Proximal Cysteines that Enhance Lysine N-Acetylation of Cytosolic Proteins in Mice Are Less Conserved in Longer-Living Species
Acetyl-coenzyme A (CoA) is an abundant metabolite that can also alter protein function through non-enzymatic N-acetylation of protein lysines. This N-acetylation is greatly enhanced in vitro if an adjacent cysteine undergoes initial S-acetylation, as this can lead to S→N transfer of the acetyl moiet...
Saved in:
| Published in | Cell reports (Cambridge) Vol. 24; no. 6; pp. 1445 - 1455 |
|---|---|
| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
07.08.2018
Cell Press Elsevier |
| Subjects | |
| Online Access | Get full text |
| ISSN | 2211-1247 2211-1247 |
| DOI | 10.1016/j.celrep.2018.07.007 |
Cover
| Abstract | Acetyl-coenzyme A (CoA) is an abundant metabolite that can also alter protein function through non-enzymatic N-acetylation of protein lysines. This N-acetylation is greatly enhanced in vitro if an adjacent cysteine undergoes initial S-acetylation, as this can lead to S→N transfer of the acetyl moiety. Here, using modeled mouse structures of 619 proteins N-acetylated in mouse liver, we show lysine N-acetylation is greater in vivo if a cysteine is within ∼10 Å. Extension to the genomes of 52 other mammalian and bird species shows pairs of proximal cysteine and N-acetylated lysines are less conserved, implying most N-acetylation is detrimental. Supporting this, there is less conservation of cytosolic pairs of proximal cysteine and N-acetylated lysines in species with longer lifespans. As acetyl-CoA levels are linked to nutrient supply, these findings suggest how dietary restriction could extend lifespan and how pathologies resulting from dietary excess may occur.
[Display omitted]
•Creation of a mouse structural library of in vivo lysine N-acetylation on 619 proteins•Proximal cysteines enhance protein lysine N-acetylation in vivo•Proximal N-acetylated lysine and cysteine residues are less conserved•Conservation of these proximal residues is lower in species with longer lifespans
Acetyl-CoA non-enzymatically N-acetylates protein lysines. Using proteins N-acetylated in mouse liver, James et al. show N-acetylation is greater if a cysteine is within ∼10 Å. These pairs of proximal cysteine and N-acetylated lysines are less conserved in species with longer lifespans. This might explain how dietary restriction extends lifespan. |
|---|---|
| AbstractList | Acetyl-coenzyme A (CoA) is an abundant metabolite that can also alter protein function through non-enzymatic N-acetylation of protein lysines. This N-acetylation is greatly enhanced in vitro if an adjacent cysteine undergoes initial S-acetylation, as this can lead to S→N transfer of the acetyl moiety. Here, using modeled mouse structures of 619 proteins N-acetylated in mouse liver, we show lysine N-acetylation is greater in vivo if a cysteine is within ∼10 Å. Extension to the genomes of 52 other mammalian and bird species shows pairs of proximal cysteine and N-acetylated lysines are less conserved, implying most N-acetylation is detrimental. Supporting this, there is less conservation of cytosolic pairs of proximal cysteine and N-acetylated lysines in species with longer lifespans. As acetyl-CoA levels are linked to nutrient supply, these findings suggest how dietary restriction could extend lifespan and how pathologies resulting from dietary excess may occur. : Acetyl-CoA non-enzymatically N-acetylates protein lysines. Using proteins N-acetylated in mouse liver, James et al. show N-acetylation is greater if a cysteine is within ∼10 Å. These pairs of proximal cysteine and N-acetylated lysines are less conserved in species with longer lifespans. This might explain how dietary restriction extends lifespan. Acetyl-coenzyme A (CoA) is an abundant metabolite that can also alter protein function through non-enzymatic N-acetylation of protein lysines. This N-acetylation is greatly enhanced in vitro if an adjacent cysteine undergoes initial S-acetylation, as this can lead to S→N transfer of the acetyl moiety. Here, using modeled mouse structures of 619 proteins N-acetylated in mouse liver, we show lysine N-acetylation is greater in vivo if a cysteine is within ∼10 Å. Extension to the genomes of 52 other mammalian and bird species shows pairs of proximal cysteine and N-acetylated lysines are less conserved, implying most N-acetylation is detrimental. Supporting this, there is less conservation of cytosolic pairs of proximal cysteine and N-acetylated lysines in species with longer lifespans. As acetyl-CoA levels are linked to nutrient supply, these findings suggest how dietary restriction could extend lifespan and how pathologies resulting from dietary excess may occur. [Display omitted] •Creation of a mouse structural library of in vivo lysine N-acetylation on 619 proteins•Proximal cysteines enhance protein lysine N-acetylation in vivo•Proximal N-acetylated lysine and cysteine residues are less conserved•Conservation of these proximal residues is lower in species with longer lifespans Acetyl-CoA non-enzymatically N-acetylates protein lysines. Using proteins N-acetylated in mouse liver, James et al. show N-acetylation is