SCF ubiquitin ligases in the maintenance of genome stability
In response to genotoxic stress, eukaryotic cells activate the DNA damage response (DDR), a series of pathways that coordinate cell cycle arrest and DNA repair to prevent deleterious mutations. In addition, cells possess checkpoint mechanisms that prevent aneuploidy by regulating the number of centr...
Saved in:
Published in | Trends in biochemical sciences (Amsterdam. Regular ed.) Vol. 37; no. 2; pp. 66 - 73 |
---|---|
Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
England
Elsevier Ltd
01.02.2012
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | In response to genotoxic stress, eukaryotic cells activate the DNA damage response (DDR), a series of pathways that coordinate cell cycle arrest and DNA repair to prevent deleterious mutations. In addition, cells possess checkpoint mechanisms that prevent aneuploidy by regulating the number of centrosomes and spindle assembly. Among these mechanisms, ubiquitin-mediated degradation of key proteins has an important role in the regulation of the DDR, centrosome duplication and chromosome segregation. This review discusses the functions of a group of ubiquitin ligases, the SCF (SKP1-CUL1-F-box protein) family, in the maintenance of genome stability. Given that general proteasome inhibitors are currently used as anticancer agents, a better understanding of the ubiquitylation of specific targets by specific ubiquitin ligases may result in improved cancer therapeutics. |
---|---|
AbstractList | In response to genotoxic stress, eukaryotic cells activate the DNA damage response (DDR), a series of pathways that coordinate cell cycle arrest and DNA repair to prevent deleterious mutations. In addition, cells possess checkpoint mechanisms that prevent aneuploidy by regulating the number of centrosomes and spindle assembly. Among these mechanisms, ubiquitin-mediated degradation of key proteins has an important role in the regulation of the DDR, centrosome duplication and chromosome segregation. This review discusses the functions of a group of ubiquitin ligases, the SCF (SKP1-CUL1-F-box protein) family, in the maintenance of genome stability. Given that general proteasome inhibitors are currently used as anticancer agents, a better understanding of the ubiquitylation of specific targets by specific ubiquitin ligases may result in improved cancer therapeutics. In response to genotoxic stress, eukaryotic cells activate the DNA damage response (DDR), a series of pathways that coordinate cell cycle arrest and DNA repair to prevent deleterious mutations. In addition, cells possess checkpoint mechanisms that prevent aneuploidy by regulating the number of centrosomes and the spindle assembly. Among these mechanisms, ubiquitin-mediated degradation of key proteins has an important role in the regulation of the DDR, centrosome duplication and chromosome segregation. This review discusses the functions of a group of ubiquitin ligases, the SCF (SKP1-CUL1-F-box protein) family, in the maintenance of genome stability. Given that general proteasome inhibitors are currently used as anticancer agents, a better understanding of the ubiquitylation of specific targets by specific ubiquitin ligases may result in improved cancer therapeutics. |
Author | Silverman, Joshua S. Pagano, Michele Skaar, Jeffrey R. |
AuthorAffiliation | 3 Department of Pathology, New York University School of Medicine, 522 First Avenue, Smilow Research Building 1107, New York, NY 10016, USA 2 NYU Cancer Institute, New York University School of Medicine, 522 First Avenue, Smilow Research Building 1107, New York, NY 10016, USA 1 Department of Radiation Oncology, New York University School of Medicine, 522 First Avenue, Smilow Research Building 1107, New York, NY 10016, USA 4 Howard Hughes Medical Institute |
AuthorAffiliation_xml | – name: 3 Department of Pathology, New York University School of Medicine, 522 First Avenue, Smilow Research Building 1107, New York, NY 10016, USA – name: 2 NYU Cancer Institute, New York University School of Medicine, 522 First Avenue, Smilow Research Building 1107, New York, NY 10016, USA – name: 4 Howard Hughes Medical Institute – name: 1 Department of Radiation Oncology, New York University School of Medicine, 522 First Avenue, Smilow Research Building 1107, New York, NY 10016, USA |
Author_xml | – sequence: 1 givenname: Joshua S. surname: Silverman fullname: Silverman, Joshua S. organization: Department of Radiation Oncology, New York University School of Medicine, 522 First Avenue, Smilow Research Building 1107, New York, NY 10016, USA – sequence: 2 givenname: Jeffrey R. surname: Skaar fullname: Skaar, Jeffrey R. organization: NYU Cancer Institute, New York University School of Medicine, 522 First Avenue, Smilow Research Building 1107, New York, NY 10016, USA – sequence: 3 givenname: Michele surname: Pagano fullname: Pagano, Michele email: Michele.pagano@nyumc.org organization: NYU Cancer Institute, New York University School of Medicine, 522 First Avenue, Smilow Research Building 1107, New York, NY 10016, USA |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/22099186$$D View this record in MEDLINE/PubMed |
BookMark | eNp9kc1q3DAUhUVJaSZpX6CL1rtm46mufm0IgTI0bSHQRZq1kO3riQZbSiQ5kLevhklCu8lGEkffPRzpnJAjHzwS8hHoGiior7t1dl1aMwpQhDWl4g1ZAVesFpypI7KirWpqWvRjcpLSjlKQWst35Jgx2rbQqBU5v95cVkvn7heXna8mt7UJU1WO-Rar2Tqf0VvfYxXGaos-zFilbDs3ufz4nrwd7ZTww9N-Sm4uv__Z_Kyvfv_4tfl2VfcSINdKtKAslJwIg7YaKWvQyo5zqmEYGxi7lnWirAr5IJTmI5OsZ1JIO9gB-Sm5OPjeLd2MQ48-RzuZu-hmGx9NsM78f-PdrdmGB8OZbqRQxeDLk0EM9wumbGaXepwm6zEsybQMBBMgm0KevUpCyU65kkIUlB3QPoaUIo4vgYCafUFmZ_YFmX1Be60UUYY-_fuUl5HnRgrw-QCMNhi7jS6Zm-vioEqPFJjWhTg_EFi-_MFhNKl3WCoaXMQ-myG41xL8BVJKrHM |
CitedBy_id | crossref_primary_10_1016_j_clinsp_2024_100365 crossref_primary_10_1074_mcp_R112_021154 crossref_primary_10_1038_onc_2017_277 crossref_primary_10_1074_jbc_M112_426882 crossref_primary_10_4161_cc_23408 crossref_primary_10_1128_MCB_00095_18 crossref_primary_10_4161_cc_24854 crossref_primary_10_1016_j_bbamcr_2013_02_028 crossref_primary_10_1016_j_celrep_2016_03_083 crossref_primary_10_1093_nar_gkz058 crossref_primary_10_1016_j_semcdb_2020_04_021 crossref_primary_10_3389_fcell_2022_859582 crossref_primary_10_1126_scisignal_aak9660 crossref_primary_10_1021_cr400585q crossref_primary_10_1097_MOH_0000000000000156 crossref_primary_10_1016_j_yexcr_2020_112300 crossref_primary_10_2147_COPD_S311222 crossref_primary_10_1038_s41419_020_02755_9 crossref_primary_10_1080_14728222_2018_1410140 crossref_primary_10_1186_s12967_015_0570_5 crossref_primary_10_1016_j_bbrc_2018_10_179 crossref_primary_10_1091_mbc_e12_07_0548 crossref_primary_10_4161_cc_24231 crossref_primary_10_1016_j_semcdb_2012_02_004 crossref_primary_10_3390_ijms23010084 crossref_primary_10_1007_s10689_021_00244_2 crossref_primary_10_1038_s41389_020_0235_y crossref_primary_10_1016_j_cub_2013_04_032 crossref_primary_10_18632_aging_204780 crossref_primary_10_1016_j_ceb_2013_07_004 crossref_primary_10_1038_cr_2013_44 crossref_primary_10_1038_s10038_024_01255_4 crossref_primary_10_3390_biom12020229 crossref_primary_10_1038_s41380_023_02379_3 crossref_primary_10_1128_MCB_00706_13 crossref_primary_10_1091_mbc_E19_12_0725 crossref_primary_10_1038_s41586_022_04789_9 crossref_primary_10_1038_s41431_018_0292_2 crossref_primary_10_1016_j_mam_2012_09_001 crossref_primary_10_1111_febs_15828 crossref_primary_10_1016_j_ijbiomac_2021_08_195 crossref_primary_10_3390_biom5020590 crossref_primary_10_1016_j_cell_2020_08_034 crossref_primary_10_1371_journal_pone_0101844 crossref_primary_10_1016_j_cellimm_2019_02_004 crossref_primary_10_1593_neo_12580 crossref_primary_10_3390_genes14030615 crossref_primary_10_1016_j_abb_2022_109501 crossref_primary_10_1016_j_devcel_2017_06_010 crossref_primary_10_1038_srep41626 crossref_primary_10_1074_jbc_M113_475707 crossref_primary_10_1371_journal_pone_0057530 crossref_primary_10_1016_j_febslet_2012_04_038 crossref_primary_10_1128_MCB_00904_12 crossref_primary_10_1371_journal_pone_0147096 crossref_primary_10_1093_hmg_ddab265 crossref_primary_10_1074_jbc_M116_772475 crossref_primary_10_1093_nar_gku876 crossref_primary_10_1007_s10495_013_0897_4 crossref_primary_10_1016_j_semcancer_2015_09_008 crossref_primary_10_1016_j_tcb_2012_10_011 crossref_primary_10_1093_nar_gkv325 crossref_primary_10_1128_JVI_02501_13 crossref_primary_10_3390_cancers12030531 crossref_primary_10_1016_j_bbrc_2018_03_085 crossref_primary_10_1016_j_mcpro_2023_100695 crossref_primary_10_1016_j_aanat_2024_152224 crossref_primary_10_1038_s41467_023_39374_9 crossref_primary_10_1021_pr400291p crossref_primary_10_1111_imr_12236 crossref_primary_10_1016_j_molcel_2013_03_023 crossref_primary_10_1038_srep05573 crossref_primary_10_1038_nature14978 |
