Assembly and structure of protein phosphatase 2A
Protein phosphatase 2A (PP2A) represents a conserved family of important protein serine/threonine phosphatases in species ranging from yeast to human. The PP2A core enzyme comprises a scaffold subunit and a catalytic subunit. The heterotrimeric PP2A holoenzyme consists of the core enzyme and a varia...
Saved in:
| Published in | Science China. Life sciences Vol. 52; no. 2; pp. 135 - 146 |
|---|---|
| Main Author | |
| Format | Journal Article |
| Language | English |
| Published |
Beijing
Science China Press
01.02.2009
Springer Nature B.V |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1674-7305 1006-9305 1869-1889 1862-2798 |
| DOI | 10.1007/s11427-009-0018-3 |
Cover
| Abstract | Protein phosphatase 2A (PP2A) represents a conserved family of important protein serine/threonine phosphatases in species ranging from yeast to human. The PP2A core enzyme comprises a scaffold subunit and a catalytic subunit. The heterotrimeric PP2A holoenzyme consists of the core enzyme and a variable regulatory subunit. The catalytic subunit of PP2A is subject to reversible methylation, medi-ated by two conserved enzymes. Both the PP2A core and holoenzymes are regulated through interac-tion with a large number of cellular cofactors. Recent biochemical and structural investigation reveals critical insights into the assembly and function of the PP2A core enzyme as well as two families of holoenzyme. This review focuses on the molecular mechanisms revealed by these latest advances. |
|---|---|
| AbstractList | Protein phosphatase 2A (PP2A) represents a conserved family of important protein serine/threonine phosphatases in species ranging from yeast to human. The PP2A core enzyme comprises a scaffold subunit and a catalytic subunit. The heterotrimeric PP2A holoenzyme consists of the core enzyme and a variable regulatory subunit. The catalytic subunit of PP2A is subject to reversible methylation, mediated by two conserved enzymes. Both the PP2A core and holoenzymes are regulated through interaction with a large number of cellular cofactors. Recent biochemical and structural investigation reveals critical insights into the assembly and function of the PP2A core enzyme as well as two families of holoenzyme. This review focuses on the molecular mechanisms revealed by these latest advances. Protein phosphatase 2A (PP2A) represents a conserved family of important protein serine/threonine phosphatases in species ranging from yeast to human. The PP2A core enzyme comprises a scaffold subunit and a catalytic subunit. The heterotrimeric PP2A holoenzyme consists of the core enzyme and a variable regulatory subunit. The catalytic subunit of PP2A is subject to reversible methylation, medi-ated by two conserved enzymes. Both the PP2A core and holoenzymes are regulated through interac-tion with a large number of cellular cofactors. Recent biochemical and structural investigation reveals critical insights into the assembly and function of the PP2A core enzyme as well as two families of holoenzyme. This review focuses on the molecular mechanisms revealed by these latest advances. Protein phosphatase 2A (PP2A) represents a conserved family of important protein serine/threonine phosphatases in species ranging from yeast to human. The PP2A core enzyme comprises a scaffold subunit and a catalytic subunit. The heterotrimeric PP2A holoenzyme consists of the core enzyme and a variable regulatory subunit. The catalytic subunit of PP2A is subject to reversible methylation, mediated by two conserved enzymes. Both the PP2A core and holoenzymes are regulated through interaction with a large number of cellular cofactors. Recent biochemical and structural investigation reveals critical insights into the assembly and function of the PP2A core enzyme as well as two families of holoenzyme. This review focuses on the molecular mechanisms revealed by these latest advances.Protein phosphatase 2A (PP2A) represents a conserved family of important protein serine/threonine phosphatases in species ranging from yeast to human. The PP2A core enzyme comprises a scaffold subunit and a catalytic subunit. The heterotrimeric PP2A holoenzyme consists of the core enzyme and a variable regulatory subunit. The catalytic subunit of PP2A is subject to reversible methylation, mediated by two conserved enzymes. Both the PP2A core and holoenzymes are regulated through interaction with a large number of cellular cofactors. Recent biochemical and structural investigation reveals critical insights into the assembly and function of the PP2A core enzyme as well as two families of holoenzyme. This review focuses on the molecular mechanisms revealed by these latest advances. Issue Title: Special Issue: In Memoriam: Professor Ray Wu Protein phosphatase 2A (PP2A) represents a conserved family of important protein serine/threonine phosphatases in species ranging from yeast to human. The PP2A core enzyme comprises a scaffold subunit and a catalytic subunit. The heterotrimeric PP2A holoenzyme consists of the core enzyme and a variable regulatory subunit. The catalytic subunit of PP2A is subject to reversible methylation, mediated by two conserved enzymes. Both the PP2A core and holoenzymes are regulated through interaction with a large number of cellular cofactors. Recent biochemical and structural investigation reveals critical insights into the assembly and function of the PP2A core enzyme as well as two families of holoenzyme. This review focuses on the molecular mechanisms revealed by these latest advances. |
| Author | Shi, YiGong |
| Author_xml | – sequence: 1 givenname: YiGong surname: Shi fullname: Shi, YiGong email: shi-lab@tsinghua.edu.cn organization: Center for Structural Biology, Department of Biological Sciences and Biotechnology, and School of Medicine, Tsinghua University |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/19277525$$D View this record in MEDLINE/PubMed |
| BookMark | eNp9kctqHDEQRUVwiB_xB2RjGge860SlR0taDsaxDYZskrVQq9WeNj3SWFIv_PcuM5MHBlsgSohzqy51j8lBTDEQ8gXoN6BUfS8AgqmWUoMXdMs_kCPQnWlBa3OA706JVnEqD8lpKQ8UD-eUKfWJHILBKpk8InRVStj081Pj4tCUmhdflxyaNDbbnGqYYrNdp7Jdu-pKaNjqM_k4urmE0309Ib9_XP26vGnvfl7fXq7uWi8M1DYIppUzo-Zc6t5wEBxcwN8eYPAyeA50MCOEwWMZJPQjYwyE0oYNspP8hFzs-qKNxyWUajdT8WGeXQxpKbZTFDjCCH59BT6kJUf0ZpnSquNGSYHU-ZsUE1JJZTRCZ3to6TdhsNs8bVx-sn_WhYDaAT6nUnIYrZ-qq1OKNbtptkDtSzZ2l43FbOxLNpajEl4p_zZ_R8N2moJsvA_5n-f3RPt1-HWK94-o-28S5UKbjhn-DIJbqBY |
| CitedBy_id | crossref_primary_10_1038_s41392_022_01038_3 crossref_primary_10_1016_j_bone_2011_06_004 crossref_primary_10_4161_cc_24637 crossref_primary_10_1007_s11427_009_0094_4 crossref_primary_10_1155_2012_659649 crossref_primary_10_1371_journal_pone_0101846 crossref_primary_10_1016_j_str_2016_09_010 crossref_primary_10_1016_j_bbamcr_2014_06_008 crossref_primary_10_1074_jbc_M111_306456 crossref_primary_10_1021_cb300597g crossref_primary_10_1016_j_bbrc_2020_04_123 crossref_primary_10_1093_hr_uhad067 crossref_primary_10_1371_journal_pone_0065967 crossref_primary_10_1016_j_plantsci_2022_111490 crossref_primary_10_1534_genetics_111_138040 crossref_primary_10_1002_cbf_1691 crossref_primary_10_1007_s13277_016_5036_8 crossref_primary_10_1007_s11434_010_4239_4 crossref_primary_10_3390_ijms20153776 crossref_primary_10_1007_s11427_010_4105_2 crossref_primary_10_1007_s11434_011_4679_5 crossref_primary_10_1016_j_str_2018_07_010 crossref_primary_10_1128_spectrum_00104_23 crossref_primary_10_3390_cancers13194766 crossref_primary_10_3724_SP_J_1206_2011_00241 crossref_primary_10_1111_j_1742_4658_2010_07864_x crossref_primary_10_1016_j_mce_2017_11_005 crossref_primary_10_1002_cm_20519 crossref_primary_10_1016_j_anireprosci_2024_107457 crossref_primary_10_1002_yea_1778 crossref_primary_10_1021_jf5007165 crossref_primary_10_3390_biomedicines11061638 crossref_primary_10_1007_s11427_010_4112_3 crossref_primary_10_1007_s11434_010_4229_6 crossref_primary_10_1074_jbc_RA118_006319 crossref_primary_10_3724_SP_J_1206_2010_00555 crossref_primary_10_1038_labinvest_2016_82 crossref_primary_10_1074_jbc_M109_093294 crossref_primary_10_1039_C1MB05340J crossref_primary_10_1124_mol_114_095984 crossref_primary_10_3724_SP_J_1206_2010_00474 |