greater if a cysteine is within ∼10 Å. These pairs of proximal cysteine and N-acetylated lysines are less conserved in species with longer lifespans. This might explain how dietary restriction extends lifespan. Acetyl-coenzyme A (CoA) is an abundant metabolite that can also alter protein function through non-enzymatic N -acetylation of protein lysines. This N- acetylation is greatly enhanced in vitro if an adjacent cysteine undergoes initial S- acetylation, as this can lead to S→N transfer of the acetyl moiety. Here, using modeled mouse structures of 619 proteins N -acetylated in mouse liver, we show lysine N- acetylation is greater in vivo if a cysteine is within ∼10 Å. Extension to the genomes of 52 other mammalian and bird species shows pairs of proximal cysteine and N- acetylated lysines are less conserved, implying most N- acetylation is detrimental. Supporting this, there is less conservation of cytosolic pairs of proximal cysteine and N- acetylated lysines in species with longer lifespans. As acetyl-CoA levels are linked to nutrient supply, these findings suggest how dietary restriction could extend lifespan and how pathologies resulting from dietary excess may occur. • Creation of a mouse structural library of in vivo lysine N- acetylation on 619 proteins • Proximal cysteines enhance protein lysine N- acetylation in vivo • Proximal N- acetylated lysine and cysteine residues are less conserved • Conservation of these proximal residues is lower in species with longer lifespans Acetyl-CoA non-enzymatically N -acetylates protein lysines. Using proteins N -acetylated in mouse liver, James et al. show N- acetylation is greater if a cysteine is within ∼10 Å. These pairs of proximal cysteine and N- acetylated lysines are less conserved in species with longer lifespans. This might explain how dietary restriction extends lifespan. Acetyl-coenzyme A (CoA) is an abundant metabolite that can also alter protein function through non-enzymatic N-acetylation of protein lysines. This N-acetylation is greatly enhanced in vitro if an adjacent cysteine undergoes initial S-acetylation, as this can lead to S→N transfer of the acetyl moiety. Here, using modeled mouse structures of 619 proteins N-acetylated in mouse liver, we show lysine N-acetylation is greater in vivo if a cysteine is within ∼10 Å. Extension to the genomes of 52 other mammalian and bird species shows pairs of proximal cysteine and N-acetylated lysines are less conserved, implying most N-acetylation is detrimental. Supporting this, there is less conservation of cytosolic pairs of proximal cysteine and N-acetylated lysines in species with longer lifespans. As acetyl-CoA levels are linked to nutrient supply, these findings suggest how dietary restriction could extend lifespan and how pathologies resulting from dietary excess may occur. Acetyl-coenzyme A (CoA) is an abundant metabolite that can also alter protein function through non-enzymatic N-acetylation of protein lysines. This N-acetylation is greatly enhanced in vitro if an adjacent cysteine undergoes initial S-acetylation, as this can lead to S→N transfer of the acetyl moiety. Here, using modeled mouse structures of 619 proteins N-acetylated in mouse liver, we show lysine N-acetylation is greater in vivo if a cysteine is within ∼10 Å. Extension to the genomes of 52 other mammalian and bird species shows pairs of proximal cysteine and N-acetylated lysines are less conserved, implying most N-acetylation is detrimental. Supporting this, there is less conservation of cytosolic pairs of proximal cysteine and N-acetylated lysines in species with longer lifespans. As acetyl-CoA levels are linked to nutrient supply, these findings suggest how dietary restriction could extend lifespan and how pathologies resulting from dietary excess may occur.Acetyl-coenzyme A (CoA) is an abundant metabolite that can also alter protein function through non-enzymatic N-acetylation of protein lysines. This N-acetylation is greatly enhanced in vitro if an adjacent cysteine undergoes initial S-acetylation, as this can lead to S→N transfer of the acetyl moiety. Here, using modeled mouse structures of 619 proteins N-acetylated in mouse liver, we show lysine N-acetylation is greater in vivo if a cysteine is within ∼10 Å. Extension to the genomes of 52 other mammalian and bird species shows pairs of proximal cysteine and N-acetylated lysines are less conserved, implying most N-acetylation is detrimental. Supporting this, there is less conservation of cytosolic pairs of proximal cysteine and N-acetylated lysines in species with longer lifespans. As acetyl-CoA levels are linked to nutrient supply, these findings suggest how dietary restriction could extend lifespan and how pathologies resulting from dietary excess may occur. |
| Author | James, Andrew M. Smith, Anthony C. Smith, Cassandra L. Robinson, Alan J. Murphy, Michael P. |
| AuthorAffiliation | 1 Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK |
| AuthorAffiliation_xml | – name: 1 Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK |
| Author_xml | – sequence: 1 givenname: Andrew M. surname: James fullname: James, Andrew M. email: aj@mrc-mbu.cam.ac.uk organization: Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK – sequence: 2 givenname: Anthony C. surname: Smith fullname: Smith, Anthony C. organization: Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK – sequence: 3 givenname: Cassandra L. surname: Smith fullname: Smith, Cassandra L. organization: Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK – sequence: 4 givenname: Alan J. surname: Robinson fullname: Robinson, Alan J. organization: Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK – sequence: 5 givenname: Michael P. surname: Murphy fullname: Murphy, Michael P. email: mpm@mrc-mbu.cam.ac.uk organization: Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/30089256$$D View this record in MEDLINE/PubMed |
| BookMark | eNqFUk1vEzEUtFARLaX_ACEfuexie73eNQekKCpQafmQgLPleN8mjjZ2sJ2oufDb8TahajmAL8_ym5lne-Y5OnPeAUIvKSkpoeLNujQwBtiWjNC2JE1JSPMEXTBGaUEZb84e7M_RVYxrkpcglEr-DJ1XhLSS1eIC_foa_K3d6BHPDzGBdRBxWumEr91KOwO4O8R8iD8XMwPpMOpkvcN-yPDkox-twVlhIkZsHf5kM2UWMg1ixHPvIoQ99FOr824Joejs3rol_rYFYyG-QE8HPUa4OtVL9OP99ff5x6L78uFmPusKUzOZCtG3Enot29pUVTUQRljbDFARoEIOhnPZNJKbWhtRDaymDe85GMNYzSpW13V1iW6Our3Xa7UN-cXhoLy26u7Ah6XSIVkzgmJStKblslpwzsVAFqSnlFYNtAxyHbLWu6PWdrfYQG_ApaDHR6KPO86u1NLvlSCSMTFd5vVJIPifO4hJbWzMfo7agd9FxUgrmKBN3Wboq4ez7of8MTAD-BFggo8xwHAPoURNUVFrdYyKmqKiSKNyVDLt7V80Y9Odt_nGdvwf-fQBkB3bWwgqZi9zWHobwKT8pfbfAr8BxUbb2A |
| CitedBy_id | crossref_primary_10_1021_acschembio_4c00174 crossref_primary_10_1016_j_tibs_2018_07_002 crossref_primary_10_1021_jacsau_4c01143 crossref_primary_10_1186_s10020_023_00684_9 crossref_primary_10_1016_j_chembiol_2021_10_010 crossref_primary_10_1016_j_mam_2021_101053 crossref_primary_10_1021_acs_jmedchem_2c00075 crossref_primary_10_1038_s41598_020_77261_1 crossref_primary_10_1038_s41589_024_01805_z crossref_primary_10_1042_BCJ20220251 crossref_primary_10_1021_acsabm_0c01275 crossref_primary_10_1111_mmi_14322 crossref_primary_10_1038_s41580_018_0081_3 crossref_primary_10_1038_s41598_023_31900_5 crossref_primary_10_1016_j_devcel_2020_06_035 crossref_primary_10_1016_j_tibs_2019_06_003 crossref_primary_10_1038_s41467_019_09024_0 crossref_primary_10_1016_j_celrep_2023_112388 crossref_primary_10_3389_fphar_2022_1015642 crossref_primary_10_1016_j_cbpa_2020_10_002 crossref_primary_10_1073_pnas_2212220119 crossref_primary_10_1038_s44318_024_00200_7 crossref_primary_10_1016_j_freeradbiomed_2025_03_025 crossref_primary_10_7554_eLife_69802 crossref_primary_10_1042_CS20190559 crossref_primary_10_3390_ijms222312930 crossref_primary_10_1371_journal_pone_0312733 crossref_primary_10_1016_j_chembiol_2022_04_005 crossref_primary_10_3390_molecules29153496 crossref_primary_10_1111_febs_15331 |
| Cites_doi | 10.15252/embj.201591271 10.1093/nar/gks1155 10.1016/j.chembiol.2015.06.010 10.1074/jbc.R116.771915 10.1074/jbc.M113.486753 10.1016/j.cmet.2014.03.014 10.1016/j.chembiol.2016.11.009 10.1016/S0167-4838(00)00291-0 10.1016/j.cmet.2013.07.013 10.1016/j.tibs.2018.02.002 10.1016/j.tibs.2015.12.006 10.1042/BCJ20170129 10.1074/mcp.M117.067587 10.1016/j.cmet.2015.05.014 10.1016/S0076-6879(03)74020-8 10.1016/j.celrep.2013.07.024 10.1038/nature10815 10.1016/j.semcdb.2017.08.007 10.1073/pnas.1302961110 10.15252/embr.201541132 10.1016/j.celrep.2017.02.018 10.1016/j.cell.2014.02.049 10.1111/j.1742-4658.2010.07576.x 10.1038/nsmb.2555 10.1016/j.molcel.2011.07.019 10.1016/j.molcel.2014.03.027 10.1126/science.289.5487.2126 10.1074/mcp.M111.012658 10.1038/ncomms1255 10.1186/s12934-016-0590-8 10.1016/j.tem.2015.06.001 10.1196/annals.1433.021 |
| ContentType | Journal Article |
| Copyright | 2018 The Author(s) Copyright © 2018 The Author(s). Published by Elsevier Inc. All rights reserved. 2018 The Author(s) 2018 |
| Copyright_xml | – notice: 2018 The Author(s) – notice: Copyright © 2018 The Author(s). Published by Elsevier Inc. All rights reserved. – notice: 2018 The Author(s) 2018 |
| DBID | 6I. AAFTH AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8 5PM DOA |
| DOI | 10.1016/j.celrep.2018.07.007 |
| DatabaseName | ScienceDirect Open Access Titles Elsevier:ScienceDirect:Open Access CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic PubMed Central (Full Participant titles) 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 |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Biology |
| EISSN | 2211-1247 |
| EndPage | 1455 |
| ExternalDocumentID | oai_doaj_org_article_2968c8493b4446f0b0d11137e82e113f PMC6092265 30089256 10_1016_j_celrep_2018_07_007 S2211124718310842 |
| Genre | Research Support, Non-U.S. Gov't Journal Article |
| GrantInformation_xml | – fundername: Wellcome Trust grantid: 110158/Z/15/Z – fundername: Medical Research Council grantid: MC_U105663142 – fundername: Medical Research Council grantid: MC_U105674181 |
| GroupedDBID | 0R~ 0SF 4.4 457 53G 5VS 6I. AACTN AAEDT AAEDW AAFTH AAIKJ AAKRW AALRI AAUCE AAXUO ABMAC ABMWF ACGFO ACGFS ADBBV ADEZE AENEX AEXQZ AFTJW AGHFR AITUG ALKID ALMA_UNASSIGNED_HOLDINGS AMRAJ BAWUL BCNDV DIK EBS EJD FCP FDB FRP GROUPED_DOAJ GX1 IXB KQ8 M41 M48 NCXOZ O-L O9- OK1 RCE RIG ROL SSZ AAMRU AAYWO AAYXX ACVFH ADCNI ADVLN AEUPX AFPUW AIGII AKBMS AKRWK AKYEP APXCP CITATION HZ~ IPNFZ CGR CUY CVF ECM EIF NPM 7X8 5PM |