Cites_doi | 10.1038/nature02082 10.1371/journal.pone.0000128 10.1126/science.1160462 10.1038/nbt.1646 10.1074/jbc.M509855200 10.1016/j.febslet.2011.05.056 10.1016/j.molcel.2006.06.013 10.1128/MCB.06570-11 10.1002/jcp.21791 10.1186/1471-2091-8-S1-S9 10.2174/156800911794519734 10.1074/jbc.M110.111518 10.4161/cc.9.3.10513 10.1016/j.molcel.2010.09.019 10.1073/pnas.0501873102 10.1038/35077232 10.1016/S0092-8674(00)00010-6 10.1016/j.semcdb.2011.03.002 10.1016/j.febslet.2010.05.031 10.1016/S1534-5807(03)00154-0 10.1073/pnas.0913813107 10.1016/j.molcel.2009.06.030 10.1016/j.ccr.2008.05.017 10.1007/1-4020-3764-3_14 10.1158/0008-5472.CAN-09-1284 10.1146/annurev.biochem.67.1.425 10.1016/j.ccr.2010.06.015 10.1038/onc.2010.584 10.1242/jcs.068502 10.1128/MCB.05733-11 10.1038/nrm1471 10.1073/pnas.0812256106 10.1016/j.molcel.2006.06.016 10.1128/MCB.22.23.8375-8387.2002 10.1038/nature08467 10.1016/j.cub.2004.09.083 10.1083/jcb.200712027 10.1038/nature07185 10.1016/j.cell.2008.05.043 10.1016/j.molcel.2005.07.019 10.1016/j.jhep.2010.06.009 10.1016/j.cell.2004.06.023 10.1038/nrc1011 10.1083/jcb.200808049 10.1038/nature08011 10.1101/gad.914401 10.1038/nrm2163 10.1073/pnas.0307700101 10.1038/ncb2282 10.1101/gad.1255304 10.1038/nrc2396 10.4161/cc.9.2.10445 10.1074/jbc.M802474200 10.1101/gad.13.17.2242 10.1038/nature07884 10.1101/gad.2021311 10.1016/j.cub.2008.11.037 10.1016/j.ceb.2009.08.004 10.1158/0008-5472.CAN-09-0869 10.1101/gad.8.14.1627 10.1038/nature06780 10.1182/blood-2010-03-272567 10.1038/onc.2010.96 10.1038/ncb1320 10.1038/nature09140 10.1038/nrm1547 10.1073/pnas.0610856104 10.1016/j.molcel.2006.09.007 10.1038/sj.onc.1208278 10.1126/science.1160489 10.1016/j.cub.2006.08.026 10.1111/j.1349-7006.2009.01178.x 10.1126/science.1140321 10.1007/978-1-4419-6199-0_6 10.1038/nature06641 10.1091/mbc.e09-01-0008 10.1101/gad.1157503 10.4161/cc.10.7.15249 10.1128/MCB.01085-08 10.1038/nbt.1645 10.1146/annurev.med.50.1.57 10.1038/ncb1969 10.1146/annurev.biochem.78.101807.093809 10.4161/cc.7.19.6775 |
ContentType | Journal Article |
Copyright | 2011 Elsevier Ltd Copyright © 2011 Elsevier Ltd. All rights reserved. 2011 Elsevier Ltd. All rights reserved. 2011 |
Copyright_xml | – notice: 2011 Elsevier Ltd – notice: Copyright © 2011 Elsevier Ltd. All rights reserved. – notice: 2011 Elsevier Ltd. All rights reserved. 2011 |
DBID | FBQ CGR CUY CVF ECM EIF NPM AAYXX CITATION 8FD FR3 P64 RC3 7X8 5PM |
DOI | 10.1016/j.tibs.2011.10.004 |
DatabaseName | AGRIS Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef Technology Research Database Engineering Research Database Biotechnology and BioEngineering Abstracts Genetics Abstracts MEDLINE - Academic PubMed Central (Full Participant titles) |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef Genetics Abstracts Engineering Research Database Technology Research Database Biotechnology and BioEngineering Abstracts MEDLINE - Academic |
DatabaseTitleList | Genetics Abstracts 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: FBQ name: AGRIS url: http://www.fao.org/agris/Centre.asp?Menu_1ID=DB&Menu_2ID=DB1&Language=EN&Content=http://www.fao.org/agris/search?Language=EN sourceTypes: Publisher |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Biology |
EISSN | 1362-4326 0968-0004 |
EndPage | 73 |
ExternalDocumentID | 10_1016_j_tibs_2011_10_004 22099186 US201600001277 S0968000411001733 |
Genre | Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural |
GrantInformation_xml | – fundername: NIGMS NIH HHS grantid: R01 GM057587-11 – fundername: NCI NIH HHS grantid: R37-CA076584 – fundername: NCI NIH HHS grantid: R37 CA076584 – fundername: NCI NIH HHS grantid: R37 CA076584-12 – fundername: NIGMS NIH HHS grantid: R01 GM057587-13 – fundername: NIGMS NIH HHS grantid: R01 GM057587 – fundername: NCI NIH HHS grantid: R21 CA125173 – fundername: NIGMS NIH HHS grantid: R01 GM057587-12 – fundername: NCI NIH HHS grantid: R21-CA161108 – fundername: NCI NIH HHS grantid: R21 CA161108 – fundername: National Cancer Institute : NCI grantid: R37 CA076584-13 || CA – fundername: National Institute of General Medical Sciences : NIGMS grantid: R01 GM057587-12 || GM – fundername: National Cancer Institute : NCI grantid: R21 CA125173-01 || CA – fundername: National Cancer Institute : NCI grantid: R37 CA076584-12 || CA – fundername: National Institute of General Medical Sciences : NIGMS grantid: R01 GM057587-11 || GM – fundername: National Institute of General Medical Sciences : NIGMS grantid: R01 GM057587-13 || GM |
GroupedDBID | --- --K --M -DZ -~X .55 .GJ .~1 0R~ 123 1B1 1CY 1RT 1~. 1~5 29Q 3EH 3O- 4.4 457 4G. 53G 5VS 7-5 71M 85S 8P~ 9JM 9M8 AABNK AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AAXUO ABFNM ABFRF ABGSF ABJNI ABLJU ABMAC ABOCM ABUDA ABXDB ABYKQ ACDAQ ACGFO ACGFS ACGOD ACKIV ACNCT ACPRK ACRLP ADBBV ADEZE ADUVX AEBSH AEFWE AEHWI AEKER AENEX AFKWA AFRAH AFTJW AFXIZ AGHFR AGRDE AGUBO AGYEJ AHHHB AHPSJ AIEXJ AIKHN AITUG AJBFU AJOXV ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ASPBG AVWKF AXJTR AZFZN BKOJK BLXMC CS3 D0L DOVZS DU5 EBS EFJIC EFLBG EJD EO8 EO9 EP2 EP3 F5P FA8 FDB FEDTE FGOYB FIRID FNPLU FYGXN G-2 G-Q GBLVA HLW HVGLF HZ~ H~9 IH2 IHE J1W KOM LX3 M41 MO0 MVM N9A O-L O9- OAUVE OHT OZT P-8 P-9 P2P PC. PQQKQ Q38 R2- RIG RNS ROL RPZ RXW SBG SCC SDF SDG SDP SES SEW SPCBC SSU SSZ T5K TAE UQL WUQ X7M XFK XPP Y6R ZCA ZMT ~G- ABPIF ABPTK AEQTP FBQ AAHBH AAMRU AAXKI ADVLN AKRWK CGR CUY CVF ECM EIF NPM AAYXX CITATION 8FD FR3 P64 RC3 7X8 5PM |
ID | FETCH-LOGICAL-c511t-64916a1201e1d7a7e028ea5b33071df81fb92b4fb96e3d4673f252c2545adade3 |
IEDL.DBID | AIKHN |
ISSN | 0968-0004 |
IngestDate | Tue Sep 17 21:21:49 EDT 2024 Sat Aug 17 00:34:47 EDT 2024 Fri Aug 16 11:57:59 EDT 2024 Thu Sep 26 17:14:47 EDT 2024 Sat Sep 28 07:58:31 EDT 2024 Wed Dec 27 19:13:18 EST 2023 Fri Feb 23 02:16:41 EST 2024 |
IsDoiOpenAccess | false |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 2 |
Language | English |
License | Copyright © 2011 Elsevier Ltd. All rights reserved. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c511t-64916a1201e1d7a7e028ea5b33071df81fb92b4fb96e3d4673f252c2545adade3 |
Notes | http://dx.doi.org/10.1016/j.tibs.2011.10.004 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
OpenAccessLink | https://europepmc.org/articles/pmc3278546?pdf=render |
PMID | 22099186 |
PQID | 1028036544 |
PQPubID | 23462 |
PageCount | 8 |
ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_3278546 proquest_miscellaneous_921424158 proquest_miscellaneous_1028036544 crossref_primary_10_1016_j_tibs_2011_10_004 pubmed_primary_22099186 fao_agris_US201600001277 elsevier_sciencedirect_doi_10_1016_j_tibs_2011_10_004 |
PublicationCentury | 2000 |
PublicationDate | 2012-02-01 |
PublicationDateYYYYMMDD | 2012-02-01 |
PublicationDate_xml | – month: 02 year: 2012 text: 2012-02-01 day: 01 |
PublicationDecade | 2010 |
PublicationPlace | England |
PublicationPlace_xml | – name: England |
PublicationTitle | Trends in biochemical sciences (Amsterdam. Regular ed.) |
PublicationTitleAlternate | Trends Biochem Sci |
PublicationYear | 2012 |
Publisher | Elsevier Ltd |
Publisher_xml | – name: Elsevier Ltd |
References | Guardavaccaro (bib0360) 2008; 452 Bekker-Jensen, Mailand (bib0370) 2011; 585 Melixetian (bib0150) 2009; 11 Pawar (bib0220) 2010; 107 (2011) Genetic reevaluation of the role of F-box proteins in cyclin D1 degradation. Zimmerman, Erikson (bib0145) 2007; 104 Zhang (bib0300) 2009; 35 Lingle (bib0065) 2005; 570 Milhollen (bib0405) 2010; 116 Cunha-Ferreira (bib0345) 2009; 19 Okabe (bib0215) 2006; 1 Busino (bib0115) 2003; 426 Piva (bib0315) 2002; 22 Zhang (bib0295) 2005; 19 Puklowski (bib0325) 2011; 13 Skaar, Pagano (bib0095) 2009; 21 Inuzuka (bib0175) 2010; 18 Watanabe (bib0275) 2004; 101 Agami, Bernards (bib0200) 2000; 102 Santra (bib0225) 2009; 459 Fang, Zhang (bib0055) 2011; 22 Guderian (bib0350) 2010; 123 D’Angiolella (bib0320) 2010; 466 Westbrook (bib0365) 2008; 452 Derheimer, Kastan (bib0045) 2010; 584 Pontano (bib0255) 2008; 28 Jia, Sun (bib0400) 2011; 11 Orlicky (bib0415) 2010; 28 Barbash (bib0205) 2008; 14 Li, Hao (bib0240) 2010; 285 Macurek (bib0260) 2008; 455 Guardavaccaro (bib0355) 2003; 4 Jin (bib0105) 2004; 18 Barbash (bib0235) 2011; 30 Musacchio, Salmon (bib0050) 2007; 8 Cardozo, Pagano (bib0100) 2004; 5 Sorensen (bib0155) 2010; 9 Hershko, Ciechanover (bib0075) 1998; 67 Korzeniewski (bib0335) 2009; 69 Welcker (bib0390) 2004; 14 Honaker, Piwnica-Worms (bib0135) 2010; 29 Mamely (bib0285) 2006; 16 Petroski, Deshaies (bib0090) 2005; 6 Tanaka, Hirota (bib0060) 2009; 100 Bakkenist, Kastan (bib0040) 2004; 118 Myer (bib0140) 2005; 24 Lukas (bib0195) 1994; 9 Abraham (bib0020) 2001; 15 Bassermann (bib0265) 2008; 134 Merry (bib0305) 2010; 9 Cardozo, Pagano (bib0410) 2007; 8 Kanie, T. Jin (bib0120) 2003; 17 Jin (bib0130) 2008; 283 Cheng, Chen (bib0180) 2011; 10 Kanemori (bib0165) 2005; 102 Kim, Diehl (bib0185) 2009; 220 Seki (bib0270) 2008; 181 Yen, Elledge (bib0380) 2008; 322 Aghajan (bib0420) 2010; 28 Freed (bib0310) 1999; 13 Lin (bib0210) 2006; 24 Peschiaroli (bib0280) 2006; 23 Duensing, Duensing (bib0070) 2010; 676 Pagano (bib0190) 1994; 8 Soucy (bib0395) 2009; 458 Mailand (bib0290) 2006; 23 Shiloh (bib0025) 2003; 3 Barbash, Diehl (bib0230) 2008; 7 Jackson, Bartek (bib0005) 2009; 461 Hoare (bib0015) 2010; 53 Ciccia, Elledge (bib0035) 2010; 40 Uchida (bib0160) 2009; 69 Yen (bib0385) 2008; 322 Polo, Jackson (bib0030) 2011; 25 Matsuoka (bib0375) 2007; 316 Frescas, Pagano (bib0110) 2008; 8 Lee (bib0245) 2006; 281 Rogers (bib0340) 2009; 184 Vaites (bib0250) 2011; 31 Schwartz, Ciechanover (bib0080) 1999; 50 Xia (bib0170) 2009; 106 Deshaies, Joazeiro (bib0085) 2009; 78 Isoda (bib0125) 2009; 20 Habedanck (bib0330) 2005; 7 Hoeijmakers (bib0010) 2001; 411 18809569 - Mol Cell Biol. 2008 Dec;28(23):7245-58 20965415 - Mol Cell. 2010 Oct 22;40(2):179-204 17426725 - Nat Rev Mol Cell Biol. 2007 May;8(5):379-93 15498494 - Curr Biol. 2004 Oct 26;14(20):1852-7 14681206 - Genes Dev. 2003 Dec 15;17(24):3062-74 16275645 - J Biol Chem. 2006 Jan 13;281(2):759-68 20708156 - Cancer Cell. 2010 Aug 9;18(2):147-59 17264206 - Proc Natl Acad Sci U S A. 2007 Feb 6;104(6):1847-52 19638579 - Cancer Res. 2009 Aug 15;69(16):6438-44 16934469 - Curr Biol. 2006 Oct 10;16(19):1950-5 19432891 - Cancer Sci. 2009 Jul;100(7):1158-65 16885022 - Mol Cell. 2006 Aug 4;23(3):319-29 19360080 - Nature. 