| Cites_doi | 10.1016/j.cell.2007.06.034 10.1002/prot.340110407 10.1126/science.1058040 10.1016/S0968-0004(97)01060-8 10.1093/emboj/19.21.5682 10.1128/MCB.11.4.1988 10.1042/bj20031643 10.1038/35057062 10.1038/nature04664 10.1016/S0014-5793(01)02127-5 10.1042/bj2560283 10.1016/j.molcel.2006.07.008 10.1021/bi00455a010 10.1021/bi991646a 10.1074/jbc.C600100200 10.1074/jbc.M401444200 10.1074/jbc.274.20.14382 10.1074/jbc.275.8.5535 10.1128/MCB.11.4.1996 10.1073/pnas.72.5.1858 10.1021/bi990902g 10.1074/jbc.274.36.25490 10.1074/jbc.M008694200 10.1016/j.devcel.2006.03.010 10.1038/sj.onc.1201259 10.1016/0306-4522(94)90400-6 10.1128/MCB.17.3.1692 10.1126/science.1100537 10.1128/EC.4.6.1029-1040.2005 10.1107/S0021889891004399 10.1101/gad.259903 10.1126/science.282.5387.284 10.1126/science.1132814 10.1016/j.bbrc.2007.01.085 10.1016/j.cell.2006.09.025 10.1016/S0092-8674(00)80963-0 10.1016/j.molcel.2006.07.027 10.1111/j.1432-1033.1994.00899.x 10.1016/S0092-8674(00)00192-6 10.1016/S0896-6273(00)80250-0 10.1038/sj.onc.1204059 10.1371/journal.pbio.0050155 10.1016/j.gde.2004.12.004 10.1021/bi00465a002 10.1046/j.0014-2956.2001.02680.x 10.1042/bj3270481 10.1038/nature04663 10.1128/MCB.12.11.4872 10.1038/nsmb1254 10.1006/bbrc.1994.2383 10.1016/j.cell.2004.05.018 10.1093/emboj/19.21.5672 10.1016/0014-5793(90)80245-E 10.1016/j.yexcr.2007.07.030 10.1091/mbc.12.1.185 10.1038/175169a0 10.1016/j.molcel.2008.08.006 10.1371/journal.pbio.0050202 10.1074/jbc.M704861200 10.1073/pnas.86.22.8669 10.1083/jcb.129.2.397 10.1038/sj.onc.1204279 10.1042/bj3530417 10.1074/jbc.M704059200 10.1042/bj3390241 10.1016/0006-3002(56)90273-6 10.1038/nmeth731 10.1016/0014-5793(93)80850-T 10.1073/pnas.93.12.6043 10.1016/0092-8674(95)90405-0 10.1073/pnas.73.11.4070 10.1016/S0092-8674(00)81419-1 10.1073/pnas.91.12.5562 10.1016/j.cell.2006.11.033 10.1038/nature05351 10.1021/bi7007118 10.1016/j.cell.2008.02.041 10.1016/S0955-0674(99)00074-5 10.1074/jbc.M211717200 10.1016/S0021-9258(17)42124-7 10.1016/S0021-9258(18)32257-9 10.1126/scisignal.792001pe1 10.1128/JVI.68.1.123-129.1994 10.1074/jbc.M102621200 10.1016/S0021-9258(19)52289-X 10.1016/S0021-9258(19)38660-0 10.1016/S0021-9258(19)36497-X 10.1016/S0021-9258(19)36692-X 10.1016/S0021-9258(17)32138-5 10.1152/physrev.1993.73.4.673 10.18388/abp.2001_3858 10.1046/j.1471-4159.1995.65062804.x |
| ContentType | Journal Article |
| Copyright | Science in China Press and Springer-Verlag GmbH 2009 Science in China Press and Springer-Verlag GmbH 2009. |
| Copyright_xml | – notice: Science in China Press and Springer-Verlag GmbH 2009 – notice: Science in China Press and Springer-Verlag GmbH 2009. |
| DBID | 2RA 92L CQIGP W94 WU4 ~WA AAYXX CITATION CGR CUY CVF ECM EIF NPM 3V. 7QP 7TK 7U9 7X2 7X7 7XB 88A 88E 8AO 8FE 8FH 8FI 8FJ 8FK ABUWG AFKRA ATCPS AZQEC BBNVY BENPR BHPHI CCPQU DWQXO FYUFA GHDGH GNUQQ H94 HCIFZ K9. LK8 M0K M0S M1P M7P PHGZM PHGZT PJZUB PKEHL PPXIY PQEST PQGLB PQQKQ PQUKI PRINS 7X8 |
| DOI | 10.1007/s11427-009-0018-3 |
| DatabaseName | 维普期刊资源整合服务平台 中文科技期刊数据库-CALIS站点 中文科技期刊数据库-7.0平台 中文科技期刊数据库-自然科学 中文科技期刊数据库-自然科学-生物科学 中文科技期刊数据库- 镜像站点 CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed ProQuest Central (Corporate) Calcium & Calcified Tissue Abstracts Neurosciences Abstracts Virology and AIDS Abstracts ProQuest Agricultural Science Health & Medical Collection ProQuest Central (purchase pre-March 2016) Biology Database (Alumni Edition) Medical Database (Alumni Edition) ProQuest Pharma Collection ProQuest SciTech Collection ProQuest Natural Science Journals Hospital Premium Collection Hospital Premium Collection (Alumni Edition) ProQuest Central (Alumni) (purchase pre-March 2016) ProQuest Central (Alumni) ProQuest Central UK/Ireland Agricultural & Environmental Science Collection ProQuest Central Essentials Biological Science Collection ProQuest Central Natural Science Collection ProQuest One ProQuest Central Health Research Premium Collection Health Research Premium Collection (Alumni) ProQuest Central Student AIDS and Cancer Research Abstracts SciTech Premium Collection ProQuest Health & Medical Complete (Alumni) ProQuest Biological Science Collection Agricultural Science Database ProQuest Health & Medical Collection Medical Database Biological Science Database (Proquest) ProQuest Central Premium ProQuest One Academic ProQuest Health & Medical Research Collection ProQuest One Academic Middle East (New) ProQuest One Health & Nursing ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Applied & Life Sciences ProQuest One Academic ProQuest One Academic UKI Edition ProQuest Central China MEDLINE - Academic |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) Agricultural Science Database ProQuest Central Student ProQuest One Academic Middle East (New) ProQuest Central Essentials ProQuest Health & Medical Complete (Alumni) ProQuest Central (Alumni Edition) SciTech Premium Collection ProQuest One Community College ProQuest One Health & Nursing ProQuest Natural Science Collection ProQuest Pharma Collection ProQuest Central China ProQuest Biology Journals (Alumni Edition) ProQuest Central ProQuest One Applied & Life Sciences ProQuest Health & Medical Research Collection Health Research Premium Collection Health and Medicine Complete (Alumni Edition) Natural Science Collection ProQuest Central Korea Health & Medical Research Collection Agricultural & Environmental Science Collection Biological Science Collection AIDS and Cancer Research Abstracts ProQuest Central (New) ProQuest Medical Library (Alumni) Virology and AIDS Abstracts ProQuest Biological Science Collection ProQuest One Academic Eastern Edition Agricultural Science Collection ProQuest Hospital Collection Health Research Premium Collection (Alumni) Biological Science Database ProQuest SciTech Collection Neurosciences Abstracts ProQuest Hospital Collection (Alumni) ProQuest Health & Medical Complete ProQuest Medical Library ProQuest One Academic UKI Edition ProQuest One Academic Calcium & Calcified Tissue Abstracts ProQuest One Academic (New) ProQuest Central (Alumni) MEDLINE - Academic |
| DatabaseTitleList | AIDS and Cancer Research Abstracts MEDLINE - Academic Agricultural Science Database MEDLINE |
| Database_xml | – sequence: 1 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: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database – sequence: 3 dbid: BENPR name: ProQuest Central url: http://www.proquest.com/pqcentral?accountid=15518 sourceTypes: Aggregation Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Biology |
| DocumentTitleAlternate | Assembly and structure of protein phosphatase 2A |
| EISSN | 1869-1889 1862-2798 |
| EndPage | 146 |
| ExternalDocumentID | 1893737001 19277525 10_1007_s11427_009_0018_3 1003489629 |
| Genre | Review Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural |
| GrantInformation_xml | – fundername: NCI NIH HHS grantid: R01 CA123155 |
| GroupedDBID | --- -A0 -EM -Y2 1N0 2B. 2C. 2RA 2VQ 3V. 4.4 406 40D 40G 53G 5VR 5VS 7X7 88A 88E 8AO 8FE 8FH 8FI 8FJ 8TC 92E 92I 92L 92Q 93N AAAVM AAFGU AAHNG AAIAL AANXM AANZL AARHV AATNV AATVU AAUYE AAYFA AAYQN ABDZT ABECU ABFGW ABFTV ABJNI ABJOX ABKAS ABKCH ABMQK ABQBU ABSXP ABTEG ABTKH ABTMW ABUWG ACAOD ACBMV ACBRV ACBXY ACBYP ACGFS ACHSB ACIGE ACIHN ACIPQ ACOKC ACPRK ACREN ACTTH ACVWB ACWMK ACZOJ ADINQ ADKNI ADKPE ADMDM ADOXG ADRFC ADURQ ADYFF ADZKW AEAQA AEFTE AEJRE AEOHA AEPYU AESKC AESTI AEVLU AEVTX AEXYK AFGXO AFKRA AFLOW AFNRJ AFQWF AFUIB AGDGC AGGBP AGJBK AGMZJ AGQMX AHBYD AHMBA AHSBF AHYZX AIAKS AILAN AIMYW AITGF AJDOV AJRNO AJZVZ AKQUC ALMA_UNASSIGNED_HOLDINGS AMKLP AMTXH AMXSW AMYLF AXYYD BBNVY BENPR BGNMA BHPHI BPHCQ BVXVI C6C CAG CCEZO CCPQU CCVFK COF CQIGP CSCUP DIK DNIVK DPUIP EBLON EBS EIOEI EJD EMOBN F5P FA0 FERAY FIGPU FINBP FNLPD FSGXE FYUFA GGCAI GJIRD GX1 H4N HCIFZ HG6 HMCUK HZ~ IKXTQ IWAJR J-C JZLTJ KOV KQ8 LK8 LLZTM M0L M1P M4Y M7P NPVJJ NQJWS NU0 O9J OK1 PQQKQ PROAC PSQYO PT4 Q2X RIG RNS ROL RSV SBL SCL SNE SNPRN SNX SOHCF SOJ SPISZ SRMVM SSLCW STPWE SV3 TCJ TGP TR2 TSG U2A UG4 UKHRP UOJIU UTJUX UZXMN VFIZW W94 WK8 WU4 Z7U Z87 ZMTXR ~WA .86 123 6NX ACGFO ADHHG AFGCZ AMYQR BA0 CHBEP CJPJV CS3 CW9 HF~ HLICF IHE I~X O9- QOS RPX S27 SDH T13 VC2 AAYXX CITATION CGR CUY CVF ECM EIF NPM -SA -S~ 0R~ 7QP 7TK 7U9 7X2 7XB 8FK AACDK AAJBT AASML ABAKF ABBRH ABDBE ABRTQ ACDTI ACPIV AEFQL AEMSY AFDZB AGQEE AGRTI AHPBZ AIGIU ATCPS ATHPR AYFIA AZQEC CAJEA DWQXO GNUQQ H94 K9. M0K PHGZM PHGZT PJZUB PKEHL PPXIY PQEST PQGLB PQUKI PRINS Q-- SJYHP U1G U5K AAYZH 7X8 |