| ID | FETCH-LOGICAL-c529t-6d89eda985c333f020287fe30e169fc4497794c5ac63f25174d4ecc2252325553 |
| IEDL.DBID | M48 |
| ISSN | 2211-1247 |
| IngestDate | Wed Aug 27 01:20:09 EDT 2025 Thu Aug 21 14:06:24 EDT 2025 Thu Sep 04 19:26:57 EDT 2025 Mon Jul 21 06:08:02 EDT 2025 Thu Apr 24 23:11:05 EDT 2025 Tue Jul 01 02:58:57 EDT 2025 Wed May 17 02:14:14 EDT 2023 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 6 |
| Language | English |
| License | This is an open access article under the CC BY license. Copyright © 2018 The Author(s). Published by Elsevier Inc. All rights reserved. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c529t-6d89eda985c333f020287fe30e169fc4497794c5ac63f25174d4ecc2252325553 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Lead Contact These authors contributed equally |
| OpenAccessLink | http://journals.scholarsportal.info/openUrl.xqy?doi=10.1016/j.celrep.2018.07.007 |
| PMID | 30089256 |
| PQID | 2086261758 |
| PQPubID | 23479 |
| PageCount | 11 |
| ParticipantIDs | doaj_primary_oai_doaj_org_article_2968c8493b4446f0b0d11137e82e113f pubmedcentral_primary_oai_pubmedcentral_nih_gov_6092265 proquest_miscellaneous_2086261758 pubmed_primary_30089256 crossref_primary_10_1016_j_celrep_2018_07_007 crossref_citationtrail_10_1016_j_celrep_2018_07_007 elsevier_sciencedirect_doi_10_1016_j_celrep_2018_07_007 |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | 2018-08-07 |
| PublicationDateYYYYMMDD | 2018-08-07 |
| PublicationDate_xml | – month: 08 year: 2018 text: 2018-08-07 day: 07 |
| PublicationDecade | 2010 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States |
| PublicationTitle | Cell reports (Cambridge) |
| PublicationTitleAlternate | Cell Rep |
| PublicationYear | 2018 |
| Publisher | Elsevier Inc Cell Press Elsevier |
| Publisher_xml | – name: Elsevier Inc – name: Cell Press – name: Elsevier |
| References | Kanfi, Naiman, Amir, Peshti, Zinman, Nahum, Bar-Joseph, Cohen (bib10) 2012; 483 Peleg, Feller, Forne, Schiller, Sévin, Schauer, Regnard, Straub, Prestel, Klima (bib18) 2016; 17 James, Hoogewijs, Logan, Hall, Ding, Fearnley, Murphy (bib9) 2017; 18 Trub, Hirschey (bib27) 2018; 43 Green, Levine (bib7) 2014; 157 Wagner, Payne (bib30) 2013; 288 Fiser, Sali (bib5) 2003; 374 Kuczyńska-Wiśnik, Moruno-Algara, Stojowska-Swędrzyńska, Laskowska (bib11) 2016; 15 Olzscha, Fedorov, Kessler, Knapp, La Thangue (bib16) 2017; 24 Weinert, Schölz, Wagner, Iesmantavicius, Su, Daniel, Choudhary (bib31) 2013; 4 Nakamura, Yoshimori (bib15) 2018; 41 Cohen, Guo, Hurtado, Kwong, Mills, Trojanowski, Lee (bib3) 2011; 2 Weinert, Satpathy, Hansen, Lyon, Jensen, Choudhary (bib33) 2017; 16 Requejo, Hurd, Costa, Murphy (bib22) 2010; 277 Pan, Finkel (bib17) 2017; 292 Wagner, Hirschey (bib29) 2014; 54 Cohen, Friedmann, Hwang, Marmorstein, Lee (bib4) 2013; 20 Pietrocola, Galluzzi, Bravo-San Pedro, Madeo, Kroemer (bib20) 2015; 21 Schwarzenbolz, Mende, Henle (bib24) 2008; 1126 Lin, Defossez, Guarente (bib12) 2000; 289 Satoh, Brace, Rensing, Cliften, Wozniak, Herzog, Yamada, Imai (bib23) 2013; 18 Peng, Lu, Xie, Cheng, Chen, Tan, Luo, Zhang, He, Yang (bib19) 2011; 10 Tacutu, Craig, Budovsky, Wuttke, Lehmann, Taranukha, Costa, Fraifeld, de Magalhães (bib25) 2013; 41 McDonnell, Peterson, Bomze, Hirschey (bib14) 2015; 26 Ma, Gladyshev (bib13) 2017; 70 Rardin, Newman, Held, Cusack, Sorensen, Li, Schilling, Mooney, Kahn, Verdin, Gibson (bib21) 2013; 110 Baeza, Smallegan, Denu (bib1) 2016; 41 Gould, Evans, Martínez-Acedo, Marino, Gladyshev, Carroll, Ischiropoulos (bib6) 2015; 22 Bizzozero, Bixler, Pastuszyn (bib2) 2001; 1545 Tan, Peng, Anderson, Chhoy, Xie, Dai, Park, Chen, Huang, Zhang (bib26) 2014; 19 Tsuchiya, Peak-Chew, Newell, Miller-Aidoo, Mangal, Zhyvoloup, Bakovic, Malanchuk, Pereira, Kotiadis (bib28) 2017; 474 Hirschey, Shimazu, Jing, Grueter, Collins, Aouizerat, Stančáková, Goetzman, Lam, Schwer (bib8) 2011; 44 Weinert, Moustafa, Iesmantavicius, Zechner, Choudhary (bib32) 2015; 34 Nakamura (10.1016/j.celrep.2018.07.007_bib15) 2018; 41 Tan (10.1016/j.celrep.2018.07.007_bib26) 2014; 19 Trub (10.1016/j.celrep.2018.07.007_bib27) 2018; 43 Olzscha (10.1016/j.celrep.2018.07.007_bib16) 2017; 24 Requejo (10.1016/j.celrep.2018.07.007_bib22) 2010; 277 Tacutu (10.1016/j.celrep.2018.07.007_bib25) 2013; 41 Baeza (10.1016/j.celrep.2018.07.007_bib1) 2016; 41 Green (10.1016/j.celrep.2018.07.007_bib7) 2014; 157 James (10.1016/j.celrep.2018.07.007_bib9) 2017; 18 Hirschey (10.1016/j.celrep.2018.07.007_bib8) 2011; 44 Peng (10.1016/j.celrep.2018.07.007_bib19) 2011; 10 Lin (10.1016/j.celrep.2018.07.007_bib12) 2000; 289 Bizzozero (10.1016/j.celrep.2018.07.007_bib2) 2001; 1545 Weinert (10.1016/j.celrep.2018.07.007_bib33) 2017; 16 Schwarzenbolz (10.1016/j.celrep.2018.07.007_bib24) 2008; 1126 McDonnell (10.1016/j.celrep.2018.07.007_bib14) 2015; 26 Cohen (10.1016/j.celrep.2018.07.007_bib4) 2013; 20 Wagner (10.1016/j.celrep.2018.07.007_bib29) 2014; 54 Weinert (10.1016/j.celrep.2018.07.007_bib32) 2015; 34 Peleg (10.1016/j.celrep.2018.07.007_bib18) 2016; 17 Cohen (10.1016/j.celrep.2018.07.007_bib3) 2011; 2 Fiser (10.1016/j.celrep.2018.07.007_bib5) 2003; 374 Kanfi (10.1016/j.celrep.2018.07.007_bib10) 2012; 483 Kuczyńska-Wiśnik (10.1016/j.celrep.2018.07.007_bib11) 2016; 15 Pietrocola (10.1016/j.celrep.2018.07.007_bib20) 2015; 21 Rardin (10.1016/j.celrep.2018.07.007_bib21) 2013; 110 Tsuchiya (10.1016/j.celrep.2018.07.007_bib28) 2017; 474 Gould (10.1016/j.celrep.2018.07.007_bib6) 2015; 22 Weinert (10.1016/j.celrep.2018.07.007_bib31) 2013; 4 Ma (10.1016/j.celrep.2018.07.007_bib13) 2017; 70 Satoh (10.1016/j.celrep.2018.07.007_bib23) 2013; 18 Wagner (10.1016/j.celrep.2018.07.007_bib30) 2013; 288 Pan (10.1016/j.celrep.2018.07.007_bib17) 2017; 292 |