2009 Apr 9;458(7239):732-6 20181953 - J Biol Chem. 2010 Apr 30;285(18):13896-906 20581845 - Nat Biotechnol. 2010 Jul;28(7):738-42 10929713 - Cell. 2000 Jul 7;102(1):55-66 20739078 - J Hepatol. 2010 Nov;53(5):950-61 11544175 - Genes Dev. 2001 Sep 1;15(17):2177-96 18047746 - BMC Biochem. 2007;8 Suppl 1:S9 21386656 - Cell Cycle. 2011 Apr 1;10(7):1162-6 7958844 - Genes Dev. 1994 Jul 15;8(14):1627-39 21725316 - Nat Cell Biol. 2011 Aug;13(8):1004-9 12612651 - Nat Rev Cancer. 2003 Mar;3(3):155-68 19679553 - Cancer Res. 2009 Aug 15;69(16):6668-75 15688063 - Nat Rev Mol Cell Biol. 2005 Jan;6(1):9-20 21911473 - Mol Cell Biol. 2011 Nov;31(22):4513-23 12417738 - Mol Cell Biol. 2002 Dec;22(23):8375-87 8108113 - Oncogene. 1994 Mar;9(3):707-18 15640846 - Oncogene. 2005 Jan 10;24(2):299-305 17205132 - PLoS One. 2006;1:e128 17525332 - Science. 2007 May 25;316(5828):1160-6 17081987 - Mol Cell. 2006 Nov 3;24(3):355-66 18988847 - Science. 2008 Nov 7;322(5903):918-23 21363960 - Genes Dev. 2011 Mar 1;25(5):409-33 19412162 - Nature. 2009 Jun 4;459(7247):722-5 20581844 - Nat Biotechnol. 2010 Jul;28(7):733-7 21247385 - Curr Cancer Drug Targets. 2011 Mar;11(3):347-56 15520277 - Genes Dev. 2004 Nov 1;18(21):2573-80 18354482 - Nature. 2008 Mar 20;452(7185):365-9 19415697 - J Cell Physiol. 2009 Aug;220(2):292-6 20525923 - Blood. 2010 Sep 2;116(9):1515-23 19171756 - J Cell Biol. 2009 Jan 26;184(2):225-39 20023404 - Cell Cycle. 2010 Jan 15;9(2):279-83 19489725 - Annu Rev Biochem. 2009;78:399-434 19716789 - Mol Cell. 2009 Aug 28;35(4):442-53 14603323 - Nature. 2003 Nov 6;426(6962):87-91 21664912 - FEBS Lett. 2011 Sep 16;585(18):2914-9 18818515 - Cell Cycle. 2008 Oct;7(19):2983-6 20439707 - Proc Natl Acad Sci U S A. 2010 May 18;107(20):9210-5 16244668 - Nat Cell Biol. 2005 Nov;7(11):1140-6 19244340 - Mol Biol Cell. 2009 Apr;20(8):2186-95 15340381 - Nat Rev Mol Cell Biol. 2004 Sep;5(9):739-51 18727509 - Adv Exp Med Biol. 2005;570:393-421 20596027 - Nature. 2010 Jul 1;466(7302):138-42 18500245 - Nat Rev Cancer. 2008 Jun;8(6):438-49 19084407 - Curr Biol. 2009 Jan 13;19(1):43-9 20580718 - FEBS Lett. 2010 Sep 10;584(17):3675-81 19847258 - Nature. 2009 Oct 22;461(7267):1071-8 18662541 - Cell. 2008 Jul 25;134(2):256-67 19196987 - Proc Natl Acad Sci U S A. 2009 Feb 24;106(8):2629-34 15845771 - Proc Natl Acad Sci U S A. 2005 May 3;102(18):6279-84 16137618 - Mol Cell. 2005 Sep 2;19(5):607-18 18598945 - Cancer Cell. 2008 Jul 8;14(1):68-78 10485847 - Genes Dev. 1999 Sep 1;13(17):2242-57 20516151 - J Cell Sci. 2010 Jul 1;123(Pt 13):2163-9 16885021 - Mol Cell. 2006 Aug 4;23(3):307-18 20348946 - Oncogene. 2010 Jun 10;29(23):3324-34 12791266 - Dev Cell. 2003 Jun;4(6):799-812 11357144 - Nature. 2001 May 17;411(6835):366-74 19775879 - Curr Opin Cell Biol. 2009 Dec;21(6):816-24 15070733 - Proc Natl Acad Sci U S A. 2004 Mar 30;101(13):4419-24 18378770 - J Cell Biol. 2008 Apr 7;181(1):65-78 19734889 - Nat Cell Biol. 2009 Oct;11(10):1247-53 20687471 - Adv Exp Med Biol. 2010;676:93-103 18615013 - Nature. 2008 Sep 4;455(7209):119-23 20090422 - Cell Cycle. 2010 Feb 1;9(3):450-5 21392584 - Semin Cell Dev Biol. 2011 Aug;22(6):595-601 18988848 - Science. 2008 Nov 7;322(5903):923-9 21242966 - Oncogene. 2011 Apr 28;30(17):1995-2002 15242640 - Cell. 2004 Jul 9;118(1):9-17 18354483 - Nature. 2008 Mar 20;452(7185):370-4 18480045 - J Biol Chem. 2008 Jul 11;283(28):19322-8 10073263 - Annu Rev Med. 1999;50:57-74 9759494 - Annu Rev Biochem. 1998;67:425-79 Rogers (10.1016/j.tibs.2011.10.004_bib0340) 2009; 184 Westbrook (10.1016/j.tibs.2011.10.004_bib0365) 2008; 452 Pagano (10.1016/j.tibs.2011.10.004_bib0190) 1994; 8 Matsuoka (10.1016/j.tibs.2011.10.004_bib0375) 2007; 316 Hoare (10.1016/j.tibs.2011.10.004_bib0015) 2010; 53 Ciccia (10.1016/j.tibs.2011.10.004_bib0035) 2010; 40 Jackson (10.1016/j.tibs.2011.10.004_bib0005) 2009; 461 Lee (10.1016/j.tibs.2011.10.004_bib0245) 2006; 281 Lukas (10.1016/j.tibs.2011.10.004_bib0195) 1994; 9 Agami (10.1016/j.tibs.2011.10.004_bib0200) 2000; 102 Barbash (10.1016/j.tibs.2011.10.004_bib0230) 2008; 7 Guardavaccaro (10.1016/j.tibs.2011.10.004_bib0355) 2003; 4 Orlicky (10.1016/j.tibs.2011.10.004_bib0415) 2010; 28 Petroski (10.1016/j.tibs.2011.10.004_bib0090) 2005; 6 Skaar (10.1016/j.tibs.2011.10.004_bib0095) 2009; 21 Bakkenist (10.1016/j.tibs.2011.10.004_bib0040) 2004; 118 Deshaies (10.1016/j.tibs.2011.10.004_bib0085) 2009; 78 Pontano (10.1016/j.tibs.2011.10.004_bib0255) 2008; 28 Merry (10.1016/j.tibs.2011.10.004_bib0305) 2010; 9 Bekker-Jensen (10.1016/j.tibs.2011.10.004_bib0370) 2011; 585 Fang (10.1016/j.tibs.2011.10.004_bib0055) 2011; 22 Vaites (10.1016/j.tibs.2011.10.004_bib0250) 2011; 31 Hoeijmakers (10.1016/j.tibs.2011.10.004_bib0010) 2001; 411 Shiloh (10.1016/j.tibs.2011.10.004_bib0025) 2003; 3 Yen (10.1016/j.tibs.2011.10.004_bib0380) 2008; 322 Lingle (10.1016/j.tibs.2011.10.004_bib0065) 2005; 570 Soucy (10.1016/j.tibs.2011.10.004_bib0395) 2009; 458 Polo (10.1016/j.tibs.2011.10.004_bib0030) 2011; 25 Tanaka (10.1016/j.tibs.2011.10.004_bib0060) 2009; 100 Barbash (10.1016/j.tibs.2011.10.004_bib0205) 2008; 14 Busino (10.1016/j.tibs.2011.10.004_bib0115) 2003; 426 Jin (10.1016/j.tibs.2011.10.004_bib0130) 2008; 283 Zhang (10.1016/j.tibs.2011.10.004_bib0295) 2005; 19 Kanemori (10.1016/j.tibs.2011.10.004_bib0165) 2005; 102 D’Angiolella (10.1016/j.tibs.2011.10.004_bib0320) 2010; 466 Puklowski (10.1016/j.tibs.2011.10.004_bib0325) 2011; 13 Pawar (10.1016/j.tibs.2011.10.004_bib0220) 2010; 107 Milhollen (10.1016/j.tibs.2011.10.004_bib0405) 2010; 116 Santra (10.1016/j.tibs.2011.10.004_bib0225) 2009; 459 Musacchio (10.1016/j.tibs.2011.10.004_bib0050) 2007; 8 Korzeniewski (10.1016/j.tibs.2011.10.004_bib0335) 2009; 69 Lin (10.1016/j.tibs.2011.10.004_bib0210) 2006; 24 Okabe (10.1016/j.tibs.2011.10.004_bib0215) 2006; 1 Sorensen (10.1016/j.tibs.2011.10.004_bib0155) 2010; 9 Aghajan (10.1016/j.tibs.2011.10.004_bib0420) 2010; 28 Honaker (10.1016/j.tibs.2011.10.004_bib0135) 2010; 29 Xia (10.1016/j.tibs.2011.10.004_bib0170) 2009; 106 Li (10.1016/j.tibs.2011.10.004_bib0240) 2010; 285 Piva (10.1016/j.tibs.2011.10.004_bib0315) 2002; 22 Cheng (10.1016/j.tibs.2011.10.004_bib0180) 2011; 10 Mamely (10.1016/j.tibs.2011.10.004_bib0285) 2006; 16 Melixetian (10.1016/j.tibs.2011.10.004_bib0150) 2009; 11 Myer (10.1016/j.tibs.2011.10.004_bib0140) 2005; 24 Yen (10.1016/j.tibs.2011.10.004_bib0385) 2008; 322 Kim (10.1016/j.tibs.2011.10.004_bib0185) 2009; 220 Jin (10.1016/j.tibs.2011.10.004_bib0105) 2004; 18 Derheimer (10.1016/j.tibs.2011.10.004_bib0045) 2010; 584 Schwartz (10.1016/j.tibs.2011.10.004_bib0080) 1999; 50 Zhang (10.1016/j.tibs.2011.10.004_bib0300) 2009; 35 Duensing (10.1016/j.tibs.2011.10.004_bib0070) 2010; 676 Frescas (10.1016/j.tibs.2011.10.004_bib0110) 2008; 8 Isoda (10.1016/j.tibs.2011.10.004_bib0125) 2009; 20 Macurek (10.1016/j.tibs.2011.10.004_bib0260) 2008; 455 Abraham (10.1016/j.tibs.2011.10.004_bib0020) 2001; 15 Freed (10.1016/j.tibs.2011.10.004_bib0310) 1999; 13 Seki (10.1016/j.tibs.2011.10.004_bib0270) 2008; 181 10.1016/j.tibs.2011.10.004_bib0425 Guderian (10.1016/j.tibs.2011.10.004_bib0350) 2010; 123 Peschiaroli (10.1016/j.tibs.2011.10.004_bib0280) 2006; 23 Jin (10.1016/j.tibs.2011.10.004_bib0120) 2003; 17 Inuzuka (10.1016/j.tibs.2011.10.004_bib0175) 2010; 18 Cardozo (10.1016/j.tibs.2011.10.004_bib0410) 2007; 8 Watanabe (10.1016/j.tibs.2011.10.004_bib0275) 2004; 101 Guardavaccaro (10.1016/j.tibs.2011.10.004_bib0360) 2008; 452 Bassermann (10.1016/j.tibs.2011.10.004_bib0265) 2008; 134 Cardozo (10.1016/j.tibs.2011.10.004_bib0100) 2004; 5 Hershko (10.1016/j.tibs.2011.10.004_bib0075) 1998; 67 Habedanck (10.1016/j.tibs.2011.10.004_bib0330) 2005; 7 Cunha-Ferreira (10.1016/j.tibs.2011.10.004_bib0345) 2009; 19 Uchida (10.1016/j.tibs.2011.10.004_bib0160) 2009; 69 Zimmerman (10.1016/j.tibs.2011.10.004_bib0145) 2007; 104 Welcker (10.1016/j.tibs.2011.10.004_bib0390) 2004; 14 Barbash (10.1016/j.tibs.2011.10.004_bib0235) 2011; 30 Mailand (10.1016/j.tibs.2011.10.004_bib0290) 2006; 23 Jia (10.1016/j.tibs.2011.10.004_bib0400) 2011; 11 |