| ID | FETCH-LOGICAL-c491t-e4287a9f83358b931431aee42b11dc5ec310d9f1edcd9fd51bf222147892d5653 |
| IEDL.DBID | U2A |
| ISSN | 1674-7305 1006-9305 |
| IngestDate | Thu Sep 04 15:25:03 EDT 2025 Tue Oct 07 05:54:22 EDT 2025 Sat Oct 25 08:57:25 EDT 2025 Thu Jan 02 22:04:24 EST 2025 Thu Apr 24 22:58:31 EDT 2025 Wed Oct 01 04:56:48 EDT 2025 Fri Feb 21 02:45:07 EST 2025 Wed Feb 14 10:32:46 EST 2024 |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 2 |
| Keywords | PP2A protein phosphorylation mechanism structure dephosphorylation |
| Language | English |
| License | http://www.springer.com/tdm |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c491t-e4287a9f83358b931431aee42b11dc5ec310d9f1edcd9fd51bf222147892d5653 |
| Notes | SHI Yi Gong Center for Structural Biology, Department of Biological Sciences and Biotechnology, and School of Medicine, Tsinghua University, Beijing 100084, China 11-5841/Q ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 ObjectType-Review-3 content type line 23 |
| PMID | 19277525 |
| PQID | 224575798 |
| PQPubID | 54335 |
| PageCount | 12 |
| ParticipantIDs | proquest_miscellaneous_67013892 proquest_journals_2787639754 proquest_journals_224575798 pubmed_primary_19277525 crossref_citationtrail_10_1007_s11427_009_0018_3 crossref_primary_10_1007_s11427_009_0018_3 springer_journals_10_1007_s11427_009_0018_3 chongqing_primary_1003489629 |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | 2009-02-01 |
| PublicationDateYYYYMMDD | 2009-02-01 |
| PublicationDate_xml | – month: 02 year: 2009 text: 2009-02-01 day: 01 |
| PublicationDecade | 2000 |
| PublicationPlace | Beijing |
| PublicationPlace_xml | – name: Beijing – name: China – name: Dordrecht |
| PublicationSubtitle | Life Sciences |
| PublicationTitle | Science China. Life sciences |
| PublicationTitleAbbrev | SCI CHINA SER C |
| PublicationTitleAlternate | Science China: Life Science |
| PublicationYear | 2009 |
| Publisher | Science China Press Springer Nature B.V |
| Publisher_xml | – name: Science China Press – name: Springer Nature B.V |
| References | Turowski, Fernandez, Favre (CR34) 1995; 129 Witman, Cleveland, Weingarten (CR70) 1976; 73 Conti, Uy, Leighton (CR55) 1998; 94 van Hoof, Cayla, Bosch (CR90) 1994; 226 Kraulis (CR93) 1991; 24 Xu, Chen, Zhang (CR28) 2008; 31 Lee, Stock (CR21) 1993; 268 Ruediger, Pham, Walter (CR49) 2001; 20 Scheidtmann, Mumby, Rundell (CR46) 1991; 11 Mumby (CR16) 2007; 130 Drewes, Mandelkow, Baumann (CR72) 1993; 336 Ikehara, Ikehara, Imamura (CR27) 2007; 354 Sontag, Nunbhakdi-Craig, Lee (CR64) 1996; 17 CR31 Kins, Crameri, Evans (CR68) 2001; 276 Leulliot, Vicentini, Jordens (CR86) 2006; 23 Xie, Clarke (CR20) 1993; 268 Prickett, Brautigan (CR91) 2004; 279 Hunter (CR1) 1995; 80 Nicholls, Sharp, Honig (CR92) 1991; 11 Chung, Nairn, Murata (CR29) 1999; 38 Goedert, Jakes, Qi (CR63) 1995; 65 Kitajima, Sakuno, Ishiguro (CR52) 2006; 441 Lee, Pallas (CR35) 2007; 282 MacKintosh, Beattie, Klumpp (CR51) 1990; 264 Ruediger, Roeckel, Fait (CR42) 1992; 12 Chernoff, Li, Cheng (CR10) 1983; 258 Ruediger, Hentz, Fait (CR43) 1994; 68 Longin, Jordens, Martens (CR80) 2004; 380 Kremmer, Ohst, Kiefer (CR44) 1997; 17 Gong, Lidsky, Wegiel (CR66) 2000; 275 Ogris, Gibson, Pallas (CR26) 1997; 15 Graham, Weaver, Mao (CR56) 2000; 103 Bennecib, Gong, Grundke-Iqbal (CR67) 2000; 490 Lander, Linton, Birren (CR5) 2001; 409 Venter, Adams, Myers (CR7) 2001; 291 Cayla, Goris, Hermann (CR89) 1990; 29 Janssens, Goris (CR11) 2001; 353 Janssens, Jordens, Stevens (CR60) 2003; 278 Kong, Fox, Mu (CR30) 2004; 306 Sontag, Nunbhakdi-Craig, Lee (CR65) 1999; 274 Yang, Roe, Prickett (CR88) 2007; 46 Lee, Chen, Tolstykh (CR17) 1996; 93 Xing, Li, Chen (CR81) 2008; 133 Xie, Clarke (CR19) 1994; 203 Longin, Zwaenepoel, Martens (CR82) 2008; 314 Groves, Hanlon, Turowski (CR38) 1999; 96 Ikehara, Ikehara, Imamura (CR61) 2007; 354 Kamibayashi, Estes, Lickteig (CR58) 1994; 269 Li, Virshup (CR59) 2002; 269 Kamibayashi, Lickteig, Estes (CR57) 1992; 267 Longin, Zwaenepoel, Louis (CR77) 2007; 282 Xu, Xing, Chen (CR22) 2006; 127 Johnson, Hunter (CR6) 2005; 2 Bialojan, Takai (CR50) 1988; 256 Chao, Xing, Chen (CR85) 2006; 23 Wang, Esplin, Li (CR48) 1998; 282 Tang, Shu, Qi (CR54) 2006; 10 Lechward, Awotunde, Swiatek (CR13) 2001; 48 De Baere, Derua, Janssens (CR33) 1999; 38 Walter, Ferre, Espiritu (CR37) 1989; 86 Cho, Xu (CR39) 2007; 445 Magnusdottir, Stenmark, Flodin (CR87) 2006; 281 Gong, Grundke-Iqbal, Iqbal (CR73) 1994; 61 Xie, Clarke (CR18) 1994; 269 Hemmings, Adams-Pearson, Maurer (CR36) 1990; 29 Hombauer, Weismann, Mudrak (CR84) 2007; 5 Tolstykh, Lee, Vafai (CR24) 2000; 19 Xing, Xu, Chen (CR23) 2006; 127 Yu, Du, Moreno (CR75) 2001; 12 Virshup (CR12) 2000; 12 Sutherland, Wosilait (CR3) 1955; 175 Weingarten, Lockwood, Hwo (CR69) 1975; 72 Alonso, Sasin, Bottini (CR8) 2004; 117 Cho, Morrone, Sablina (CR41) 2007; 5 Fischer, Krebs (CR2) 1955; 216 Kloeker, Bryant, Strack (CR76) 1997; 327 Mumby, Walter (CR14) 1993; 73 Krebs, Fischer (CR4) 1956; 20 Gentry, Li, Wei (CR78) 2005; 4 Cohen (CR9) 1997; 22 Chen, Xu, Bao (CR40) 2007; 14 Wu, Tolstykh, Lee (CR32) 2000; 19 Fellner, Lackner, Hombauer (CR83) 2003; 17 Yang, Lickteig, Estes (CR45) 1991; 11 Ogris, Du, Nelson (CR79) 1999; 274 Ruediger, Pham, Walter (CR47) 2001; 20 Alonso, Zaidi, Grundke-Iqbal (CR71) 1994; 91 Wei, Ashby, Moreno (CR25) 2001; 276 Goedert, Spillantini (CR62) 2006; 314 Riedel, Katis, Katou (CR53) 2006; 441 Janssens, Goris, van Hoof (CR15) 2005; 15 Bryant, Westphal, Wadzinski (CR74) 1999; 339 M. Goedert (18_CR62) 2006; 314 M. S. Gentry (18_CR78) 2005; 4 R. Ruediger (18_CR47) 2001; 20 E. Kremmer (18_CR44) 1997; 17 H. Xie (18_CR18) 1994; 269 Y. Xing (18_CR23) 2006; 127 C. Kamibayashi (18_CR58) 1994; 269 V. Janssens (18_CR60) 2003; 278 E. Ogris (18_CR26) 1997; 15 Y. Xing (18_CR81) 2008; 133 P. T. Cohen (18_CR9) 1997; 22 M. R. Groves (18_CR38) 1999; 96 A. Nicholls (18_CR92) 1991; 11 X. Li (18_CR59) 2002; 269 D. M. Virshup (18_CR12) 2000; 12 G. Walter (18_CR37) 1989; 86 I. Baere De (18_CR33) 1999; 38 P. Turowski (18_CR34) 1995; 129 R. Ruediger (18_CR42) 1992; 12 A. Alonso (18_CR8) 2004; 117 S. Kloeker (18_CR76) 1997; 327 E. Sontag (18_CR65) 1999; 274 U. S. Cho (18_CR41) 2007; 5 J. C. Venter (18_CR7) 2001; 291 S. Longin (18_CR80) 2004; 380 H. Xie (18_CR20) 1993; 268 T. Fellner (18_CR83) 2003; 17 Y. Chao (18_CR85) 2006; 23 S. Kins (18_CR68) 2001; 276 M. D. Weingarten (18_CR69) 1975; 72 V. Janssens (18_CR15) 2005; 15 T. Hunter (18_CR1) 1995; 80 Y. Xu (18_CR28) 2008; 31 K. H. Scheidtmann (18_CR46) 1991; 11 E. H. Fischer (18_CR2) 1955; 216 V. Janssens (18_CR11) 2001; 353 Y. Chen (18_CR40) 2007; 14 E. Conti (18_CR55) 1998; 94 M. Goedert (18_CR63) 1995; 65 J. Yang (18_CR88) 2007; 46 J. A. Lee (18_CR35) 2007; 282 C. G. Riedel (18_CR53) 2006; 441 P. J. Kraulis (18_CR93) 1991; 24 T. A. Graham (18_CR56) 2000; 103 Z. Tang (18_CR54) 2006; 10 C. Kamibayashi (18_CR57) 1992; 267 T. D. Prickett (18_CR91) 2004; 279 X. X. Yu (18_CR75) 2001; 12 M. Kong (18_CR30) 2004; 306 G. B. Witman (18_CR70) 1976; 73 J. Lee (18_CR21) 1993; 268 U. S. Cho (18_CR39) 2007; 445 J. Lee (18_CR17) 1996; 93 E. W. Sutherland Jr (18_CR3) 1955; 175 E. G. Krebs (18_CR4) 1956; 20 J. Chernoff (18_CR10) 1983; 258 M. Mumby (18_CR16) 2007; 130 H. Chung (18_CR29) 1999; 38 T. Ikehara (18_CR27) 2007; 354 A. C. Alonso (18_CR71) 1994; 91 T. S. Kitajima (18_CR52) 2006; 441 J. Wu (18_CR32) 2000; 19 E. Sontag (18_CR64) 1996; 17 M. Bennecib (18_CR67) 2000; 490 E. S. Lander (18_CR5) 2001; 409 K. Lechward (18_CR13) 2001; 48 B. A. Hemmings (18_CR36) 1990; 29 X. Cayla (18_CR89) 1990; 29 G. Drewes (18_CR72) 1993; 336 T. Tolstykh (18_CR24) 2000; 19 N. Leulliot (18_CR86) 2006; 23 18_CR31 S. S. Wang (18_CR48) 1998; 282 R. Ruediger (18_CR49) 2001; 20 C. Bialojan (18_CR50) 1988; 256 J. C. Bryant (18_CR74) 1999; 339 S. Longin (18_CR77) 2007; 282 S. A. Johnson (18_CR6) 2005; 2 Y. Xu (18_CR22) 2006; 127 C. MacKintosh (18_CR51) 1990; 264 C. X. Gong (18_CR73) 1994; 61 T. Ikehara (18_CR61) 2007; 354 M. C. Mumby (18_CR14) 1993; 73 H. Xie (18_CR19) 1994; 203 E. Ogris (18_CR79) 1999; 274 A. Magnusdottir (18_CR87) 2006; 281 H. Wei (18_CR25) 2001; 276 C. X. Gong (18_CR66) 2000; 275 S. Longin (18_CR82) 2008; 314 S. I. Yang (18_CR45) 1991; 11 H. Hombauer (18_CR84) 2007; 5 R. Ruediger (18_CR43) 1994; 68 C. Hoof van (18_CR90) 1994; 226 |
