib82) 2014; 24 Gallagher, Williamson, Chan (bib106) 2016; 5 Altun, Besche, Overkleeft, Piccirillo, Edelmann, Kessler, Goldberg, Ulfhake (bib172) 2010; 285 Dubiel, Pratt, Ferrell, Rechsteiner (bib63) 1992; 267 Salazar, Rojo, Velasco, de Sagarra, Cuadrado (bib133) 2006; 281 Arima, Kinoshita, Mishima, Kanazawa, Kaneko, Mizushima, Ichinose, Nakamura, Hetz (10.1016/j.redox.2017.07.008_bib152) 2012; 13 Di Cola (10.1016/j.redox.2017.07.008_bib64) 1992; 41 Konig (10.1016/j.redox.2017.07.008_bib102) 2016; 42 Stewart (10.1016/j.redox.2017.07.008_bib49) 2010; 30 Jung (10.1016/j.redox.2017.07.008_bib178) 2009; 483 Murakami (10.1016/j.redox.2017.07.008_bib51) 1992; 360 Karademir (10.1016/j.redox.2017.07.008_bib31) 2014; 75 Bryan (10.1016/j.redox.2017.07.008_bib129) 2013; 85 Kapphahn (10.1016/j.redox.2017.07.008_bib177) 2007; 84 Cuervo (10.1016/j.redox.2017.07.008_bib119) 2014; 24 Stoka (10.1016/j.redox.2017.07.008_bib101) 2016 Gavilan (10.1016/j.redox.2017.07.008_bib75) 2009; 108 Steffen (10.1016/j.redox.2017.07.008_bib154) 2010; 40 Jung (10.1016/j.redox.2017.07.008_bib22) 2013; 1 Kastle (10.1016/j.redox.2017.07.008_bib198) 2012; 53 Wehmer (10.1016/j.redox.2017.07.008_bib35) 2016; 79 Huber (10.1016/j.redox.2017.07.008_bib114) 2016; 39 Zanker (10.1016/j.redox.2017.07.008_bib59) 2013; 191 Korolchuk (10.1016/j.redox.2017.07.008_bib184) 2010; 584 Sahu (10.1016/j.redox.2017.07.008_bib123) 2011; 20 Mishto (10.1016/j.redox.2017.07.008_bib60) 2014; 44 Lemasters (10.1016/j.redox.2017.07.008_bib108) 2005; 8 De Duve (10.1016/j.redox.2017.07.008_bib103) 1963; 208 Ashizawa (10.1016/j.redox.2017.07.008_bib46) 2012; 3 Vriend (10.1016/j.redox.2017.07.008_bib56) 2015; 58 Mony (10.1016/j.redox.2017.07.008_bib98) 2016; 12 Ulbricht (10.1016/j.redox.2017.07.008_bib125) 2015; 11 Sha (10.1016/j.redox.2017.07.008_bib82) 2014; 24 Unno (10.1016/j.redox.2017.07.008_bib197) 2002; 10 Jonsson (10.1016/j.redox.2017.07.008_bib10) 2007; 44 Poole (10.1016/j.redox.2017.07.008_bib14) 2015; 80 Clague (10.1016/j.redox.2017.07.008_bib41) 2015; 25 Agarwal (10.1016/j.redox.2017.07.008_bib71) 2010; 87 Kalinina (10.1016/j.redox.2017.07.008_bib15) 2014; 79 Caniard (10.1016/j.redox.2017.07.008_bib67) 2015; 7 Reeg (10.1016/j.redox.2017.07.008_bib30) 2016; 99 Schafer (10.1016/j.redox.2017.07.008_bib2) 2001; 30 Xing (10.1016/j.redox.2017.07.008_bib80) 2013; 110 Silva (10.1016/j.redox.2017.07.008_bib88) 2008; 275 Mailloux (10.1016/j.redox.2017.07.008_bib16) 2014; 2 Arima (10.1016/j.redox.2017.07.008_bib73) 2011; 108 Schmidt (10.1016/j.redox.2017.07.008_bib164) 2014; 1843 Ott (10.1016/j.redox.2017.07.008_bib182) 2016; 101 Kim (10.1016/j.redox.2017.07.008_bib113) 2013; 152 Huang (10.1016/j.redox.2017.07.008_bib130) 2015; 26 Liu (10.1016/j.redox.2017.07.008_bib145) 2008; 1783 McCarthy (10.1016/j.redox.2017.07.008_bib68) 2015; 6 Handy (10.1016/j.redox.2017.07.008_bib13) 2012; 16 Vangala (10.1016/j.redox.2017.07.008_bib151) 2016; 26 Bulteau (10.1016/j.redox.2017.07.008_bib167) 2002; 397 Settembre (10.1016/j.redox.2017.07.008_bib96) 2013; 14 Nitta (10.1016/j.redox.2017.07.008_bib79) 2010; 32 Husom (10.1016/j.redox.2017.07.008_bib171) 2004; 421 Wardyn (10.1016/j.redox.2017.07.008_bib139) 2015; 43 Zmijewski (10.1016/j.redox.2017.07.008_bib87) 2009; 284 Perkins (10.1016/j.redox.2017.07.008_bib11) 2015; 40 Radhakrishnan (10.1016/j.redox.2017.07.008_bib150) 2014; 3 Suzuki (10.1016/j.redox.2017.07.008_bib7) 2016; 6 Kunimoto (10.1016/j.redox.2017.07.008_bib72) 2013; 227 Mao (10.1016/j.redox.2017.07.008_bib58) 2008; 65 Lilienbaum (10.1016/j.redox.2017.07.008_bib20) 2013; 4 Ott (10.1016/j.redox.2017.07.008_bib170) 2016; 10 Sautin (10.1016/j.redox.2017.07.008_bib1) 2008; 27 Kravtsova-Ivantsiv (10.1016/j.redox.2017.07.008_bib48) 2012; 125 Rom (10.1016/j.redox.2017.07.008_bib144) 2016; 98 Yun (10.1016/j.redox.2017.07.008_bib187) 2008; 105 Sitte (10.1016/j.redox.2017.07.008_bib175) 2000; 14 Kansanen (10.1016/j.redox.2017.07.008_bib128) 2013; 1 Ferrington (10.1016/j.redox.2017.07.008_bib165) 2004; 578 Metzger (10.1016/j.redox.2017.07.008_bib45) 2014; 1843 Sen (10.1016/j.redox.2017.07.008_bib141) 1986; 47 Wolberger (10.1016/j.redox.2017.07.008_bib53) 2014; 23 Seah (10.1016/j.redox.2017.07.008_bib195) 2016; 12 Konig (10.1016/j.redox.2017.07.008_bib168) 2017; 11 Kaushik (10.1016/j.redox.2017.07.008_bib183) 2008; 19 Zanker (10.1016/j.redox.2017.07.008_bib62) 2014; 44 Ullrich (10.1016/j.redox.2017.07.008_bib90) 1999; 96 Li (10.1016/j.redox.2017.07.008_bib100) 2011; 68 Orlowski (10.1016/j.redox.2017.07.008_bib25) 2000; 383 Jung (10.1016/j.redox.2017.07.008_bib92) 2014; 2 Henderson (10.1016/j.redox.2017.07.008_bib84) 2011; 286 Lasch (10.1016/j.redox.2017.07.008_bib29) 2001; 276 Salazar (10.1016/j.redox.2017.07.008_bib133) 2006; 281 Pickering (10.1016/j.redox.2017.07.008_bib74) 2015; 125 Feng (10.1016/j.redox.2017.07.008_bib104) 2014; 24 Jadhav (10.1016/j.redox.2017.07.008_bib126) 2011; 5 Shaik (10.1016/j.redox.2017.07.008_bib109) 2016; 15 Merker (10.1016/j.redox.2017.07.008_bib156) 2000; 375 Demasi (10.1016/j.redox.2017.07.008_bib86) 2001; 389 Piao (10.1016/j.redox.2017.07.008_bib97) 2016; 1371 Jager (10.1016/j.redox.2017.07.008_bib24) 1999; 291 Gallagher (10.1016/j.redox.2017.07.008_bib106) 2016; 5 Altun (10.1016/j.redox.2017.07.008_bib172) 2010; 285 Kiffin (10.1016/j.redox.2017.07.008_bib181) 2007; 120 Groll (10.1016/j.redox.2017.07.008_bib26) 2000; 7 Bandyopadhyay (10.1016/j.redox.2017.07.008_bib122) 2008; 28 Wenzel (10.1016/j.redox.2017.07.008_bib27) 1995; 2 Bakondi (10.1016/j.redox.2017.07.008_bib158) 2011; 50 Pickering (10.1016/j.redox.2017.07.008_bib135) 2012; 287 Jung (10.1016/j.redox.2017.07.008_bib21) 2006; 40 Yin (10.1016/j.redox.2017.07.008_bib162) 1996; 21 Morozova (10.1016/j.redox.2017.07.008_bib117) 2016; 291 Merker (10.1016/j.redox.2017.07.008_bib157) 2003; 17 Zhao (10.1016/j.redox.2017.07.008_bib47) 2010; 107 Carroll (10.1016/j.redox.2017.07.008_bib179) 2013; 55 Cheong (10.1016/j.redox.2017.07.008_bib111) 2015; 25 Rock (10.1016/j.redox.2017.07.008_bib5) 1994; 78 Lapierre (10.1016/j.redox.2017.07.008_bib196) 2015; 11 Pacifici (10.1016/j.redox.2017.07.008_bib28) 1989; 7 Schulman (10.1016/j.redox.2017.07.008_bib43) 2009; 10 Pickering (10.1016/j.redox.2017.07.008_bib94) 2012; 523 Hohn (10.1016/j.redox.2017.07.008_bib169) 2013; 1 Fort (10.1016/j.redox.2017.07.008_bib83) 2015; 7 Phadwal (10.1016/j.redox.2017.07.008_bib127) 2015; 2015 Catalgol (10.1016/j.redox.2017.07.008_bib159) 2010; 48 Tonoki (10.1016/j.redox.2017.07.008_bib189) 2009; 29 Tsukamoto (10.1016/j.redox.2017.07.008_bib99) 2013; 59 Demasi (10.1016/j.redox.2017.07.008_bib166) 2013; 2 Baraibar (10.1016/j.redox.2017.07.008_bib163) 2012; 109 Hohn (10.1016/j.redox.2017.07.008_bib89) 2014; 2 Stricher (10.1016/j.redox.2017.07.008_bib121) 2013; 9 Chondrogianni (10.1016/j.redox.2017.07.008_bib190) 2000; 35 Ben-Neriah (10.1016/j.redox.2017.07.008_bib146) 2011; 12 Stratford (10.1016/j.redox.2017.07.008_bib76) 2006; 580 Hohn (10.1016/j.redox.2017.07.008_bib160) 2012; 53 Ferrington (10.1016/j.redox.2017.07.008_bib66) 2012; 109 Chondrogianni (10.1016/j.redox.2017.07.008_bib176) 2003; 278 Diaz-Villanueva (10.1016/j.redox.2017.07.008_bib57) 2015; 16 Esclatine (10.1016/j.redox.2017.07.008_bib105) 2009; 335 Stadtman (10.1016/j.redox.2017.07.008_bib9) 2006; 40 Wright (10.1016/j.redox.2017.07.008_bib78) 1995; 181 Kim (10.1016/j.redox.2017.07.008_bib147) 2010; 22 Rabl (10.1016/j.redox.2017.07.008_bib32) 2008; 30 La Penna (10.1016/j.redox.2017.07.008_bib4) 2013; 117 Arendt (10.1016/j.redox.2017.07.008_bib23) 1997; 94 Hohn (10.1016/j.redox.2017.07.008_bib161) 2011; 50 Bedford (10.1016/j.redox.2017.07.008_bib36) 2010; 20 Theodore (10.1016/j.redox.2017.07.008_bib131) 2008; 283 Eisenberg (10.1016/j.redox.2017.07.008_bib194) 2009; 11 Valko (10.1016/j.redox.2017.07.008_bib3) 2016; 90 Murata (10.1016/j.redox.2017.07.008_bib81) 2007; 316 Desvergne (10.1016/j.redox.2017.07.008_bib55) 2014; 75 Liepe (10.1016/j.redox.2017.07.008_bib85) 2015; 4 Radhakrishnan (10.1016/j.redox.2017.07.008_bib153) 2010; 38 Li (10.1016/j.redox.2017.07.008_bib118) 2012; 69 Hohn (10.1016/j.redox.2017.07.008_bib39) 2016; 25 Hoshi (10.1016/j.redox.2017.07.008_bib6) 2001; 531 Cascio (10.1016/j.redox.2017.07.008_bib38) 2002; 21 Kaushik (10.1016/j.redox.2017.07.008_bib120) 2012; 66 Aizawa (10.1016/j.redox.2017.07.008_bib37) 1996; 218 Mauro (10.1016/j.redox.2017.07.008_bib142) 2011; 13 Chondrogianni (10.1016/j.redox.2017.07.008_bib185) 2015; 29 Klionsky (10.1016/j.redox.2017.07.008_bib115) 2014; 10 Shang (10.1016/j.redox.2017.07.008_bib93) 2011; 51 Katsiki (10.1016/j.redox.2017.07.008_bib191) 2007; 10 Dubiel (10.1016/j.redox.2017.07.008_bib63) 1992; 267 Zhou (10.1016/j.redox.2017.07.008_bib50) 2007; 405 Pickering (10.1016/j.redox.2017.07.008_bib77) 2012; 287 Tai (10.1016/j.redox.2017.07.008_bib42) 2008; 9 Jung (10.1016/j.redox.2017.07.008_bib17) 2009; 30 Stadtman (10.1016/j.redox.2017.07.008_bib8) 2005; 1703 Kish-Trier (10.1016/j.redox.2017.07.008_bib34) 2013; 42 Kapeta (10.1016/j.redox.2017.07.008_bib137) 2010; 285 Sitte (10.1016/j.redox.2017.07.008_bib174) 2000; 14 Zhang (10.1016/j.redox.2017.07.008_bib180) 2008; 14 van Deventer (10.1016/j.redox.2017.07.008_bib69) 2010; 142 Papaevgeniou (10.1016/j.redox.2017.07.008_bib192) 2016; 25 Kuehn (10.1016/j.redox.2017.07.008_bib65) 1996; 329 Israel (10.1016/j.redox.2017.07.008_bib140) 2010; 2 Tsvetkov (10.1016/j.redox.2017.07.008_bib40) 2014; 289 Hulpke (10.1016/j.redox.2017.07.008_bib61) 2013; 38 Radhakrishnan (10.1016/j.redox.2017.07.008_bib149) 2010; 38 Bauckman (10.1016/j.redox.2017.07.008_bib110) 2015; 75 Schultz (10.1016/j.redox.2017.07.008_bib148) 2010; 2 Levine (10.1016/j.redox.2017.07.008_bib19) 1996; 93 Schwartz (10.1016/j.redox.2017.07.008_bib52) 2009; 49 Huh (10.1016/j.redox.2017.07.008_bib12) 2012; 16 Xilouri (10.1016/j.redox.2017.07.008_bib116) 2016 Kwak (10.1016/j.redox.2017.07.008_bib136) 2003; 23 Vilchez (10.1016/j.redox.2017.07.008_bib188) 2012; 489 Szabo (10.1016/j.redox.2017.07.008_bib91) 2011; 66 Jang (10.1016/j.redox.2017.07.008_bib138) 2014; 32 Ristic (10.1016/j.redox.2017.07.008_bib44) 2014; 7 Yuan (10.1016/j.redox.2017.07.008_bib124) 2016 Madeo (10.1016/j.redox.2017.07.008_bib193) 2015; 125 Kastle (10.1016/j.redox.2017.07.008_bib199) 2011; 93 Chondrogianni (10.1016/j.redox.2017.07.008_bib186) 2005; 280 Johnston-Carey (10.1016/j.redox.2017.07.008_bib70) 2015; 51 Hayashi (10.1016/j.redox.2017.07.008_bib173) 1998; 102 Gallagher (10.1016/j.redox.2017.07.008_bib112) 2013; 55 Luciani (10.1016/j.redox.2017.07.008_bib33) 2005; 88 Urbe (10.1016/j.redox.201 12736271 - J Biol Chem. 2003 Jul 25;278(30):28026-37 18084892 - Subcell Biochem. 2007;44:115-41 21284655 - Allergy. 2011 Jul;66(7):811-4 18435761 - FEBS J. 2008 Jun;275(11):2942-55 27187479 - Cells. 2016 May 13;5(2):null 20385835 - Proc Natl Acad Sci U S A. 2010 Apr 27;107(17):7704-9 27125852 - Ageing Res Rev. 2016 Dec;32:22-37 25688236 - Front Microbiol. 2015 Jan 29;6:21 26886723 - Antioxid Redox Signal. 2016 Dec 1;25(16):855-869 18158642 - Arch Physiol Biochem. 2007 Oct-Dec;113(4-5):163-72 26067716 - Trends Biochem Sci. 2015 Aug;40(8):435-45 20940294 - J Biol Chem. 2010 Dec 17;285(51):39597-608 26393687 - Elife. 2015 Sep 22;4:e07545 27095633 - Biofactors. 2016 May;42(3):307-15 23080372 - J Reprod Dev. 2013;59(1):33-9 19802559 - Curr Top Microbiol Immunol. 2009;335:33-70 11099467 - FASEB J. 2000 Dec;14(15):2495-502 20025963 - Free Radic Biol Med. 2010 Mar 1;48(5):673-80 22298430 - Mol Biol Cell. 2012 Mar;23 (6):1095-103 11115501 - J Biol Chem. 2001 Mar 23;276(12):9492-502 26599426 - Ann N Y Acad Sci. 2016 May;1371(1):45-54 25749165 - Biochemistry (Mosc). 2014 Dec;79(13):1562-83 27050453 - Autophagy. 2016;12 (4):619-31 20427185 - Trends Cell Biol. 2010 Jul;20(7):391-401 19801973 - Nat Cell Biol. 2009 Nov;11(11):1305-14 11795886 - Arch Biochem Biophys. 2002 Jan 15;397(2):298-304 22308036 - J Biol Chem. 2012 Mar 23;287(13):10021-31 20723753 - Cell. 2010 Aug 20;142(4):517-8 20045355 - Immunity. 2010 Jan 29;32(1):29-40 17540904 - Science. 2007 Jun 1;316(5829):1349-53 17518699 - Rejuvenation Res. 2007 Jun;10(2):157-72 8619639 - Arch Biochem Biophys. 1996 May 1;329(1):87-96 28160744 - Redox Biol. 2017 Apr;11:673-681 3096580 - Cell. 1986 Dec 26;47(6):921-8 18241676 - Biochim Biophys Acta. 2008 May;1783(5):713-27 8573136 - Biochem Biophys Res Commun. 1996 Jan 5;218(1):224-8 19135972 - Arch Biochem Biophys. 2009 Mar 1;483(1):127-35 24313818 - J Phys Chem B. 2013 Dec 27;117(51):16455-67 26540298 - Aging (Albany NY). 2015 Oct;7(10):776-92 22251901 - Nat Rev Mol Cell Biol. 2012 Jan 18;13(2):89-102 23638318 - Int J Biochem Mol Biol. 2013 Mar 31;4(1):1-26 22982048 - Free Radic Biol Med. 2012 Nov 1;53(9):1760-9 12897070 - FASEB J. 2003 Oct;17(13):1963-5 25836756 - Autophagy. 2015;11(6):867-80 22080117 - Cell Mol Life Sci. 2012 Apr;69(7):1125-36 22564544 - Arch Biochem Biophys. 2012 Jul 15;523(2):181-90 25433365 - Free Radic Biol Med. 2015 Mar;80:148-57 22375140 - Front Microbiol. 2012 Feb 23;3:66 14612418 - Mol Cell Biol. 2003 Dec;23 (23 ):8786-94 18644871 - Mol Cell Biol. 2008 Sep;28(18):5747-63 8986759 - Proc Natl Acad Sci U S A. 1996 Dec 24;93(26):15036-40 27928720 - J Physiol Sci. 2016 Dec 7;:null 27929071 - Sci Rep. 2016 Dec 08;6:38299 23332761 - Cell. 2013 Jan 17;152(1-2):290-303 14678786 - Arch Biochem Biophys. 2004 Jan 1;421(1):67-76 19075009 - Mol Cell Biol. 2009 Feb;29(4):1095-106 26671266 - Autophagy. 2016;12 (2):261-72 19549781 - J Biol Chem. 2009 Aug 14;284(33):22213-21 22727424 - Prog Mol Biol Transl Sci. 2012;109:249-75 22146081 - Antioxid Redox Signal. 2012 Jun 1;16(11):1323-67 25497060 - Methods. 2015 Mar;75:120-7 23709680 - J Immunol. 2013 Jul 1;191(1):52-9 21772280 - Nat Immunol. 2011 Jul 19;12(8):715-23 11097171 - Arch Biochem Biophys. 2000 Nov 1;383(1):1-16 23569244 - Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):6979-84 25943340 - Genome Biol Evol. 2015 May 04;7(5):1363-79 27825071 - Redox Biol. 2016 Dec;10 :266-273 21238931 - Dev Cell. 2011 Jan 18;20(1):131-9 27498116 - Free Radic Biol Med. 2016 Oct;99:153-166 23849087 - Trends Biochem Sci. 2013 Aug;38(8):412-20 21402121 - Biochimie. 2011 Jun;93(6):1076-9 23994620 - Biochim Biophys Acta. 2014 Jan;1843(1):13-25 25369242 - J Pineal Res. 2015 Jan;58(1):1-11 23059540 - Pharmacol Res. 2012 Dec;66(6):484-93 24403057 - Protein Sci. 2014 Apr;23 (4):344-53 24024136 - Redox Biol. 2013 Jan 18;1:45-9 15798367 - Rejuvenation Res. 2005 Spring;8(1):3-5 18694732 - Biochem Pharmacol. 2008 Dec 1;76(11):1485-9 19012754 - J Neurochem. 2009 Jan;108(1):260-72 24448410 - Elife. 2014;3:e01856 15589823 - FEBS Lett. 2004 Dec 17;578(3):217-23 22922647 - Nature. 2012 Sep 13;489(7415):263-8 10683247 - Arch Biochem Biophys. 2000 Mar 1;375(1):50-4 11339815 - Arch Biochem Biophys. 2001 May 15;389(2):254-63 15680221 - Biochim Biophys Acta. 2005 Jan 17;1703(2):135-40 20068043 - J Biol Chem. 2010 Mar 12;285(11):8171-84 18679578 - Cell Mol Life Sci. 2008 Dec;65(24):3971-80 27098648 - Crit Rev Biochem Mol Biol. 2015 Jul-Aug;51(4):268-81 24596095 - J Biol Chem. 2014 Apr 18;289(16):11272-81 27115480 - Cell Cycle. 2016 Jul 17;15(14 ):1805-6 18467495 - Proc Natl Acad Sci U S A. 2008 May 13;105(19):7094-9 20385086 - Mol Cell. 2010 Apr 9;38(1):17-28 12032076 - EMBO J. 2002 Jun 3;21(11):2636-45 1334232 - Nature. 1992 Dec 10;360(6404):597-9 24070467 - Essays Biochem. 2013;55:1-15 10339569 - Proc Natl Acad Sci U S A. 1999 May 25;96(11):6223-8 21129723 - Am J Hum Genet. 2010 Dec 10;87(6):866-72 8087844 - Cell. 1994 Sep 9;78(5):761-71 10360685 - Mech Ageing Dev. 1999 Mar 15;107(3):323-32 26343967 - Arch Toxicol. 2016 Jan;90(1):1-37 27676297 - Curr Biol. 2016 Sep 26;26(18):R834-5 25906909 - Trends Cell Biol. 2015 Jul;25(7):417-26 16806194 - FEBS Lett. 2006 Jul 10;580(16):3989-94 25654554 - J Clin Invest. 2015 Jan;125(1):85-93 25231383 - Eur J Immunol. 2014 Dec;44(12):3508-21 22389393 - J Cell Sci. 2012 Feb 1;125(Pt 3):539-48 17258201 - Exp Eye Res. 2007 Apr;84(4):646-54 24281119 - Cancers (Basel). 2010 Jun 21;2(2):1354-78 10452902 - J Mol Biol. 1999 Aug 27;291(4):997-1013 23609508 - Nat Rev Mol Cell Biol. 2013 May;14(5):283-96 25191222 - Front Mol Neurosci. 