References_xml | – volume: 53 start-page: 950 year: 2010 end-page: 961 ident: bib0015 article-title: Ageing, telomeres, senescence, and liver injury publication-title: J. Hepatol. contributor: fullname: Hoare – volume: 100 start-page: 1158 year: 2009 end-page: 1165 ident: bib0060 article-title: Chromosome segregation machinery and cancer publication-title: Cancer Sci. contributor: fullname: Hirota – volume: 102 start-page: 55 year: 2000 end-page: 66 ident: bib0200 article-title: Distinct initiation and maintenance mechanisms cooperate to induce G1 cell cycle arrest in response to DNA damage publication-title: Cell contributor: fullname: Bernards – volume: 40 start-page: 179 year: 2010 end-page: 204 ident: bib0035 article-title: The DNA damage response: making it safe to play with knives publication-title: Mol. Cell contributor: fullname: Elledge – volume: 459 start-page: 722 year: 2009 end-page: 725 ident: bib0225 article-title: F-box protein FBXO31 mediates cyclin D1 degradation to induce G1 arrest after DNA damage publication-title: Nature contributor: fullname: Santra – volume: 585 start-page: 2914 year: 2011 end-page: 2919 ident: bib0370 article-title: The ubiquitin- and SUMO-dependent signaling response to DNA double-strand breaks publication-title: FEBS Lett. contributor: fullname: Mailand – volume: 283 start-page: 19322 year: 2008 end-page: 19328 ident: bib0130 article-title: Differential roles for checkpoint kinases in DNA damage-dependent degradation of the Cdc25A protein phosphatase publication-title: J. Biol. Chem. contributor: fullname: Jin – volume: 29 start-page: 3324 year: 2010 end-page: 3334 ident: bib0135 article-title: Casein kinase 1 functions as both penultimate and ultimate kinase in regulating Cdc25A destruction publication-title: Oncogene contributor: fullname: Piwnica-Worms – volume: 10 start-page: 1162 year: 2011 end-page: 1166 ident: bib0180 article-title: The phenotype of MDM2 auto-degradation after DNA damage is due to epitope masking by phosphorylation publication-title: Cell Cycle contributor: fullname: Chen – volume: 134 start-page: 256 year: 2008 end-page: 267 ident: bib0265 article-title: The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response checkpoint publication-title: Cell contributor: fullname: Bassermann – volume: 23 start-page: 307 year: 2006 end-page: 318 ident: bib0290 article-title: Destruction of Claspin by SCF publication-title: Mol. Cell contributor: fullname: Mailand – volume: 69 start-page: 6668 year: 2009 end-page: 6675 ident: bib0335 article-title: Cullin 1 functions as a centrosomal suppressor of centriole multiplication by regulating polo-like kinase 4 protein levels publication-title: Cancer Res. contributor: fullname: Korzeniewski – volume: 123 start-page: 2163 year: 2010 end-page: 2169 ident: bib0350 article-title: Plk4 publication-title: J. Cell Sci. contributor: fullname: Guderian – volume: 25 start-page: 409 year: 2011 end-page: 433 ident: bib0030 article-title: Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications publication-title: Genes Dev. contributor: fullname: Jackson – volume: 19 start-page: 43 year: 2009 end-page: 49 ident: bib0345 article-title: The SCF/Slimb ubiquitin ligase limits centrosome amplification through degradation of SAK/PLK4 publication-title: Curr. Biol. contributor: fullname: Cunha-Ferreira – volume: 7 start-page: 2983 year: 2008 end-page: 2986 ident: bib0230 article-title: SCF publication-title: Cell Cycle contributor: fullname: Diehl – volume: 184 start-page: 225 year: 2009 end-page: 239 ident: bib0340 article-title: The SCF Slimb ubiquitin ligase regulates Plk4/Sak levels to block centriole reduplication publication-title: J. Cell Biol. contributor: fullname: Rogers – volume: 116 start-page: 1515 year: 2010 end-page: 1523 ident: bib0405 article-title: MLN4924, a NEDD8-activating enzyme inhibitor, is active in diffuse large B-cell lymphoma models: rationale for treatment of NF-κB-dependent lymphoma publication-title: Blood contributor: fullname: Milhollen – volume: 28 start-page: 738 year: 2010 end-page: 742 ident: bib0420 article-title: Chemical genetics screen for enhancers of rapamycin identifies a specific inhibitor of an SCF family E3 ubiquitin ligase publication-title: Nat. Biotechnol. contributor: fullname: Aghajan – volume: 8 start-page: 438 year: 2008 end-page: 449 ident: bib0110 article-title: Deregulated proteolysis by the F-box proteins SKP2 and β-TrCP: tipping the scales of cancer publication-title: Nat. Rev. Cancer contributor: fullname: Pagano – volume: 8 start-page: 1627 year: 1994 end-page: 1639 ident: bib0190 article-title: Cyclin D1-mediated inhibition of repair and replicative DNA synthesis in human fibroblasts publication-title: Genes Dev. contributor: fullname: Pagano – volume: 9 start-page: 279 year: 2010 end-page: 283 ident: bib0305 article-title: Targeting the checkpoint kinase Chk1 in cancer therapy publication-title: Cell Cycle contributor: fullname: Merry – volume: 21 start-page: 816 year: 2009 end-page: 824 ident: bib0095 article-title: Control of cell growth by the SCF and APC/C ubiquitin ligases publication-title: Curr. Opin. Cell Biol. contributor: fullname: Pagano – volume: 8 start-page: 379 year: 2007 end-page: 393 ident: bib0050 article-title: The spindle-assembly checkpoint in space and time publication-title: Nat. Rev. Mol. Cell Biol. contributor: fullname: Salmon – volume: 426 start-page: 87 year: 2003 end-page: 91 ident: bib0115 article-title: Degradation of Cdc25A by β-TrCP during S phase and in response to DNA damage publication-title: Nature contributor: fullname: Busino – volume: 466 start-page: 138 year: 2010 end-page: 142 ident: bib0320 article-title: SCF publication-title: Nature contributor: fullname: D’Angiolella – volume: 22 start-page: 8375 year: 2002 end-page: 8387 ident: bib0315 article-title: In vivo interference with Skp1 function leads to genetic instability and neoplastic transformation publication-title: Mol. Cell. Biol. contributor: fullname: Piva – volume: 7 start-page: 1140 year: 2005 end-page: 1146 ident: bib0330 article-title: The Polo kinase Plk4 functions in centriole duplication publication-title: Nat. Cell Biol. contributor: fullname: Habedanck – volume: 676 start-page: 93 year: 2010 end-page: 103 ident: bib0070 article-title: Centrosomes, polyploidy and cancer publication-title: Adv. Exp. Med. Biol. contributor: fullname: Duensing – volume: 452 start-page: 370 year: 2008 end-page: 374 ident: bib0365 article-title: SCF publication-title: Nature contributor: fullname: Westbrook – volume: 5 start-page: 739 year: 2004 end-page: 751 ident: bib0100 article-title: The SCF ubiquitin ligase: insights into a molecular machine publication-title: Nat. Rev. Mol. Cell Biol. contributor: fullname: Pagano – volume: 322 start-page: 918 year: 2008 end-page: 923 ident: bib0385 article-title: Global protein stability profiling in mammalian cells publication-title: Science contributor: fullname: Yen – volume: 107 start-page: 9210 year: 2010 end-page: 9215 ident: bib0220 article-title: C/EBPδ targets cyclin D1 for proteasome-mediated degradation via induction of CDC27/APC3 expression publication-title: Proc. Natl. Acad. Sci. U.S.A. contributor: fullname: Pawar – volume: 9 start-page: 450 year: 2010 end-page: 455 ident: bib0155 article-title: NEK11: linking CHK1 and CDC25A in DNA damage checkpoint signaling publication-title: Cell Cycle contributor: fullname: Sorensen – volume: 31 start-page: 4513 year: 2011 end-page: 4523 ident: bib0250 article-title: The Fbx4 tumor suppressor regulates cyclin D1 accumulation and prevents neoplastic transformation publication-title: Mol. Cell. Biol. contributor: fullname: Vaites – volume: 452 start-page: 365 year: 2008 end-page: 369 ident: bib0360 article-title: Control of chromosome stability by the β-TrCP-REST-Mad2 axis publication-title: Nature contributor: fullname: Guardavaccaro – volume: 22 start-page: 595 year: 2011 end-page: 601 ident: bib0055 article-title: Aneuploidy and tumorigenesis publication-title: Semin. Cell Dev. Biol. contributor: fullname: Zhang – volume: 16 start-page: 1950 year: 2006 end-page: 1955 ident: bib0285 article-title: Polo-like kinase-1 controls proteasome-dependent degradation of Claspin during checkpoint recovery publication-title: Curr. Biol. contributor: fullname: Mamely – volume: 220 start-page: 292 year: 2009 end-page: 296 ident: bib0185 article-title: Nuclear cyclin D1: an oncogenic driver in human cancer publication-title: J. Cell. Physiol. contributor: fullname: Diehl – volume: 570 start-page: 393 year: 2005 end-page: 421 ident: bib0065 article-title: Deregulation of the centrosome cycle and the origin