| References_xml | – volume: 130 start-page: 21 year: 2007 end-page: 24 ident: CR16 article-title: PP2A: unveiling a reluctant tumor suppressor publication-title: Cell doi: 10.1016/j.cell.2007.06.034 – volume: 11 start-page: 281 year: 1991 end-page: 296 ident: CR92 article-title: Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons publication-title: Proteins: Struct Funct Genet doi: 10.1002/prot.340110407 – volume: 291 start-page: 1304 year: 2001 end-page: 1351 ident: CR7 article-title: The sequence of the human genome publication-title: Science doi: 10.1126/science.1058040 – volume: 22 start-page: 245 year: 1997 end-page: 251 ident: CR9 article-title: Novel protein serine/threonine phosphatases: variety is the spice of life publication-title: Trends Biochem Sci doi: 10.1016/S0968-0004(97)01060-8 – volume: 19 start-page: 5682 year: 2000 end-page: 5691 ident: CR24 article-title: Carboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory B subunits publication-title: Embo J doi: 10.1093/emboj/19.21.5682 – volume: 11 start-page: 1988 year: 1991 end-page: 1995 ident: CR45 article-title: Control of protein phosphatase 2A by simian virus 40 small-t antigen publication-title: Mol Cell Biol doi: 10.1128/MCB.11.4.1988 – volume: 267 start-page: 21864 year: 1992 end-page: 21872 ident: CR57 article-title: Expression of the A subunit of protein phosphatase 2A and characterization of its interactions with the catalytic and regulatory subunits publication-title: J Biol Chem – volume: 380 start-page: 111 year: 2004 end-page: 119 ident: CR80 article-title: An inactive protein phosphatase 2A population is associated with methylesterase and can be re-activated by the phosphotyrosyl phosphatase activator publication-title: Biochem J doi: 10.1042/bj20031643 – volume: 409 start-page: 860 year: 2001 end-page: 921 ident: CR5 article-title: Initial sequencing and analysis of the human genome publication-title: Nature doi: 10.1038/35057062 – volume: 276 start-page: 38193 year: 2001 end-page: 38200 ident: CR68 article-title: Reduced protein phosphatase 2A activity induces hyperphosphorylation and altered compartmentalization of tau in transgenic mice publication-title: J Biol Chem – volume: 441 start-page: 53 year: 2006 end-page: 61 ident: CR53 article-title: Protein phosphatase 2A protects centromeric sister chromatid cohesion during meiosis I publication-title: Nature doi: 10.1038/nature04664 – volume: 490 start-page: 15 year: 2000 end-page: 22 ident: CR67 article-title: Role of protein phosphatase-2A and -1 in the regulation of GSK-3, cdk5 and cdc2 and the phosphorylation of tau in rat forebrain publication-title: FEBS Lett doi: 10.1016/S0014-5793(01)02127-5 – volume: 256 start-page: 283 year: 1988 end-page: 290 ident: CR50 article-title: Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics publication-title: Biochem J doi: 10.1042/bj2560283 – volume: 23 start-page: 413 year: 2006 end-page: 424 ident: CR86 article-title: Crystal structure of the PP2A phosphatase activator: implications for its PP2A-specific PPIase activity publication-title: Mol Cell doi: 10.1016/j.molcel.2006.07.008 – volume: 29 start-page: 658 year: 1990 end-page: 667 ident: CR89 article-title: Isolation and characterization of a tyrosyl phosphatase activator from rabbit skeletal muscle and oocytes publication-title: Biochemistry doi: 10.1021/bi00455a010 – volume: 268 start-page: 19192 year: 1993 end-page: 19195 ident: CR21 article-title: Protein phosphatase 2A catalytic subunit is methyl-esterified at its carboxyl terminus by a novel methyltransferase publication-title: J Biol Chem – volume: 38 start-page: 16539 year: 1999 end-page: 16547 ident: CR33 article-title: Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue publication-title: Biochemistry doi: 10.1021/bi991646a – volume: 281 start-page: 22434 year: 2006 end-page: 22438 ident: CR87 article-title: The crystal structure of a human PP2A phosphatase activator reveals a novel fold and highly conserved cleft implicated in protein-protein interactions publication-title: J Biol Chem doi: 10.1074/jbc.C600100200 – volume: 279 start-page: 38912 year: 2004 end-page: 38920 ident: CR91 article-title: Overlapping binding sites in protein phosphatase 2A for association with regulatory A and alpha-4 (mTap42) subunits publication-title: J Biol Chem doi: 10.1074/jbc.M401444200 – volume: 274 start-page: 14382 year: 1999 end-page: 14391 ident: CR79 article-title: A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A publication-title: J Biol Chem doi: 10.1074/jbc.274.20.14382 – volume: 65 start-page: 804 year: 1995 end-page: 807 ident: CR63 article-title: Protein phosphatase 2A is the major enzyme in brain that dephosphorylates tau protein phosphorylated by proline-directed protein kinases or cyclic AMP-dependent protein kinase publication-title: J Neurochem – volume: 275 start-page: 5535 year: 2000 end-page: 5544 ident: CR66 article-title: Phosphorylation of microtubule- associated protein tau is regulated by protein phosphatase 2A in mammalian brain. Implications for neurofibrillary degeneration in Alzheimer’s disease publication-title: J Biol Chem doi: 10.1074/jbc.275.8.5535 – volume: 11 start-page: 1996 year: 1991 end-page: 2003 ident: CR46 article-title: Dephosphorylation of simian virus 40 large-T antigen and p53 protein by protein phosphatase 2A: inhibition by small-t antigen publication-title: Mol Cell Biol doi: 10.1128/MCB.11.4.1996 – volume: 72 start-page: 1858 year: 1975 end-page: 1862 ident: CR69 article-title: A protein factor essential for microtubule assembly publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.72.5.1858 – volume: 38 start-page: 10371 year: 1999 end-page: 10376 ident: CR29 article-title: Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic subunit favors association with the alpha 4 subunit which promotes dephosphorylation of elongation factor-2 publication-title: Biochemistry doi: 10.1021/bi990902g – volume: 274 start-page: 25490 year: 1999 end-page: 25498 ident: CR65 article-title: Molecular interactions among protein phosphatase 2A, tau, and microtubules. Implications for the regulation of tau phosphorylation and the development of tauopathies publication-title: J Biol Chem doi: 10.1074/jbc.274.36.25490 – volume: 276 start-page: 1570 year: 2001 end-page: 1577 ident: CR25 article-title: Carboxymethylation of the PP2A catalytic subunit in is required for efficient interaction with the B-type subunits Cdc55p and Rts1p publication-title: J Biol Chem doi: 10.1074/jbc.M008694200 – volume: 10 start-page: 575 year: 2006 end-page: 585 ident: CR54 article-title: PP2A is required for centromeric localization of Sgo1 and proper chromosome segregation publication-title: Dev Cell doi: 10.1016/j.devcel.2006.03.010 – volume: 15 start-page: 911 year: 1997 end-page: 917 ident: CR26 