2014 Aug 19;7:72 27412984 - Antioxid Redox Signal. 2016 Dec 1;25(16):902-917 26551702 - Biochem Soc Trans. 2015 Aug;43(4):621-6 21554762 - BMC Proc. 2011 May 28;5 Suppl 2:S4 11368918 - Free Radic Biol Med. 2001 Jun 1;30(11):1191-212 23747565 - Biochim Biophys Acta. 2014 Jan;1843(1):47-60 23414347 - Annu Rev Biophys. 2013;42:29-49 20976518 - Cell Mol Life Sci. 2011 Mar;68(5):749-63 24070473 - Essays Biochem. 2013;55:79-92 27405763 - J Biol Chem. 2016 Aug 26;291(35):18096-106 20600852 - Cell Signal. 2010 Nov;22(11):1645-54 18834306 - Annu Rev Pharmacol Toxicol. 2009;49:73-96 14025755 - Sci Am. 1963 May;208:64-72 24024146 - Redox Biol. 2013 Jan 19;1:140-4 7773788 - Nat Struct Biol. 1995 Mar;2(3):199-204 17090414 - Free Radic Res. 2006 Dec;40(12):1250-8 24657946 - Autophagy. 2014 Apr;10(4):549-51 11062564 - Nat Struct Biol. 2000 Nov;7(11):1062-7 25866968 - J Clin Invest. 2015 May;125(5):2059-68 21530648 - Free Radic Biol Med. 2011 Jul 1;51(1):5-16 23942189 - Dermatology. 2013;227(1):26-30 25453035 - Front Cell Dev Biol. 2014 Nov 17;2:68 23219527 - Biochem Pharmacol. 2013 Mar 15;85(6):705-17 18690243 - Nat Med. 2008 Sep;14(9):959-65 21852578 - Proc Natl Acad Sci U S A. 2011 Sep 6;108(36):14914-9 17284523 - J Cell Sci. 2007 Mar 1;120(Pt 5):782-91 25395451 - FASEB J. 2015 Feb;29(2):611-22 26358187 - Cell Res. 2015 Oct;25(10 ):1085-6 26461299 - Free Radic Biol Med. 2014 Oct;75 Suppl 1:S18 26330623 - Cold Spring Harb Protoc. 2015 Sep 01;2015(9):pdb.prot086272 25714469 - Autophagy. 2015;11(3):538-46 22727420 - Prog Mol Biol Transl Sci. 2012;109:75-112 24024151 - Redox Biol. 2013 Jan 19;1:178-82 16551619 - J Biol Chem. 2006 May 26;281(21):14841-51 25399798 - Eur J Immunol. 2014 Dec;44(12):3500-3 21167934 - Free Radic Biol Med. 2011 Mar 1;50(5):585-91 24998528 - Curr Biol. 2014 Jul 21;24(14 ):1573-83 27112802 - Mol Aspects Med. 2016 Jun;49:1-7 24563857 - Redox Biol. 2014 Jan 14;2:388-94 20040365 - FEBS Lett. 2010 Apr 2;584(7):1393-8 27498189 - Int J Biochem Cell Biol. 2016 Oct;79:437-442 1429590 - J Biol Chem. 1992 Nov 5;267(31):22369-77 20385764 - Mol Cell Biol. 2010 Jun;30(12 ):3099-110 26738803 - Free Radic Biol Med. 2016 Sep;98 :218-230 24396728 - Redox Biol. 2013 Dec 14;2:44-51 26225966 - Int J Mol Sci. 2015 Jul 28;16(8):17193-230 27484893 - Ageing Res Rev. 2016 Dec;32:13-21 27789294 - Free Radic Biol Med. 2016 Dec;101:325-333 18337468 - Mol Biol Cell. 2008 May;19(5):2179-92 20300203 - Cold Spring Harb Perspect Biol. 2010 Mar;2(3):a000158 26827287 - Curr Opin Cell Biol. 2016 Apr;39:8-14 15661736 - J Biol Chem. 2005 Mar 25;280(12):11840-50 11053662 - Exp Gerontol. 2000 Sep;35(6-7):721-8 24895273 - Stem Cells. 2014 Oct;32(10):2616-25 11179387 - J Physiol. 2001 Feb 15;531(Pt 1):1-11 18471981 - Mol Cell. 2008 May 9;30(3):360-8 19371762 - Mol Aspects Med. 2009 Aug;30(4):191-296 26419687 - J Nutr Biochem. 2015 Dec;26(12 ):1401-13 7699330 - J Exp Med. 1995 Apr 1;181(4):1459-71 9663792 - Mech Ageing Dev. 1998 May 1;102(1):55-66 24281265 - Cell Res. 2014 Jan;24(1):92-104 21245377 - Mol Cell Biol. 2011 Mar;31(6):1121-33 18931696 - Nat Rev Neurosci. 2008 Nov;9(11):826-38 24121476 - Autophagy. 2013 Dec;9(12):1937-54 24366339 - Cell Res. 2014 Jan;24(1):24-41 19352404 - Nat Rev Mol Cell Biol. 2009 May;10 (5):319-31 22683819 - Free Radic Biol Med. 2012 Oct 1;53(7):1468-77 21454622 - J Biol Chem. 2011 May 20;286(20):17495-502 9207060 - Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7156-61 21902452 - Antioxid Redox Signal. 2012 Feb 1;16(3):229-43 16631520 - Free Radic Biol Med. 2006 Apr 15;40(8):1303-12 1428780 - Ital J Biochem. 1992 Jul-Aug;41(4):213-24 2558981 - Free Radic Biol Med. 1989;7(5):521-36 26461349 - Free Radic Biol Med. 2014 Oct;75 Suppl 1:S35 8902532 - Free Radic Biol Med. 1996;21(6):871-88 20932482 - Mol Cell. 2010 Oct 8;40(1):147-58 11099468 - FASEB J. 2000 Dec;14(15):2503-10 17373909 - Biochem J. 2007 Jul 15;405(2):341-9 18238777 - J Biol Chem. 2008 Apr 4;283(14):8984-94 21968997 - Nat Cell Biol. 2011 Aug 28;13(10):1272-9 18600514 - Nucleosides Nucleotides Nucleic Acids. 2008 Jun;27(6):608-19 20977936 - Free Radic Biol Med. 2011 Jan 1;50(1):86-92 24070476 - Essays Biochem. 2013;55:119-31 15665121 - Biophys J. 2005 Apr;88(4):2422-32 12015144 - Structure. 2002 May;10(5):609-18 25460724 - Redox Biol. 2014;2:99-104 |
References_xml | – volume: 5 year: 2016 ident: bib106 article-title: Advances in autophagy regulatory mechanisms publication-title: Cells – volume: 20 start-page: 391 year: 2010 end-page: 401 ident: bib36 article-title: Assembly, structure, and function of the 26S proteasome publication-title: Trends Cell Biol. – volume: 9 start-page: 1937 year: 2013 end-page: 1954 ident: bib121 article-title: HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting publication-title: Autophagy – volume: 23 start-page: 8786 year: 2003 end-page: 8794 ident: bib136 article-title: Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway publication-title: Mol. Cell Biol. – volume: 51 start-page: 5 year: 2011 end-page: 16 ident: bib93 article-title: Ubiquitin-proteasome pathway and cellular responses to oxidative stress publication-title: Free Radic. Biol. Med. – volume: 38 start-page: 17 year: 2010 end-page: 28 ident: bib149 article-title: Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells publication-title: Mol. Cell – volume: 6 start-page: 21 year: 2015 ident: bib68 article-title: The immunoproteasome and viral infection: a complex regulator of inflammation publication-title: Front. Microbiol. – volume: 108 start-page: 260 year: 2009 end-page: 272 ident: bib75 article-title: Age-related increase in the immunoproteasome content in rat hippocampus: molecular and functional aspects publication-title: J. Neurochem. – volume: 11 start-page: 538 year: 2015 end-page: 546 ident: bib125 article-title: Induction and adaptation of chaperone-assisted selective autophagy CASA in response to resistance exercise in human skeletal muscle publication-title: Autophagy – volume: 30 start-page: 191 year: 2009 end-page: 296 ident: bib17 article-title: The proteasomal system publication-title: Mol. Asp. Med. – volume: 94 start-page: 7156 year: 1997 end-page: 7161 ident: bib23 article-title: Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation publication-title: Proc. Natl. Acad. Sci. USA – year: 2016 ident: bib101 article-title: Lysosomal cathepsins and their regulation in aging and neurodegeneration publication-title: Ageing Res. Rev. – year: 2016 ident: bib116 article-title: Chaperone mediated autophagy in aging: starve to prosper publication-title: Ageing Res. Rev. – volume: 24 start-page: 92 year: 2014 end-page: 104 ident: bib119 article-title: Chaperone-mediated autophagy: roles in disease and aging publication-title: Cell Res. – volume: 79 start-page: 1562 year: 2014 end-page: 1583 ident: bib15 article-title: Role of glutathione, glutathione transferase, and glutaredoxin in regulation of redox-dependent processes publication-title: Biochemistry – volume: 285 start-page: 8171 year: 2010 end-page: 8184 ident: bib137 article-title: Nuclear erythroid factor 2-mediated proteasome activation delays senescence in human fibroblasts publication-title: J. Biol. Chem. – volume: 22 start-page: 1645 year: 2010 end-page: 1654 ident: bib147 article-title: Suppression of NF-kappaB signaling by KEAP1 regulation of IKKbeta activity through autophagic degradation and inhibition of phosphorylation publication-title: Cell. Signal. – volume: 142 start-page: 517 year: 2010 end-page: 518 ident: bib69 article-title: The immunoproteasome cleans up after inflammation publication-title: Cell – volume: 531 start-page: 1 year: 2001 end-page: 11 ident: bib6 article-title: Regulation of cell function by methionine oxidation and reduction publication-title: J. Physiol. – volume: 40 start-page: 147 year: 2010 end-page: 158 ident: bib154 article-title: Proteasomal degradation is transcriptionally controlled by TCF11 via an ERAD-dependent feedback loop publication-title: Mol. Cell – volume: 276 start-page: 9492 year: 2001 end-page: 9502 ident: bib29 article-title: Hydrogen peroxide-induced structural alterations of RNAse A publication-title: J. Biol. Chem. – volume: 102 start-page: 55 year: 1998 end-page: 66 ident: bib173 article-title: Age-related changes in the 20S and 26S proteasome activities in the liver of male F344 rats publication-title: Mech. Ageing Dev. – volume: 69 start-page: 1125 year: 2012 end-page: 1136 ident: bib118 article-title: Microautophagy: lesser-known self-eating publication-title: Cell Mol. Life Sci. – volume: 98 start-page: 218 year: 2016 end-page: 230 ident: bib144 article-title: The role of E3 ubiquitin-ligases MuRF-1 and MAFbx in loss of skeletal muscle mass publication-title: Free Radic. Biol. Med. – year: 2016 ident: bib124 article-title: Cardioprotection of exercise preconditioning involving heat shock protein 70 and concurrent autophagy: a potential chaperone-assisted selective macroautophagy effect publication-title: J. Physiol. Sci. – volume: 7 start-page: 1363 year: 2015 end-page: 1379 ident: bib83 article-title: Evolution of proteasome regulators in eukaryotes publication-title: Genome Biol. Evol. – volume: 7 start-page: 776 year: 2015 end-page: 792 ident: bib67 article-title: Proteasome function is not impaired in healthy aging of the lung publication-title: Aging – volume: 10 start-page: 157 year: 2007 end-page: 172 ident: bib191 article-title: The olive constituent oleuropein exhibits proteasome stimulatory properties in vitro and confers life span extension of human embryonic fibroblasts publication-title: Rejuvenation Res. – volume: 117 start-page: 16455 year: 2013 end-page: 16467 ident: bib4 article-title: Identifying, by first-principles simulations, Cu[amyloid-beta] species making Fenton-type reactions in Alzheimer's disease publication-title: J. Phys. Chem. B – volume: 152 start-page: 290 year: 2013 end-page: 303 ident: bib113 article-title: Differential regulation of distinct Vps34 complexes by AMPK in nutrient stress and autophagy publication-title: Cell – volume: 59 start-page: 33 year: 2013 end-page: 39 ident: bib99 article-title: Functional analysis of lysosomes during mouse preimplantation embryo development publication-title: J. Reprod. Dev. – volume: 191 start-page: 52 year: 2013 end-page: 59 ident: bib59 article-title: Mixed proteasomes function to increase viral peptide diversity and broaden antiviral CD8+ T cell responses publication-title: J. Immunol. – volume: 108 start-page: 14914 year: 2011 end-page: 14919 ident: bib73 article-title: Proteasome assembly defect due to a proteasome subunit beta type 8 (PSMB8) mutation causes the autoinflammatory disorder, Nakajo-Nishimura syndrome publication-title: Proc. Natl. Acad. Sci. USA – volume: 31 start-page: 1121 year: 2011 end-page: 1133 ident: bib134 article-title: SCF/{beta}-TrCP promotes glycogen synthase kinase 3-dependent degradation of the Nrf2 transcription factor in a Keap1-independent manner publication-title: Mol. Cell Biol. – volume: 110 start-page: 6979 year: 2013 end-page: 6984 ident: bib80 article-title: Thymoproteasome subunit-beta5T generates peptide-MHC complexes specialized for positive selection publication-title: Proc. Natl. Acad. Sci. USA – volume: 25 start-page: 1085 year: 2015 end-page: 1086 ident: bib111 article-title: mTORC1 maintains metabolic balance publication-title: Cell Res. – volume: 29 start-page: 611 year: 2015 end-page: 622 ident: bib185 article-title: 20S proteasome activation promotes life span extension and resistance to proteotoxicity in Caenorhabditis elegans publication-title: FASEB J.: Off. Publ. Fed. Am. Soc. Exp. Biol. – volume: 9 start-page: 826 year: 2008 end-page: 838 ident: bib42 article-title: Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction publication-title: Nat. Rev. Neurosci. – volume: 68 start-page: 749 year: 2011 end-page: 763 ident: bib100 article-title: Chaperone-mediated autophagy: machinery, regulation and biological consequences publication-title: Cell Mol. Life Sci. – volume: 3 start-page: e01856 year: 2014 ident: bib150 article-title: p97-dependent retrotranslocation and proteolytic processing govern formation of active Nrf1 upon proteasome inhibition publication-title: Elife – volume: 283 start-page: 8984 year: 2008 end-page: 8994 ident: bib131 article-title: Multiple nuclear localization signals function in the nuclear import of the transcription factor Nrf2 publication-title: J. Biol. Chem. – volume: 7 start-page: 1062 year: 2000 end-page: 1067 ident: bib26 article-title: A gated channel into the proteasome core particle publication-title: Nat. Struct. Biol. – volume: 35 start-page: 721 year: 2000 end-page: 728 ident: bib190 article-title: Fibroblast cultures from healthy centenarians have an active proteasome publication-title: Exp. Gerontol. – volume: 80 start-page: 148 year: 2015 end-page: 157 ident: bib14 article-title: The basics of thiols and cysteines in redox biology and chemistry publication-title: Free Radic. Biol. Med. – volume: 383 start-page: 1 year: 2000 end-page: 16 ident: bib25 article-title: Catalytic activities of the 20 S proteasome, a multicatalytic proteinase complex publication-title: Arch. Biochem. Biophys. – volume: 11 start-page: 673 year: 2017 end-page: 681 ident: bib168 article-title: Mitochondrial contribution to lipofuscin formation publication-title: Redox Biol. – volume: 14 start-page: 959 year: 2008 end-page: 965 ident: bib180 article-title: Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function publication-title: Nat. Med. – volume: 11 start-page: 1305 year: 2009 end-page: 1314 ident: bib194 article-title: Induction of autophagy by spermidine promotes longevity publication-title: Nat. Cell Biol. – volume: 109 start-page: 249 year: 2012 end-page: 275 ident: bib163 article-title: Changes of the proteasomal system during the aging process publication-title: Prog. Mol. Biol. Transl. Sci. – volume: 2 start-page: a000158 year: 2010 ident: bib140 article-title: The IKK complex, a central regulator of NF-kappaB activation publication-title: Cold Spring Harb. Perspect. Biol. – volume: 30 start-page: 1191 year: 2001 end-page: 1212 ident: bib2 article-title: Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple publication-title: Free Radic. Biol. Med. – volume: 227 start-page: 26 year: 2013 end-page: 30 ident: bib72 article-title: A new infant case of Nakajo-Nishimura syndrome with a genetic mutation in the immunoproteasome subunit: an overlapping entity with JMP and CANDLE syndrome related to PSMB8 mutations publication-title: Dermatology – volume: 96 start-page: 6223 year: 1999 end-page: 6228 ident: bib155 article-title: Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones publication-title: Proc. Natl. Acad. Sci. USA – volume: 2 start-page: 44 year: 2013 end-page: 51 ident: bib166 article-title: Redox regulation of the proteasome via S-glutathionylation publication-title: Redox Biol. – volume: 88 start-page: 2422 year: 2005 end-page: 2432 ident: bib33 article-title: A mathematical model of protein degradation by the proteasome publication-title: Biophys. J. – volume: 10 start-page: 319 year: 2009 end-page: 331 ident: bib43 article-title: Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways publication-title: Nat. Rev. Mol. Cell Biol. – volume: 44 start-page: 115 year: 2007 end-page: 141 ident: bib10 article-title: The peroxiredoxin repair proteins publication-title: Subcell. Biochem. – volume: 87 start-page: 866 year: 2010 end-page: 872 ident: bib71 article-title: PSMB8 encoding the beta5i proteasome subunit is mutated in joint contractures, muscle atrophy, microcytic anemia, and panniculitis-induced lipodystrophy syndrome publication-title: Am. J. Hum. Genet. – volume: 1843 start-page: 47 year: 2014 end-page: 60 ident: bib45 article-title: RING-type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination publication-title: Biochim. Biophys. Acta – volume: 15 start-page: 1805 year: 2016 end-page: 1806 ident: bib109 article-title: Mitochondrial autophagy