of chromosomal instability in cancer publication-title: Adv. Exp. Med. Biol. contributor: fullname: Lingle – volume: 19 start-page: 607 year: 2005 end-page: 618 ident: bib0295 article-title: Genotoxic stress targets human Chk1 for degradation by the ubiquitin-proteasome pathway publication-title: Mol. Cell contributor: fullname: Zhang – volume: 104 start-page: 1847 year: 2007 end-page: 1852 ident: bib0145 article-title: Polo-like kinase 3 is required for entry into S phase publication-title: Proc. Natl. Acad. Sci. U.S.A. contributor: fullname: Erikson – volume: 101 start-page: 4419 year: 2004 end-page: 4424 ident: bib0275 article-title: M-phase kinases induce phospho-dependent ubiquitination of somatic Wee1 by SCF publication-title: Proc. Natl. Acad. Sci. U.S.A. contributor: fullname: Watanabe – volume: 13 start-page: 1004 year: 2011 end-page: 1009 ident: bib0325 article-title: The SCF-FBXW5 E3-ubiquitin ligase is regulated by PLK4 and targets HsSAS-6 to control centrosome duplication publication-title: Nat. Cell Biol. contributor: fullname: Puklowski – volume: 11 start-page: 347 year: 2011 end-page: 356 ident: bib0400 article-title: SCF E3 ubiquitin ligases as anticancer targets publication-title: Curr. Cancer Drug Targets contributor: fullname: Sun – volume: 9 start-page: 707 year: 1994 end-page: 718 ident: bib0195 article-title: Cyclin D1 protein oscillates and is essential for cell cycle progression in human tumour cell lines publication-title: Oncogene contributor: fullname: Lukas – volume: 18 start-page: 147 year: 2010 end-page: 159 ident: bib0175 article-title: Phosphorylation by casein kinase I promotes the turnover of the Mdm2 oncoprotein via the SCF publication-title: Cancer Cell contributor: fullname: Inuzuka – volume: 458 start-page: 732 year: 2009 end-page: 736 ident: bib0395 article-title: An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer publication-title: Nature contributor: fullname: Soucy – volume: 24 start-page: 299 year: 2005 end-page: 305 ident: bib0140 article-title: The Plk3-Cdc25 circuit publication-title: Oncogene contributor: fullname: Myer – volume: 67 start-page: 425 year: 1998 end-page: 479 ident: bib0075 article-title: The ubiquitin system publication-title: Annu. Rev. Biochem. contributor: fullname: Ciechanover – volume: 17 start-page: 3062 year: 2003 end-page: 3074 ident: bib0120 article-title: SCF publication-title: Genes Dev. contributor: fullname: Jin – volume: 28 start-page: 733 year: 2010 end-page: 737 ident: bib0415 article-title: An allosteric inhibitor of substrate recognition by the SCF(Cdc4) ubiquitin ligase publication-title: Nat. Biotechnol. contributor: fullname: Orlicky – volume: 8 start-page: S9 year: 2007 ident: bib0410 article-title: Wrenches in the works: drug discovery targeting the SCF ubiquitin ligase and APC/C complexes publication-title: BMC Biochem. contributor: fullname: Pagano – volume: 20 start-page: 2186 year: 2009 end-page: 2195 ident: bib0125 article-title: The extracellular signal-regulated kinase-mitogen-activated protein kinase pathway phosphorylates and targets Cdc25A for SCF publication-title: Mol. Biol. Cell contributor: fullname: Isoda – volume: 15 start-page: 2177 year: 2001 end-page: 2196 ident: bib0020 article-title: Cell cycle checkpoint signaling through the ATM and ATR kinases publication-title: Genes Dev. contributor: fullname: Abraham – volume: 50 start-page: 57 year: 1999 end-page: 74 ident: bib0080 article-title: The ubiquitin-proteasome pathway and pathogenesis of human diseases publication-title: Annu. Rev. Med. contributor: fullname: Ciechanover – volume: 118 start-page: 9 year: 2004 end-page: 17 ident: bib0040 article-title: Initiating cellular stress responses publication-title: Cell contributor: fullname: Kastan – volume: 411 start-page: 366 year: 2001 end-page: 374 ident: bib0010 article-title: Genome maintenance mechanisms for preventing cancer publication-title: Nature contributor: fullname: Hoeijmakers – volume: 102 start-page: 6279 year: 2005 end-page: 6284 ident: bib0165 article-title: β-TrCP recognizes a previously undescribed nonphosphorylated destruction motif in Cdc25A and Cdc25B phosphatases publication-title: Proc. Natl. Acad. Sci. U.S.A. contributor: fullname: Kanemori – volume: 285 start-page: 13896 year: 2010 end-page: 13906 ident: bib0240 article-title: Structural basis of dimerization-dependent ubiquitination by the SCF publication-title: J. Biol. Chem. contributor: fullname: Hao – volume: 6 start-page: 9 year: 2005 end-page: 20 ident: bib0090 article-title: Function and regulation of cullin-RING ubiquitin ligases publication-title: Nat. Rev. Mol. Cell Biol. contributor: fullname: Deshaies – volume: 1 start-page: e128 year: 2006 ident: bib0215 article-title: A critical role for FBXW8 and MAPK in cyclin D1 degradation and cancer cell proliferation publication-title: PLoS ONE contributor: fullname: Okabe – volume: 24 start-page: 355 year: 2006 end-page: 366 ident: bib0210 article-title: Phosphorylation-dependent ubiquitination of cyclin D1 by the SCF publication-title: Mol. Cell contributor: fullname: Lin – volume: 11 start-page: 1247 year: 2009 end-page: 1253 ident: bib0150 article-title: NEK11 regulates CDC25A degradation and the IR-induced G2/M checkpoint publication-title: Nat. Cell Biol. contributor: fullname: Melixetian – volume: 584 start-page: 3675 year: 2010 end-page: 3681 ident: bib0045 article-title: Multiple roles of ATM in monitoring and maintaining DNA integrity publication-title: FEBS Lett. contributor: fullname: Kastan – volume: 455 start-page: 119 year: 2008 end-page: 123 ident: bib0260 article-title: Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery publication-title: Nature contributor: fullname: Macurek – volume: 461 start-page: 1071 year: 2009 end-page: 1078 ident: bib0005 article-title: The DNA-damage response in human biology and disease publication-title: Nature contributor: fullname: Bartek – volume: 281 start-page: 759 year: 2006 end-page: 768 ident: bib0245 article-title: The F-box protein FBX4 targets PIN2/TRF1 for ubiquitin-mediated degradation and regulates telomere maintenance publication-title: J. Biol. Chem. contributor: fullname: Lee – volume: 28 start-page: 7245 year: 2008 end-page: 7258 ident: bib0255 article-title: Genotoxic stress-induced cyclin D1 phosphorylation and proteolysis are required for genomic stability publication-title: Mol. Cell. Biol. contributor: fullname: Pontano – volume: 4 start-page: 799 year: 2003 end-page: 812 ident: bib0355 article-title: Control of meiotic and mitotic progression by the F box protein β-Trcp1 publication-title: Dev. Cell contributor: fullname: Guardavaccaro – volume: 18 start-page: 2573 year: 2004 end-page: 2580 ident: bib0105 article-title: Systematic analysis and nomenclature of mammalian F-box proteins publication-title: Genes Dev. contributor: fullname: Jin – volume: 78 start-page: 399 year: 2009 end-page: 434 ident: bib0085 article-title: RING domain E3 ubiquitin ligases publication-title: Annu. Rev. Biochem. contributor: fullname: Joazeiro – volume: 69 start-page: 6438 year: 2009 end-page: 6444 ident: bib0160 article-title: Stress-activated mitogen-activated protein kinases c-Jun NH publication-title: Cancer Res. contributor: fullname: Uchida – volume: 23 start-page: 319 year: 2006 end-page: 329 ident: bib0280 article-title: SCF publication-title: Mol. Cell contributor: fullname: Peschiaroli – volume: 14 start-page: 1852 year: 2004 end-page: 1857 ident: bib0390 article-title: A nucleolar isoform of the Fbw7 ubiquitin ligase regulates c-Myc and cell size publication-title: Curr. Biol. contributor: fullname: Welcker – volume: 3 start-page: 155 year: 2003 end-page: 168 ident: bib0025 article-title: ATM and related protein kinases: safeguarding genome integrity publication-title: Nat. Rev. Cancer contributor: fullname: Shiloh – volume: 14 start-page: 68 year: 2008 end-page: 78 ident: bib0205 article-title: Mutations in Fbx4 inhibit dimerization of the SCF(Fbx4) ligase and contribute to cyclin D1 overexpression in human cancer publication-title: Cancer Cell contributor: fullname: Barbash – volume: 316 start-page: 1160 year: 2007 end-page: 1166 ident: bib0375 article-title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage publication-title: Science contributor: fullname: Matsuoka – volume: 30 start-page: 1995 year: 2011 end-page: 2002 ident: bib0235 article-title: Phosphorylation-dependent regulation of SCF publication-title: Oncogene contributor: fullname: Barbash – volume: 13 start-page: 2242 year: 1999 end-page: 2257 ident: bib0310 article-title: Components of an SCF ubiquitin ligase localize to the centrosome and regulate the centrosome duplication cycle publication-title: Genes Dev. contributor: fullname: Freed – volume: 106 start-page: 2629 year: 2009 end-page: 2634 ident: bib0170 article-title: Phosphorylation of p53 by IκB kinase 2 promotes its degradation by β-TrCP