article-title: Protein phosphatase 2A subunit assembly: the catalytic subunit carboxy terminus is important for binding cellular B subunit but not polyomavirus middle tumor antigen publication-title: Oncogene doi: 10.1038/sj.onc.1201259 – volume: 61 start-page: 765 year: 1994 end-page: 772 ident: CR73 article-title: Dephosphorylation of Alzheimer’s disease abnormally phosphorylated tau by protein phosphatase-2A publication-title: Neuroscience doi: 10.1016/0306-4522(94)90400-6 – volume: 269 start-page: 20139 year: 1994 end-page: 20148 ident: CR58 article-title: Comparison of heterotrimeric protein phosphatase 2A containing different B subunits publication-title: J Biol Chem – volume: 17 start-page: 1692 year: 1997 end-page: 1701 ident: CR44 article-title: Separation of PP2A core enzyme and holoenzyme with monoclonal antibodies against the regulatory A subunit: abundant expression of both forms in cells publication-title: Mol Cell Biol doi: 10.1128/MCB.17.3.1692 – volume: 306 start-page: 695 year: 2004 end-page: 698 ident: CR30 article-title: The PP2A-associated protein alpha4 is an essential inhibitor of apoptosis publication-title: Science doi: 10.1126/science.1100537 – volume: 4 start-page: 1029 year: 2005 end-page: 1040 ident: CR78 article-title: A novel assay for protein phosphatase 2A (PP2A) complexes reveals differential effects of covalent modifications on different Saccharomyces cerevisiae PP2A heterotrimers publication-title: Eukaryot Cell doi: 10.1128/EC.4.6.1029-1040.2005 – volume: 24 start-page: 946 year: 1991 end-page: 950 ident: CR93 article-title: Molscript: a program to produce both detailed and schematic plots of protein structures publication-title: J Appl Crystallogr doi: 10.1107/S0021889891004399 – volume: 17 start-page: 2138 year: 2003 end-page: 2150 ident: CR83 article-title: A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) publication-title: Genes Dev doi: 10.1101/gad.259903 – volume: 282 start-page: 284 year: 1998 end-page: 287 ident: CR48 article-title: Alterations of the PPP2R1B gene in human lung and colon cancer publication-title: Science doi: 10.1126/science.282.5387.284 – volume: 73 start-page: 673 year: 1993 end-page: 699 ident: CR14 article-title: Protein serine/threonine phosphatases: structure, regulation, and functions in cell growth publication-title: Physiol Rev – volume: 216 start-page: 121 year: 1955 end-page: 132 ident: CR2 article-title: Conversion of phosphorylase b to phosphorylase a in muscle extracts publication-title: J Biol Chem – volume: 314 start-page: 777 year: 2006 end-page: 781 ident: CR62 article-title: A century of Alzheimer’s disease publication-title: Science doi: 10.1126/science.1132814 – volume: 354 start-page: 1052 year: 2007 end-page: 1057 ident: CR27 article-title: Methylation of the C-terminal leucine residue of the PP2A catalytic subunit is unnecessary for the catalytic activity and the binding of regulatory subunit (PR55/B) publication-title: Biochem Biophys Res Commun doi: 10.1016/j.bbrc.2007.01.085 – volume: 127 start-page: 341 year: 2006 end-page: 353 ident: CR23 article-title: Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins publication-title: Cell doi: 10.1016/j.cell.2006.09.025 – volume: 96 start-page: 99 year: 1999 end-page: 110 ident: CR38 article-title: The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs publication-title: Cell doi: 10.1016/S0092-8674(00)80963-0 – volume: 23 start-page: 535 year: 2006 end-page: 546 ident: CR85 article-title: Structure and Mechanism of the Phosphotyrosyl Phosphatase Activator publication-title: Mol Cell doi: 10.1016/j.molcel.2006.07.027 – volume: 226 start-page: 899 year: 1994 end-page: 907 ident: CR90 article-title: The phosphotyrosyl phosphatase activator of protein phosphatase 2A. A novel purification method, immunological and enzymic characterization publication-title: Eur J Biochem doi: 10.1111/j.1432-1033.1994.00899.x – volume: 103 start-page: 885 year: 2000 end-page: 896 ident: CR56 article-title: Crystal structure of a beta-catenin/Tcf complex publication-title: Cell doi: 10.1016/S0092-8674(00)00192-6 – volume: 17 start-page: 1201 year: 1996 end-page: 1207 ident: CR64 article-title: Regulation of the phosphorylation state and microtubule-binding activity of Tau by protein phosphatase 2A publication-title: Neuron doi: 10.1016/S0896-6273(00)80250-0 – volume: 68 start-page: 123 year: 1994 end-page: 129 ident: CR43 article-title: Molecular model of the A subunit of protein phosphatase 2A: interaction with other subunits and tumor antigens publication-title: J Virol – volume: 20 start-page: 10 year: 2001 end-page: 15 ident: CR47 article-title: Disruption of protein phosphatase 2A subunit interaction in human cancers with mutations in the A alpha subunit gene publication-title: Oncogene doi: 10.1038/sj.onc.1204059 – volume: 5 start-page: e155 year: 2007 ident: CR84 article-title: Generation of active protein phosphatase 2A is coupled to holoenzyme assembly publication-title: PLoS Biol doi: 10.1371/journal.pbio.0050155 – volume: 15 start-page: 34 year: 2005 end-page: 41 ident: CR15 article-title: PP2A: the expected tumor suppressor publication-title: Curr Opin Genet Dev doi: 10.1016/j.gde.2004.12.004 – volume: 29 start-page: 3166 year: 1990 end-page: 3173 ident: CR36 article-title: alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure publication-title: Biochemistry doi: 10.1021/bi00465a002 – volume: 269 start-page: 546 year: 2002 end-page: 552 ident: CR59 article-title: Two conserved domains in regulatory B subunits mediate binding to the A subunit of protein phosphatase 2A publication-title: Eur J Biochem doi: 10.1046/j.0014-2956.2001.02680.x – volume: 48 start-page: 921 year: 2001 end-page: 933 ident: CR13 article-title: Protein phosphatase 2A: variety of forms and diversity of functions publication-title: Acta Biochim Pol – volume: 327 start-page: 481 issue: Pt2 year: 1997 end-page: 486 ident: CR76 article-title: Carboxymethylation of nuclear protein serine/threonine phosphatase X publication-title: Biochem J doi: 10.1042/bj3270481 – volume: 441 start-page: 46 year: 2006 end-page: 52 ident: CR52 article-title: Shugoshin collaborates with protein phosphatase 2A to protect cohesin publication-title: Nature doi: 10.1038/nature04663 – volume: 354 start-page: 1052 year: 2007 end-page: 1057 ident: CR61 article-title: Methylation of the C-terminal leucine residue of the PP2A catalytic subunit is unnecessary for the catalytic activity and the binding of regulatory subunit (PR55/B) publication-title: Biochem Biophys Res Commun doi: 10.1016/j.bbrc.2007.01.085 – volume: 12 start-page: 4872 year: 1992 end-page: 4882 ident: CR42 article-title: Identification of binding sites on the regulatory A subunit of protein phosphatase 2A for the catalytic C subunit and for tumor antigens of simian virus 40 and polyomavirus publication-title: Mol Cell Biol doi: 10.1128/MCB.12.11.4872 – volume: 14 start-page: 527 year: 2007 end-page: 534 ident: CR40 article-title: Structural and biochemical insights into the regulation of protein phosphatase 2A by small t antigen of SV40 publication-title: Nat Struct Mol Biol doi: 10.1038/nsmb1254 – volume: 203 start-page: 1710 year: 1994 end-page: 1715 ident: CR19 article-title: An enzymatic activity in bovine brain that catalyzes the reversal of the C-terminal methyl esterification of protein phosphatase 2A publication-title: Biochem Biophys Res Commun doi: 10.1006/bbrc.1994.2383 – volume: 268 start-page: 13364 year: 1993 end-page: 13371 ident: CR20 article-title: Methyl esterification of C-terminal leucine residues in cytosolic 36-kDa polypeptides of bovine brain. A novel eucaryotic protein carboxyl methylation reaction publication-title: J Biol Chem – volume: 117 start-page: 699 year: 2004 end-page: 711 ident: CR8 article-title: Protein tyrosine phosphatases in the human genome publication-title: Cell doi: 10.1016/j.cell.2004.05.018 – volume: 19 start-page: 