| References_xml | – volume: 70 start-page: 190 year: 2017 end-page: 203 ident: bib13 article-title: Molecular signatures of longevity: insights from cross-species comparative studies publication-title: Semin. Cell Dev. Biol. – volume: 17 start-page: 455 year: 2016 end-page: 469 ident: bib18 article-title: Life span extension by targeting a link between metabolism and histone acetylation in Drosophila publication-title: EMBO Rep. – volume: 15 start-page: 189 year: 2016 ident: bib11 article-title: The effect of protein acetylation on the formation and processing of inclusion bodies and endogenous protein aggregates in Escherichia coli cells publication-title: Microb. Cell Fact. – volume: 34 start-page: 2620 year: 2015 end-page: 2632 ident: bib32 article-title: Analysis of acetylation stoichiometry suggests that SIRT3 repairs nonenzymatic acetylation lesions publication-title: EMBO J. – volume: 474 start-page: 2489 year: 2017 end-page: 2508 ident: bib28 article-title: Protein CoAlation: a redox-regulated protein modification by coenzyme A in mammalian cells publication-title: Biochem. J. – volume: 1545 start-page: 278 year: 2001 end-page: 288 ident: bib2 article-title: Structural determinants influencing the reaction of cysteine-containing peptides with palmitoyl-coenzyme A and other thioesters publication-title: Biochim. Biophys. Acta – volume: 26 start-page: 486 year: 2015 end-page: 492 ident: bib14 article-title: SIRT3 regulates progression and development of diseases of aging publication-title: Trends Endocrinol. Metab. – volume: 277 start-page: 1465 year: 2010 end-page: 1480 ident: bib22 article-title: Cysteine residues exposed on protein surfaces are the dominant intramitochondrial thiol and may protect against oxidative damage publication-title: FEBS J. – volume: 157 start-page: 65 year: 2014 end-page: 75 ident: bib7 article-title: To be or not to be? How selective autophagy and cell death govern cell fate publication-title: Cell – volume: 4 start-page: 842 year: 2013 end-page: 851 ident: bib31 article-title: Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation publication-title: Cell Rep. – volume: 20 start-page: 756 year: 2013 end-page: 762 ident: bib4 article-title: The microtubule-associated tau protein has intrinsic acetyltransferase activity publication-title: Nat. Struct. Mol. Biol. – volume: 19 start-page: 605 year: 2014 end-page: 617 ident: bib26 article-title: Lysine glutarylation is a protein posttranslational modification regulated by SIRT5 publication-title: Cell Metab. – volume: 292 start-page: 6452 year: 2017 end-page: 6460 ident: bib17 article-title: Key proteins and pathways that regulate lifespan publication-title: J. Biol. Chem. – volume: 1126 start-page: 248 year: 2008 end-page: 252 ident: bib24 article-title: Model studies on protein glycation: influence of cysteine on the reactivity of arginine and lysine residues toward glyoxal publication-title: Ann. N Y Acad. Sci. – volume: 16 start-page: 759 year: 2017 end-page: 769 ident: bib33 article-title: Accurate quantification of site-specific acetylation stoichiometry reveals the impact of sirtuin deacetylase cobb on the e. Coli acetylome publication-title: Mol. Cell. Proteomics – volume: 289 start-page: 2126 year: 2000 end-page: 2128 ident: bib12 article-title: Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae publication-title: Science – volume: 54 start-page: 5 year: 2014 end-page: 16 ident: bib29 article-title: Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases publication-title: Mol. Cell – volume: 10 year: 2011 ident: bib19 article-title: The first identification of lysine malonylation substrates and its regulatory enzyme. Mol publication-title: Cell Proteomics – volume: 41 start-page: D1027 year: 2013 end-page: D1033 ident: bib25 article-title: Human Ageing Genomic Resources: integrated databases and tools for the biology and genetics of ageing publication-title: Nucleic Acids Res. – volume: 2 start-page: 252 year: 2011 ident: bib3 article-title: The acetylation of tau inhibits its function and promotes pathological tau aggregation publication-title: Nat. Commun. – volume: 374 start-page: 461 year: 2003 end-page: 491 ident: bib5 article-title: Modeller: generation and refinement of homology-based protein structure models publication-title: Methods Enzymol. – volume: 110 start-page: 6601 year: 2013 end-page: 6606 ident: bib21 article-title: Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways publication-title: Proc. Natl. Acad. Sci. USA – volume: 43 start-page: 369 year: 2018 end-page: 379 ident: bib27 article-title: Reactive acyl-coa species modify proteins and induce carbon stress