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Con l'acronimo mwawPCNA viene identificata l'mwbaantigene nucleare di proliferazione cellulare (in inglese mwbqProliferating Cell Nuclear Antigen, da cui l'acronimo); PCNA è una mwbgproteina ad azione di fattore di processività per la DNA-mwbwpolimerasi-δ, individuata nelle cellule eucariotiche. La struttura di tale proteina è in grado di assumere una peculiare conformazione la quale le consente di contattare il DNA (mwcaDNA clamp) e di promuovere l'azione della polimerasi durante la replicazione del DNA.

La proteina PCNA codificata dal gene PCNA si localizza nel nucleo delle cellule mwegeucariotiche, fa parte dei cofattori della DNA polimerasi delta, la loro reciproca associazione aumenta la processività nella sintesi del filamento guida durante la replicazione del DNA. In risposta ad un danno al DNA questa proteina viene mwewubiquitinata e quindi coinvolta nella via di riparazione del DNA RAD6-dipendente. Il gene PCNA codifica per due mwfavarianti di mwfqtrascrizione della proteina. Pseudogeni di PCNA sono stati individuati sul cromosoma 4 e sul cromosoma Xcite-ref-entrez-1-0[1].

• Espressione di PCNA all'interno del nucleo durante la sintesi del DNA

• Ruolo di PCNA nella riparazione del DNA

• Interazioni

• Note

• Bibliografia

• Collegamenti esterni

PCNA è stata originariamente identificata come un mwhqantigene espresso nei nuclei delle cellule durante la fase di sintesi del DNAcite-ref-pmid1350788-2-0[2]. Parte della proteina è stata sequenziata e la sequenza è stata utilizzata per consentire l'isolamento di un clone a mwigcDNAcite-ref-pmid2884104-3-0[3]. PCNA aiuta a mantenere la DNA polimerasi delta (Pol δ) ancorata al DNA. PCNA viene bloccatocite-ref-bowman-2004-4-0[4] al DNA attraverso l'azione del mwlafattore di replicazione C (RFC)cite-ref-pmid10051561-5-0[5], il quale fa parte degli eteropentameri della classe AAA+ ATPasi dipendenti. L'espressione del gene PCNA è sotto il controllo del fattore di trascrizione E2Fcite-ref-pmid12468739-6-0[6].

La DNA polimerasi delta è coinvolta nella sintesi di filamenti di DNA danneggiati e quindi rimossi durante la riparazione del DNA, PCNA consentendo alla DNA polimerasi delta il contatto con il filamento danneggiato svolge un ruolo importante sia per la sintesi del DNA che per la sua riparazionecite-ref-pmid1348971-7-0[7]cite-ref-pmid16227586-8-0[8].

PCNA interviene anche nella via di tolleranza danno al DNA denominata riparazione post-replicazione (mwqapost-replication repair o PRR)cite-ref-pmid16956796-9-0[9] In PRR, avvengono due sotto-percorsi:

• Il percorso translesione, che viene svolto da DNA polimerasi specializzate in grado di integrare le basi del DNA danneggiato nei loro siti attivi (a differenza delle normali polimerasi replicative), e quindi evitare il danno.

• Il superamento del danno tramite il reclutamento dei meccanismi di mwsaricombinazione degli omologhi.

PCNA è fondamentale per l'attivazione di questi percorsi e per la scelta di quale percorso di riparazione viene utilizzato dalla cellula.

La proteina PCNA subisce mwswmodifiche post-traduzionali quali ubiquitinazionecite-ref-hoege-2002-10-0[10]: Se la lisina numero 164 del peptide viene mono-ubiquinata si avrà l'attivazione del meccanismo di riparazione translesione, Se invece si verifica una poli-ubiquitinazione che coinvolge la lisina 63cite-ref-hoege-2002-10-1[10], si attiverà il secondo percorso di riparazione. Inoltre, se la lisina-164 (ed in misura minore, la lisina-127) di PCNA vanno incontro al processo di sumolazione (piccole modificatore ubiquitino-simili, SUMO) viene inibito il secondo percorso di riparazionecite-ref-hoege-2002-10-2[10]. Questo effetto di inibizione nella riparazione si verifica perché la PCNA sumolata, recluta un DNA elicasi denominato Srs2cite-ref-pmid15931174-11-0[11], tale elicasi disturba l'azione della nucleoproteina RAD51 la quale è fondamentale per l'inizio della ricombinazione omologacite-ref-pmid15931174-11-1[11].