5672 year: 2000 end-page: 5681 ident: CR32 article-title: Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits publication-title: Embo J doi: 10.1093/emboj/19.21.5672 – volume: 264 start-page: 187 year: 1990 end-page: 192 ident: CR51 article-title: Cyanobacterial micro-cystin- LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants publication-title: FEBS Lett doi: 10.1016/0014-5793(90)80245-E – volume: 314 start-page: 68 year: 2008 end-page: 81 ident: CR82 article-title: Spatial control of protein phosphatase 2A (de)methylation publication-title: Exp Cell Res doi: 10.1016/j.yexcr.2007.07.030 – volume: 12 start-page: 185 year: 2001 end-page: 199 ident: CR75 article-title: Methylation of the protein phosphatase 2A catalytic subunit is essential for association of Balpha regulatory subunit but not SG2NA, striatin, or polyomavirus middle tumor antigen publication-title: Mol Biol Cell doi: 10.1091/mbc.12.1.185 – volume: 175 start-page: 169 year: 1955 end-page: 170 ident: CR3 article-title: Inactivation and activation of liver phosphorylase publication-title: Nature doi: 10.1038/175169a0 – volume: 31 start-page: 873 year: 2008 end-page: 885 ident: CR28 article-title: Structure of a protein phosphatase 2A holoenzyme: insights into B55-mediated Tau dephosphorylation publication-title: Mol Cell doi: 10.1016/j.molcel.2008.08.006 – volume: 5 start-page: e202 year: 2007 ident: CR41 article-title: Structural basis of PP2A inhibition by small t antigen publication-title: PLoS Biol doi: 10.1371/journal.pbio.0050202 – volume: 269 start-page: 1981 year: 1994 end-page: 1984 ident: CR18 article-title: Protein phosphatase 2A is reversibly modified by methyl esterification at its C-terminal leucine residue in bovine brain publication-title: J Biol Chem – volume: 282 start-page: 30974 year: 2007 end-page: 30984 ident: CR35 article-title: Leucine carboxyl methyltransferase-1 is necessary for normal progression through mitosis in mammalian cells publication-title: J Biol Chem doi: 10.1074/jbc.M704861200 – volume: 86 start-page: 8669 year: 1989 end-page: 8672 ident: CR37 article-title: Molecular cloning and sequence of cDNA encoding polyoma medium tumor antigen-associated 61-kDa protein publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.86.22.8669 – volume: 129 start-page: 397 year: 1995 end-page: 410 ident: CR34 article-title: Differential methylation and altered conformation of cytoplasmic and nuclear forms of protein phosphatase 2A during cell cycle progression publication-title: J Cell Biol doi: 10.1083/jcb.129.2.397 – volume: 20 start-page: 1892 year: 2001 end-page: 1899 ident: CR49 article-title: Alterations in protein phosphatase 2A subunit interaction in human carcinomas of the lung and colon with mutations in the A beta subunit gene publication-title: Oncogene doi: 10.1038/sj.onc.1204279 – volume: 353 start-page: 417 year: 2001 end-page: 439 ident: CR11 article-title: Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling publication-title: Biochem J doi: 10.1042/bj3530417 – volume: 282 start-page: 26971 year: 2007 end-page: 26980 ident: CR77 article-title: Selection of protein phosphatase 2A regulatory subunits is mediated by the C terminus of the catalytic Subunit publication-title: J Biol Chem doi: 10.1074/jbc.M704059200 – volume: 339 start-page: 241 year: 1999 end-page: 246 ident: CR74 article-title: Methylated C-terminal leucine residue of PP2A catalytic subunit is important for binding of regulatory Balpha subunit publication-title: Biochem J doi: 10.1042/bj3390241 – volume: 20 start-page: 150 year: 1956 end-page: 157 ident: CR4 article-title: The phosphorylase b to a converting enzyme of rabbit skeletal muscle publication-title: Biochim Biophys Acta doi: 10.1016/0006-3002(56)90273-6 – ident: CR31 – volume: 2 start-page: 17 year: 2005 end-page: 25 ident: CR6 article-title: Kinomics: methods for deciphering the kinome publication-title: Nat Methods doi: 10.1038/nmeth731 – volume: 336 start-page: 425 year: 1993 end-page: 432 ident: CR72 article-title: Dephosphorylation of tau protein and Alzheimer paired helical filaments by calcineurin and phosphatase-2A publication-title: FEBS Lett doi: 10.1016/0014-5793(93)80850-T – volume: 93 start-page: 6043 year: 1996 end-page: 6047 ident: CR17 article-title: A specific protein carboxyl methylesterase that demethylates phosphoprotein phosphatase 2A in bovine brain publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.93.12.6043 – volume: 80 start-page: 225 year: 1995 end-page: 236 ident: CR1 article-title: Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling publication-title: Cell doi: 10.1016/0092-8674(95)90405-0 – volume: 73 start-page: 4070 year: 1976 end-page: 4074 ident: CR70 article-title: Tubulin requires tau for growth onto microtubule initiating sites publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.73.11.4070 – volume: 94 start-page: 193 year: 1998 end-page: 204 ident: CR55 article-title: Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha publication-title: Cell doi: 10.1016/S0092-8674(00)81419-1 – volume: 91 start-page: 5562 year: 1994 end-page: 5566 ident: CR71 article-title: Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.91.12.5562 – volume: 127 start-page: 1239 year: 2006 end-page: 1251 ident: CR22 article-title: Structure of the protein phosphatase 2A holoenzyme publication-title: Cell doi: 10.1016/j.cell.2006.11.033 – volume: 445 start-page: 53 year: 2007 end-page: 57 ident: CR39 article-title: Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme publication-title: Nature doi: 10.1038/nature05351 – volume: 46 start-page: 8807 year: 2007 end-page: 8815 ident: CR88 article-title: The structure of Tap42/alpha4 reveals a tetratricopeptide repeat-like fold and provides insights into PP2A regulation publication-title: Biochemistry doi: 10.1021/bi7007118 – volume: 133 start-page: 154 year: 2008 end-page: 163 ident: CR81 article-title: Structural mechanism of demethylation and inactivation of protein phosphatase 2A publication-title: Cell doi: 10.1016/j.cell.2008.02.041 – volume: 12 start-page: 180 year: 2000 end-page: 185 ident: CR12 article-title: Protein phosphatase 2A: a panoply of enzymes publication-title: Curr Opin Cell Biol doi: 10.1016/S0955-0674(99)00074-5 – volume: 278 start-page: 10697 year: 2003 end-page: 10706 ident: CR60 article-title: Identification and functional analysis of two Ca -binding EF-hand motifs in the B″/PR72 subunit of protein phosphatase 2A publication-title: J Biol Chem doi: 10.1074/jbc.M211717200 – volume: 258 start-page: 7852 year: 1983 end-page: 7857 ident: CR10 article-title: Characterization of a phosphotyrosyl protein phosphatase activity associated with a phosphoseryl protein phosphatase of Mr = 95,000 from bovine heart publication-title: J Biol Chem – volume: 31 start-page: 873 year: 2008 ident: 18_CR28 publication-title: Mol Cell doi: 10.1016/j.molcel.2008.08.006 – volume: 72 start-page: 1858 year: 1975 ident: 18_CR69 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.72.5.1858 – volume: 354 start-page: 1052 year: 2007 ident: 18_CR27 publication-title: Biochem Biophys Res Commun doi: 10.1016/j.bbrc.2007.01.085 – volume: 353 start-page: 417 year: 2001 ident: 18_CR11 publication-title: Biochem J doi: 10.1042/bj3530417 – volume: 269 start-page: 1981 year: 1994 ident: 18_CR18 publication-title: J Biol Chem doi: 10.1016/S0021-9258(17)42124-7 – volume: 441 start-page: 46 year: 2006 ident: 18_CR52 publication-title: Nature doi: 10.1038/nature04663 – volume: 409 start-page: 860 year: 2001 ident: 18_CR5 publication-title: Nature doi: 10.1038/35057062 – volume: 103 start-page: 885 year: 2000 ident: 18_CR56 publication-title: Cell doi: 10.1016/S0092-8674(00)00192-6 – volume: 20 start-page: 1892 year: 2001 ident: 18_CR49 publication-title: Oncogene doi: 10.1038/sj.onc.1204279 – volume: 17 start-page: 1201 year: 1996 ident: 18_CR64 publication-title: Neuron doi: 10.1016/S0896-6273(00)80250-0 – volume: 279 start-page: 38912 year: 2004 ident: 18_CR91 publication-title: J Biol Chem doi: 10.1074/jbc.M401444200 – volume: 291 start-page: 1304 year: 2001 ident: 18_CR7 publication-title: Science doi: 10.1126/science.1058040 – volume: 203 start-page: 1710 year: 1994 ident: 18_CR19 publication-title: Biochem Biophys Res Commun doi: 10.1006/bbrc.1994.2383 – volume: 327 start-page: 481 issue: Pt2 year: 1997 ident: 18_CR76 publication-title: Biochem J doi: 10.1042/bj3270481 – volume: 258 start-page: 7852 year: 1983 ident: 18_CR10 publication-title: J Biol Chem doi: 10.1016/S0021-9258(18)32257-9 – ident: 18_CR31 doi: 10.1126/scisignal.792001pe1 – volume: 94 start-page: 193 year: 1998 ident: 18_CR55 publication-title: Cell doi: 10.1016/S0092-8674(00)81419-1 – volume: 68 start-page: 123 year: 1994 ident: 18_CR43 publication-title: J Virol doi: 10.1128/JVI.68.1.123-129.1994 – volume: 5 start-page: e202 year: 2007 ident: 18_CR41 publication-title: PLoS Biol doi: 10.1371/journal.pbio.0050202 – volume: 127 start-page: 1239 year: 2006 ident: 18_CR22 publication-title: Cell doi: 10.1016/j.cell.2006.11.033 – volume: 127 start-page: 341 year: 2006 ident: 18_CR23 publication-title: Cell doi: 10.1016/j.cell.2006.09.025 – volume: 276 start-page: 38193 year: 2001 ident: 18_CR68 publication-title: J Biol Chem doi: 10.1074/jbc.M102621200 – volume: 216 start-page: 121 year: 1955 ident: 18_CR2 publication-title: J Biol Chem doi: 10.1016/S0021-9258(19)52289-X – volume: 5 start-page: e155 year: 2007 ident: 18_CR84 publication-title: PLoS Biol doi: 10.1371/journal.pbio.0050155 – volume: 336 start-page: 425 year: 1993 ident: 18_CR72 publication-title: FEBS Lett doi: 10.1016/0014-5793(93)80850-T – volume: 93 start-page: 6043 year: 1996 ident: 18_CR17 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.93.12.6043 – volume: 269 start-page: 546 year: 2002 ident: 18_CR59 publication-title: Eur J Biochem doi: 10.1046/j.0014-2956.2001.02680.x – volume: 278 start-page: 10697 year: 2003 ident: 18_CR60 publication-title: J Biol Chem doi: 10.1074/jbc.M211717200 – volume: 130 start-page: 21 year: 2007 ident: 18_CR16 publication-title: Cell doi: 10.1016/j.cell.2007.06.034 – volume: 11 start-page: 1996 year: 1991 ident: 18_CR46 publication-title: Mol Cell Biol doi: 10.1128/MCB.11.4.1996 – volume: 380 start-page: 111 year: 2004 ident: 18_CR80 publication-title: Biochem J doi: 10.1042/bj20031643 – volume: 86 start-page: 8669 year: 1989 ident: 18_CR37 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.86.22.8669 – volume: 91 start-page: 5562 year: 1994 ident: 18_CR71 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.91.12.5562 – volume: 23 start-page: 535 year: 2006 ident: 18_CR85 publication-title: Mol Cell doi: 10.1016/j.molcel.2006.07.027 – volume: 268 start-page: 13364 year: 1993 ident: 18_CR20 publication-title: J Biol Chem doi: 10.1016/S0021-9258(19)38660-0 – volume: 17 start-page: 1692 year: 1997 ident: 18_CR44 publication-title: Mol Cell Biol doi: 10.1128/MCB.17.3.1692 – volume: 38 start-page: 10371 year: 1999 ident: 18_CR29 publication-title: Biochemistry doi: 10.1021/bi990902g – volume: 22 start-page: 245 year: 1997 ident: 18_CR9 publication-title: Trends Biochem Sci doi: 10.1016/S0968-0004(97)01060-8 – volume: 275 start-page: 5535 year: 2000 ident: 18_CR66 publication-title: J Biol Chem doi: 10.1074/jbc.275.8.5535 – volume: 12 start-page: 180 year: 2000 ident: 18_CR12 publication-title: Curr Opin Cell Biol doi: 10.1016/S0955-0674(99)00074-5 – volume: 80 start-page: 225 year: 1995 ident: 18_CR1 publication-title: Cell doi: 10.1016/0092-8674(95)90405-0 – volume: 20 start-page: 150 year: 1956 ident: 18_CR4 publication-title: Biochim Biophys Acta doi: 10.1016/0006-3002(56)90273-6 – volume: 10 start-page: 575 year: 2006 ident: 18_CR54 publication-title: Dev Cell doi: 10.1016/j.devcel.2006.03.010 – volume: 274 start-page: 14382 year: 1999 ident: 18_CR79 publication-title: J Biol Chem doi: 10.1074/jbc.274.20.14382 – volume: 175 start-page: 169 year: 1955 ident: 18_CR3 publication-title: Nature doi: 10.1038/175169a0 – volume: 441 start-page: 53 year: 2006 ident: 18_CR53 publication-title: Nature doi: 10.1038/nature04664 – volume: 268 start-page: 19192 year: 1993 ident: 18_CR21 publication-title: J Biol Chem doi: 10.1016/S0021-9258(19)36497-X – volume: 129 start-page: 397 year: 1995 ident: 18_CR34 publication-title: J Cell Biol doi: 10.1083/jcb.129.2.397 – volume: 46 start-page: 8807 year: 2007 ident: 18_CR88 publication-title: Biochemistry doi: 10.1021/bi7007118 – volume: 12 start-page: 4872 year: 1992 ident: 18_CR42 publication-title: Mol Cell Biol doi: 10.1128/MCB.12.11.4872 – volume: 29 start-page: 658 year: 1990 ident: 18_CR89 publication-title: Biochemistry doi: 10.1021/bi00455a010 – volume: 282 start-page: 284 year: 1998 ident: 18_CR48 publication-title: Science doi: 10.1126/science.282.5387.284 – volume: 354 start-page: 1052 year: 2007 ident: 18_CR61 publication-title: Biochem Biophys Res Commun doi: 10.1016/j.bbrc.2007.01.085 – volume: 23 start-page: 413 year: 2006 ident: 18_CR86 publication-title: Mol Cell doi: 10.1016/j.molcel.2006.07.008 – volume: 267 start-page: 21864 year: 1992 ident: 18_CR57 publication-title: J Biol Chem doi: 10.1016/S0021-9258(19)36692-X – volume: 339 start-page: 241 year: 1999 ident: 18_CR74 publication-title: Biochem J doi: 10.1042/bj3390241 – volume: 281 start-page: 22434 year: 2006 ident: 18_CR87 publication-title: J Biol Chem doi: 10.1074/jbc.C600100200 – volume: 29 start-page: 3166 year: 1990 ident: 18_CR36 publication-title: Biochemistry doi: 10.1021/bi00465a002 – volume: 19 start-page: 5682 year: 2000 ident: 18_CR24 publication-title: Embo J doi: 10.1093/emboj/19.21.5682 – volume: 269 start-page: 20139 year: 1994 ident: 18_CR58 publication-title: J Biol Chem doi: 10.1016/S0021-9258(17)32138-5 – volume: 73 start-page: 4070 year: 1976 ident: 18_CR70 publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.73.11.4070 – volume: 4 start-page: 1029 year: 2005 ident: 18_CR78 publication-title: Eukaryot Cell doi: 10.1128/EC.4.6.1029-1040.2005 – volume: 306 start-page: 695 year: 2004 ident: 18_CR30 publication-title: Science doi: 10.1126/science.1100537 – volume: 256 start-page: 283 year: 1988 ident: 18_CR50 publication-title: Biochem J doi: 10.1042/bj2560283 – volume: 276 start-page: 1570 year: 2001 ident: 18_CR25 publication-title: J Biol Chem doi: 10.1074/jbc.M008694200 – volume: 38 start-page: 16539 year: 1999 ident: 18_CR33 publication-title: Biochemistry doi: 10.1021/bi991646a – volume: 96 start-page: 99 year: 1999 ident: 18_CR38 publication-title: Cell doi: 10.1016/S0092-8674(00)80963-0 – volume: 17 start-page: 2138 year: 2003 ident: 18_CR83 publication-title: Genes Dev doi: 10.1101/gad.259903 – volume: 73 start-page: 673 year: 1993 ident: 18_CR14 publication-title: Physiol Rev doi: 10.1152/physrev.1993.73.4.673 – volume: 12 start-page: 185 year: 2001 ident: 18_CR75 publication-title: Mol Biol Cell doi: 10.1091/mbc.12.1.185 – volume: 15 start-page: 34 year: 2005 ident: 18_CR15 publication-title: Curr Opin Genet Dev doi: 10.1016/j.gde.2004.12.004 – volume: 20 start-page: 10 year: 2001 ident: 18_CR47 publication-title: Oncogene doi: 10.1038/sj.onc.1204059 – volume: 490 start-page: 15 year: 2000 ident: 18_CR67 publication-title: FEBS Lett doi: 10.1016/S0014-5793(01)02127-5 – volume: 24 start-page: 946 year: 1991 ident: 18_CR93 publication-title: J Appl Crystallogr doi: 10.1107/S0021889891004399 – volume: 314 start-page: 68 year: 2008 ident: 18_CR82 publication-title: Exp Cell Res doi: 10.1016/j.yexcr.2007.07.030 – volume: 282 start-page: 30974 year: 2007 ident: 18_CR35 publication-title: J Biol Chem doi: 10.1074/jbc.M704861200 – volume: 314 start-page: 777 year: 2006 ident: 18_CR62 publication-title: Science doi: 10.1126/science.1132814 – volume: 274 start-page: 25490 year: 1999 ident: 18_CR65 publication-title: J Biol Chem doi: 10.1074/jbc.274.36.25490 – volume: 11 start-page: 1988 