publication-title: Trends Biochem. Sci. – volume: 44 start-page: 177 year: 2011 end-page: 190 ident: bib8 article-title: SIRT3 deficiency and mitochondrial protein hyperacetylation accelerate the development of the metabolic syndrome publication-title: Mol. Cell – volume: 41 start-page: 231 year: 2016 end-page: 244 ident: bib1 article-title: Mechanisms and dynamics of protein acetylation in mitochondria publication-title: Trends Biochem. Sci. – volume: 288 start-page: 29036 year: 2013 end-page: 29045 ident: bib30 article-title: Widespread and enzyme-independent Nε-acetylation and Nε-succinylation of proteins in the chemical conditions of the mitochondrial matrix publication-title: J. Biol. Chem. – volume: 41 start-page: 65 year: 2018 end-page: 72 ident: bib15 article-title: Autophagy and longevity publication-title: Mol. Cells – volume: 18 start-page: 2105 year: 2017 end-page: 2112 ident: bib9 article-title: Non-enzymatic n-acetylation of lysine residues by acetylCoA often occurs via a proximal s-acetylated thiol intermediate sensitive to glyoxalase ii publication-title: Cell Rep. – volume: 22 start-page: 965 year: 2015 end-page: 975 ident: bib6 article-title: Site-specific proteomic mapping identifies selectively modified regulatory cysteine residues in functionally distinct protein networks publication-title: Chem. Biol. – volume: 24 start-page: 9 year: 2017 end-page: 23 ident: bib16 article-title: Cbp/p300 bromodomains regulate amyloid-like protein aggregation upon aberrant lysine acetylation publication-title: Cell Chem. Biol. – volume: 21 start-page: 805 year: 2015 end-page: 821 ident: bib20 article-title: Acetyl coenzyme A: a central metabolite and second messenger publication-title: Cell Metab. – volume: 483 start-page: 218 year: 2012 end-page: 221 ident: bib10 article-title: The sirtuin SIRT6 regulates lifespan in male mice publication-title: Nature – volume: 18 start-page: 416 year: 2013 end-page: 430 ident: bib23 article-title: Sirt1 extends life span and delays aging in mice through the regulation of Nk2 homeobox 1 in the DMH and LH publication-title: Cell Metab. – volume: 34 start-page: 2620 year: 2015 ident: 10.1016/j.celrep.2018.07.007_bib32 article-title: Analysis of acetylation stoichiometry suggests that SIRT3 repairs nonenzymatic acetylation lesions publication-title: EMBO J. doi: 10.15252/embj.201591271 – volume: 41 start-page: D1027 year: 2013 ident: 10.1016/j.celrep.2018.07.007_bib25 article-title: Human Ageing Genomic Resources: integrated databases and tools for the biology and genetics of ageing publication-title: Nucleic Acids Res. doi: 10.1093/nar/gks1155 – volume: 22 start-page: 965 year: 2015 ident: 10.1016/j.celrep.2018.07.007_bib6 article-title: Site-specific proteomic mapping identifies selectively modified regulatory cysteine residues in functionally distinct protein networks publication-title: Chem. Biol. doi: 10.1016/j.chembiol.2015.06.010 – volume: 292 start-page: 6452 year: 2017 ident: 10.1016/j.celrep.2018.07.007_bib17 article-title: Key proteins and pathways that regulate lifespan publication-title: J. Biol. Chem. doi: 10.1074/jbc.R116.771915 – volume: 288 start-page: 29036 year: 2013 ident: 10.1016/j.celrep.2018.07.007_bib30 article-title: Widespread and enzyme-independent Nε-acetylation and Nε-succinylation of proteins in the chemical conditions of the mitochondrial matrix publication-title: J. Biol. Chem. doi: 10.1074/jbc.M113.486753 – volume: 19 start-page: 605 year: 2014 ident: 10.1016/j.celrep.2018.07.007_bib26 article-title: Lysine glutarylation is a protein posttranslational modification regulated by SIRT5 publication-title: Cell Metab. doi: 10.1016/j.cmet.2014.03.014 – volume: 24 start-page: 9 year: 2017 ident: 10.1016/j.celrep.2018.07.007_bib16 article-title: Cbp/p300 bromodomains regulate amyloid-like protein aggregation upon aberrant lysine acetylation publication-title: Cell Chem. Biol. doi: 10.1016/j.chembiol.2016.11.009 – volume: 1545 start-page: 278 year: 2001 ident: 10.1016/j.celrep.2018.07.007_bib2 article-title: Structural determinants influencing the reaction of cysteine-containing peptides with palmitoyl-coenzyme A and other thioesters publication-title: Biochim. Biophys. Acta doi: 10.1016/S0167-4838(00)00291-0 – volume: 18 start-page: 416 year: 2013 ident: 10.1016/j.celrep.2018.07.007_bib23 article-title: Sirt1 extends life span and delays aging in mice through the regulation of Nk2 homeobox 1 in the DMH and LH publication-title: Cell Metab. doi: 10.1016/j.cmet.2013.07.013 – volume: 43 start-page: 369 year: 2018 ident: 10.1016/j.celrep.2018.07.007_bib27 article-title: Reactive acyl-coa species modify proteins and induce carbon stress publication-title: Trends Biochem. Sci. doi: 10.1016/j.tibs.2018.02.002 – volume: 41 start-page: 231 year: 2016 ident: 10.1016/j.celrep.2018.07.007_bib1 article-title: Mechanisms and dynamics of protein acetylation in mitochondria publication-title: Trends Biochem. Sci. doi: 10.1016/j.tibs.2015.12.006 – volume: 474 start-page: 2489 year: 2017 ident: 10.1016/j.celrep.2018.07.007_bib28 article-title: Protein CoAlation: a redox-regulated protein modification by coenzyme A in mammalian cells publication-title: Biochem. J. doi: 10.1042/BCJ20170129 – volume: 16 start-page: 759 year: 2017 ident: 10.1016/j.celrep.2018.07.007_bib33 article-title: Accurate quantification of site-specific acetylation stoichiometry reveals the impact of sirtuin deacetylase cobb on the e. Coli acetylome publication-title: Mol. Cell. Proteomics doi: 10.1074/mcp.M117.067587 – volume: 21 start-page: 805 year: 2015 ident: 10.1016/j.celrep.2018.07.007_bib20 article-title: Acetyl coenzyme A: a central metabolite and second messenger publication-title: Cell Metab. doi: 10.1016/j.cmet.2015.05.014 – volume: 374 start-page: 461 year: 2003 ident: 10.1016/j.celrep.2018.07.007_bib5 article-title: Modeller: generation and refinement of homology-based protein structure models publication-title: Methods Enzymol. doi: 10.1016/S0076-6879(03)74020-8 – volume: 4 start-page: 842 year: 2013 ident: 10.1016/j.celrep.2018.07.007_bib31 article-title: Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation publication-title: Cell Rep. doi: 10.1016/j.celrep.2013.07.024 – volume: 483 start-page: 218 year: 2012 ident: 10.1016/j.celrep.2018.07.007_bib10 article-title: The sirtuin SIRT6 regulates lifespan in male mice publication-title: Nature doi: 10.1038/nature10815 – volume: 70 start-page: 190 year: 2017 ident: 10.1016/j.celrep.2018.07.007_bib13 article-title: Molecular signatures of longevity: insights from cross-species comparative studies publication-title: Semin. Cell Dev. Biol. doi: 10.1016/j.semcdb.2017.08.007 – volume: 110 start-page: 6601 year: 2013 ident: 10.1016/j.celrep.2018.07.007_bib21 article-title: Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1302961110 – volume: 17 start-page: 455 year: 2016 ident: 10.1016/j.celrep.2018.07.007_bib18 article-title: Life span extension by targeting a link between metabolism and histone acetylation in Drosophila publication-title: EMBO Rep. doi: 10.15252/embr.201541132 – volume: 18 start-page: 2105 year: 2017 ident: 10.1016/j.celrep.2018.07.007_bib9 article-title: Non-enzymatic n-acetylation of lysine residues by acetylCoA often occurs via a proximal s-acetylated thiol intermediate sensitive to glyoxalase ii publication-title: Cell Rep. doi: 10.1016/j.celrep.2017.02.018 – volume: 157 start-page: 65 year: 2014 ident: 10.1016/j.celrep.2018.07.007_bib7 article-title: To be or not to be? How selective autophagy and cell death govern cell fate publication-title: Cell doi: 10.1016/j.cell.2014.02.049 – volume: 277 start-page: 1465 year: 2010 ident: 10.1016/j.celrep.2018.07.007_bib22 article-title: Cysteine residues exposed on protein surfaces are the dominant intramitochondrial thiol and may protect against oxidative damage publication-title: FEBS J. doi: 10.1111/j.1742-4658.2010.07576.x – volume: 20 start-page: 756 year: 2013 ident: 10.1016/j.celrep.2018.07.007_bib4 article-title: The microtubule-associated tau protein has intrinsic acetyltransferase activity publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb.2555 – volume: 44 start-page: 177 year: 2011 ident: 10.1016/j.celrep.2018.07.007_bib8 article-title: SIRT3 deficiency and mitochondrial protein hyperacetylation accelerate the development of the metabolic syndrome publication-title: Mol. Cell doi: 10.1016/j.molcel.2011.07.019 – volume: 54 start-page: 5 year: 2014 ident: 10.1016/j.celrep.2018.07.007_bib29 article-title: Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases publication-title: Mol. Cell doi: 10.1016/j.molcel.2014.03.027 – volume: 289 start-page: 2126 year: 2000 ident: 10.1016/j.celrep.2018.07.007_bib12 article-title: Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae publication-title: Science doi: 10.1126/science.289.5487.2126 – volume: 10 year: 2011 ident: 10.1016/j.celrep.2018.07.007_bib19 article-title: The first identification of lysine malonylation substrates and its regulatory enzyme. Mol publication-title: Cell Proteomics doi: 10.1074/mcp.M111.012658 – volume: 41 start-page: 65 year: 2018 ident: 10.1016/j.celrep.2018.07.007_bib15 article-title: Autophagy and longevity publication-title: Mol. Cells – volume: 2 start-page: 252 year: 2011 ident: 10.1016/j.celrep.2018.07.007_bib3 article-title: The acetylation of tau inhibits its function and promotes pathological tau aggregation publication-title: Nat. Commun. doi: 10.1038/ncomms1255 – volume: 15 start-page: 189 year: 2016 ident: 10.1016/j.celrep.2018.07.007_bib11 article-title: The effect of protein acetylation on the formation and processing of inclusion bodies and endogenous protein aggregates in Escherichia coli cells publication-title: Microb. Cell Fact. doi: 10.1186/s12934-016-0590-8 – volume: 26 start-page: 486 year: 2015 ident: 10.1016/j.celrep.2018.07.007_bib14 article-title: SIRT3 regulates progression and development of diseases of aging publication-title: Trends Endocrinol. Metab. doi: 10.1016/j.tem.2015.06.001 – volume: 1126 start-page: 248 year: 2008 ident: 10.1016/j.celrep.2018.07.007_bib24 article-title: Model studies on protein glycation: influence of cysteine on the reactivity of arginine and lysine residues toward glyoxal publication-title: Ann. N Y Acad. Sci. doi: 10.1196/annals.1433.021 |
| SSID | ssj0000601194 |
| Score | 2.3625324 |