promotes healthy aging publication-title: Cell Cycle – volume: 578 start-page: 217 year: 2004 end-page: 223 ident: bib165 article-title: Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal publication-title: FEBS Lett. – volume: 107 start-page: 323 year: 1999 end-page: 332 ident: bib18 article-title: Methionine residues may protect proteins from critical oxidative damage publication-title: Mech. Ageing Dev. – volume: 125 start-page: 539 year: 2012 end-page: 548 ident: bib48 article-title: Non-canonical ubiquitin-based signals for proteasomal degradation publication-title: J. Cell Sci. – volume: 55 start-page: 79 year: 2013 end-page: 92 ident: bib107 article-title: Selective autophagy publication-title: Essays Biochem. – volume: 181 start-page: 1459 year: 1995 end-page: 1471 ident: bib78 article-title: Coordinate regulation of the human TAP1 and LMP2 genes from a shared bidirectional promoter publication-title: J. Exp. Med. – volume: 75 start-page: S35 year: 2014 ident: bib31 article-title: Heat shock proteins and proteasomal degradation in normal and tumor cells publication-title: Free Radic. Biol. Med – volume: 284 start-page: 22213 year: 2009 end-page: 22221 ident: bib87 article-title: S-glutathionylation of the Rpn2 regulatory subunit inhibits 26 S proteasomal function publication-title: J. Biol. Chem. – volume: 107 start-page: 7704 year: 2010 end-page: 7709 ident: bib47 article-title: Distinct consequences of posttranslational modification by linear versus K63-linked polyubiquitin chains publication-title: Proc. Natl. Acad. Sci. USA – volume: 55 start-page: 119 year: 2013 end-page: 131 ident: bib179 article-title: Autophagy and ageing: implications for age-related neurodegenerative diseases publication-title: Essays Biochem. – volume: 44 start-page: 3508 year: 2014 end-page: 3521 ident: bib60 article-title: Proteasome isoforms exhibit only quantitative differences in cleavage and epitope generation publication-title: Eur. J. Immunol. – volume: 397 start-page: 298 year: 2002 end-page: 304 ident: bib167 article-title: Age-dependent declines in proteasome activity in the heart publication-title: Arch. Biochem. Biophys. – volume: 6 start-page: 38299 year: 2016 ident: bib7 article-title: Methionine sulfoxides in serum proteins as potential clinical biomarkers of oxidative stress publication-title: Sci. Rep. – volume: 21 start-page: 2636 year: 2002 end-page: 2645 ident: bib38 article-title: Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes publication-title: EMBO J. – volume: 30 start-page: 3099 year: 2010 end-page: 3110 ident: bib49 article-title: Ubiquitin-independent degradation of antiapoptotic MCL-1 publication-title: Mol. Cell. Biol. – volume: 27 start-page: 608 year: 2008 end-page: 619 ident: bib1 article-title: Uric acid: the oxidant-antioxidant paradox publication-title: Nucleosides Nucleotides Nucleic Acids – volume: 49 start-page: 1 year: 2016 end-page: 7 ident: bib95 article-title: Adaptive homeostasis publication-title: Mol. Asp. Med. – volume: 285 start-page: 39597 year: 2010 end-page: 39608 ident: bib172 article-title: Muscle wasting in aged, sarcopenic rats is associated with enhanced activity of the ubiquitin proteasome pathway publication-title: J. Biol. Chem. – volume: 75 start-page: S18 year: 2014 ident: bib55 article-title: Circadian modulation of proteasome activities and removal of carbonylated proteins publication-title: Free Radic. Biol. Med. – volume: 523 start-page: 181 year: 2012 end-page: 190 ident: bib94 article-title: Differential roles of proteasome and immunoproteasome regulators Pa28alphabeta, Pa28gamma and Pa200 in the degradation of oxidized proteins publication-title: Arch. Biochem. Biophys. – volume: 42 start-page: 307 year: 2016 end-page: 315 ident: bib102 article-title: Quantification of age-related changes of alpha-tocopherol in lysosomal membranes in murine tissues and human fibroblasts publication-title: Biofactors – volume: 11 start-page: 867 year: 2015 end-page: 880 ident: bib196 article-title: Transcriptional and epigenetic regulation of autophagy in aging publication-title: Autophagy – volume: 289 start-page: 11272 year: 2014 end-page: 11281 ident: bib40 article-title: NADH binds and stabilizes the 26S proteasomes independent of ATP publication-title: J. Biol. Chem. – volume: 208 start-page: 64 year: 1963 end-page: 72 ident: bib103 article-title: The lysosome publication-title: Sci. Am. – volume: 1783 start-page: 713 year: 2008 end-page: 727 ident: bib145 article-title: NF-kappaB/p65 antagonizes Nrf2-ARE pathway by depriving CBP from Nrf2 and facilitating recruitment of HDAC3 to MafK publication-title: Biochim. Biophys. Acta – volume: 286 start-page: 17495 year: 2011 end-page: 17502 ident: bib84 article-title: Dependence of proteasome processing rate on substrate unfolding publication-title: J. Biol. Chem. – volume: 1703 start-page: 135 year: 2005 end-page: 140 ident: bib8 article-title: Methionine oxidation and aging publication-title: Biochim. Biophys. Acta – volume: 335 start-page: 33 year: 2009 end-page: 70 ident: bib105 article-title: Macroautophagy signaling and regulation publication-title: Curr. Top. Microbiol. Immunol. – volume: 24 start-page: 24 year: 2014 end-page: 41 ident: bib104 article-title: The machinery of macroautophagy publication-title: Cell Res. – volume: 12 start-page: 261 year: 2016 end-page: 272 ident: bib195 article-title: Autophagy-mediated longevity is modulated by lipoprotein biogenesis publication-title: Autophagy – volume: 12 start-page: 715 year: 2011 end-page: 723 ident: bib146 article-title: Inflammation meets cancer, with NF-kappaB as the matchmaker publication-title: Nat. Immunol. – volume: 329 start-page: 87 year: 1996 end-page: 96 ident: bib65 article-title: Proteasome activator PA28 and its interaction with 20 S proteasomes publication-title: Arch. Biochem. Biophys. – volume: 389 start-page: 254 year: 2001 end-page: 263 ident: bib86 article-title: Glutathiolation of the proteasome is enhanced by proteolytic inhibitors publication-title: Arch. Biochem. Biophys. – volume: 66 start-page: 811 year: 2011 end-page: 814 ident: bib91 article-title: PARP-1: a new player in the asthma field? publication-title: Allergy – volume: 40 start-page: 435 year: 2015 end-page: 445 ident: bib11 article-title: Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling publication-title: Trends Biochem. Sci. – volume: 584 start-page: 1393 year: 2010 end-page: 1398 ident: bib184 article-title: Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems publication-title: FEBS Lett. – volume: 44 start-page: 3500 year: 2014 end-page: 3503 ident: bib62 article-title: Standard and immunoproteasomes show similar peptide degradation specificities publication-title: Eur. J. Immunol. – volume: 23 start-page: 344 year: 2014 end-page: 353 ident: bib53 article-title: Mechanisms for regulating deubiquitinating enzymes publication-title: Protein Sci. – volume: 4 start-page: 1 year: 2013 end-page: 26 ident: bib20 article-title: Relationship between the proteasomal system and autophagy publication-title: Int. J. Biochem. Mol. Biol. – volume: 21 start-page: 871 year: 1996 end-page: 888 ident: bib162 article-title: Biochemical basis of lipofuscin, ceroid, and age pigment-like fluorophores publication-title: Free Radic. Biol. Med. – volume: 125 start-page: 85 year: 2015 end-page: 93 ident: bib193 article-title: Essential role for autophagy in life span extension publication-title: J. Clin. Investig. – volume: 55 start-page: 1 year: 2013 end-page: 15 ident: bib112 article-title: Early signalling events of autophagy publication-title: Essays Biochem. – volume: 291 start-page: 997 year: 1999 end-page: 1013 ident: bib24 article-title: Proteasome beta-type subunits: unequal roles of propeptides in core particle maturation and a hierarchy of active site function publication-title: J. Mol. Biol. – volume: 267 start-page: 22369 year: 1992 end-page: 22377 ident: bib63 article-title: Purification of an 11 S regulator of the multicatalytic protease publication-title: J. Biol. Chem. – volume: 287 start-page: 10021 year: 2012 end-page: 10031 ident: bib77 article-title: Nrf2-dependent induction of proteasome and Pa28alphabeta regulator are required for adaptation to oxidative stress publication-title: J. Biol. Chem. – volume: 48 start-page: 673 year: 2010 end-page: 680 ident: bib159 article-title: Chromatin repair after oxidative stress: role of PARP-mediated proteasome activation publication-title: Free Radic. Biol. Med. – volume: 47 start-page: 921 year: 1986 end-page: 928 ident: bib141 article-title: Inducibility of kappa immunoglobulin enhancer-binding protein Nf-kappa B by a posttranslational mechanism publication-title: Cell – volume: 8 start-page: 3 year: 2005 end-page: 5 ident: bib108 article-title: Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging publication-title: Rejuvenation Res. – volume: 275 start-page: 2942 year: 2008 end-page: 2955 ident: bib88 article-title: Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome publication-title: FEBS J. – volume: 53 start-page: 1468 year: 2012 end-page: 1477 ident: bib198 article-title: Chaperones, but not oxidized proteins, are ubiquitinated after oxidative stress publication-title: Free Radic. Biol. Med. – volume: 99 start-page: 153 year: 2016 end-page: 166 ident: bib30 article-title: The molecular chaperone Hsp70 promotes the proteolytic removal of oxidatively damaged proteins by the proteasome publication-title: Free Radic. Biol. Med. – volume: 93 start-page: 15036 year: 1996 end-page: 15040 ident: bib19 article-title: Methionine residues as endogenous antioxidants in proteins publication-title: Proc. Natl. Acad. Sci. USA – volume: 218 start-page: 224 year: 1996 end-page: 228 ident: bib37 article-title: Activation of the proteasome during Xenopus egg activation implies a link between proteasome activation and intracellular calcium release publication-title: Biochem. Biophys. Res. Commun. – volume: 16 start-page: 17193 year: 2015 end-page: 17230 ident: bib57 article-title: Protein folding and mechanisms of proteostasis publication-title: Int. J. Mol. Sci. – volume: 12 start-page: 619 year: 2016 end-page: 631 ident: bib98 article-title: A lysosome-centered view of nutrient homeostasis publication-title: Autophagy – volume: 40 start-page: 1250 year: 2006 end-page: 1258 ident: bib9 article-title: Protein oxidation and aging publication-title: Free Radic. Res. – volume: 360 start-page: 597 year: 1992 end-page: 599 ident: bib51 article-title: Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination publication-title: Nature – volume: 66 start-page: 484 year: 2012 end-page: 493 ident: bib120 article-title: Chaperones in autophagy publication-title: Pharmacol. Res. – volume: 1 start-page: 140 year: 2013 end-page: 144 ident: bib169 article-title: Lipofuscin: formation, effects and role of macroautophagy publication-title: Redox Biol. – volume: 405 start-page: 341 year: 2007 end-page: 349 ident: bib50 article-title: Proteasome-mediated CCAAT/enhancer-binding protein delta (C/EBPdelta) degradation is ubiquitin-independent publication-title: Biochem. J. – volume: 13 start-page: 1272 year: 2011 end-page: 1279 ident: bib142 article-title: NF-kappaB controls energy homeostasis and metabolic adaptation by upregulating mitochondrial respiration publication-title: Nat. Cell Biol. – volume: 375 start-page: 50 year: 2000 end-page: 54 ident: bib156 article-title: Hydrogen peroxide-mediated protein oxidation in young and old human MRC-5 fibroblasts publication-title: Arch. Biochem. Biophys. – volume: 19 start-page: 2179 year: 2008 end-page: 2192 ident: bib183 article-title: Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy publication-title: Mol. Biol. Cell – volume: 2 start-page: 68 year: 2014 ident: bib16 article-title: S-glutathionylation reactions in mitochondrial function and disease publication-title: Front. Cell Dev. Biol. – volume: 42 start-page: 29 year: 2013 end-page: 49 ident: bib34 article-title: Structural biology of the proteasome publication-title: Annu. Rev. Biophys. – volume: 85 start-page: 705 year: 2013 end-page: 717 ident: bib129 article-title: The Nrf2 cell defence pathway: Keap1-dependent and -independent mechanisms of regulation publication-title: Biochem. Pharmacol. – volume: 1371 start-page: 45 year: 2016 end-page: 54 ident: bib97 article-title: Targeting the lysosome in cancer publication-title: Ann. N.Y. Acad. Sci. – volume: 50 start-page: 86 year: 2011 end-page: 92 ident: bib158 article-title: Age-related loss of stress-induced nuclear proteasome activation is due to low PARP-1 activity publication-title: Free Radic. Biol. Med. – volume: 41 start-page: 213 year: 1992 end-page: 224 ident: bib64 article-title: Human erythrocyte contains a factor that stimulates the peptidase activities of multicatalytic proteinase complex publication-title: Ital. J. Biochem. – volume: 96 start-page: 6223 year: 1999 end-page: 6228 ident: bib90 article-title: Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones publication-title: Proc. Natl. Acad. Sci. USA – volume: 26 start-page: R834 year: 2016 end-page: 835 ident: bib151 article-title: Nrf1 can be processed and activated in a proteasome-independent manner publication-title: Curr. Biol. – volume: 483 start-page: 127 year: 2009 end-page: 135 ident: bib178 article-title: Age-related differences in oxidative protein-damage in young and senescent fibroblasts publication-title: Arch. Biochem. Biophys. – volume: 10 start-page: 609 year: 2002 end-page: 618 ident: bib197 article-title: The structure of the mammalian 20S proteasome at 2.75 A resolution publication-title: Structure – volume: 2 start-page: 199 year: 1995 end-page: 204 ident: bib27 article-title: Conformational constraints in protein degradation by the 20S proteasome publication-title: Nat. Struct. Biol. – volume: 287 start-page: 10021 year: 2012 end-page: 10031 ident: bib135 article-title: Nrf2-dependent induction of proteasome and Pa28alphabeta regulator are required for adaptation to oxidative stress publication-title: J. Biol. Chem. – volume: 109 start-page: 75 year: 2012 end-page: 112 ident: bib66 article-title: Immunoproteasomes: structure, function, and antigen presentation publication-title: Prog. Mol. Biol. Transl. Sci. – volume: 10 start-page: 266 year: 2016 end-page: 273 ident: bib170 article-title: Macroautophagy is impaired in old murine brain tissue as well as in senescent human fibroblasts publication-title: Redox Biol. – volume: 24 start-page: 1573 year: 2014 end-page: 1583 ident: bib82 article-title: Proteasome-mediated processing of Nrf1 is essential for coordinate induction of all proteasome subunits and p97 publication-title: Curr. Biol. – volume: 20 start-page: 131 year: 2011 end-page: 139 ident: bib123 article-title: Microautophagy of cytosolic proteins by late endosomes publication-title: Dev. Cell – volume: 93 start-page: 1076 year: 2011 end-page: 1079 ident: bib199 article-title: Proteins bearing oxidation-induced carbonyl groups are not preferentially ubiquitinated publication-title: Biochimie – volume: 2 start-page: 388 year: 2014 end-page: 394 ident: bib89 article-title: The proteasome and the degradation of oxidized proteins: part III-Redox regulation of the proteasomal system publication-title: Redox Biol. – volume: 316 start-page: 1349 year: 2007 end-page: 1353 ident: bib81 article-title: Regulation of CD8+ T cell development by thymus-specific proteasomes publication-title: Science – volume: 90 start-page: 1 year: 2016 end-page: 37 ident: bib3 article-title: Redox- and non-redox-metal-induced formation of free radicals and their role in human disease publication-title: Arch. Toxicol. – volume: 14 start-page: 2495 year: 2000 end-page: 2502 ident: bib175 article-title: Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: Part I--effects of proliferative senescence publication-title: FASEB J.: Off. Publ. Fed. Am. Soc. Exp. Biol. – volume: 4 start-page: e07545 year: 2015 ident: bib85 article-title: Quantitative time-resolved analysis reveals