PCNA può interagire con: Ku70,cite-ref-pmid12171929-12-0[12]cite-ref-pmid11239001-13-0[13] MSH3,cite-ref-pmid12171929-12-1[12]cite-ref-pmid11274057-14-0[14]cite-ref-pmid11005803-15-0[15] Werner syndrome ATP-dependent helicase,cite-ref-pmid12633936-16-0[16]cite-ref-pmid10871373-17-0[17] RFC2,cite-ref-pmid12171929-12-2[12]cite-ref-pmid9228079-18-0[18]cite-ref-pmid8093561-19-0[19] RFC3,cite-ref-pmid12171929-12-3[12]cite-ref-pmid12766176-20-0[20] RFC1,cite-ref-pmid12171929-12-4[12]cite-ref-pmid12192049-21-0[21]cite-ref-pmid8861969-22-0[22]cite-ref-pmid8999859-23-0[23]cite-ref-pmid10353443-24-0[24] RFC4,cite-ref-pmid12171929-12-5[12]cite-ref-pmid9228079-18-1[18] RFC5,cite-ref-pmid12171929-12-6[12]cite-ref-pmid9228079-18-2[18]cite-ref-pmid8999859-23-1[23] GADD45G,cite-ref-pmid11022036-25-0[25]cite-ref-pmid10455148-26-0[26] CDC25C,cite-ref-pmid11896603-27-0[27] MUTYH,cite-ref-pmid11092888-28-0[28] Flap structure-specific endonuclease 1,cite-ref-pmid12853968-29-0[29]cite-ref-pmid11430825-30-0[30]cite-ref-pmid9545252-31-0[31]cite-ref-pmid9305916-32-0[32]cite-ref-pmid8876181-33-0[33]cite-ref-pmid11601988-34-0[34]cite-ref-pmid11313979-35-0[35] Cyclin O,cite-ref-pmid12171929-12-7[12]cite-ref-pmid10393198-36-0[36] CHTF18,cite-ref-pmid12171929-12-8[12] Y box binding protein 1,cite-ref-pmid9927044-37-0[37] Cyclin D1,cite-ref-pmid7908906-38-0[38]cite-ref-pmid8101826-39-0[39] Annexin A2,cite-ref-pmid12171929-12-9[12] MSH6,cite-ref-pmid12171929-12-10[12]cite-ref-pmid11274057-14-1[14]cite-ref-pmid11005803-15-1[15] DNMT1,cite-ref-pmid10888872-40-0[40]cite-ref-pmid12354094-41-0[41]cite-ref-pmid9302295-42-0[42] mwas0HDAC1,cite-ref-pmid11929879-43-0[43] KCTD13,cite-ref-pmid11593007-44-0[44] XRCC1,cite-ref-pmid15107487-45-0[45] Cyclin-dependent kinase 4,cite-ref-pmid8101826-39-1[39]cite-ref-pmid8259215-46-0[46] Ku80,cite-ref-pmid12171929-12-11[12]cite-ref-pmid11239001-13-1[13]cite-ref-pmid12393188-47-0[47] HUS1,cite-ref-pmid11077446-48-0[48] GADD45A,cite-ref-pmid7973727-49-0[49]cite-ref-pmid7478510-50-0[50]cite-ref-pmid10828065-51-0[51]cite-ref-pmid7784094-52-0[52]cite-ref-pmid10973963-53-0[53] POLD2,cite-ref-pmid11986310-54-0[54] ING1,cite-ref-pmid11682605-55-0[55] POLH,cite-ref-pmid11585903-56-0[56] KIAA0101,cite-ref-pmid11313979-35-1[35] POLDIP2,cite-ref-pmid12522211-57-0[57] EP300,cite-ref-pmid11268218-58-0[58] mwayoMCL1,cite-ref-pmid10978339-59-0[59] POLD3,cite-ref-pmid12171929-12-12[12]cite-ref-pmid11595739-60-0[60] Cyclin-dependent kinase inhibitor 1C,cite-ref-pmid9465025-61-0[61] POLL,cite-ref-pmid11784855-62-0[62]cite-ref-pmid12368291-63-0[63]cite-ref-pmid12081642-64-0[64] Ubiquitin Ccite-ref-pmid18719106-65-0[65]cite-ref-pmid18316726-66-0[66]cite-ref-pmid18284681-67-0[67] and mwabcP21.cite-ref-pmid8861969-22-1[22]cite-ref-pmid9545252-31-1[31]cite-ref-pmid11313979-35-2[35]cite-ref-pmid9465025-61-1[61]cite-ref-pmid16189514-68-0[68]cite-ref-pmid12930846-69-0[69]cite-ref-pmid8861913-70-0[70]cite-ref-pmid11350925-71-0[71]