year: 1991 ident: 18_CR45 publication-title: Mol Cell Biol doi: 10.1128/MCB.11.4.1988 – volume: 19 start-page: 5672 year: 2000 ident: 18_CR32 publication-title: Embo J doi: 10.1093/emboj/19.21.5672 – volume: 133 start-page: 154 year: 2008 ident: 18_CR81 publication-title: Cell doi: 10.1016/j.cell.2008.02.041 – volume: 48 start-page: 921 year: 2001 ident: 18_CR13 publication-title: Acta Biochim Pol doi: 10.18388/abp.2001_3858 – volume: 65 start-page: 804 year: 1995 ident: 18_CR63 publication-title: J Neurochem doi: 10.1046/j.1471-4159.1995.65062804.x – volume: 226 start-page: 899 year: 1994 ident: 18_CR90 publication-title: Eur J Biochem doi: 10.1111/j.1432-1033.1994.00899.x – volume: 117 start-page: 699 year: 2004 ident: 18_CR8 publication-title: Cell doi: 10.1016/j.cell.2004.05.018 – volume: 445 start-page: 53 year: 2007 ident: 18_CR39 publication-title: Nature doi: 10.1038/nature05351 – volume: 15 start-page: 911 year: 1997 ident: 18_CR26 publication-title: Oncogene doi: 10.1038/sj.onc.1201259 – volume: 14 start-page: 527 year: 2007 ident: 18_CR40 publication-title: Nat Struct Mol Biol doi: 10.1038/nsmb1254 – volume: 282 start-page: 26971 year: 2007 ident: 18_CR77 publication-title: J Biol Chem doi: 10.1074/jbc.M704059200 – volume: 2 start-page: 17 year: 2005 ident: 18_CR6 publication-title: Nat Methods doi: 10.1038/nmeth731 – volume: 11 start-page: 281 year: 1991 ident: 18_CR92 publication-title: Proteins: Struct Funct Genet doi: 10.1002/prot.340110407 – volume: 61 start-page: 765 year: 1994 ident: 18_CR73 publication-title: Neuroscience doi: 10.1016/0306-4522(94)90400-6 – volume: 264 start-page: 187 year: 1990 ident: 18_CR51 publication-title: FEBS Lett doi: 10.1016/0014-5793(90)80245-E |
| SSID | ssj0000330277 ssj0039548 |
| Score | 2.0081878 |
| SecondaryResourceType | review_article |
| Snippet | Protein phosphatase 2A (PP2A) represents a conserved family of important protein serine/threonine phosphatases in species ranging from yeast to human. The PP2A... Issue Title: Special Issue: In Memoriam: Professor Ray Wu Protein phosphatase 2A (PP2A) represents a conserved family of important protein serine/threonine... |
| SourceID | proquest pubmed crossref springer chongqing |
| SourceType | Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 135 |
| SubjectTerms | Biomedical and Life Sciences Biopolymers Catalytic Domain Cofactors dephosphorylation In Memoriam: Professor Ray Wu Life Sciences mechanism Methylation Models, Molecular Molecular modelling Phosphoprotein phosphatase phosphorylation PP2A protein Protein Conformation Protein phosphatase Protein Phosphatase 2 - chemistry Protein Phosphatase 2 - metabolism Protein structure structure Threonine |
| SummonAdditionalLinks | – databaseName: ProQuest Central dbid: BENPR link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1La9wwEB7SDYVeSpO-3KSJDz21iFq2ZEuHUtKQEAoJJSSQm5EsqVtI7U13c8i_74z8WEqanAyWLYaZkWakT_oG4EPAIK2tkqwSRjCBMZCZUnoWHJdWKStt5Ok-PStPLsX3K3m1AafjXRg6VjnOiXGidl1De-SfMdRgZlFp9XVxw6hoFIGrYwUNM1RWcF8iw9gT2MyJGGsGm9-Ozn6cT5suWUEwXSy4UtI5RHT2EemM1-m4yCsW4YKMK1YQ38K8a3_eYBT5N27dS0bvAakxPh2_gOdDYpke9J6wBRu-3YanfanJu5eQEbr7217fpaZ1ac8ae_vHp11II1XDrzZdzLvlYm5WGNfS_OAVXB4fXRyesKFaAmuE5ivmafFjdKBbVMrqAhMhbjy-tZy7RvoGEzmnA_euwYeT3AbMDbiolM4dpnXFa5i1XevfQmqCylyeBVytSFGgtZyTWahcKQmLKUQCu5Ne6kXPikHkx4VQusx1AtmoqroZmMap4MV1veZIJk3XqGk6U6fqIoGP0y_rDh_8eGfUfz2MuGU9-QcK95_Wipj3dCVR9v2pGUcSwSOm9d3tsi6riNrmCbzpbbqWRKPTyFwm8Gk08rrrB8V896iYO_CsB6boZMwuzNDu_j3mNyu7N3jtX-Pz8Pk priority: 102 providerName: ProQuest |
| Title | Assembly and structure of protein phosphatase 2A |
| URI | http://lib.cqvip.com/qk/60112X/200902/1003489629.html https://link.springer.com/article/10.1007/s11427-009-0018-3 https://www.ncbi.nlm.nih.gov/pubmed/19277525 https://www.proquest.com/docview/224575798 https://www.proquest.com/docview/2787639754 https://www.proquest.com/docview/67013892 |
| Volume | 52 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| journalDatabaseRights | – providerCode: PRVBFR databaseName: Free Medical Journals customDbUrl: eissn: 1869-1889 dateEnd: 20091231 omitProxy: true ssIdentifier: ssj0039548 issn: 1674-7305 databaseCode: DIK dateStart: 19960101 isFulltext: true titleUrlDefault: http://www.freemedicaljournals.com providerName: Flying Publisher – providerCode: PRVPQU databaseName: Health & Medical Collection customDbUrl: eissn: 1869-1889 dateEnd: 20181231 omitProxy: true ssIdentifier: ssj0000330277 issn: 1674-7305 databaseCode: 7X7 dateStart: 19970201 isFulltext: true titleUrlDefault: https://search.proquest.com/healthcomplete providerName: ProQuest – providerCode: PRVPQU databaseName: ProQuest Central customDbUrl: http://www.proquest.com/pqcentral?accountid=15518 eissn: 1869-1889 dateEnd: 20181231 omitProxy: true ssIdentifier: ssj0000330277 issn: 1674-7305 databaseCode: BENPR dateStart: 19970201 isFulltext: true titleUrlDefault: https://www.proquest.com/central providerName: ProQuest – providerCode: PRVAVX databaseName: SpringerLink Journals (ICM) customDbUrl: eissn: 1869-1889 dateEnd: 20091231 omitProxy: true ssIdentifier: ssj0039548 issn: 1674-7305 databaseCode: U2A dateStart: 19970201 isFulltext: true titleUrlDefault: http://www.springerlink.com/journals/ providerName: Springer Nature |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1NT9wwEB0VEBKXCtpCA3TJgVMrS7Fjx_ZxqRatkEBVxUp7i-LYZpEg2XaXA_-ecT42qoBDT5ESxxnN2J7nPPsZ4NxjktZGCSJ5wQnHHEiKTDjiLRVGKSNMo9N9fZNNZ_xqLubdPu5Vv9q9pySbkXrY7EY5k6T5mZ9QRdIt2BFBzQsb8YyN--E3DQpmDcWJU2WNrbmnMt-qIggqLOrq7g9-7t_E9AptvmJKmwR0uQ8fO-QYj9tQH8AHV32C3fYsyefPkAT69tE8PMdFZeNWFvbpr4trHzdaDPdVvFzUq-WiWGPiitn4C8wuJ7c_p6Q7DoGUXNM1cWF2U2gftkkpo1NEOrRweNdQakvhSkRqVnvqbIkXK6jxmPwpl0ozi7gtPYTtqq7cV4gLrxLLEo_TEcFTDIe1IvHSZiKQLSmP4HTjl3zZyl4EdeOUK50xHUHSuyovOynxcKLFQz6IIAdP5-jpsGhO5WkE3zevDBW-W_ik93_edalVjlgDoaXUCo1746kM0npaCrT9bPMYu0rgP4rK1U-rPJMNLcsiOGpjOliimZSCiQh-9EEeqn7XzOP_Kn0Cey0TFZbCnMI2tgP3DQHN2oxgS87lCHYuJje_fo-a5vwCx-PpKQ |
| linkProvider | Springer Nature |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1Lb9QwEB6VVgguiGcJLdQHuIAs4sRO7EOFCrTa0naFUCv1ZpzYYZHaZNvdCu2P478xdh4rVMqtp0hxYo3GY8_Y3_gbgNcVOmlVSEFzbjjl6AOpyYSjlWWikLIQReDpPhpnoxP-5VScrsDv_i6MT6vs18SwUNum9Gfk79HVYGSRK_lhekF90SgPrvYVNExXWcFuB4ax7l7HgVv8wh3cbHv_Mw73myTZ2z3-NKJdkQFacsXm1Pk9g1GVv3wkC5Vi_MCMw7cFY7YUrsT4x6qKOVviwwpWVOhSGc-lSixGQyn2ewfWeMoV7v3WPu6Ov34bDnni1MOCocBL5vMecXL1yGq4vsd4ktMAT8RM0tTzO0ya-scFeq2__eS14PcacBv84d5DeNAFsmSntbxHsOLqx3C3LW25eAKxR5PPi7MFMbUlLUvt1aUjTUUCNcTPmkwnzWw6MXP0oyTZeQont6K4Z7BaN7V7DsRUMrZJXOHuSPAUrcNaEVe5zYTHflIeweagFz1tWTg82XLKpcoSFUHcq0qXHbO5L7BxppeczF7TGjXtc_ikTiN4O_yy7PDGjzd6_etuhs_0YI8o3D9ac8_0p3KBsm8NzThzPRxjatdczXSWB5Q4iWC9HdOlJAqNRiQignf9IC-7vlHMF_8VcwvujY6PDvXh_vhgA-63oJjPytmEVbQB9xJjq3nxqrNgAt9ve9L8Aa4JLW4 |
| linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1Lb9wgEB7loUa9VE2fbl4-9NQKxWAwcFylXSV9RD10pdyQMZCttLW33c0h_76DH2tFSQ49WTIYo5nB8-EPPgDeB0zS2ipBJC854ZgDSVkIT4KjwiplhW11ur9fFucz_uVKXPXnnK6G1e4DJdntaYgqTfX6dOnC6bjxjXImSftjP6OK5Nuwy6NOAgb0jE2GT3Ee1cxauhOnzRoje6A1H2oiiivMm_r6D776bpK6hzzvsaZtMpo-h2c9ikwnndv3YcvXL-BJd67k7UvIIpX72y5u07J2aScRe_PXp01IW12GX3W6nDer5bxcYxJL2eQVzKaff56dk_5oBFJxTdfEx5lOqUPcMqWszhH10NLjXUupq4SvELU5Hah3FV6coDYgEKBcKs0cYrj8NezUTe3fQloGlTmWBZyaCJ6ja5wTWZCuEJF4yXkChxu7mGUngRGVjnOudMF0AtlgKlP1suLxdIuFGQWRo6UNWjouoFMmT-DD5pGxwUcrHwz2N_3wWhnEHQgzpVbYuQdKZZTZ01Jg3082xThsIhdS1r65WZlCthQtS-BN59OxJ5pJKZhI4OPg5LHpR7v57r9qn8Dej09T8-3i8usBPO0IqrhC5hB2MCT8EeKctT1uY_kf2WLt0A |
| 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=Assembly+and+structure+of+protein+phosphatase+2A&rft.jtitle=Science+China.+Life+sciences&rft.au=Shi+YiGong&rft.date=2009-02-01&rft.pub=Springer+Nature+B.V&rft.issn=1674-7305&rft.eissn=1869-1889&rft.volume=52&rft.issue=2&rft.spage=135&rft.epage=146&rft_id=info:doi/10.1007%2Fs11427-009-0018-3&rft.externalDBID=NO_FULL_TEXT |
| thumbnail_s | http://utb.summon.serialssolutions.com/2.0.0/image/custom?url=http%3A%2F%2Fimage.cqvip.com%2Fvip1000%2Fqk%2F60112X%2F60112X.jpg |