intricate, differential regulation of standard- and immuno-proteasomes publication-title: Elife – volume: 39 start-page: 8 year: 2016 end-page: 14 ident: bib114 article-title: Lysosomal signaling in control of degradation pathways publication-title: Curr. Opin. Cell Biol. – volume: 78 start-page: 761 year: 1994 end-page: 771 ident: bib5 article-title: Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules publication-title: Cell – volume: 7 start-page: 521 year: 1989 end-page: 536 ident: bib28 article-title: Macroxyproteinase (M.O.P.): a 670 kDa proteinase complex that degrades oxidatively denatured proteins in red blood cells publication-title: Free Radic. Biol. Med – volume: 280 start-page: 11840 year: 2005 end-page: 11850 ident: bib186 article-title: Overexpression of proteasome beta5 assembled subunit increases the amount of proteasome and confers ameliorated response to oxidative stress and higher survival rates publication-title: J. Biol. Chem. – volume: 1843 start-page: 13 year: 2014 end-page: 25 ident: bib164 article-title: Regulation of proteasome activity in health and disease publication-title: Biochim. Biophys. Acta – volume: 75 start-page: 120 year: 2015 end-page: 127 ident: bib110 article-title: Selective autophagy: xenophagy publication-title: Methods – volume: 25 start-page: 902 year: 2016 end-page: 917 ident: bib39 article-title: Metabolic Syndrome, Redox State, and the Proteasomal System publication-title: Antioxid. Redox Signal – volume: 3 start-page: 66 year: 2012 ident: bib46 article-title: The ubiquitin system and Kaposi's sarcoma-associated Herpesvirus publication-title: Front. Microbiol. – volume: 43 start-page: 621 year: 2015 end-page: 626 ident: bib139 article-title: Dissecting molecular cross-talk between Nrf2 and NF-kappaB response pathways publication-title: Biochem. Soc. Trans. – volume: 25 start-page: 417 year: 2015 end-page: 426 ident: bib41 article-title: The demographics of the ubiquitin system publication-title: Trends Cell Biol. – volume: 1 start-page: 178 year: 2013 end-page: 182 ident: bib22 article-title: The proteasome and the degradation of oxidized proteins: Part I-structure of proteasomes publication-title: Redox Biol. – volume: 26 start-page: 1401 year: 2015 end-page: 1413 ident: bib130 article-title: The complexity of the Nrf2 pathway: beyond the antioxidant response publication-title: J. Nutr. Biochem. – volume: 38 start-page: 412 year: 2013 end-page: 420 ident: bib61 article-title: The MHC I loading complex: a multitasking machinery in adaptive immunity publication-title: Trends Biochem. Sci. – volume: 40 start-page: 1303 year: 2006 end-page: 1312 ident: bib21 article-title: Intracellular distribution of oxidized proteins and proteasome in HT22 cells during oxidative stress publication-title: Free Radic. Biol. Med. – volume: 58 start-page: 1 year: 2015 end-page: 11 ident: bib56 article-title: Melatonin feedback on clock genes: a theory involving the proteasome publication-title: J. Pineal Res. – volume: 105 start-page: 7094 year: 2008 end-page: 7099 ident: bib187 article-title: Proteasomal adaptation to environmental stress links resistance to proteotoxicity with longevity in Caenorhabditis elegans publication-title: Proc. Natl. Acad. Sci. USA – volume: 25 start-page: 855 year: 2016 end-page: 869 ident: bib192 article-title: 18alpha-glycyrrhetinic acid proteasome activator decelerates aging and alzheimer's disease progression in caenorhabditis elegans and neuronal cultures publication-title: Antioxid. Redox Signal. – volume: 2 start-page: 1354 year: 2010 end-page: 1378 ident: bib148 article-title: The nrf1 and nrf2 balance in oxidative stress regulation and androgen signaling in prostate cancer cells publication-title: Cancers – volume: 49 start-page: 73 year: 2009 end-page: 96 ident: bib52 article-title: Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology publication-title: Annu Rev. Pharmacol. Toxicol. – volume: 125 start-page: 2059 year: 2015 end-page: 2068 ident: bib74 article-title: Lifespan of mice and primates correlates with immunoproteasome expression publication-title: J. Clin. Investig. – volume: 14 start-page: 283 year: 2013 end-page: 296 ident: bib96 article-title: Signals from the lysosome: a control centre for cellular clearance and energy metabolism publication-title: Nat. Rev. Mol. Cell Biol. – volume: 7 start-page: 72 year: 2014 ident: bib44 article-title: An optimal ubiquitin-proteasome pathway in the nervous system: the role of deubiquitinating enzymes publication-title: Front. Mol. Neurosci. – volume: 17 start-page: 1963 year: 2003 end-page: 1965 ident: bib157 article-title: Stability of the nuclear protein turnover during cellular senescence of human fibroblasts publication-title: FASEB J. – volume: 2015 year: 2015 ident: bib127 article-title: Analyzing the colocalization of MAP1LC3 and lysosomal markers in primary cells publication-title: Cold Spring Harb. Protoc. – volume: 32 start-page: 29 year: 2010 end-page: 40 ident: bib79 article-title: Thymoproteasome shapes immunocompetent repertoire of CD8+ T cells publication-title: Immunity – volume: 278 start-page: 28026 year: 2003 end-page: 28037 ident: bib176 article-title: Central role of the proteasome in senescence and survival of human fibroblasts: induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation publication-title: J. Biol. Chem. – volume: 489 start-page: 263 year: 2012 end-page: 268 ident: bib188 article-title: RPN-6 determines C. elegans longevity under proteotoxic stress conditions publication-title: Nature – volume: 51 start-page: 268 year: 2015 end-page: 281 ident: bib70 article-title: The Immunoproteasome in oxidative stress, aging, and disease publication-title: Crit. Rev. Biochem. Mol. Biol. – volume: 29 start-page: 1095 year: 2009 end-page: 1106 ident: bib189 article-title: Genetic evidence linking age-dependent attenuation of the 26S proteasome with the aging process publication-title: Mol. Cell Biol. – volume: 23 start-page: 1095 year: 2012 end-page: 1103 ident: bib54 article-title: Systematic survey of deubiquitinase localization identifies USP21 as a regulator of centrosome- and microtubule-associated functions publication-title: Mol. Biol. Cell – volume: 580 start-page: 3989 year: 2006 end-page: 3994 ident: bib76 article-title: Proteasome response to interferon-gamma is altered in senescent human fibroblasts publication-title: FEBS Lett. – volume: 32 start-page: 2616 year: 2014 end-page: 2625 ident: bib138 article-title: Nrf2, a regulator of the proteasome, controls self-renewal and pluripotency in human embryonic stem cells publication-title: Stem Cells – volume: 421 start-page: 67 year: 2004 end-page: 76 ident: bib171 article-title: Altered proteasome function and subunit composition in aged muscle publication-title: Arch. Biochem. Biophys. – volume: 291 start-page: 18096 year: 2016 end-page: 18106 ident: bib117 article-title: Structural and biological interaction of hsc-70 protein with phosphatidylserine in endosomal microautophagy publication-title: J. Biol. Chem. – volume: 14 start-page: 2503 year: 2000 end-page: 2510 ident: bib174 article-title: Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: Part II--aging of nondividing cells publication-title: FASEB J.: Off. Publ. Fed. Am. Soc. Exp. Biol. – volume: 65 start-page: 3971 year: 2008 end-page: 3980 ident: bib58 article-title: REGgamma, a proteasome activator and beyond? publication-title: Cell Mol. Life Sci. – volume: 113 start-page: 163 year: 2007 end-page: 172 ident: bib143 article-title: Regulation of NADPH oxidase subunit p22(phox) by NF-kB in human aortic smooth muscle cells publication-title: Arch. Physiol. Biochem. – volume: 84 start-page: 646 year: 2007 end-page: 654 ident: bib177 article-title: Age-dependent inhibition of proteasome chymotrypsin-like activity in the retina publication-title: Exp. Eye Res. – volume: 2 start-page: 99 year: 2014 end-page: 104 ident: bib92 article-title: The proteasome and the degradation of oxidized proteins: Part II - protein oxidation and proteasomal degradation publication-title: Redox Biol. – volume: 101 start-page: 325 year: 2016 end-page: 333 ident: bib182 article-title: Reduced autophagy leads to an impaired ferritin turnover in senescent fibroblasts publication-title: Free Radic. Biol. Med. – volume: 76 start-page: 1485 year: 2008 end-page: 1489 ident: bib132 article-title: Activation of Nrf2-antioxidant signaling attenuates NFkappaB-inflammatory response and elicits apoptosis publication-title: Biochem. Pharmacol. – volume: 28 start-page: 5747 year: 2008 end-page: 5763 ident: bib122 article-title: The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane publication-title: Mol. Cell Biol. – volume: 281 start-page: 14841 year: 2006 end-page: 14851 ident: bib133 article-title: Glycogen synthase kinase-3beta inhibits the xenobiotic and antioxidant cell response by direct phosphorylation and nuclear exclusion of the transcription factor Nrf2 publication-title: J. Biol. Chem. – volume: 10 start-page: 549 year: 2014 end-page: 551 ident: bib115 article-title: Autophagosomes, phagosomes, autolysosomes, phagolysosomes, autophagolysosomes... wait, I'm confused publication-title: Autophagy – volume: 1 start-page: 45 year: 2013 end-page: 49 ident: bib128 article-title: The Keap1-Nrf2 pathway: mechanisms of activation and dysregulation in cancer publication-title: Redox Biol. – volume: 53 start-page: 1760 year: 2012 end-page: 1769 ident: bib160 article-title: Lipofuscin is formed independently of macroautophagy and lysosomal activity in stress-induced prematurely senescent human fibroblasts publication-title: Free Radic. Biol. Med. – volume: 50 start-page: 585 year: 2011 end-page: 591 ident: bib161 article-title: Lipofuscin inhibits the proteasome by binding to surface motifs publication-title: Free Radic. Biol. Med. – volume: 120 start-page: 782 year: 2007 end-page: 791 ident: bib181 article-title: Altered dynamics of the lysosomal receptor for chaperone-mediated autophagy with age publication-title: J. Cell Sci. – volume: 16 start-page: 229 year: 2012 end-page: 243 ident: bib12 article-title: Peroxiredoxin 3 is a key molecule regulating adipocyte oxidative stress, mitochondrial biogenesis, and adipokine expression publication-title: Antioxid. Redox Signal – volume: 30 start-page: 360 year: 2008 end-page: 368 ident: bib32 article-title: Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases publication-title: Mol. Cell – volume: 38 start-page: 17 year: 2010 end-page: 28 ident: bib153 article-title: Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells publication-title: Mol. Cell – volume: 79 start-page: 437 year: 2016 end-page: 442 ident: bib35 article-title: Recent advances in the structural biology of the 26S proteasome publication-title: Int. J. Biochem. Cell Biol. – volume: 5 start-page: S4 year: 2011 ident: bib126 article-title: Mining the TRAF6/p62 interactome for a selective ubiquitination motif publication-title: BMC Proc. – volume: 13 start-page: 89 year: 2012 end-page: 102 ident: bib152 article-title: The unfolded protein response: controlling cell fate decisions under ER stress and beyond publication-title: Nat. Rev. Mol. Cell Biol. – volume: 16 start-page: 1323 year: 2012 end-page: 1367 ident: bib13 article-title: Redox regulation of mitochondrial function publication-title: Antioxid. Redox Signal – volume: 107 start-page: 323 year: 1999 ident: 10.1016/j.redox.2017.07.008_bib18 article-title: Methionine residues may protect proteins from critical oxidative damage publication-title: Mech. Ageing Dev. doi: 10.1016/S0047-6374(98)00152-3 – volume: 287 start-page: 10021 year: 2012 ident: 10.1016/j.redox.2017.07.008_bib77 article-title: Nrf2-dependent induction of proteasome and Pa28alphabeta regulator are required for adaptation to oxidative stress publication-title: J. Biol. Chem. doi: 10.1074/jbc.M111.277145 – volume: 125 start-page: 2059 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib74 article-title: Lifespan of mice and primates correlates with immunoproteasome expression publication-title: J. Clin. Investig. doi: 10.1172/JCI80514 – volume: 20 start-page: 391 year: 2010 ident: 10.1016/j.redox.2017.07.008_bib36 article-title: Assembly, structure, and function of the 26S proteasome publication-title: Trends Cell Biol. doi: 10.1016/j.tcb.2010.03.007 – volume: 276 start-page: 9492 year: 2001 ident: 10.1016/j.redox.2017.07.008_bib29 article-title: Hydrogen peroxide-induced structural alterations of RNAse A publication-title: J. Biol. Chem. doi: 10.1074/jbc.M008528200 – volume: 107 start-page: 7704 year: 2010 ident: 10.1016/j.redox.2017.07.008_bib47 article-title: Distinct consequences of posttranslational modification by linear versus K63-linked polyubiquitin chains publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.0908764107 – volume: 108 start-page: 260 year: 2009 ident: 10.1016/j.redox.2017.07.008_bib75 article-title: Age-related increase in the immunoproteasome content in rat hippocampus: molecular and functional aspects publication-title: J. Neurochem. doi: 10.1111/j.1471-4159.2008.05762.x – volume: 21 start-page: 2636 year: 2002 ident: 10.1016/j.redox.2017.07.008_bib38 article-title: Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes publication-title: EMBO J. doi: 10.1093/emboj/21.11.2636 – volume: 117 start-page: 16455 year: 2013 ident: 10.1016/j.redox.2017.07.008_bib4 article-title: Identifying, by first-principles simulations, Cu[amyloid-beta] species making Fenton-type reactions in Alzheimer's disease publication-title: J. Phys. Chem. B doi: 10.1021/jp410046w – volume: 10 start-page: 157 year: 2007 ident: 10.1016/j.redox.2017.07.008_bib191 article-title: The olive constituent oleuropein exhibits proteasome stimulatory properties in vitro and confers life span extension of human embryonic fibroblasts publication-title: Rejuvenation Res. doi: 10.1089/rej.2006.0513 – volume: 88 start-page: 2422 year: 2005 ident: 10.1016/j.redox.2017.07.008_bib33 article-title: A mathematical model of protein degradation by the proteasome publication-title: Biophys. J. doi: 10.1529/biophysj.104.049221 – volume: 23 start-page: 8786 year: 2003 ident: 10.1016/j.redox.2017.07.008_bib136 article-title: Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway publication-title: Mol. Cell Biol. doi: 10.1128/MCB.23.23.8786-8794.2003 – volume: 11 start-page: 867 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib196 article-title: Transcriptional and epigenetic regulation of autophagy in aging publication-title: Autophagy doi: 10.1080/15548627.2015.1034410 – volume: 267 start-page: 22369 year: 1992 ident: 10.1016/j.redox.2017.07.008_bib63 article-title: Purification of an 11 S regulator of the multicatalytic protease publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)41681-X – volume: 84 start-page: 646 year: 2007 ident: 10.1016/j.redox.2017.07.008_bib177 article-title: Age-dependent inhibition of proteasome chymotrypsin-like activity in the retina publication-title: Exp. Eye Res. doi: 10.1016/j.exer.2006.12.002 – volume: 96 start-page: 6223 year: 1999 ident: 10.1016/j.redox.2017.07.008_bib90 article-title: Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.96.11.6223 – volume: 26 start-page: 1401 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib130 article-title: The complexity of the Nrf2 pathway: beyond the antioxidant response publication-title: J. Nutr. Biochem. doi: 10.1016/j.jnutbio.2015.08.001 – volume: 99 start-page: 153 year: 2016 ident: 10.1016/j.redox.2017.07.008_bib30 article-title: The molecular chaperone Hsp70 promotes the proteolytic removal of oxidatively damaged proteins by the proteasome publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2016.08.002 – volume: 11 start-page: 673 year: 2017 ident: 10.1016/j.redox.2017.07.008_bib168 article-title: Mitochondrial contribution to lipofuscin formation publication-title: Redox Biol. doi: 10.1016/j.redox.2017.01.017 – volume: 283 start-page: 8984 year: 2008 ident: 10.1016/j.redox.2017.07.008_bib131 article-title: Multiple nuclear localization signals function in the nuclear import of the transcription factor Nrf2 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M709040200 – volume: 75 start-page: S35 issue: Suppl 1 year: 2014 ident: 10.1016/j.redox.2017.07.008_bib31 article-title: Heat shock proteins and proteasomal degradation in normal and tumor cells publication-title: Free Radic. Biol. Med doi: 10.1016/j.freeradbiomed.2014.10.774 – volume: 32 start-page: 29 year: 2010 ident: 10.1016/j.redox.2017.07.008_bib79 article-title: Thymoproteasome shapes immunocompetent repertoire of CD8+ T cells publication-title: Immunity doi: 10.1016/j.immuni.2009.10.009 – volume: 280 start-page: 11840 year: 2005 ident: 10.1016/j.redox.2017.07.008_bib186 article-title: Overexpression of proteasome beta5 assembled subunit increases the amount of proteasome and confers ameliorated response to oxidative stress and higher survival rates publication-title: J. Biol. Chem. doi: 10.1074/jbc.M413007200 – volume: 1843 start-page: 47 year: 2014 ident: 10.1016/j.redox.2017.07.008_bib45 article-title: RING-type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbamcr.2013.05.026 – volume: 25 start-page: 855 year: 2016 ident: 10.1016/j.redox.2017.07.008_bib192 article-title: 18alpha-glycyrrhetinic acid proteasome activator decelerates aging and alzheimer's disease progression in caenorhabditis elegans and neuronal cultures publication-title: Antioxid. Redox Signal. doi: 10.1089/ars.2015.6494 – volume: 4 start-page: e07545 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib85 article-title: Quantitative time-resolved analysis reveals intricate, differential regulation of standard- and immuno-proteasomes publication-title: Elife doi: 10.7554/eLife.07545 – volume: 42 start-page: 307 year: 2016 ident: 10.1016/j.redox.2017.07.008_bib102 article-title: Quantification of age-related changes of alpha-tocopherol in lysosomal membranes in murine tissues and human fibroblasts publication-title: Biofactors doi: 10.1002/biof.1274 – volume: 75 start-page: S18 issue: Suppl 1 year: 2014 ident: 10.1016/j.redox.2017.07.008_bib55 article-title: Circadian modulation of proteasome activities and removal of carbonylated proteins publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2014.10.631 – volume: 24 start-page: 1573 year: 2014 ident: 10.1016/j.redox.2017.07.008_bib82 article-title: Proteasome-mediated processing of Nrf1 is essential for coordinate induction of all proteasome subunits and p97 publication-title: Curr. Biol. doi: 10.1016/j.cub.2014.06.004 – volume: 29 start-page: 611 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib185 article-title: 20S proteasome activation promotes life span extension and resistance to proteotoxicity in Caenorhabditis elegans publication-title: FASEB J.: Off. Publ. Fed. Am. Soc. Exp. Biol. doi: 10.1096/fj.14-252189 – volume: 42 start-page: 29 year: 2013 ident: 10.1016/j.redox.2017.07.008_bib34 article-title: Structural biology of the proteasome publication-title: Annu. Rev. Biophys. doi: 10.1146/annurev-biophys-083012-130417 – volume: 25 start-page: 902 year: 2016 ident: 10.1016/j.redox.2017.07.008_bib39 article-title: Metabolic Syndrome, Redox State, and the Proteasomal System publication-title: Antioxid. Redox Signal doi: 10.1089/ars.2016.6815 – volume: 23 start-page: 1095 year: 2012 ident: 10.1016/j.redox.2017.07.008_bib54 article-title: Systematic survey of deubiquitinase localization identifies USP21 as a regulator of centrosome- and microtubule-associated functions publication-title: Mol. Biol. Cell doi: 10.1091/mbc.e11-08-0668 – volume: 375 start-page: 50 year: 2000 ident: 10.1016/j.redox.2017.07.008_bib156 article-title: Hydrogen peroxide-mediated protein oxidation in young and old human MRC-5 fibroblasts publication-title: Arch. Biochem. Biophys. doi: 10.1006/abbi.1999.1657 – volume: 58 start-page: 1 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib56 article-title: Melatonin feedback on clock genes: a theory involving the proteasome publication-title: J. Pineal Res. doi: 10.1111/jpi.12189 – volume: 8 start-page: 3 year: 2005 ident: 10.1016/j.redox.2017.07.008_bib108 article-title: Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging publication-title: Rejuvenation Res. doi: 10.1089/rej.2005.8.3 – volume: 12 start-page: 715 year: 2011 ident: 10.1016/j.redox.2017.07.008_bib146 article-title: Inflammation meets cancer, with NF-kappaB as the matchmaker publication-title: Nat. Immunol. doi: 10.1038/ni.2060 – volume: 14 start-page: 2503 year: 2000 ident: 10.1016/j.redox.2017.07.008_bib174 article-title: Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: Part II--aging of nondividing cells publication-title: FASEB J.: Off. Publ. Fed. Am. Soc. Exp. Biol. doi: 10.1096/fj.00-0210com – volume: 79 start-page: 1562 year: 2014 ident: 10.1016/j.redox.2017.07.008_bib15 article-title: Role of glutathione, glutathione transferase, and glutaredoxin in regulation of redox-dependent processes publication-title: Biochemistry – volume: 80 start-page: 148 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib14 article-title: The basics of thiols and cysteines in redox biology and chemistry publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2014.11.013 – year: 2016 ident: 10.1016/j.redox.2017.07.008_bib116 article-title: Chaperone mediated autophagy in aging: starve to prosper publication-title: Ageing Res. Rev. doi: 10.1016/j.arr.2016.07.001 – volume: 50 start-page: 86 year: 2011 ident: 10.1016/j.redox.2017.07.008_bib158 article-title: Age-related loss of stress-induced nuclear proteasome activation is due to low PARP-1 activity publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2010.10.700 – volume: 291 start-page: 997 year: 1999 ident: 10.1016/j.redox.2017.07.008_bib24 article-title: Proteasome beta-type subunits: unequal roles of propeptides in core particle maturation and a hierarchy of active site function publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1999.2995 – volume: 24 start-page: 24 year: 2014 ident: 10.1016/j.redox.2017.07.008_bib104 article-title: The machinery of macroautophagy publication-title: Cell Res. doi: 10.1038/cr.2013.168 – volume: 25 start-page: 417 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib41 article-title: The demographics of the ubiquitin system publication-title: Trends Cell Biol. doi: 10.1016/j.tcb.2015.03.002 – volume: 7 start-page: 776 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib67 article-title: Proteasome function is not impaired in healthy aging of the lung publication-title: Aging doi: 10.18632/aging.100820 – volume: 66 start-page: 484 year: 2012 ident: 10.1016/j.redox.2017.07.008_bib120 article-title: Chaperones in autophagy publication-title: Pharmacol. Res. doi: 10.1016/j.phrs.2012.10.002 – volume: 3 start-page: e01856 year: 2014 ident: 10.1016/j.redox.2017.07.008_bib150 article-title: p97-dependent retrotranslocation and proteolytic processing govern formation of active Nrf1 upon proteasome inhibition publication-title: Elife doi: 10.7554/eLife.01856 – volume: 397 start-page: 298 year: 2002 ident: 10.1016/j.redox.2017.07.008_bib167 article-title: Age-dependent declines in proteasome activity in the heart publication-title: Arch. Biochem. Biophys. doi: 10.1006/abbi.2001.2663 – volume: 2 start-page: 199 year: 1995 ident: 10.1016/j.redox.2017.07.008_bib27 article-title: Conformational constraints in protein degradation by the 20S proteasome publication-title: Nat. Struct. Biol. doi: 10.1038/nsb0395-199 – volume: 152 start-page: 290 year: 2013 ident: 10.1016/j.redox.2017.07.008_bib113 article-title: Differential regulation of distinct Vps34 complexes by AMPK in nutrient stress and autophagy publication-title: Cell doi: 10.1016/j.cell.2012.12.016 – volume: 87 start-page: 866 year: 2010 ident: 10.1016/j.redox.2017.07.008_bib71 article-title: PSMB8 encoding the beta5i proteasome subunit is mutated in joint contractures, muscle atrophy, microcytic anemia, and panniculitis-induced lipodystrophy syndrome publication-title: Am. J. Hum. Genet. doi: 10.1016/j.ajhg.2010.10.031 – volume: 30 start-page: 360 year: 2008 ident: 10.1016/j.redox.2017.07.008_bib32 article-title: Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases publication-title: Mol. Cell doi: 10.1016/j.molcel.2008.03.004 – volume: 275 start-page: 2942 year: 2008 ident: 10.1016/j.redox.2017.07.008_bib88 article-title: Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome publication-title: FEBS J. doi: 10.1111/j.1742-4658.2008.06441.x – volume: 329 start-page: 87 year: 1996 ident: 10.1016/j.redox.2017.07.008_bib65 article-title: Proteasome activator PA28 and its interaction with 20 S proteasomes publication-title: Arch. Biochem. Biophys. doi: 10.1006/abbi.1996.0195 – volume: 6 start-page: 21 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib68 article-title: The immunoproteasome and viral infection: a complex regulator of inflammation publication-title: Front. Microbiol. doi: 10.3389/fmicb.2015.00021 – volume: 284 start-page: 22213 year: 2009 ident: 10.1016/j.redox.2017.07.008_bib87 article-title: S-glutathionylation of the Rpn2 regulatory subunit inhibits 26 S proteasomal function publication-title: J. Biol. Chem. doi: 10.1074/jbc.M109.028902 – volume: 285 start-page: 39597 year: 2010 ident: 10.1016/j.redox.2017.07.008_bib172 article-title: Muscle wasting in aged, sarcopenic rats is associated with enhanced activity of the ubiquitin proteasome pathway publication-title: J. Biol. Chem. doi: 10.1074/jbc.M110.129718 – volume: 289 start-page: 11272 year: 2014 ident: 10.1016/j.redox.2017.07.008_bib40 article-title: NADH binds and stabilizes the 26S proteasomes independent of ATP publication-title: J. Biol. Chem. doi: 10.1074/jbc.M113.537175 – volume: 43 start-page: 621 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib139 article-title: Dissecting molecular cross-talk between Nrf2 and NF-kappaB response pathways publication-title: Biochem. Soc. Trans. doi: 10.1042/BST20150014 – volume: 69 start-page: 1125 year: 2012 ident: 10.1016/j.redox.2017.07.008_bib118 article-title: Microautophagy: lesser-known self-eating publication-title: Cell Mol. Life Sci. doi: 10.1007/s00018-011-0865-5 – volume: 93 start-page: 15036 year: 1996 ident: 10.1016/j.redox.2017.07.008_bib19 article-title: Methionine residues as endogenous antioxidants in proteins publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.93.26.15036 – volume: 3 start-page: 66 year: 2012 ident: 10.1016/j.redox.2017.07.008_bib46 article-title: The ubiquitin system and Kaposi's sarcoma-associated Herpesvirus publication-title: Front. Microbiol. doi: 10.3389/fmicb.2012.00066 – volume: 22 start-page: 1645 year: 2010 ident: 10.1016/j.redox.2017.07.008_bib147 article-title: Suppression of NF-kappaB signaling by KEAP1 regulation of IKKbeta activity through autophagic degradation and inhibition of phosphorylation publication-title: Cell. Signal. doi: 10.1016/j.cellsig.2010.06.004 – volume: 584 start-page: 1393 year: 2010 ident: 10.1016/j.redox.2017.07.008_bib184 article-title: Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems publication-title: FEBS Lett. doi: 10.1016/j.febslet.2009.12.047 – volume: 1 start-page: 45 year: 2013 ident: 10.1016/j.redox.2017.07.008_bib128 article-title: The Keap1-Nrf2 pathway: mechanisms of activation and dysregulation in cancer publication-title: Redox Biol. doi: 10.1016/j.redox.2012.10.001 – volume: 5 year: 2016 ident: 10.1016/j.redox.2017.07.008_bib106 article-title: Advances in autophagy regulatory mechanisms publication-title: Cells doi: 10.3390/cells5020024 – volume: 31 start-page: 1121 year: 2011 ident: 10.1016/j.redox.2017.07.008_bib134 article-title: SCF/{beta}-TrCP promotes glycogen synthase kinase 3-dependent degradation of the Nrf2 transcription factor in a Keap1-independent manner publication-title: Mol. Cell Biol. doi: 10.1128/MCB.01204-10 – volume: 109 start-page: 75 year: 2012 ident: 10.1016/j.redox.2017.07.008_bib66 article-title: Immunoproteasomes: structure, function, and antigen presentation publication-title: Prog. Mol. Biol. Transl. Sci. doi: 10.1016/B978-0-12-397863-9.00003-1 – volume: 68 start-page: 749 year: 2011 ident: 10.1016/j.redox.2017.07.008_bib100 article-title: Chaperone-mediated autophagy: machinery, regulation and biological consequences publication-title: Cell Mol. Life Sci. doi: 10.1007/s00018-010-0565-6 – volume: 40 start-page: 147 year: 2010 ident: 10.1016/j.redox.2017.07.008_bib154 article-title: Proteasomal degradation is transcriptionally controlled by TCF11 via an ERAD-dependent feedback loop publication-title: Mol. Cell doi: 10.1016/j.molcel.2010.09.012 – volume: 580 start-page: 3989 year: 2006 ident: 10.1016/j.redox.2017.07.008_bib76 article-title: Proteasome response to interferon-gamma is altered in senescent human fibroblasts publication-title: FEBS Lett. doi: 10.1016/j.febslet.2006.06.029 – volume: 24 start-page: 92 year: 2014 ident: 10.1016/j.redox.2017.07.008_bib119 article-title: Chaperone-mediated autophagy: roles in disease and aging publication-title: Cell Res. doi: 10.1038/cr.2013.153 – volume: 101 start-page: 325 year: 2016 ident: 10.1016/j.redox.2017.07.008_bib182 article-title: Reduced autophagy leads to an impaired ferritin turnover in senescent fibroblasts publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2016.10.492 – volume: 389 start-page: 254 year: 2001 ident: 10.1016/j.redox.2017.07.008_bib86 article-title: Glutathiolation of the proteasome is enhanced by proteolytic inhibitors publication-title: Arch. Biochem. Biophys. doi: 10.1006/abbi.2001.2332 – volume: 1703 start-page: 135 year: 2005 ident: 10.1016/j.redox.2017.07.008_bib8 article-title: Methionine oxidation and aging publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbapap.2004.08.010 – volume: 5 start-page: S4 issue: Suppl 2 year: 2011 ident: 10.1016/j.redox.2017.07.008_bib126 article-title: Mining the TRAF6/p62 interactome for a selective ubiquitination motif publication-title: BMC Proc. doi: 10.1186/1753-6561-5-S2-S4 – volume: 78 start-page: 761 year: 1994 ident: 10.1016/j.redox.2017.07.008_bib5 article-title: Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules publication-title: Cell doi: 10.1016/S0092-8674(94)90462-6 – volume: 125 start-page: 539 year: 2012 ident: 10.1016/j.redox.2017.07.008_bib48 article-title: Non-canonical ubiquitin-based signals for proteasomal degradation publication-title: J. Cell Sci. doi: 10.1242/jcs.093567 – volume: 40 start-page: 1303 year: 2006 ident: 10.1016/j.redox.2017.07.008_bib21 article-title: Intracellular distribution of oxidized proteins and proteasome in HT22 cells during oxidative stress publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2005.11.023 – volume: 1 start-page: 178 year: 2013 ident: 10.1016/j.redox.2017.07.008_bib22 article-title: The proteasome and the degradation of oxidized proteins: Part I-structure of proteasomes publication-title: Redox Biol. doi: 10.1016/j.redox.2013.01.004 – volume: 335 start-page: 33 year: 2009 ident: 10.1016/j.redox.2017.07.008_bib105 article-title: Macroautophagy signaling and regulation publication-title: Curr. Top. Microbiol. Immunol. – volume: 10 start-page: 609 year: 2002 ident: 10.1016/j.redox.2017.07.008_bib197 article-title: The structure of the mammalian 20S proteasome at 2.75 A resolution publication-title: Structure doi: 10.1016/S0969-2126(02)00748-7 – volume: 109 start-page: 249 year: 2012 ident: 10.1016/j.redox.2017.07.008_bib163 article-title: Changes of the proteasomal system during the aging process publication-title: Prog. Mol. Biol. Transl. Sci. doi: 10.1016/B978-0-12-397863-9.00007-9 – volume: 55 start-page: 119 year: 2013 ident: 10.1016/j.redox.2017.07.008_bib179 article-title: Autophagy and ageing: implications for age-related neurodegenerative diseases publication-title: Essays Biochem. doi: 10.1042/bse0550119 – volume: 53 start-page: 1760 year: 2012 ident: 10.1016/j.redox.2017.07.008_bib160 article-title: Lipofuscin is formed independently of macroautophagy and lysosomal activity in stress-induced