cite-note-entrez-11. ↑ mwad4mwad8mwaeaEntrez Gene: PCNA proliferating cell nuclear antigen, su mwaeencbi.nlm.nih.gov.

cite-note-pmid1350788-22. ↑ mwaeuLeonardi E, Girlando S, Serio G, Mauri FA, Perrone G, Scampini S, Dalla Palma P, Barbareschi M, mwaeymwaecPCNA and Ki67 expression in breast carcinoma: correlations with clinical and biological variables, in mwaegJ. Clin. Pathol., vol.mwaek 45, n.mwaeo 5, 1992, pp.mwaes 416–9, mwaewDOI:mwae010.1136/jcp.45.5.416, mwae4PMIDmwae8 mwafa1350788.

cite-note-pmid2884104-33. ↑ mwafuMatsumoto K, Moriuchi T, Koji T, Nakane PK, mwafymwafcMolecular cloning of cDNA coding for rat proliferating cell nuclear antigen (PCNA)/cyclinmwafo, in mwagiEmbo J., vol.mwagm 6, n.mwagq 3, 1987, pp.mwagu 637–42, mwagyPMIDmwagc mwagg2884104.

cite-note-bowman-2004-44. ↑ mwag0Bowman GD, O'Donnell M, Kuriyan J, mwag4mwag8Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex, in mwahaNature, vol.mwahe 429, n.mwahi 6993, 2004, pp.mwahm 724–30, mwahqDOI:mwahu10.1038/nature02585, mwahyPMIDmwahc mwahg15201901.

cite-note-pmid10051561-55. ↑ mwah0Zhang G, Gibbs E, Kelman Z, O'Donnell M, Hurwitz J, mwah4mwah8Studies on the interactions between human replication factor C and human proliferating cell nuclear antigen, in mwaiaProc. Natl. Acad. Sci. U.S.A., vol.mwaie 96, n.mwaii 5, 1999, pp.mwaim 1869–74, mwaiqDOI:mwaiu10.1073/pnas.96.5.1869, mwaiyPMCmwaic mwaig26703, mwaikPMIDmwaio mwais10051561.

cite-note-pmid12468739-66. ↑ mwajaEgelkrout EM, Mariconti L, Settlage SB, Cella R, Robertson D, Hanley-Bowdoin L, mwajemwajiTwo E2F elements regulate the proliferating cell nuclear antigen promoter differently during leaf development, in mwajmPlant Cell, vol.mwajq 14, n.mwaju 12, 2002, pp.mwajy 3225–36, mwajcDOI:mwajg10.1105/tpc.006403, mwajkPMIDmwajo mwajs12468739.

cite-note-pmid1348971-77. ↑ mwakaShivji KK, Kenny MK, Wood RD, mwakeProliferating cell nuclear antigen is required for DNA excision repair, in mwakiCell, vol.mwakm 69, n.mwakq 2, aprile 1992, pp.mwaku 367–74, mwakyPMIDmwakc mwakg1348971.

cite-note-pmid16227586-88. ↑ mwak0Essers J, Theil AF, Baldeyron C, van Cappellen WA, Houtsmuller AB, Kanaar R, Vermeulen W, mwak4mwak8Nuclear dynamics of PCNA in DNA replication and repair, in mwalaMol. Cell. Biol., vol.mwale 25, n.mwali 21, 2005, pp.mwalm 9350–9, mwalqDOI:mwalu10.1128/MCB.25.21.9350-9359.2005, mwalyPMIDmwalc mwalg16227586.