| Snippet | Acetyl-coenzyme A (CoA) is an abundant metabolite that can also alter protein function through non-enzymatic N-acetylation of protein lysines. This... Acetyl-coenzyme A (CoA) is an abundant metabolite that can also alter protein function through non-enzymatic N -acetylation of protein lysines. This N-... |
| SourceID | doaj pubmedcentral proquest pubmed crossref elsevier |
| SourceType | Open Website Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 1445 |
| SubjectTerms | Acetylation Animals Cysteine - metabolism Cytosol - metabolism Lysine - metabolism Mice |
| SummonAdditionalLinks | – databaseName: DOAJ Directory of Open Access Journals dbid: DOA link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV3Pa9swFBalUOhlrD-2Zd2KCr2aKpYsS8cstJSSlhwa6E3Yskw8OnskLjSX_u17T7JDsh5y6ckQP1mR9fT0yfr0PUIuLRtmpVUaBpKTkYgLG-WF1ZEQqbIw_8pY4AHn-wd5OxN3T8nTRqov5IQFeeDw4q5iLZVVQvNcQMmS5azA7OipU7GDa4nRl2m2sZgKMRi1zHBLOY6RsxWLtD8358ld1j0vHMpVDpXX7sRsshvzkpfv35qe3sPP_1mUG9PSzWfyqcOTdBTacUT2XH1MDkKGydUJeZsumtfqD1iMUbIZOe60nWctva7n2N90skLiO32IRta1q0CMo00J5m2zRM1gOkUlh6pe0qqm9xBWoC4oBgGSYrJPJEwWeGvS-O-Dkwq_UFCf1t4tT8ns5vpxfBt1KRcim8S6jWShtCsyrRLLOS8BS8KKqnScuaHUpRUC4KIWNsms5CWqnYlCgBNAUABkliQJ_0L266Z23whNAShoKVSOp1WZ5lmhYR5MLYxzJ3TuBoT3L9zYTo8c02I8m5549tuEbjLYTYbhRnk6ING61N-gx7HD_hf25doW1bT9D-BjpvMxs8vHBiTtPcF0wCQADnhUtaP6i95xDIxb3IzJate8LMEI15IA3tSAfA2OtP6THICZBiwK9W652FYrtu_U1dxrg0umAVAn3z-i2WfkEJvi6Y7pD7LfLl7cT4BgbX7uR9s_ZqorKg priority: 102 providerName: Directory of Open Access Journals – databaseName: ScienceDirect Open Access Journals (Elsevier) dbid: IXB link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3fa9swEBalUNjLWLtuy_oDFfoq4liyLD22oaWUJBS6QN6ELcuLR2eXxIXlpX9772Q7xNtDYU8h9ilSrNPdJ_nuO0IubTBKcqs0LCQnmQgzy9LMaiZErCz4XxkKTHCezuTdXNwvosUeGXe5MBhW2dr-xqZ7a91eGbZPc_hcFMPHEPYu4J3AuAJEUQLtMGaVYhLf4np7zoJ8IyNfDxHlGTboMuh8mJd1TyuHxJUj5Vk8sa7sjofyRP49R_UvEP07nnLHQd1-Ih9bZEmvmsEfkj1XHpGDptbk5jN5fVhVf4rfIDFG8maMdqf1MqnpTbnEmaeTDYbA0xm7sq7eNCFytMpBvK7WyB5MH5DToSjXtCjpFAwM9AXNwFRSLPuJoZMZ3ppU_qRwUuBZBfUF7t36mMxvb36M71hbfIHZKNQ1k5nSLku0iiznPAdUCXur3PHAjaTOrRAAHLWwUWIlz5H3TGQC1AHMA2C0KIr4F7JfVqX7RmgMkEFLoVLMWw00TzINkxZbWPFO6NQNCO8euLEtMzkWyHgyXQjaL9NMk8FpMgG-Mo8HhG1bPTfMHO_IX-NcbmWRV9tfqFY_TatYJtRSWSU0TwXoaR6kQQZKxmOnQgef-YDEnSaYnprCTxXvdH_RKY6BFYyvZZLSVS9rEMJdJcA4NSBfG0XaDpIDRNOASqHfnor1_kX_TlksPUu4DDRA6-j7f4_4hHzAbz7aMT4l-_XqxZ0BAqvTc7_E3gCSri3I priority: 102 providerName: Elsevier |
| Title | Proximal Cysteines that Enhance Lysine N-Acetylation of Cytosolic Proteins in Mice Are Less Conserved in Longer-Living Species |
| URI | https://dx.doi.org/10.1016/j.celrep.2018.07.007 https://www.ncbi.nlm.nih.gov/pubmed/30089256 https://www.proquest.com/docview/2086261758 https://pubmed.ncbi.nlm.nih.gov/PMC6092265 https://doaj.org/article/2968c8493b4446f0b0d11137e82e113f |
| Volume | 24 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV3Pb5swFLaqTpN2mbpfXbqu8qRdmQg2xj5MVVq16qYk6mGRcrPAmIYpgw2olFz6t_c9A9nYD3UXIoHBBL_n99n-_D1C3ht_HGdGKnAkKzwepMZLUqM8ziNpIP6KgOMG59lcXC3452W43CN9ztbuA9Z_HdphPqlFtf6w-bE9BYf_-JOrZey6sqg-OZZOihO3lz9yK0ZI5usAf9s3o8YZLjUHAXK5Ah71--n-8aBBvHKy_oOw9Scs_Z1d-Uu4ujwgTzucSSetYTwje7Z4Th63mSe3L8jddVVu8m9Q4hylnJH7TptV3NCLYoV2QKdbJMTTuTcxttm2hDlaZlC8KWvUEqbXqPCQFzXNCzqD7gbqgtug46SYBBSJlClempZu3nCa48wFdenubf2SLC4vvpxfeV0qBs-EgWo8kUpl01jJ0DDGMsCYMNLKLPPtWKjMcA4wUnETxkawDFXQeMrBOKCzAMQWhiF7RfaLsrCvCY0AQCjBZYK7WH3F4lRBfIwM-L_lKrEjwvoPrk2nU47pMta6J6R91W0zaWwm7eMCejQi3u6u761OxwPlz7Atd2VRZdudKKsb3TmtDpSQRnLFEg5Wm_mJn0JoYJGVgYXfbESi3hJ0B1haIAKPyh-o_l1vOBr8GRdp4sKWtzUUwjEmgDo5IoetIe1ekgFgU4BRod6BiQ3-xfBKka-cZrjwFQDt8Og_6n1DnuCbOpZjdEz2m-rWvgXk1SQnbsYCjp-WZyfOse4Blt4s3A |
| linkProvider | Scholars Portal |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3PT9swFLYQE9ou09jY6NiYkbhaTWMnsY9QgcqWVkgDqTcrcZw1CBLUBmm97G_nPSepCByQdooU27ETvx-fnefvEXJsvFGSG6lAkWzIhJ8ZlmZGMSEiacD_hr7AA87TWTi5Fj_nwXyLjLuzMBhW2dr-xqY7a93eGbZfc3hfFMPfPqxdwDuBcQWIIgXY4TeABjwU7Yv56WajBQlHRi4hIjZg2KI7QufivIy9XVpkrhxJR-OJiWWfuCjH5N_zVC-R6POAyice6vwDed9CS3rSjH6XbNnyI9lpkk2uP5F_l8vqb3EHNcbI3ozh7rReJDU9Kxc49TReYww8nbETY-t1EyNHqxyq19UK6YPpJZI6FOWKFiWdgoWBvqAZ2EqKeT8xdjLDorhyW4VxgZsV1GW4t6s9cn1-djWesDb7AjOBr2oWZlLZLFEyMJzzHGAlLK5yyz07ClVuhADkqIQJEhPyHInPRCZAHsA-AEgLgoB_JttlVdp9QiPADCoUMsWDq57iSaZg1iIDKm-FSu2A8O6Da9NSk2OGjFvdxaDd6GaaNE6T9vCfeTQgbNPqvqHmeKX-Kc7lpi4Sa7sb1fKPbiVL-yqURgrFUwGCmnupl4GU8chK38I1H5CokwTdk1N4VPFK90ed4GhQYfwvk5S2elhBJVxWAo6TA_KlEaTNIDlgNAWwFPrtiVjvLfolZbFwNOGgCoCtg6__PeIf5O3kahrr-GL264C8wxIX-hh9I9v18sF-BzhWp4dO3R4BwYow6w |
| 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=Proximal+Cysteines+that+Enhance+Lysine+N-Acetylation+of+Cytosolic+Proteins+in+Mice+Are+Less+Conserved+in+Longer-Living+Species&rft.jtitle=Cell+reports+%28Cambridge%29&rft.au=James%2C+Andrew+M&rft.au=Smith%2C+Anthony+C&rft.au=Smith%2C+Cassandra+L&rft.au=Robinson%2C+Alan+J&rft.date=2018-08-07&rft.issn=2211-1247&rft.eissn=2211-1247&rft.volume=24&rft.issue=6&rft.spage=1445&rft_id=info:doi/10.1016%2Fj.celrep.2018.07.007&rft.externalDBID=NO_FULL_TEXT |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2211-1247&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2211-1247&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2211-1247&client=summon |