prematurely senescent human fibroblasts publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2012.08.591 – volume: 32 start-page: 2616 year: 2014 ident: 10.1016/j.redox.2017.07.008_bib138 article-title: Nrf2, a regulator of the proteasome, controls self-renewal and pluripotency in human embryonic stem cells publication-title: Stem Cells doi: 10.1002/stem.1764 – volume: 7 start-page: 72 year: 2014 ident: 10.1016/j.redox.2017.07.008_bib44 article-title: An optimal ubiquitin-proteasome pathway in the nervous system: the role of deubiquitinating enzymes publication-title: Front. Mol. Neurosci. doi: 10.3389/fnmol.2014.00072 – volume: 142 start-page: 517 year: 2010 ident: 10.1016/j.redox.2017.07.008_bib69 article-title: The immunoproteasome cleans up after inflammation publication-title: Cell doi: 10.1016/j.cell.2010.08.002 – volume: 85 start-page: 705 year: 2013 ident: 10.1016/j.redox.2017.07.008_bib129 article-title: The Nrf2 cell defence pathway: Keap1-dependent and -independent mechanisms of regulation publication-title: Biochem. Pharmacol. doi: 10.1016/j.bcp.2012.11.016 – volume: 94 start-page: 7156 year: 1997 ident: 10.1016/j.redox.2017.07.008_bib23 article-title: Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.94.14.7156 – volume: 59 start-page: 33 year: 2013 ident: 10.1016/j.redox.2017.07.008_bib99 article-title: Functional analysis of lysosomes during mouse preimplantation embryo development publication-title: J. Reprod. Dev. doi: 10.1262/jrd.2012-096 – volume: 227 start-page: 26 year: 2013 ident: 10.1016/j.redox.2017.07.008_bib72 article-title: A new infant case of Nakajo-Nishimura syndrome with a genetic mutation in the immunoproteasome subunit: an overlapping entity with JMP and CANDLE syndrome related to PSMB8 mutations publication-title: Dermatology doi: 10.1159/000351323 – volume: 102 start-page: 55 year: 1998 ident: 10.1016/j.redox.2017.07.008_bib173 article-title: Age-related changes in the 20S and 26S proteasome activities in the liver of male F344 rats publication-title: Mech. Ageing Dev. doi: 10.1016/S0047-6374(98)00011-6 – volume: 1783 start-page: 713 year: 2008 ident: 10.1016/j.redox.2017.07.008_bib145 article-title: NF-kappaB/p65 antagonizes Nrf2-ARE pathway by depriving CBP from Nrf2 and facilitating recruitment of HDAC3 to MafK publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbamcr.2008.01.002 – volume: 44 start-page: 3508 year: 2014 ident: 10.1016/j.redox.2017.07.008_bib60 article-title: Proteasome isoforms exhibit only quantitative differences in cleavage and epitope generation publication-title: Eur. J. Immunol. doi: 10.1002/eji.201444902 – volume: 25 start-page: 1085 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib111 article-title: mTORC1 maintains metabolic balance publication-title: Cell Res. doi: 10.1038/cr.2015.107 – volume: 30 start-page: 1191 year: 2001 ident: 10.1016/j.redox.2017.07.008_bib2 article-title: Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple publication-title: Free Radic. Biol. Med. doi: 10.1016/S0891-5849(01)00480-4 – volume: 40 start-page: 1250 year: 2006 ident: 10.1016/j.redox.2017.07.008_bib9 article-title: Protein oxidation and aging publication-title: Free Radic. Res. doi: 10.1080/10715760600918142 – volume: 65 start-page: 3971 year: 2008 ident: 10.1016/j.redox.2017.07.008_bib58 article-title: REGgamma, a proteasome activator and beyond? publication-title: Cell Mol. Life Sci. doi: 10.1007/s00018-008-8291-z – volume: 39 start-page: 8 year: 2016 ident: 10.1016/j.redox.2017.07.008_bib114 article-title: Lysosomal signaling in control of degradation pathways publication-title: Curr. Opin. Cell Biol. doi: 10.1016/j.ceb.2016.01.006 – volume: 10 start-page: 549 year: 2014 ident: 10.1016/j.redox.2017.07.008_bib115 article-title: Autophagosomes, phagosomes, autolysosomes, phagolysosomes, autophagolysosomes... wait, I'm confused publication-title: Autophagy doi: 10.4161/auto.28448 – volume: 20 start-page: 131 year: 2011 ident: 10.1016/j.redox.2017.07.008_bib123 article-title: Microautophagy of cytosolic proteins by late endosomes publication-title: Dev. Cell doi: 10.1016/j.devcel.2010.12.003 – volume: 98 start-page: 218 year: 2016 ident: 10.1016/j.redox.2017.07.008_bib144 article-title: The role of E3 ubiquitin-ligases MuRF-1 and MAFbx in loss of skeletal muscle mass publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2015.12.031 – volume: 26 start-page: R834 year: 2016 ident: 10.1016/j.redox.2017.07.008_bib151 article-title: Nrf1 can be processed and activated in a proteasome-independent manner publication-title: Curr. Biol. doi: 10.1016/j.cub.2016.08.008 – volume: 55 start-page: 1 year: 2013 ident: 10.1016/j.redox.2017.07.008_bib112 article-title: Early signalling events of autophagy publication-title: Essays Biochem. doi: 10.1042/bse0550001 – volume: 287 start-page: 10021 year: 2012 ident: 10.1016/j.redox.2017.07.008_bib135 article-title: Nrf2-dependent induction of proteasome and Pa28alphabeta regulator are required for adaptation to oxidative stress publication-title: J. Biol. Chem. doi: 10.1074/jbc.M111.277145 – volume: 29 start-page: 1095 year: 2009 ident: 10.1016/j.redox.2017.07.008_bib189 article-title: Genetic evidence linking age-dependent attenuation of the 26S proteasome with the aging process publication-title: Mol. Cell Biol. doi: 10.1128/MCB.01227-08 – volume: 38 start-page: 412 year: 2013 ident: 10.1016/j.redox.2017.07.008_bib61 article-title: The MHC I loading complex: a multitasking machinery in adaptive immunity publication-title: Trends Biochem. Sci. doi: 10.1016/j.tibs.2013.06.003 – volume: 7 start-page: 1062 year: 2000 ident: 10.1016/j.redox.2017.07.008_bib26 article-title: A gated channel into the proteasome core particle publication-title: Nat. Struct. Biol. doi: 10.1038/80992 – volume: 30 start-page: 191 year: 2009 ident: 10.1016/j.redox.2017.07.008_bib17 article-title: The proteasomal system publication-title: Mol. Asp. Med. doi: 10.1016/j.mam.2009.04.001 – volume: 19 start-page: 2179 year: 2008 ident: 10.1016/j.redox.2017.07.008_bib183 article-title: Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy publication-title: Mol. Biol. Cell doi: 10.1091/mbc.e07-11-1155 – volume: 110 start-page: 6979 year: 2013 ident: 10.1016/j.redox.2017.07.008_bib80 article-title: Thymoproteasome subunit-beta5T generates peptide-MHC complexes specialized for positive selection publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1222244110 – volume: 2 start-page: 99 year: 2014 ident: 10.1016/j.redox.2017.07.008_bib92 article-title: The proteasome and the degradation of oxidized proteins: Part II - protein oxidation and proteasomal degradation publication-title: Redox Biol. doi: 10.1016/j.redox.2013.12.008 – volume: 47 start-page: 921 year: 1986 ident: 10.1016/j.redox.2017.07.008_bib141 article-title: Inducibility of kappa immunoglobulin enhancer-binding protein Nf-kappa B by a posttranslational mechanism publication-title: Cell doi: 10.1016/0092-8674(86)90807-X – volume: 383 start-page: 1 year: 2000 ident: 10.1016/j.redox.2017.07.008_bib25 article-title: Catalytic activities of the 20 S proteasome, a multicatalytic proteinase complex publication-title: Arch. Biochem. Biophys. doi: 10.1006/abbi.2000.2036 – volume: 578 start-page: 217 year: 2004 ident: 10.1016/j.redox.2017.07.008_bib165 article-title: Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal publication-title: FEBS Lett. doi: 10.1016/j.febslet.2004.11.003 – volume: 105 start-page: 7094 year: 2008 ident: 10.1016/j.redox.2017.07.008_bib187 article-title: Proteasomal adaptation to environmental stress links resistance to proteotoxicity with longevity in Caenorhabditis elegans publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.0707025105 – volume: 51 start-page: 268 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib70 article-title: The Immunoproteasome in oxidative stress, aging, and disease publication-title: Crit. Rev. Biochem. Mol. Biol. doi: 10.3109/10409238.2016.1172554 – volume: 38 start-page: 17 year: 2010 ident: 10.1016/j.redox.2017.07.008_bib149 article-title: Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells publication-title: Mol. Cell doi: 10.1016/j.molcel.2010.02.029 – volume: 79 start-page: 437 year: 2016 ident: 10.1016/j.redox.2017.07.008_bib35 article-title: Recent advances in the structural biology of the 26S proteasome publication-title: Int. J. Biochem. Cell Biol. doi: 10.1016/j.biocel.2016.08.008 – volume: 11 start-page: 538 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib125 article-title: Induction and adaptation of chaperone-assisted selective autophagy CASA in response to resistance exercise in human skeletal muscle publication-title: Autophagy doi: 10.1080/15548627.2015.1017186 – volume: 66 start-page: 811 year: 2011 ident: 10.1016/j.redox.2017.07.008_bib91 article-title: PARP-1: a new player in the asthma field? publication-title: Allergy doi: 10.1111/j.1398-9995.2011.02551.x – volume: 13 start-page: 1272 year: 2011 ident: 10.1016/j.redox.2017.07.008_bib142 article-title: NF-kappaB controls energy homeostasis and metabolic adaptation by upregulating mitochondrial respiration publication-title: Nat. Cell Biol. doi: 10.1038/ncb2324 – volume: 2 start-page: 388 year: 2014 ident: 10.1016/j.redox.2017.07.008_bib89 article-title: The proteasome and the degradation of oxidized proteins: part III-Redox regulation of the proteasomal system publication-title: Redox Biol. doi: 10.1016/j.redox.2013.12.029 – volume: 14 start-page: 283 year: 2013 ident: 10.1016/j.redox.2017.07.008_bib96 article-title: Signals from the lysosome: a control centre for cellular clearance and energy metabolism publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm3565 – volume: 489 start-page: 263 year: 2012 ident: 10.1016/j.redox.2017.07.008_bib188 article-title: RPN-6 determines C. elegans longevity under proteotoxic stress conditions publication-title: Nature doi: 10.1038/nature11315 – volume: 48 start-page: 673 year: 2010 ident: 10.1016/j.redox.2017.07.008_bib159 article-title: Chromatin repair after oxidative stress: role of PARP-mediated proteasome activation publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2009.12.010 – volume: 285 start-page: 8171 year: 2010 ident: 10.1016/j.redox.2017.07.008_bib137 article-title: Nuclear erythroid factor 2-mediated proteasome activation delays senescence in human fibroblasts publication-title: J. Biol. Chem. doi: 10.1074/jbc.M109.031575 – volume: 2 start-page: 1354 year: 2010 ident: 10.1016/j.redox.2017.07.008_bib148 article-title: The nrf1 and nrf2 balance in oxidative stress regulation and androgen signaling in prostate cancer cells publication-title: Cancers doi: 10.3390/cancers2021354 – volume: 113 start-page: 163 year: 2007 ident: 10.1016/j.redox.2017.07.008_bib143 article-title: Regulation of NADPH oxidase subunit p22(phox) by NF-kB in human aortic smooth muscle cells publication-title: Arch. Physiol. Biochem. doi: 10.1080/13813450701531235 – volume: 28 start-page: 5747 year: 2008 ident: 10.1016/j.redox.2017.07.008_bib122 article-title: The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane publication-title: Mol. Cell Biol. doi: 10.1128/MCB.02070-07 – volume: 6 start-page: 38299 year: 2016 ident: 10.1016/j.redox.2017.07.008_bib7 article-title: Methionine sulfoxides in serum proteins as potential clinical biomarkers of oxidative stress publication-title: Sci. Rep. doi: 10.1038/srep38299 – volume: 44 start-page: 115 year: 2007 ident: 10.1016/j.redox.2017.07.008_bib10 article-title: The peroxiredoxin repair proteins publication-title: Subcell. Biochem. doi: 10.1007/978-1-4020-6051-9_6 – volume: 1371 start-page: 45 year: 2016 ident: 10.1016/j.redox.2017.07.008_bib97 article-title: Targeting the lysosome in cancer publication-title: Ann. N.Y. Acad. Sci. doi: 10.1111/nyas.12953 – volume: 1843 start-page: 13 year: 2014 ident: 10.1016/j.redox.2017.07.008_bib164 article-title: Regulation of proteasome activity in health and disease publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbamcr.2013.08.012 – volume: 16 start-page: 17193 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib57 article-title: Protein folding and mechanisms of proteostasis publication-title: Int. J. Mol. Sci. doi: 10.3390/ijms160817193 – volume: 421 start-page: 67 year: 2004 ident: 10.1016/j.redox.2017.07.008_bib171 article-title: Altered proteasome function and subunit composition in aged muscle publication-title: Arch. Biochem. Biophys. doi: 10.1016/j.abb.2003.10.010 – volume: 9 start-page: 1937 year: 2013 ident: 10.1016/j.redox.2017.07.008_bib121 article-title: HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting publication-title: Autophagy doi: 10.4161/auto.26448 – volume: 218 start-page: 224 year: 1996 ident: 10.1016/j.redox.2017.07.008_bib37 article-title: Activation of the proteasome during Xenopus egg activation implies a link between proteasome activation and intracellular calcium release publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.1996.0039 – volume: 1 start-page: 140 year: 2013 ident: 10.1016/j.redox.2017.07.008_bib169 article-title: Lipofuscin: formation, effects and role of macroautophagy publication-title: Redox Biol. doi: 10.1016/j.redox.2013.01.006 – volume: 53 start-page: 1468 year: 2012 ident: 10.1016/j.redox.2017.07.008_bib198 article-title: Chaperones, but not oxidized proteins, are ubiquitinated after oxidative stress publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2012.05.039 – volume: 120 start-page: 782 year: 2007 ident: 10.1016/j.redox.2017.07.008_bib181 article-title: Altered dynamics of the lysosomal receptor for chaperone-mediated autophagy with age publication-title: J. Cell Sci. doi: 10.1242/jcs.001073 – volume: 75 start-page: 120 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib110 article-title: Selective autophagy: xenophagy publication-title: Methods doi: 10.1016/j.ymeth.2014.12.005 – volume: 10 start-page: 266 year: 2016 ident: 10.1016/j.redox.2017.07.008_bib170 article-title: Macroautophagy is impaired in old murine brain tissue as well as in senescent human fibroblasts publication-title: Redox Biol. doi: 10.1016/j.redox.2016.10.015 – volume: 10 start-page: 319 year: 2009 ident: 10.1016/j.redox.2017.07.008_bib43 article-title: Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm2673 – volume: 278 start-page: 28026 year: 2003 ident: 10.1016/j.redox.2017.07.008_bib176 article-title: Central role of the proteasome in senescence and survival of human fibroblasts: induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation publication-title: J. Biol. Chem. doi: 10.1074/jbc.M301048200 – volume: 12 start-page: 619 year: 2016 ident: 10.1016/j.redox.2017.07.008_bib98 article-title: A lysosome-centered view of nutrient homeostasis publication-title: Autophagy doi: 10.1080/15548627.2016.1147671 – volume: 14 start-page: 959 year: 2008 ident: 10.1016/j.redox.2017.07.008_bib180 article-title: Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function publication-title: Nat. Med. doi: 10.1038/nm.1851 – volume: 12 start-page: 261 year: 2016 ident: 10.1016/j.redox.2017.07.008_bib195 article-title: Autophagy-mediated longevity is modulated by lipoprotein biogenesis publication-title: Autophagy doi: 10.1080/15548627.2015.1127464 – volume: 49 start-page: 1 year: 2016 ident: 10.1016/j.redox.2017.07.008_bib95 article-title: Adaptive homeostasis publication-title: Mol. Asp. Med. doi: 10.1016/j.mam.2016.04.007 – volume: 531 start-page: 1 year: 2001 ident: 10.1016/j.redox.2017.07.008_bib6 article-title: Regulation of cell function by methionine oxidation and reduction publication-title: J. Physiol. doi: 10.1111/j.1469-7793.2001.0001j.x – volume: 44 start-page: 3500 year: 2014 ident: 10.1016/j.redox.2017.07.008_bib62 article-title: Standard and immunoproteasomes show similar peptide degradation specificities publication-title: Eur. J. Immunol. doi: 10.1002/eji.201445272 – volume: 405 start-page: 341 year: 2007 ident: 10.1016/j.redox.2017.07.008_bib50 article-title: Proteasome-mediated CCAAT/enhancer-binding protein delta (C/EBPdelta) degradation is ubiquitin-independent publication-title: Biochem. J. doi: 10.1042/BJ20070082 – volume: 360 start-page: 597 year: 1992 ident: 10.1016/j.redox.2017.07.008_bib51 article-title: Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination publication-title: Nature doi: 10.1038/360597a0 – volume: 35 start-page: 721 year: 2000 ident: 10.1016/j.redox.2017.07.008_bib190 article-title: Fibroblast cultures from healthy centenarians have an active proteasome publication-title: Exp. Gerontol. doi: 10.1016/S0531-5565(00)00137-6 – year: 2016 ident: 10.1016/j.redox.2017.07.008_bib124 article-title: Cardioprotection of exercise preconditioning involving heat shock protein 70 and concurrent autophagy: a potential chaperone-assisted selective macroautophagy effect publication-title: J. Physiol. Sci. – volume: 15 start-page: 1805 year: 2016 ident: 10.1016/j.redox.2017.07.008_bib109 article-title: Mitochondrial autophagy promotes healthy aging publication-title: Cell Cycle doi: 10.1080/15384101.2016.1181876 – volume: 483 start-page: 127 year: 2009 ident: 10.1016/j.redox.2017.07.008_bib178 article-title: Age-related differences in oxidative protein-damage in young and senescent fibroblasts publication-title: Arch. Biochem. Biophys. doi: 10.1016/j.abb.2008.12.007 – volume: 55 start-page: 79 year: 2013 ident: 10.1016/j.redox.2017.07.008_bib107 article-title: Selective autophagy publication-title: Essays Biochem. doi: 10.1042/bse0550079 – volume: 4 start-page: 1 year: 2013 ident: 10.1016/j.redox.2017.07.008_bib20 article-title: Relationship between the proteasomal system and autophagy publication-title: Int. J. Biochem. Mol. Biol. – volume: 16 start-page: 229 year: 2012 ident: 10.1016/j.redox.2017.07.008_bib12 article-title: Peroxiredoxin 3 is a key molecule regulating adipocyte oxidative stress, mitochondrial biogenesis, and adipokine expression publication-title: Antioxid. Redox Signal doi: 10.1089/ars.2010.3766 – volume: 7 start-page: 521 year: 1989 ident: 10.1016/j.redox.2017.07.008_bib28 article-title: Macroxyproteinase (M.O.P.): a 670 kDa proteinase complex that degrades oxidatively denatured proteins in red blood cells publication-title: Free Radic. Biol. Med doi: 10.1016/0891-5849(89)90028-2 – volume: 208 start-page: 64 year: 1963 ident: 10.1016/j.redox.2017.07.008_bib103 article-title: The lysosome publication-title: Sci. Am. doi: 10.1038/scientificamerican0563-64 – volume: 2015 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib127 article-title: Analyzing the colocalization of MAP1LC3 and lysosomal markers in primary cells publication-title: Cold Spring Harb. Protoc. doi: 10.1101/pdb.prot086272 – volume: 51 start-page: 5 year: 2011 ident: 10.1016/j.redox.2017.07.008_bib93 article-title: Ubiquitin-proteasome pathway and cellular responses to oxidative stress publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2011.03.031 – volume: 21 start-page: 871 year: 1996 ident: 10.1016/j.redox.2017.07.008_bib162 article-title: Biochemical basis of lipofuscin, ceroid, and age pigment-like fluorophores publication-title: Free Radic. Biol. Med. doi: 10.1016/0891-5849(96)00175-X – volume: 191 start-page: 52 year: 2013 ident: 10.1016/j.redox.2017.07.008_bib59 article-title: Mixed proteasomes function to increase viral peptide diversity and broaden antiviral CD8+ T cell responses publication-title: J. Immunol. doi: 10.4049/jimmunol.1300802 – volume: 9 start-page: 826 year: 2008 ident: 10.1016/j.redox.2017.07.008_bib42 article-title: Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction publication-title: Nat. Rev. Neurosci. doi: 10.1038/nrn2499 – volume: 23 start-page: 344 year: 2014 ident: 10.1016/j.redox.2017.07.008_bib53 article-title: Mechanisms for regulating deubiquitinating enzymes publication-title: Protein Sci. doi: 10.1002/pro.2415 – volume: 16 start-page: 1323 year: 2012 ident: 10.1016/j.redox.2017.07.008_bib13 article-title: Redox regulation of mitochondrial function publication-title: Antioxid. Redox Signal doi: 10.1089/ars.2011.4123 – volume: 2 start-page: a000158 year: 2010 ident: 10.1016/j.redox.2017.07.008_bib140 article-title: The IKK complex, a central regulator of NF-kappaB activation publication-title: Cold Spring Harb. Perspect. Biol. doi: 10.1101/cshperspect.a000158 – volume: 291 start-page: 18096 year: 2016 ident: 10.1016/j.redox.2017.07.008_bib117 article-title: Structural and biological interaction of hsc-70 protein with phosphatidylserine in endosomal microautophagy publication-title: J. Biol. Chem. doi: 10.1074/jbc.M116.736744 – volume: 2 start-page: 68 year: 2014 ident: 10.1016/j.redox.2017.07.008_bib16 article-title: S-glutathionylation reactions in mitochondrial function and disease publication-title: Front. Cell Dev. Biol. doi: 10.3389/fcell.2014.00068 – volume: 316 start-page: 1349 year: 2007 ident: 10.1016/j.redox.2017.07.008_bib81 article-title: Regulation of CD8+ T cell development by thymus-specific proteasomes publication-title: Science doi: 10.1126/science.1141915 – volume: 40 start-page: 435 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib11 article-title: Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling publication-title: Trends Biochem. Sci. doi: 10.1016/j.tibs.2015.05.001 – volume: 49 start-page: 73 year: 2009 ident: 10.1016/j.redox.2017.07.008_bib52 article-title: Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology publication-title: Annu Rev. Pharmacol. Toxicol. doi: 10.1146/annurev.pharmtox.051208.165340 – volume: 14 start-page: 2495 year: 2000 ident: 10.1016/j.redox.2017.07.008_bib175 article-title: Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: Part I--effects of proliferative senescence publication-title: FASEB J.: Off. Publ. Fed. Am. Soc. Exp. Biol. doi: 10.1096/fj.00-0209com – volume: 181 start-page: 1459 year: 1995 ident: 10.1016/j.redox.2017.07.008_bib78 article-title: Coordinate regulation of the human TAP1 and LMP2 genes from a shared bidirectional promoter publication-title: J. Exp. Med. doi: 10.1084/jem.181.4.1459 – volume: 27 start-page: 608 year: 2008 ident: 10.1016/j.redox.2017.07.008_bib1 article-title: Uric acid: the oxidant-antioxidant paradox publication-title: Nucleosides Nucleotides Nucleic Acids doi: 10.1080/15257770802138558 – volume: 76 start-page: 1485 year: 2008 ident: 10.1016/j.redox.2017.07.008_bib132 article-title: Activation of Nrf2-antioxidant signaling attenuates NFkappaB-inflammatory response and elicits apoptosis publication-title: Biochem. Pharmacol. doi: 10.1016/j.bcp.2008.07.017 – volume: 281 start-page: 14841 year: 2006 ident: 10.1016/j.redox.2017.07.008_bib133 article-title: Glycogen synthase kinase-3beta inhibits the xenobiotic and antioxidant cell response by direct phosphorylation and nuclear exclusion of the transcription factor Nrf2 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M513737200 – volume: 41 start-page: 213 year: 1992 ident: 10.1016/j.redox.2017.07.008_bib64 article-title: Human erythrocyte contains a factor that stimulates the peptidase activities of multicatalytic proteinase complex publication-title: Ital. J. Biochem. – volume: 13 start-page: 89 year: 2012 ident: 10.1016/j.redox.2017.07.008_bib152 article-title: The unfolded protein response: controlling cell fate decisions under ER stress and beyond publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm3270 – volume: 7 start-page: 1363 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib83 article-title: Evolution of proteasome regulators in eukaryotes publication-title: Genome Biol. Evol. doi: 10.1093/gbe/evv068 – volume: 523 start-page: 181 year: 2012 ident: 10.1016/j.redox.2017.07.008_bib94 article-title: Differential roles of proteasome and immunoproteasome regulators Pa28alphabeta, Pa28gamma and Pa200 in the degradation of oxidized proteins publication-title: Arch. Biochem. Biophys. doi: 10.1016/j.abb.2012.04.018 – volume: 96 start-page: 6223 year: 1999 ident: 10.1016/j.redox.2017.07.008_bib155 article-title: Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.96.11.6223 – volume: 38 start-page: 17 year: 2010 ident: 10.1016/j.redox.2017.07.008_bib153 article-title: Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells publication-title: Mol. Cell doi: 10.1016/j.molcel.2010.02.029 – volume: 2 start-page: 44 year: 2013 ident: 10.1016/j.redox.2017.07.008_bib166 article-title: Redox regulation of the proteasome via S-glutathionylation publication-title: Redox Biol. doi: 10.1016/j.redox.2013.12.003 – year: 2016 ident: 10.1016/j.redox.2017.07.008_bib101 article-title: Lysosomal cathepsins and their regulation in aging and neurodegeneration publication-title: Ageing Res. Rev. doi: 10.1016/j.arr.2016.04.010 – volume: 93 start-page: 1076 year: 2011 ident: 10.1016/j.redox.2017.07.008_bib199 article-title: Proteins bearing oxidation-induced carbonyl groups are not preferentially ubiquitinated publication-title: Biochimie doi: 10.1016/j.biochi.2011.03.004 – volume: 50 start-page: 585 year: 2011 ident: 10.1016/j.redox.2017.07.008_bib161 article-title: Lipofuscin inhibits the proteasome by binding to surface motifs publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2010.12.011 – volume: 125 start-page: 85 year: 2015 ident: 10.1016/j.redox.2017.07.008_bib193 article-title: Essential role for autophagy in life span extension publication-title: J. Clin. Investig. doi: 10.1172/JCI73946 – volume: 90 start-page: 1 year: 2016 ident: 10.1016/j.redox.2017.07.008_bib3 article-title: Redox- and non-redox-metal-induced formation of free radicals and their role in human disease publication-title: Arch. Toxicol. doi: 10.1007/s00204-015-1579-5 – volume: 108 start-page: 14914 year: 2011 ident: 10.1016/j.redox.2017.07.008_bib73 article-title: Proteasome assembly defect due to a proteasome subunit beta type 8 (PSMB8) mutation causes the autoinflammatory disorder, Nakajo-Nishimura syndrome publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1106015108 – volume: 30 start-page: 3099 year: 2010 ident: 10.1016/j.redox.2017.07.008_bib49 article-title: Ubiquitin-independent degradation of antiapoptotic MCL-1 publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.01266-09 – volume: 286 start-page: 17495 year: 2011 ident: 10.1016/j.redox.2017.07.008_bib84 article-title: Dependence of proteasome processing rate on substrate unfolding publication-title: J. Biol. Chem. doi: 10.1074/jbc.M110.212027 – volume: 11 start-page: 1305 year: 2009 ident: 10.1016/j.redox.2017.07.008_bib194 article-title: Induction of autophagy by spermidine promotes longevity publication-title: Nat. Cell Biol. doi: 10.1038/ncb1975 – volume: 17 start-page: 1963 year: 2003 ident: 10.1016/j.redox.2017.07.008_bib157 article-title: Stability of the nuclear protein turnover during cellular senescence of human fibroblasts publication-title: FASEB J. doi: 10.1096/fj.03-0177fje – reference: 18694732 - Biochem Pharmacol. 2008 Dec 1;76(11):1485-9 – reference: 24596095 - J Biol Chem. 2014 Apr 18;289(16):11272-81 – reference: 21772280 - Nat Immunol. 2011 Jul 19;12(8):715-23 – reference: 20932482 - Mol Cell. 2010 Oct 8;40(1):147-58 – reference: 24024151 - Redox Biol. 2013 Jan 19;1:178-82 – reference: 27405763 - J Biol Chem. 2016 Aug 26;291(35):18096-106 – reference: 22298430 - Mol Biol Cell. 2012 Mar;23 (6):1095-103 – reference: 24563857 - Redox Biol. 2014 Jan 14;2:388-94 – reference: 23059540 - Pharmacol Res. 2012 Dec;66(6):484-93 – reference: 26067716 - Trends Biochem Sci. 2015 Aug;40(8):435-45 – reference: 22564544 - Arch Biochem Biophys. 2012 Jul 15;523(2):181-90 – reference: 27928720 - J Physiol Sci. 2016 Dec 7;:null – reference: 15798367 - Rejuvenation Res. 2005 Spring;8(1):3-5 – reference: 11062564 - Nat Struct Biol. 2000 Nov;7(11):1062-7 – reference: 19801973 - Nat Cell Biol. 2009 Nov;11(11):1305-14 – reference: 8619639 - Arch Biochem Biophys. 1996 May 1;329(1):87-96 – reference: 2558981 - Free Radic Biol Med. 1989;7(5):521-36 – reference: 26461299 - Free Radic Biol Med. 2014 Oct;75 Suppl 1:S18 – reference: 16806194 - FEBS Lett. 2006 Jul 10;580(16):3989-94 – reference: 20300203 - Cold Spring Harb Perspect Biol. 2010 Mar;2(3):a000158 – reference: 1334232 - Nature. 1992 Dec 10;360(6404):597-9 – reference: 11097171 - Arch Biochem Biophys. 2000 Nov 1;383(1):1-16 – reference: 25369242 - J Pineal Res. 2015 Jan;58(1):1-11 – reference: 11179387 - J Physiol. 2001 Feb 15;531(Pt 1):1-11 – reference: 20385764 - Mol Cell Biol. 2010 Jun;30(12 ):3099-110 – reference: 22922647 - Nature. 2012 Sep 13;489(7415):263-8 – reference: 21284655 - Allergy. 2011 Jul;66(7):811-4 – reference: 26393687 - Elife. 2015 Sep 22;4:e07545 – reference: 26358187 - Cell Res. 2015 Oct;25(10 ):1085-6 – reference: 25836756 - Autophagy. 2015;11(6):867-80 – reference: 18931696 - Nat Rev Neurosci. 2008 Nov;9(11):826-38 – reference: 12032076 - EMBO J. 2002 Jun 3;21(11):2636-45 – reference: 19135972 - Arch Biochem Biophys. 2009 Mar 1;483(1):127-35 – reference: 24070476 - Essays Biochem. 2013;55:119-31 – reference: 9207060 - Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7156-61 – reference: 12015144 - Structure. 2002 May;10(5):609-18 – reference: 17090414 - Free Radic Res. 2006 Dec;40(12):1250-8 – reference: 27098648 - Crit Rev Biochem Mol Biol. 2015 Jul-Aug;51(4):268-81 – reference: 26886723 - Antioxid Redox Signal. 2016 Dec 1;25(16):855-869 – reference: 24070467 - Essays Biochem. 2013;55:1-15 – reference: 18471981 - Mol Cell. 2008 May 9;30(3):360-8 – reference: 14612418 - Mol Cell Biol. 2003 Dec;23 (23 ):8786-94 – reference: 25453035 - Front Cell Dev Biol. 2014 Nov 17;2:68 – reference: 26461349 - Free Radic Biol Med. 2014 Oct;75 Suppl 1:S35 – reference: 26330623 - Cold Spring Harb Protoc. 2015 Sep 01;2015(9):pdb.prot086272 – reference: 17284523 - J Cell Sci. 2007 Mar 1;120(Pt 5):782-91 – reference: 20025963 - Free Radic Biol Med. 2010 Mar 1;48(5):673-80 – reference: 21167934 - Free Radic Biol Med. 2011 Mar 1;50(5):585-91 – reference: 22251901 - Nat Rev Mol Cell Biol. 2012 Jan 18;13(2):89-102 – reference: 19371762 - Mol Aspects Med. 2009 Aug;30(4):191-296 – reference: 26671266 - Autophagy. 2016;12 (2):261-72 – reference: 26225966 - Int J Mol Sci. 2015 Jul 28;16(8):17193-230 – reference: 27412984 - Antioxid Redox Signal. 2016 Dec 1;25(16):902-917 – reference: 3096580 - Cell. 1986 Dec 26;47(6):921-8 – reference: 16551619 - J Biol Chem. 2006 May 26;281(21):14841-51 – reference: 23747565 - Biochim Biophys Acta. 2014 Jan;1843(1):47-60 – reference: 22080117 - Cell Mol Life Sci. 2012 Apr;69(7):1125-36 – reference: 10339569 - Proc Natl Acad Sci U S A. 1999 May 25;96(11):6223-8 – reference: 11368918 - Free Radic Biol Med. 2001 Jun 1;30(11):1191-212 – reference: 21238931 - Dev Cell. 2011 Jan 18;20(1):131-9 – reference: 12897070 - FASEB J. 2003 Oct;17(13):1963-5 – reference: 18644871 - Mol Cell Biol. 2008 Sep;28(18):5747-63 – reference: 18679578 - Cell Mol Life Sci. 2008 Dec;65(24):3971-80 – reference: 23849087 - Trends Biochem Sci. 2013 Aug;38(8):412-20 – reference: 8573136 - Biochem Biophys Res Commun. 1996 Jan 5;218(1):224-8 – reference: 23569244 - Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):6979-84 – reference: 22308036 - J Biol Chem. 2012 Mar 23;287(13):10021-31 – reference: 15589823 - FEBS Lett. 2004 Dec 17;578(3):217-23 – reference: 8902532 - Free Radic Biol Med. 1996;21(6):871-88 – reference: 24366339 - Cell Res. 2014 Jan;24(1):24-41 – reference: 25231383 - Eur J Immunol. 2014 Dec;44(12):3508-21 – reference: 25191222 - Front Mol Neurosci. 2014 Aug 19;7:72 – reference: 22727424 - Prog Mol Biol Transl Sci. 2012;109:249-75 – reference: 16631520 - Free Radic Biol Med. 2006 Apr 15;40(8):1303-12 – reference: 23709680 - J Immunol. 2013 Jul 1;191(1):52-9 – reference: 18337468 - Mol Biol Cell. 2008 May;19(5):2179-92 – reference: 26738803 - Free Radic Biol Med. 2016 Sep;98 :218-230 – reference: 17258201 - Exp Eye Res. 2007 Apr;84(4):646-54 – reference: 27484893 - Ageing Res Rev. 2016 Dec;32:13-21 – reference: 17518699 - Rejuvenation Res. 2007 Jun;10(2):157-72 – reference: 24998528 - Curr Biol. 2014 Jul 21;24(14 ):1573-83 – reference: 26540298 - Aging (Albany NY). 