cite-note-pmid16956796-99. ↑ mwal0Lehmann AR, Fuchs RP, mwal4mwal8Gaps and forks in DNA replication: Rediscovering old models, in mwamaDNA Repair (Amst.), vol.mwame 5, n.mwami 12, dicembre 2006, pp.mwamm 1495–8, mwamqDOI:mwamu10.1016/j.dnarep.2006.07.002, mwamyPMIDmwamc mwamg16956796.

cite-note-hoege-2002-1010. ↑ mwaneHoege C, Pfander B, Moldovan GL, Pyrowolakis G, Jentsch S, mwanimwanmRAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO, in mwanqNature, vol.mwanu 419, n.mwany 6903, settembre 2002, pp.mwanc 135–41, mwangDOI:mwank10.1038/nature00991, mwanoPMIDmwans mwanw12226657.

cite-note-pmid15931174-1111. ↑ mwaomPfander B, Moldovan GL, Sacher M, Hoege C, Jentsch S, mwaoqmwaouSUMO-modified PCNA recruits Srs2 to prevent recombination during S phase, in mwaoyNature, vol.mwaoc 436, n.mwaog 7049, luglio 2005, pp.mwaok 428–33, mwaooDOI:mwaos10.1038/nature03665, mwaowPMIDmwao0 mwao415931174.

cite-note-pmid12171929-1212. ↑ mwaqsSatoshi Ohta, Shiomi Yasushi, Sugimoto Katsunori, Obuse Chikashi, Tsurimoto Toshiki, mwaqwmwaq0A proteomics approach to identify proliferating cell nuclear antigen (PCNA)-binding proteins in human cell lysates. Identification of the human CHL12/RFCs2-5 complex as a novel PCNA-binding protein, in mwaq4J. Biol. Chem., vol.mwaq8 277, n.mwara 43, United States, ottobre 2002, pp.mware 40362–7, mwariDOI:mwarm10.1074/jbc.M206194200, mwarqISSNmwaru 0021-9258, mwar0PMIDmwar4 mwar812171929.

cite-note-pmid11239001-1313. ↑ mwascA S Balajee, Geard C R, mwasgmwaskChromatin-bound PCNA complex formation triggered by DNA damage occurs independent of the ATM gene product in human cells, in mwasoNucleic Acids Res., vol.mwass 29, n.mwasw 6, England, marzo 2001, pp.mwas0 1341–51, mwas4DOI:mwas810.1093/nar/29.6.1341, mwataPMCmwate mwati29758, mwatmPMIDmwatq mwatu11239001.

cite-note-pmid11274057-1414. ↑ mwat0H E Kleczkowska, Marra G, Lettieri T, Jiricny J, mwat4mwat8hMSH3 and hMSH6 interact with PCNA and colocalize with it to replication foci, in mwauaGenes Dev., vol.mwaue 15, n.mwaui 6, United States, marzo 2001, pp.mwaum 724–36, mwauqDOI:mwauu10.1101/gad.191201, mwauyISSNmwauc 0890-9369, mwau8PMCmwava mwave312660, mwaviPMIDmwavm mwavq11274057.

cite-note-pmid11005803-1515. ↑ mwavwA B Clark, Valle F, Drotschmann K, Gary R K, Kunkel T A, mwav0mwav4Functional interaction of proliferating cell nuclear antigen with MSH2-MSH6 and MSH2-MSH3 complexes, in mwav8J. Biol. Chem., vol.mwawa 275, n.mwawe 47, UNITED STATES, novembre 2000, pp.mwawi 36498–501, mwawmDOI:mwawq10.1074/jbc.C000513200, mwawuISSNmwawy 0021-9258, mwaw4PMIDmwaw8 mwaxa11005803.

cite-note-pmid12633936-1616. ↑ mwaxyAna M Rodríguez-López, Jackson Dean A, Nehlin Jan O, Iborra Francisco, Warren Anna V, Cox Lynne S, mwaxcmwaxgCharacterisation of the interaction between WRN, the helicase/exonuclease defective in progeroid Werner's syndrome, and an essential replication factor, PCNA, in mwaxkMech. Ageing Dev., vol.mwaxo 124, n.mwaxs 2, Ireland, febbraio 2003, pp.mwaxw 167–74, mwax0DOI:mwax410.1016/S0047-6374(02)00131-8, mwax8ISSNmwaya 0047-6374, mwaygPMIDmwayk mwayo12633936.