publication-title: Proc. Natl. Acad. Sci. U.S.A. contributor: fullname: Xia – volume: 181 start-page: 65 year: 2008 end-page: 78 ident: bib0270 article-title: Plk1- and β-TrCP-dependent degradation of Bora controls mitotic progression publication-title: J. Cell Biol. contributor: fullname: Seki – volume: 35 start-page: 442 year: 2009 end-page: 453 ident: bib0300 article-title: The F box protein Fbx6 regulates Chk1 stability and cellular sensitivity to replication stress publication-title: Mol. Cell contributor: fullname: Zhang – volume: 322 start-page: 923 year: 2008 end-page: 929 ident: bib0380 article-title: Identification of SCF ubiquitin ligase substrates by global protein stability profiling publication-title: Science contributor: fullname: Elledge – volume: 426 start-page: 87 year: 2003 ident: 10.1016/j.tibs.2011.10.004_bib0115 article-title: Degradation of Cdc25A by β-TrCP during S phase and in response to DNA damage publication-title: Nature doi: 10.1038/nature02082 contributor: fullname: Busino – volume: 1 start-page: e128 year: 2006 ident: 10.1016/j.tibs.2011.10.004_bib0215 article-title: A critical role for FBXW8 and MAPK in cyclin D1 degradation and cancer cell proliferation publication-title: PLoS ONE doi: 10.1371/journal.pone.0000128 contributor: fullname: Okabe – volume: 322 start-page: 923 year: 2008 ident: 10.1016/j.tibs.2011.10.004_bib0380 article-title: Identification of SCF ubiquitin ligase substrates by global protein stability profiling publication-title: Science doi: 10.1126/science.1160462 contributor: fullname: Yen – volume: 28 start-page: 733 year: 2010 ident: 10.1016/j.tibs.2011.10.004_bib0415 article-title: An allosteric inhibitor of substrate recognition by the SCF(Cdc4) ubiquitin ligase publication-title: Nat. Biotechnol. doi: 10.1038/nbt.1646 contributor: fullname: Orlicky – volume: 281 start-page: 759 year: 2006 ident: 10.1016/j.tibs.2011.10.004_bib0245 article-title: The F-box protein FBX4 targets PIN2/TRF1 for ubiquitin-mediated degradation and regulates telomere maintenance publication-title: J. Biol. Chem. doi: 10.1074/jbc.M509855200 contributor: fullname: Lee – volume: 585 start-page: 2914 year: 2011 ident: 10.1016/j.tibs.2011.10.004_bib0370 article-title: The ubiquitin- and SUMO-dependent signaling response to DNA double-strand breaks publication-title: FEBS Lett. doi: 10.1016/j.febslet.2011.05.056 contributor: fullname: Bekker-Jensen – volume: 23 start-page: 319 year: 2006 ident: 10.1016/j.tibs.2011.10.004_bib0280 article-title: SCFβ-TrCP-mediated degradation of Claspin regulates recovery from the DNA replication checkpoint response publication-title: Mol. Cell doi: 10.1016/j.molcel.2006.06.013 contributor: fullname: Peschiaroli – ident: 10.1016/j.tibs.2011.10.004_bib0425 doi: 10.1128/MCB.06570-11 – volume: 220 start-page: 292 year: 2009 ident: 10.1016/j.tibs.2011.10.004_bib0185 article-title: Nuclear cyclin D1: an oncogenic driver in human cancer publication-title: J. Cell. Physiol. doi: 10.1002/jcp.21791 contributor: fullname: Kim – volume: 8 start-page: S9 issue: Suppl. 1 year: 2007 ident: 10.1016/j.tibs.2011.10.004_bib0410 article-title: Wrenches in the works: drug discovery targeting the SCF ubiquitin ligase and APC/C complexes publication-title: BMC Biochem. doi: 10.1186/1471-2091-8-S1-S9 contributor: fullname: Cardozo – volume: 11 start-page: 347 year: 2011 ident: 10.1016/j.tibs.2011.10.004_bib0400 article-title: SCF E3 ubiquitin ligases as anticancer targets publication-title: Curr. Cancer Drug Targets doi: 10.2174/156800911794519734 contributor: fullname: Jia – volume: 285 start-page: 13896 year: 2010 ident: 10.1016/j.tibs.2011.10.004_bib0240 article-title: Structural basis of dimerization-dependent ubiquitination by the SCFFbx4 ubiquitin ligase publication-title: J. Biol. Chem. doi: 10.1074/jbc.M110.111518 contributor: fullname: Li – volume: 9 start-page: 450 year: 2010 ident: 10.1016/j.tibs.2011.10.004_bib0155 article-title: NEK11: linking CHK1 and CDC25A in DNA damage checkpoint signaling publication-title: Cell Cycle doi: 10.4161/cc.9.3.10513 contributor: fullname: Sorensen – volume: 40 start-page: 179 year: 2010 ident: 10.1016/j.tibs.2011.10.004_bib0035 article-title: The DNA damage response: making it safe to play with knives publication-title: Mol. Cell doi: 10.1016/j.molcel.2010.09.019 contributor: fullname: Ciccia – volume: 102 start-page: 6279 year: 2005 ident: 10.1016/j.tibs.2011.10.004_bib0165 article-title: β-TrCP recognizes a previously undescribed nonphosphorylated destruction motif in Cdc25A and Cdc25B phosphatases publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0501873102 contributor: fullname: Kanemori – volume: 411 start-page: 366 year: 2001 ident: 10.1016/j.tibs.2011.10.004_bib0010 article-title: Genome maintenance mechanisms for preventing cancer publication-title: Nature doi: 10.1038/35077232 contributor: fullname: Hoeijmakers – volume: 102 start-page: 55 year: 2000 ident: 10.1016/j.tibs.2011.10.004_bib0200 article-title: Distinct initiation and maintenance mechanisms cooperate to induce G1 cell cycle arrest in response to DNA damage publication-title: Cell doi: 10.1016/S0092-8674(00)00010-6 contributor: fullname: Agami – volume: 22 start-page: 595 year: 2011 ident: 10.1016/j.tibs.2011.10.004_bib0055 article-title: Aneuploidy and tumorigenesis publication-title: Semin. Cell Dev. Biol. doi: 10.1016/j.semcdb.2011.03.002 contributor: fullname: Fang – volume: 584 start-page: 3675 year: 2010 ident: 10.1016/j.tibs.2011.10.004_bib0045 article-title: Multiple roles of ATM in monitoring and maintaining DNA integrity publication-title: FEBS Lett. doi: 10.1016/j.febslet.2010.05.031 contributor: fullname: Derheimer – volume: 4 start-page: 799 year: 2003 ident: 10.1016/j.tibs.2011.10.004_bib0355 article-title: Control of meiotic and mitotic progression by the F box protein β-Trcp1 in vivo publication-title: Dev. Cell doi: 10.1016/S1534-5807(03)00154-0 contributor: fullname: Guardavaccaro – volume: 107 start-page: 9210 year: 2010 ident: 10.1016/j.tibs.2011.10.004_bib0220 article-title: C/EBPδ targets cyclin D1 for proteasome-mediated degradation via induction of CDC27/APC3 expression publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0913813107 contributor: fullname: Pawar – volume: 35 start-page: 442 year: 2009 ident: 10.1016/j.tibs.2011.10.004_bib0300 article-title: The F box protein Fbx6 regulates Chk1 stability and cellular sensitivity to replication stress publication-title: Mol. Cell doi: 10.1016/j.molcel.2009.06.030 contributor: fullname: Zhang – volume: 14 start-page: 68 year: 2008 ident: 10.1016/j.tibs.2011.10.004_bib0205 article-title: Mutations in Fbx4 inhibit dimerization of the SCF(Fbx4) ligase and contribute to cyclin D1 overexpression in human cancer publication-title: Cancer Cell doi: 10.1016/j.ccr.2008.05.017 contributor: fullname: Barbash – volume: 570 start-page: 393 year: 2005 ident: 10.1016/j.tibs.2011.10.004_bib0065 article-title: Deregulation of the centrosome cycle and the origin of chromosomal instability in cancer publication-title: Adv. Exp. Med. Biol. doi: 10.1007/1-4020-3764-3_14 contributor: fullname: Lingle – volume: 69 start-page: 6668 year: 2009 ident: 10.1016/j.tibs.2011.10.004_bib0335 article-title: Cullin 1 functions as a centrosomal suppressor of centriole multiplication by regulating polo-like kinase 4 protein levels publication-title: Cancer Res. doi: 10.1158/0008-5472.CAN-09-1284 contributor: fullname: Korzeniewski – volume: 67 start-page: 425 year: 1998 ident: 10.1016/j.tibs.2011.10.004_bib0075 article-title: The ubiquitin system publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev.biochem.67.1.425 contributor: fullname: Hershko – volume: 18 start-page: 147 year: 2010 ident: 10.1016/j.tibs.2011.10.004_bib0175 article-title: Phosphorylation by casein kinase I promotes the turnover of the Mdm2 oncoprotein via the SCFβ-TRCP ubiquitin ligase publication-title: Cancer Cell doi: 10.1016/j.ccr.2010.06.015 contributor: fullname: Inuzuka – volume: 30 start-page: 1995 year: 2011 ident: 10.1016/j.tibs.2011.10.004_bib0235 article-title: Phosphorylation-dependent regulation of SCFFbx4 dimerization and activity involves a novel component, 14-3-3ɛ publication-title: Oncogene doi: 10.1038/onc.2010.584 contributor: fullname: Barbash – volume: 123 start-page: 2163 year: 2010 ident: 10.1016/j.tibs.2011.10.004_bib0350 article-title: Plk4 trans-autophosphorylation regulates centriole number by controlling βTrCP-mediated degradation publication-title: J. Cell Sci. doi: 10.1242/jcs.068502 contributor: fullname: Guderian – volume: 31 start-page: 4513 year: 2011 ident: 10.1016/j.tibs.2011.10.004_bib0250 article-title: The Fbx4 tumor suppressor regulates cyclin D1 accumulation and prevents neoplastic transformation publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.05733-11 contributor: fullname: Vaites – volume: 5 start-page: 739 year: 2004 ident: 10.1016/j.tibs.2011.10.004_bib0100 