2015 Oct;7(10):776-92 – reference: 19802559 - Curr Top Microbiol Immunol. 2009;335:33-70 – reference: 15680221 - Biochim Biophys Acta. 2005 Jan 17;1703(2):135-40 – reference: 24396728 - Redox Biol. 2013 Dec 14;2:44-51 – reference: 24281119 - Cancers (Basel). 2010 Jun 21;2(2):1354-78 – reference: 1429590 - J Biol Chem. 1992 Nov 5;267(31):22369-77 – reference: 27498116 - Free Radic Biol Med. 2016 Oct;99:153-166 – reference: 18158642 - Arch Physiol Biochem. 2007 Oct-Dec;113(4-5):163-72 – reference: 25714469 - Autophagy. 2015;11(3):538-46 – reference: 25654554 - J Clin Invest. 2015 Jan;125(1):85-93 – reference: 22727420 - Prog Mol Biol Transl Sci. 2012;109:75-112 – reference: 11795886 - Arch Biochem Biophys. 2002 Jan 15;397(2):298-304 – reference: 10683247 - Arch Biochem Biophys. 2000 Mar 1;375(1):50-4 – reference: 24070473 - Essays Biochem. 2013;55:79-92 – reference: 22375140 - Front Microbiol. 2012 Feb 23;3:66 – reference: 26551702 - Biochem Soc Trans. 2015 Aug;43(4):621-6 – reference: 21245377 - Mol Cell Biol. 2011 Mar;31(6):1121-33 – reference: 20385086 - Mol Cell. 2010 Apr 9;38(1):17-28 – reference: 21968997 - Nat Cell Biol. 2011 Aug 28;13(10):1272-9 – reference: 11115501 - J Biol Chem. 2001 Mar 23;276(12):9492-502 – reference: 24895273 - Stem Cells. 2014 Oct;32(10):2616-25 – reference: 11053662 - Exp Gerontol. 2000 Sep;35(6-7):721-8 – reference: 25497060 - Methods. 2015 Mar;75:120-7 – reference: 12736271 - J Biol Chem. 2003 Jul 25;278(30):28026-37 – reference: 18435761 - FEBS J. 2008 Jun;275(11):2942-55 – reference: 27789294 - Free Radic Biol Med. 2016 Dec;101:325-333 – reference: 27187479 - Cells. 2016 May 13;5(2):null – reference: 25460724 - Redox Biol. 2014;2:99-104 – reference: 19075009 - Mol Cell Biol. 2009 Feb;29(4):1095-106 – reference: 21852578 - Proc Natl Acad Sci U S A. 2011 Sep 6;108(36):14914-9 – reference: 22146081 - Antioxid Redox Signal. 2012 Jun 1;16(11):1323-67 – reference: 25749165 - Biochemistry (Mosc). 2014 Dec;79(13):1562-83 – reference: 11099467 - FASEB J. 2000 Dec;14(15):2495-502 – reference: 18690243 - Nat Med. 2008 Sep;14(9):959-65 – reference: 23219527 - Biochem Pharmacol. 2013 Mar 15;85(6):705-17 – reference: 18834306 - Annu Rev Pharmacol Toxicol. 2009;49:73-96 – reference: 25399798 - Eur J Immunol. 2014 Dec;44(12):3500-3 – reference: 23332761 - Cell. 2013 Jan 17;152(1-2):290-303 – reference: 19549781 - J Biol Chem. 2009 Aug 14;284(33):22213-21 – reference: 7699330 - J Exp Med. 1995 Apr 1;181(4):1459-71 – reference: 27825071 - Redox Biol. 2016 Dec;10 :266-273 – reference: 25866968 - J Clin Invest. 2015 May;125(5):2059-68 – reference: 18467495 - Proc Natl Acad Sci U S A. 2008 May 13;105(19):7094-9 – reference: 22389393 - J Cell Sci. 2012 Feb 1;125(Pt 3):539-48 – reference: 27929071 - Sci Rep. 2016 Dec 08;6:38299 – reference: 20068043 - J Biol Chem. 2010 Mar 12;285(11):8171-84 – reference: 25395451 - FASEB J. 2015 Feb;29(2):611-22 – reference: 23994620 - Biochim Biophys Acta. 2014 Jan;1843(1):13-25 – reference: 15665121 - Biophys J. 2005 Apr;88(4):2422-32 – reference: 24403057 - Protein Sci. 2014 Apr;23 (4):344-53 – reference: 24448410 - Elife. 2014;3:e01856 – reference: 24313818 - J Phys Chem B. 2013 Dec 27;117(51):16455-67 – reference: 27125852 - Ageing Res Rev. 2016 Dec;32:22-37 – reference: 23080372 - J Reprod Dev. 2013;59(1):33-9 – reference: 24121476 - Autophagy. 2013 Dec;9(12):1937-54 – reference: 10452902 - J Mol Biol. 1999 Aug 27;291(4):997-1013 – reference: 27498189 - Int J Biochem Cell Biol. 2016 Oct;79:437-442 – reference: 27112802 - Mol Aspects Med. 2016 Jun;49:1-7 – reference: 18238777 - J Biol Chem. 2008 Apr 4;283(14):8984-94 – reference: 9663792 - Mech Ageing Dev. 1998 May 1;102(1):55-66 – reference: 25906909 - Trends Cell Biol. 2015 Jul;25(7):417-26 – reference: 14678786 - Arch Biochem Biophys. 2004 Jan 1;421(1):67-76 – reference: 21554762 - BMC Proc. 2011 May 28;5 Suppl 2:S4 – reference: 21530648 - Free Radic Biol Med. 2011 Jul 1;51(1):5-16 – reference: 24024136 - Redox Biol. 2013 Jan 18;1:45-9 – reference: 22982048 - Free Radic Biol Med. 2012 Nov 1;53(9):1760-9 – reference: 1428780 - Ital J Biochem. 1992 Jul-Aug;41(4):213-24 – reference: 25943340 - Genome Biol Evol. 2015 May 04;7(5):1363-79 – reference: 23414347 - Annu Rev Biophys. 2013;42:29-49 – reference: 18084892 - Subcell Biochem. 2007;44:115-41 – reference: 20385835 - Proc Natl Acad Sci U S A. 2010 Apr 27;107(17):7704-9 – reference: 24281265 - Cell Res. 2014 Jan;24(1):92-104 – reference: 27676297 - Curr Biol. 2016 Sep 26;26(18):R834-5 – reference: 20940294 - J Biol Chem. 2010 Dec 17;285(51):39597-608 – reference: 14025755 - Sci Am. 1963 May;208:64-72 – reference: 20600852 - Cell Signal. 2010 Nov;22(11):1645-54 – reference: 25688236 - Front Microbiol. 2015 Jan 29;6:21 – reference: 15661736 - J Biol Chem. 2005 Mar 25;280(12):11840-50 – reference: 26827287 - Curr Opin Cell Biol. 2016 Apr;39:8-14 – reference: 21402121 - Biochimie. 2011 Jun;93(6):1076-9 – reference: 10360685 - Mech Ageing Dev. 1999 Mar 15;107(3):323-32 – reference: 21454622 - J Biol Chem. 2011 May 20;286(20):17495-502 – reference: 20045355 - Immunity. 2010 Jan 29;32(1):29-40 – reference: 27115480 - Cell Cycle. 2016 Jul 17;15(14 ):1805-6 – reference: 17373909 - Biochem J. 2007 Jul 15;405(2):341-9 – reference: 24657946 - Autophagy. 2014 Apr;10(4):549-51 – reference: 8986759 - Proc Natl Acad Sci U S A. 1996 Dec 24;93(26):15036-40 – reference: 20977936 - Free Radic Biol Med. 2011 Jan 1;50(1):86-92 – reference: 8087844 - Cell. 1994 Sep 9;78(5):761-71 – reference: 11339815 - Arch Biochem Biophys. 2001 May 15;389(2):254-63 – reference: 19352404 - Nat Rev Mol Cell Biol. 2009 May;10 (5):319-31 – reference: 27050453 - Autophagy. 2016;12 (4):619-31 – reference: 23942189 - Dermatology. 2013;227(1):26-30 – reference: 22683819 - Free Radic Biol Med. 2012 Oct 1;53(7):1468-77 – reference: 25433365 - Free Radic Biol Med. 2015 Mar;80:148-57 – reference: 26599426 - Ann N Y Acad Sci. 2016 May;1371(1):45-54 – reference: 18241676 - Biochim Biophys Acta. 2008 May;1783(5):713-27 – reference: 27095633 - Biofactors. 2016 May;42(3):307-15 – reference: 20723753 - Cell. 2010 Aug 20;142(4):517-8 – reference: 23638318 - Int J Biochem Mol Biol. 2013 Mar 31;4(1):1-26 – reference: 26419687 - J Nutr Biochem. 2015 Dec;26(12 ):1401-13 – reference: 26343967 - Arch Toxicol. 2016 Jan;90(1):1-37 – reference: 20040365 - FEBS Lett. 2010 Apr 2;584(7):1393-8 – reference: 28160744 - Redox Biol. 2017 Apr;11:673-681 – reference: 20427185 - Trends Cell Biol. 2010 Jul;20(7):391-401 – reference: 7773788 - Nat Struct Biol. 1995 Mar;2(3):199-204 – reference: 17540904 - Science. 2007 Jun 1;316(5829):1349-53 – reference: 21129723 - Am J Hum Genet. 2010 Dec 10;87(6):866-72 – reference: 24024146 - Redox Biol. 2013 Jan 19;1:140-4 – reference: 21902452 - Antioxid Redox Signal. 2012 Feb 1;16(3):229-43 – reference: 19012754 - J Neurochem. 2009 Jan;108(1):260-72 – reference: 18600514 - Nucleosides Nucleotides Nucleic Acids. 2008 Jun;27(6):608-19 – reference: 11099468 - FASEB J. 2000 Dec;14(15):2503-10 – reference: 23609508 - Nat Rev Mol Cell Biol. 2013 May;14(5):283-96 – reference: 20976518 - Cell Mol Life Sci. 2011 Mar;68(5):749-63 |
SSID | ssj0000884210 |
Score | 2.5375977 |
SecondaryResourceType | review_article |
Snippet | The production of reactive species is an inevitable by-product of metabolism and thus, life itself. Since reactive species are able to damage cellular... |
SourceID | doaj unpaywall pubmedcentral proquest pubmed crossref elsevier |
SourceType | Open Website Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
StartPage | 550 |
SubjectTerms | Aging - metabolism Animals Autophagy Glycation End Products, Advanced - metabolism Humans Lipofuscin - metabolism Lysosome Oxidative Stress Proteasome Proteostasis Redox shift Review |
SummonAdditionalLinks | – databaseName: DOAJ Directory of Open Access Journals dbid: DOA link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1NT9wwELUqJNReKqCUpnwoSBw4EJH4MzkCKkKVinoAiZtlO7bYapVF7K4K_54ZO1ntCgl66DVxnPjNOH4jj98QcmR95RSEDYVTDS24MaIwjKIggG0gXAmyjOcrfl3Lq1v-807cLZX6wpywJA-cgDtVwvO2pE5QFKujwVpfO-uccp6FJp6gprCMLQVT8R9c15xGKQJKK1YAiVGD5FBM7kIxzidM7FJRuhOLSy4tS1G9f2V1es0-XydRfpx3D-b5rxmPl1aoyw3yuaeW-Vka0ib54Lstsp6KTT5_Ice_UZJhAmxwOpqe5JOnURtFv_N0XCQ3XZvHkkXb5Pbyx83FVdHXSSgAFTErTKBeVm3JmK0AKMZUXTaMt4ay4GSAGVoFx4IKTHlRByBoVkpeKWZEBeyvZF_JWjfp_DeSA5sLrhSGc1tzsBnEx6plqGasStqYkBE6wKRdLyKOtSzGesgW-6Mjthqx1SVubtcZOVk89JA0NN5ufo74L5qiAHa8AG6he7fQ77lFRuRgPd1zicQRoKvR228_HGytYabh9onp_GQ-1cCFkV4CuBnZSbZffCNFYT8leUbUilesDGL1Tje6j2reQjBZY5_Fwn_-BaXv_wOlXfIJu0zJiXtkbfY49_tAsmb2IM6nF0UYILs priority: 102 providerName: Directory of Open Access Journals – databaseName: Scholars Portal Journals: Open Access dbid: M48 link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1La9wwEBYhJbSX0iZ9uC9cyCGHuNh62odS2tIQCik9ZCE3IclSu2Wx033Q3X_fGdne1iSEkKNtWbbm4fkGj74h5ND6wilIGzKnKppxY0RmGEVCAFtBuhJkHvdXnH2TpxP-9UJc7JChK2ovwMW1qR32k5rMZ-_WvzcfwOHf_6vVQm7NNdZpqcjEiZt_70FoomjmZz3ej5_msuQ0MhRQWrAMsI0amIiun2cUrSKp_yhoXQWlV2sr76-aS7P5Y2az_wLXySPysEec6cfORB6THd_sk72uB-XmgBx9R6aGFkDiYro4Ttv1tI5c4Gm3iyQ1TZ3GTkZPyOTky_nn06xvn5A5QcUyM4F6WdQ5Y7agDmCdKvOK8dpQFpwM4LhFcCyowJQXZQDcZqXkhWJGFAAKc_aU7DZt45-TFEBecLkwnNuSgyohbVY1Q5JjldPKhITQQUza9dzi2OJipocisl86ylajbHWO_7zLhBxvb7rsqDVuHv4J5b8dirzY8UQ7_6F7N9NKeF7nsFqK1IY0WOtLZ51TzrNQsSIhctCe7iFGBx1gqunNT3876FqDA-JfFdP4drXQAJERdYJwE_Ks0_32HSny_SnJE6JGVjFaxPhKM_0ZSb6FYLLEObOt_dxGSi_uusCX5AEedXWKr8jucr7yrwFvLe2b6EN_AdrKJQs priority: 102 providerName: Scholars Portal – databaseName: Unpaywall dbid: UNPAY link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrZ3fb9MwEMct6ITYC79h4ZeCxAMPc5fYsZ08DsQ0ITFNgkrjyXIcu2QrSdWmouOv5y4_qpVJE0g8Nr0mtX2OvyefP0fI29zFVkHYQK3KGE2MEdRwhkCAPINwxcuoPV_x-UQeT5JPZ-Ksz3_CszAQzY1hUaC2qLoTDchoqpqD8gdMr4OYLtk4ol8YgyCKI-kFN_bgSX4d69liOj6fT2-THYmbTSOyMzk5PfyG1eXAnKL9gB1qE7wQyLnG5C7V4juxwOSVpakl-G-tUNcV6PVEyruram4uf5rZ7MoqdXSfXAzt65JTLsarJh_bX3-gH_9PBzwg93oxGx523veQ3HLVI3KnK295-Zi8O0UIRA36c1ku98N6XRYtZjzsDqiEpirCtkjSEzI5-vj1wzHtKzNQK5hoqPHMybiIOM9jZkExqjTKeFIYxr2VHt4JsbfcK8-VE6kHSZhLmcSKGxGD3oz4UzKq6srtkRD0o7eRMEmSpwl4CUTkquDIT1YRy4wPCBsGRdseW47VM2Z6yE871-1IahxJHeF2ehqQ_c2P5h2142bz9zjaG1NEbrcX6sVU9zNYK-GSIoLWMqQmMp_nLrW5tco67jMeB0QOvqJ79dKpErhVefPT3wyepWFu44aNqVy9WmpQ3yhooXMD8qzztM1_ZIgSVDIJiNrywa1GbH9Tld9bfrgQXKZ4T7rx1r_ppef_aP-C7OKnLvPxJRk1i5V7BQquyV_3U_M3tNFAcg priority: 102 providerName: Unpaywall |
Title | Proteostasis, oxidative stress and aging |
URI | https://dx.doi.org/10.1016/j.redox.2017.07.008 https://www.ncbi.nlm.nih.gov/pubmed/28763764 https://www.proquest.com/docview/1925514780 https://pubmed.ncbi.nlm.nih.gov/PMC5536880 https://ars.els-cdn.com/content/image/1-s2.0-S2213231716304694-fx1_lrg.jpg https://doaj.org/article/75e4d02c5203422fbbe8cbcc7ce3f931 |
UnpaywallVersion | publishedVersion |
Volume | 13 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
journalDatabaseRights | – providerCode: PRVAON databaseName: DOAJ Directory of Open Access Journals customDbUrl: eissn: 2213-2317 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0000884210 issn: 2213-2317 databaseCode: DOA dateStart: 20130101 isFulltext: true titleUrlDefault: https://www.doaj.org/ providerName: Directory of Open Access Journals – providerCode: PRVESC databaseName: ScienceDirect Free and Delayed Access Titles customDbUrl: eissn: 2213-2317 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0000884210 issn: 2213-2317 databaseCode: IXB dateStart: 20130101 isFulltext: true titleUrlDefault: https://www.sciencedirect.com providerName: Elsevier – providerCode: PRVBFR databaseName: Free Medical Journals customDbUrl: eissn: 2213-2317 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0000884210 issn: 2213-2317 databaseCode: DIK dateStart: 20130101 isFulltext: true titleUrlDefault: http://www.freemedicaljournals.com providerName: Flying Publisher – providerCode: PRVHPJ databaseName: ROAD: Directory of Open Access Scholarly Resources customDbUrl: eissn: 2213-2317 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0000884210 issn: 2213-2317 databaseCode: M~E dateStart: 20130101 isFulltext: true titleUrlDefault: https://road.issn.org providerName: ISSN International Centre – providerCode: PRVLSH databaseName: Elsevier Journals customDbUrl: mediaType: online eissn: 2213-2317 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0000884210 issn: 2213-2317 databaseCode: AKRWK dateStart: 20130101 isFulltext: true providerName: Library Specific Holdings – providerCode: PRVAQN databaseName: PubMed Central customDbUrl: eissn: 2213-2317 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0000884210 issn: 2213-2317 databaseCode: RPM dateStart: 20130101 isFulltext: true titleUrlDefault: https://www.ncbi.nlm.nih.gov/pmc/ providerName: National Library of Medicine – providerCode: PRVFZP databaseName: Scholars Portal Journals: Open Access customDbUrl: eissn: 2213-2317 dateEnd: 20250831 omitProxy: true ssIdentifier: ssj0000884210 issn: 2213-2317 databaseCode: M48 dateStart: 20130201 isFulltext: true titleUrlDefault: http://journals.scholarsportal.info providerName: Scholars Portal |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnZ3La9wwEIdFSCntpfRdp-3iQg89xKyth2Ufk9AQCgmBdmF7EpIstS6LvWR3afLfZ0Z-EBMIpReDvbK9Gr1-skbfEPLZuMxKmDYkVpY04VqLRDOKQABTwnTF52nYX3F-kZ8t-LelWO6Rk2EvDLpV9n1_16eH3rq_Mu-tOV_X9fw7pTCTYoh7wdW9EpmgjMuwiW95PH5ngVbEaYASYPoEbxjgQ8HNC7Gc1-jiJQPEE8NM3hmgAsd_Mk7d16H33Smf7Jq1vvmrV6s7Y9Xpc_KsF5nxUZePF2TPNS_J4y7s5M0r8uUS4Qwt6MJNvTmM2-u6CvjvuNs4EuumikPwotdkcfr1x8lZ0kdMSKygYptoT12eVSljJqMWlJws0pLxSlPmbe6hrWbeMi89k04UHqSayXOeSaZFBjowZW_IftM27h2JQdd5mwrNuSk4lB7MlGXFkGssU1pqHxE6mEnZHieOUS1WavAb-6OCbRXaVqW4zF1E5HC8ad3RNB5Ofoz2H5MiCjtcaK9-qb4uKCkcr1LILUWaIfXGuMIaa6V1zJcsi0g-lJ6a1Cx4VP3w2z8NZa2gzeFCim5cu9soUMUoNMG4EXnblf34Hyki_mTOIyIntWKSiekvTf07cL2FYHmBz0zG-vMvVjr43wy-J0_xrHNN_ED2t1c79xEk1tbMwqeJWWhJcDznxYw8WlxcHv28BQctJFc |
linkProvider | Elsevier |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LT9wwEB5RUAWXqvSZtrSp1EMPRJv4ESfHgoqWFlClgrQ3y3FsmmqVrNhdAf--HuchIiSEerVjJzP22N_E428AvhQm0cK5DZEWOYmYUjxSlCAhQJE7d8Wmsb9fcXqWTi_YjxmfbcBhfxcGwyq7tb9d0_1q3ZVMOm1OFlU1-U2I86Qo0r3g6V7OnsCWQwMxxnUdzw6GHy3OjBjxrATYIMIWPfuQj_NCXs4bjPESnsUT80ze2aE8kf9oo7oPRO_HU26v64W6vVbz-Z3N6ug5POtQZvitFWQXNkz9Ap62eSdvX8LXX8jO0DhguKyW-2FzU5We_ztsb46Eqi5Dn73oFVwcfT8_nEZdyoRIc8JXkbLEpEkZU1okRDsoJ7I4p6xUhFqdWmesidXUCkuF4Zl1WK1IU5YIqnjigGBMX8Nm3dTmLYQO2Fkdc8VYkTE3fM5VFiVFYmMRk1zZAEivJqk7PnFMazGXfeDYX-l1K1G3MsZz7iyA_aHRoqXTePjxA9T_8ChyYfuC5upSdpNBCm5YGTtpCdIZElsUJtOF1kIbanOaBJD2oydHU8t1VT389s_9WEtndHiSomrTrJfSwWJEmk65Abxpx374RoIcfyJlAYjRrBgJMa6pqz-e2JtzmmbYZzTMn8do6d3_CvgJtqfnpyfy5Pjs53vYwZo2TvEDbK6u1mbP4a1V8dHb0z_d1yP5 |
linkToUnpaywall | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrZ3fb9MwEMct6ITYC79h4ZeCxAMPc5fYsZ08DsQ0ITFNgkrjyXIcu2QrSdWmouOv5y4_qpVJE0g8Nr0mtX2OvyefP0fI29zFVkHYQK3KGE2MEdRwhkCAPINwxcuoPV_x-UQeT5JPZ-Ksz3_CszAQzY1hUaC2qLoTDchoqpqD8gdMr4OYLtk4ol8YgyCKI-kFN_bgSX4d69liOj6fT2-THYmbTSOyMzk5PfyG1eXAnKL9gB1qE7wQyLnG5C7V4juxwOSVpakl-G-tUNcV6PVEyruram4uf5rZ7MoqdXSfXAzt65JTLsarJh_bX3-gH_9PBzwg93oxGx523veQ3HLVI3KnK295-Zi8O0UIRA36c1ku98N6XRYtZjzsDqiEpirCtkjSEzI5-vj1wzHtKzNQK5hoqPHMybiIOM9jZkExqjTKeFIYxr2VHt4JsbfcK8-VE6kHSZhLmcSKGxGD3oz4UzKq6srtkRD0o7eRMEmSpwl4CUTkquDIT1YRy4wPCBsGRdseW47VM2Z6yE871-1IahxJHeF2ehqQ_c2P5h2142bz9zjaG1NEbrcX6sVU9zNYK-GSIoLWMqQmMp_nLrW5tco67jMeB0QOvqJ79dKpErhVefPT3wyepWFu44aNqVy9WmpQ3yhooXMD8qzztM1_ZIgSVDIJiNrywa1GbH9Tld9bfrgQXKZ4T7rx1r_ppef_aP-C7OKnLvPxJRk1i5V7BQquyV_3U_M3tNFAcg |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Proteostasis%2C+oxidative+stress+and+aging&rft.jtitle=Redox+biology&rft.au=Korovila%2C+Ioanna&rft.au=Hugo%2C+Mart%C3%ADn&rft.au=Castro%2C+Jos%C3%A9%C2%A0Pedro&rft.au=Weber%2C+Daniela&rft.date=2017-10-01&rft.pub=Elsevier+B.V&rft.issn=2213-2317&rft.eissn=2213-2317&rft.volume=13&rft.spage=550&rft.epage=567&rft_id=info:doi/10.1016%2Fj.redox.2017.07.008&rft.externalDocID=S2213231716304694 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2213-2317&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2213-2317&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2213-2317&client=summon |