article-title: The SCF ubiquitin ligase: insights into a molecular machine publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm1471 contributor: fullname: Cardozo – volume: 106 start-page: 2629 year: 2009 ident: 10.1016/j.tibs.2011.10.004_bib0170 article-title: Phosphorylation of p53 by IκB kinase 2 promotes its degradation by β-TrCP publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0812256106 contributor: fullname: Xia – volume: 23 start-page: 307 year: 2006 ident: 10.1016/j.tibs.2011.10.004_bib0290 article-title: Destruction of Claspin by SCFβ-TrCP restrains Chk1 activation and facilitates recovery from genotoxic stress publication-title: Mol. Cell doi: 10.1016/j.molcel.2006.06.016 contributor: fullname: Mailand – volume: 22 start-page: 8375 year: 2002 ident: 10.1016/j.tibs.2011.10.004_bib0315 article-title: In vivo interference with Skp1 function leads to genetic instability and neoplastic transformation publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.22.23.8375-8387.2002 contributor: fullname: Piva – volume: 461 start-page: 1071 year: 2009 ident: 10.1016/j.tibs.2011.10.004_bib0005 article-title: The DNA-damage response in human biology and disease publication-title: Nature doi: 10.1038/nature08467 contributor: fullname: Jackson – volume: 14 start-page: 1852 year: 2004 ident: 10.1016/j.tibs.2011.10.004_bib0390 article-title: A nucleolar isoform of the Fbw7 ubiquitin ligase regulates c-Myc and cell size publication-title: Curr. Biol. doi: 10.1016/j.cub.2004.09.083 contributor: fullname: Welcker – volume: 181 start-page: 65 year: 2008 ident: 10.1016/j.tibs.2011.10.004_bib0270 article-title: Plk1- and β-TrCP-dependent degradation of Bora controls mitotic progression publication-title: J. Cell Biol. doi: 10.1083/jcb.200712027 contributor: fullname: Seki – volume: 455 start-page: 119 year: 2008 ident: 10.1016/j.tibs.2011.10.004_bib0260 article-title: Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery publication-title: Nature doi: 10.1038/nature07185 contributor: fullname: Macurek – volume: 134 start-page: 256 year: 2008 ident: 10.1016/j.tibs.2011.10.004_bib0265 article-title: The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response checkpoint publication-title: Cell doi: 10.1016/j.cell.2008.05.043 contributor: fullname: Bassermann – volume: 19 start-page: 607 year: 2005 ident: 10.1016/j.tibs.2011.10.004_bib0295 article-title: Genotoxic stress targets human Chk1 for degradation by the ubiquitin-proteasome pathway publication-title: Mol. Cell doi: 10.1016/j.molcel.2005.07.019 contributor: fullname: Zhang – volume: 53 start-page: 950 year: 2010 ident: 10.1016/j.tibs.2011.10.004_bib0015 article-title: Ageing, telomeres, senescence, and liver injury publication-title: J. Hepatol. doi: 10.1016/j.jhep.2010.06.009 contributor: fullname: Hoare – volume: 118 start-page: 9 year: 2004 ident: 10.1016/j.tibs.2011.10.004_bib0040 article-title: Initiating cellular stress responses publication-title: Cell doi: 10.1016/j.cell.2004.06.023 contributor: fullname: Bakkenist – volume: 3 start-page: 155 year: 2003 ident: 10.1016/j.tibs.2011.10.004_bib0025 article-title: ATM and related protein kinases: safeguarding genome integrity publication-title: Nat. Rev. Cancer doi: 10.1038/nrc1011 contributor: fullname: Shiloh – volume: 9 start-page: 707 year: 1994 ident: 10.1016/j.tibs.2011.10.004_bib0195 article-title: Cyclin D1 protein oscillates and is essential for cell cycle progression in human tumour cell lines publication-title: Oncogene contributor: fullname: Lukas – volume: 184 start-page: 225 year: 2009 ident: 10.1016/j.tibs.2011.10.004_bib0340 article-title: The SCF Slimb ubiquitin ligase regulates Plk4/Sak levels to block centriole reduplication publication-title: J. Cell Biol. doi: 10.1083/jcb.200808049 contributor: fullname: Rogers – volume: 459 start-page: 722 year: 2009 ident: 10.1016/j.tibs.2011.10.004_bib0225 article-title: F-box protein FBXO31 mediates cyclin D1 degradation to induce G1 arrest after DNA damage publication-title: Nature doi: 10.1038/nature08011 contributor: fullname: Santra – volume: 15 start-page: 2177 year: 2001 ident: 10.1016/j.tibs.2011.10.004_bib0020 article-title: Cell cycle checkpoint signaling through the ATM and ATR kinases publication-title: Genes Dev. doi: 10.1101/gad.914401 contributor: fullname: Abraham – volume: 8 start-page: 379 year: 2007 ident: 10.1016/j.tibs.2011.10.004_bib0050 article-title: The spindle-assembly checkpoint in space and time publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm2163 contributor: fullname: Musacchio – volume: 101 start-page: 4419 year: 2004 ident: 10.1016/j.tibs.2011.10.004_bib0275 article-title: M-phase kinases induce phospho-dependent ubiquitination of somatic Wee1 by SCFβ-TrCP publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0307700101 contributor: fullname: Watanabe – volume: 13 start-page: 1004 year: 2011 ident: 10.1016/j.tibs.2011.10.004_bib0325 article-title: The SCF-FBXW5 E3-ubiquitin ligase is regulated by PLK4 and targets HsSAS-6 to control centrosome duplication publication-title: Nat. Cell Biol. doi: 10.1038/ncb2282 contributor: fullname: Puklowski – volume: 18 start-page: 2573 year: 2004 ident: 10.1016/j.tibs.2011.10.004_bib0105 article-title: Systematic analysis and nomenclature of mammalian F-box proteins publication-title: Genes Dev. doi: 10.1101/gad.1255304 contributor: fullname: Jin – volume: 8 start-page: 438 year: 2008 ident: 10.1016/j.tibs.2011.10.004_bib0110 article-title: Deregulated proteolysis by the F-box proteins SKP2 and β-TrCP: tipping the scales of cancer publication-title: Nat. Rev. Cancer doi: 10.1038/nrc2396 contributor: fullname: Frescas – volume: 9 start-page: 279 year: 2010 ident: 10.1016/j.tibs.2011.10.004_bib0305 article-title: Targeting the checkpoint kinase Chk1 in cancer therapy publication-title: Cell Cycle doi: 10.4161/cc.9.2.10445 contributor: fullname: Merry – volume: 283 start-page: 19322 year: 2008 ident: 10.1016/j.tibs.2011.10.004_bib0130 article-title: Differential roles for checkpoint kinases in DNA damage-dependent degradation of the Cdc25A protein phosphatase publication-title: J. Biol. Chem. doi: 10.1074/jbc.M802474200 contributor: fullname: Jin – volume: 13 start-page: 2242 year: 1999 ident: 10.1016/j.tibs.2011.10.004_bib0310 article-title: Components of an SCF ubiquitin ligase localize to the centrosome and regulate the centrosome duplication cycle publication-title: Genes Dev. doi: 10.1101/gad.13.17.2242 contributor: fullname: Freed – volume: 458 start-page: 732 year: 2009 ident: 10.1016/j.tibs.2011.10.004_bib0395 article-title: An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer publication-title: Nature doi: 10.1038/nature07884 contributor: fullname: Soucy – volume: 25 start-page: 409 year: 2011 ident: 10.1016/j.tibs.2011.10.004_bib0030 article-title: Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications publication-title: Genes Dev. doi: 10.1101/gad.2021311 contributor: fullname: Polo – volume: 19 start-page: 43 year: 2009 ident: 10.1016/j.tibs.2011.10.004_bib0345 article-title: The SCF/Slimb ubiquitin ligase limits centrosome amplification through degradation of SAK/PLK4 publication-title: Curr. Biol. doi: 10.1016/j.cub.2008.11.037 contributor: fullname: Cunha-Ferreira – volume: 21 start-page: 816 year: 2009 ident: 10.1016/j.tibs.2011.10.004_bib0095 article-title: Control of cell growth by the SCF and APC/C ubiquitin ligases publication-title: Curr. Opin. Cell Biol. doi: 10.1016/j.ceb.2009.08.004 contributor: fullname: Skaar – volume: 69 start-page: 6438 year: 2009 ident: 10.1016/j.tibs.2011.10.004_bib0160 article-title: Stress-activated mitogen-activated protein kinases c-Jun NH2-terminal kinase and p38 target Cdc25B for degradation publication-title: Cancer Res. doi: 10.1158/0008-5472.CAN-09-0869 contributor: fullname: Uchida – volume: 8 start-page: 1627 year: 1994 ident: 10.1016/j.tibs.2011.10.004_bib0190 article-title: Cyclin D1-mediated inhibition of repair and replicative DNA synthesis in human fibroblasts publication-title: Genes Dev. doi: 10.1101/gad.8.14.1627 contributor: fullname: Pagano – volume: 452 start-page: 370 year: 2008 ident: 10.1016/j.tibs.2011.10.004_bib0365 article-title: SCFβ-TRCP controls oncogenic transformation and neural differentiation through REST degradation publication-title: Nature doi: 10.1038/nature06780 contributor: fullname: Westbrook – volume: 116 start-page: 1515 year: 2010 ident: 10.1016/j.tibs.2011.10.004_bib0405 article-title: MLN4924, a NEDD8-activating enzyme inhibitor, is active in diffuse large B-cell lymphoma models: rationale for treatment of NF-κB-dependent lymphoma publication-title: Blood doi: 10.1182/blood-2010-03-272567 contributor: fullname: Milhollen – volume: 29 start-page: 3324 year: 2010 ident: 10.1016/j.tibs.2011.10.004_bib0135 article-title: Casein kinase 1 functions as both penultimate and ultimate kinase in regulating Cdc25A destruction publication-title: Oncogene doi: 10.1038/onc.2010.96 contributor: fullname: Honaker – volume: 7 start-page: 1140 year: 2005 ident: 10.1016/j.tibs.2011.10.004_bib0330 article-title: The Polo kinase Plk4 functions in centriole duplication publication-title: Nat. Cell Biol. doi: 10.1038/ncb1320 contributor: fullname: Habedanck – volume: 466 start-page: 138 year: 2010 ident: 10.1016/j.tibs.2011.10.004_bib0320 article-title: SCFCyclin F controls centrosome homeostasis and mitotic fidelity through CP110 degradation publication-title: Nature doi: 10.1038/nature09140 contributor: fullname: D’Angiolella – volume: 6 start-page: 9 year: 2005 ident: 10.1016/j.tibs.2011.10.004_bib0090 article-title: Function and regulation of cullin-RING ubiquitin ligases publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm1547 contributor: fullname: Petroski – volume: 104 start-page: 1847 year: 2007 ident: 10.1016/j.tibs.2011.10.004_bib0145 article-title: Polo-like kinase 3 is required for entry into S phase publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0610856104 contributor: fullname: Zimmerman – volume: 24 start-page: 355 year: 2006 ident: 10.1016/j.tibs.2011.10.004_bib0210 article-title: Phosphorylation-dependent ubiquitination of cyclin D1 by the SCFFBX4-αB crystallin complex publication-title: Mol. Cell doi: 10.1016/j.molcel.2006.09.007 contributor: fullname: Lin – volume: 24 start-page: 299 year: 2005 ident: 10.1016/j.tibs.2011.10.004_bib0140 article-title: The Plk3-Cdc25 circuit publication-title: Oncogene doi: 10.1038/sj.onc.1208278 contributor: fullname: Myer – volume: 322 start-page: 918 year: 2008 ident: 10.1016/j.tibs.2011.10.004_bib0385 article-title: Global protein stability profiling in mammalian cells publication-title: Science doi: 10.1126/science.1160489 contributor: fullname: Yen – volume: 16 start-page: 1950 year: 2006 ident: 10.1016/j.tibs.2011.10.004_bib0285 article-title: Polo-like kinase-1 controls proteasome-dependent degradation of Claspin during checkpoint recovery publication-title: Curr. Biol. doi: 10.1016/j.cub.2006.08.026 contributor: fullname: Mamely – volume: 100 start-page: 1158 year: 2009 ident: 10.1016/j.tibs.2011.10.004_bib0060 article-title: Chromosome segregation machinery and cancer publication-title: Cancer Sci. doi: 10.1111/j.1349-7006.2009.01178.x contributor: fullname: Tanaka – volume: 316 start-page: 1160 year: 2007 ident: 10.1016/j.tibs.2011.10.004_bib0375 article-title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage publication-title: Science doi: 10.1126/science.1140321 contributor: fullname: Matsuoka – volume: 676 start-page: 93 year: 2010 ident: 10.1016/j.tibs.2011.10.004_bib0070 article-title: Centrosomes, polyploidy and cancer publication-title: Adv. Exp. Med. Biol. doi: 10.1007/978-1-4419-6199-0_6 contributor: fullname: Duensing – volume: 452 start-page: 365 year: 2008 ident: 10.1016/j.tibs.2011.10.004_bib0360 article-title: Control of chromosome stability by the β-TrCP-REST-Mad2 axis publication-title: Nature doi: 10.1038/nature06641 contributor: fullname: Guardavaccaro – volume: 20 start-page: 2186 year: 2009 ident: 10.1016/j.tibs.2011.10.004_bib0125 article-title: The extracellular signal-regulated kinase-mitogen-activated protein kinase pathway phosphorylates and targets Cdc25A for SCFβ-TRCP -dependent degradation for cell cycle arrest publication-title: Mol. Biol. Cell doi: 10.1091/mbc.e09-01-0008 contributor: fullname: Isoda – volume: 17 start-page: 3062 year: 2003 ident: 10.1016/j.tibs.2011.10.004_bib0120 article-title: SCFβ-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase publication-title: Genes Dev. doi: 10.1101/gad.1157503 contributor: fullname: Jin – volume: 10 start-page: 1162 year: 2011 ident: 10.1016/j.tibs.2011.10.004_bib0180 article-title: The phenotype of MDM2 auto-degradation after DNA damage is due to epitope masking by phosphorylation publication-title: Cell Cycle doi: 10.4161/cc.10.7.15249 contributor: fullname: Cheng – volume: 28 start-page: 7245 year: 2008 ident: 10.1016/j.tibs.2011.10.004_bib0255 article-title: Genotoxic stress-induced cyclin D1 phosphorylation and proteolysis are required for genomic stability publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.01085-08 contributor: fullname: Pontano – volume: 28 start-page: 738 year: 2010 ident: 10.1016/j.tibs.2011.10.004_bib0420 article-title: Chemical genetics screen for enhancers of rapamycin identifies a specific inhibitor of an SCF family E3 ubiquitin ligase publication-title: Nat. Biotechnol. doi: 10.1038/nbt.1645 contributor: fullname: Aghajan – volume: 50 start-page: 57 year: 1999 ident: 10.1016/j.tibs.2011.10.004_bib0080 article-title: The ubiquitin-proteasome pathway and pathogenesis of human diseases publication-title: Annu. Rev. Med. doi: 10.1146/annurev.med.50.1.57 contributor: fullname: Schwartz – volume: 11 start-page: 1247 year: 2009 ident: 10.1016/j.tibs.2011.10.004_bib0150 article-title: NEK11 regulates CDC25A degradation and the IR-induced G2/M checkpoint publication-title: Nat. Cell Biol. doi: 10.1038/ncb1969 contributor: fullname: Melixetian – volume: 78 start-page: 399 year: 2009 ident: 10.1016/j.tibs.2011.10.004_bib0085 article-title: RING domain E3 ubiquitin ligases publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev.biochem.78.101807.093809 contributor: fullname: Deshaies – volume: 7 start-page: 2983 year: 2008 ident: 10.1016/j.tibs.2011.10.004_bib0230 article-title: SCFFbx4/alphaαB-crystallin E3 ligase: when one is not enough publication-title: Cell Cycle doi: 10.4161/cc.7.19.6775 contributor: fullname: Barbash |
SSID | ssj0015775 |
Score | 2.3894842 |
SecondaryResourceType | review_article |
Snippet | In response to genotoxic stress, eukaryotic cells activate the DNA damage response (DDR), a series of pathways that coordinate cell cycle arrest and DNA repair... |
SourceID | pubmedcentral proquest crossref pubmed fao elsevier |
SourceType | Open Access Repository Aggregation Database Index Database Publisher |
StartPage | 66 |
SubjectTerms | aneuploidy Animals antineoplastic agents cell cycle checkpoints centrosomes chromosome segregation DDR DNA Damage DNA repair eukaryotic cells genome Genomic Instability genotoxicity Humans mutation proteasome endopeptidase complex proteins SKP Cullin F-Box Protein Ligases - chemistry SKP Cullin F-Box Protein Ligases - genetics SKP Cullin F-Box Protein Ligases - metabolism therapeutics ubiquitin-protein ligase Ubiquitination - genetics |
Title | SCF ubiquitin ligases in the maintenance of genome stability |
URI | https://dx.doi.org/10.1016/j.tibs.2011.10.004 https://www.ncbi.nlm.nih.gov/pubmed/22099186 https://search.proquest.com/docview/1028036544 https://search.proquest.com/docview/921424158 https://pubmed.ncbi.nlm.nih.gov/PMC3278546 |
Volume | 37 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3Pa9swFH40KYNdxtb9qLutaLDb8GLJkmXDLiUspC3tJQv0JqRY6lxap12cQy_92_dk2WEZ6w69GFuWwfqe9d5n9N4ngM-OFc5qLWN0dWXMnSzjwtIsthYDAheJYe3WCWfn2XTOTy7ExQ6M-1oYn1bZ-f7g01tv3bWMOjRHt1U1miH5zj0l8aJnVKbpAHYxHHE-hN2j49Pp-WYxQchWb9f3b4uou9qZkObVVGYVlDzbJC_-WHwaOL38Fwv9O5nyj-g0eQkvOlpJjsKbv4IdW-_Bs7DR5P1r-DYbT8jaVHfrqqlqcl1dYvBaETxF_kdutBeN8Mobliwd8bKtN5YgbWwTZ-_fwHzy_cd4Gnf7JsQLpE9NnHHkfJrioCwtpZYIe261MCnOZ1q6nDpTMMPxmNm0RE-ZOibYAn8VhS51adO3MKyXtd0HQi3XJskWhTE4u50uhE7sIkfSkifSuCSCLz1a6jbIY6g-b-xKeWyVx9a3IbYRiB5QtWVkhf77v8_tI_pKX6LfU_MZ86p4YdFcRvCpN4nCieFXO3Rtl-uV8swJw7Pg-Dh5pE_hBeeQwuQRvAtW3IyC-ZpimmcRyC37bjp4Xe7tO3X1s9XnTpnMBc8Onjja9_Acr1hIDf8Aw-bX2n5E5tOYQxh8faCH3ff9G4dHABk |
link.rule.ids | 230,315,786,790,891,4521,24144,27957,27958,45620,45714 |
linkProvider | Elsevier |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3Pa9swFH60KWO9lP1s3f3SYLdhYsmSZcMuJSyka5tLGuhNSLHUebROuziH_vd7suywjHWHXYyxJLC-Z733Gb33CeCTY4WzWssYXV0ZcyfLuLA0i63FgMBFYlh7dMLFNJvM-bcrcbUDo74WxqdVdr4_-PTWW3dPhh2aw7uqGs6QfOeeknjRMyrTdBf2uJCUD2Dv5PRsMt1sJgjZ6u36_m0RdVc7E9K8msqsgpJnm-TFH4tPu04v_8ZC_0ym_C06jZ_BQUcryUl48-ewY-sX8CQcNPnwEr7MRmOyNtX9umqqmtxU1xi8VgRvkf-RW-1FI7zyhiVLR7xs660lSBvbxNmHVzAff70cTeLu3IR4gfSpiTOOnE9TnJSlpdQSYc-tFibF9UxLl1NnCmY4XjOblugpU8cEW-CvotClLm36Ggb1srZHQKjl2iTZojAGV7fThdCJXeRIWvJEGpdE8LlHS90FeQzV5439UB5b5bH1zxDbCEQPqNoyskL__c9xR4i-0tfo99R8xrwqXtg0lxF87E2icGH43Q5d2-V6pTxzwvAsOA4nj_QpvOAcUpg8gsNgxc0smK8ppnkWgdyy76aD1-Xebqmr760-d8pkLnh2_J-z_QBPJ5cX5-r8dHr2BvaxhYU08bcwaH6u7TtkQY15333lvwCyvgIL |
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=SCF+ubiquitin+ligases+in+the+maintenance+of+genome+stability&rft.jtitle=Trends+in+biochemical+sciences+%28Amsterdam.+Regular+ed.%29&rft.au=Silverman%2C+Joshua+S&rft.au=Skaar%2C+Jeffrey+R&rft.au=Pagano%2C+Michele&rft.date=2012-02-01&rft.issn=0968-0004&rft.volume=37&rft.issue=2&rft.spage=66&rft.epage=73&rft_id=info:doi/10.1016%2Fj.tibs.2011.10.004&rft.externalDBID=NO_FULL_TEXT |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0968-0004&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0968-0004&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0968-0004&client=summon |