cite-note-pmid10871373-1717. ↑ mwazaS Huang, Beresten S, Li B, Oshima J, Ellis N A, Campisi J, mwazemwaziCharacterization of the human and mouse WRN 3'-->5' exonuclease, in mwazmNucleic Acids Res., vol.mwazq 28, n.mwazu 12, ENGLAND, giugno 2000, pp.mwazy 2396–405, mwazcDOI:mwazg10.1093/nar/28.12.2396, mwazkPMCmwazo mwazs102739, mwazwPMIDmwaz0 mwaz410871373.

cite-note-pmid9228079-1818. ↑ mwa0gJ Cai, Gibbs E, Uhlmann F, Phillips B, Yao N, O'Donnell M, Hurwitz J, mwa0kmwa0oA complex consisting of human replication factor C p40, p37, and p36 subunits is a DNA-dependent ATPase and an intermediate in the assembly of the holoenzyme, in mwa0sJ. Biol. Chem., vol.mwa0w 272, n.mwa00 30, UNITED STATES, luglio 1997, pp.mwa04 18974–81, mwa08DOI:mwa1a10.1074/jbc.272.30.18974, mwa1eISSNmwa1i 0021-9258, mwa1oPMIDmwa1s mwa1w9228079.

cite-note-pmid8093561-1919. ↑ mwa2iZ Q Pan, Chen M, Hurwitz J, mwa2mmwa2qThe subunits of activator 1 (replication factor C) carry out multiple functions essential for proliferating-cell nuclear antigen-dependent DNA synthesis, in mwa2umwa2yProc. Natl. Acad. Sci. U.S.A., vol.mwa2c 90, n.mwa2g 1, UNITED STATES, Jan. 1993, pp.mwa2k 6–10, mwa2oDOI:mwa2s10.1073/pnas.90.1.6, mwa2wISSNmwa20 0027-8424, mwa3uPMCmwa3y mwa3c45588, mwa3gPMIDmwa3k mwa3o8093561.

cite-note-pmid12766176-2020. ↑ mwa4aCarolin J Merkle, Karnitz Larry M, Henry-Sánchez John T, Chen Junjie, mwa4emwa4iCloning and characterization of hCTF18, hCTF8, and hDCC1. Human homologs of a Saccharomyces cerevisiae complex involved in sister chromatid cohesion establishment, in mwa4mJ. Biol. Chem., vol.mwa4q 278, n.mwa4u 32, United States, agosto 2003, pp.mwa4y 30051–6, mwa4cDOI:mwa4g10.1074/jbc.M211591200, mwa4kISSNmwa4o 0021-9258, mwa5iPMIDmwa5m mwa5q12766176.

cite-note-pmid12192049-2121. ↑ mwa5oTetsuo Maruyama, Farina Andrea, Dey Anup, Cheong JaeHun, Bermudez Vladimir P, Tamura Tomohiko, Sciortino Selvaggia, Shuman Jon, Hurwitz Jerard, Ozato Keiko, mwa5smwa5wA Mammalian bromodomain protein, brd4, interacts with replication factor C and inhibits progression to S phase, in mwa50Mol. Cell. Biol., vol.mwa54 22, n.mwa58 18, United States, settembre 2002, pp.mwa6a 6509–20, mwa6eDOI:mwa6i10.1128/MCB.22.18.6509-6520.2002, mwa6mISSNmwa6q 0270-7306, mwa6wPMCmwa60 mwa64135621, mwa68PMIDmwa7a mwa7e12192049.

cite-note-pmid8861969-2222. ↑ mwa7kR Fotedar, Mossi R, Fitzgerald P, Rousselle T, Maga G, Brickner H, Messier H, Kasibhatla S, Hübscher U, Fotedar A, mwa7omwa7sA conserved domain of the large subunit of replication factor C binds PCNA and acts like a dominant negative inhibitor of DNA replication in mammalian cells, in mwa7wEMBO J., vol.mwa70 15, n.mwa74 16, ENGLAND, agosto 1996, pp.mwa78 4423–33, mwa8aISSNmwa8e 0261-4189, mwa8kPMCmwa8o mwa8s452166, mwa8wPMIDmwa80 mwa848861969.

cite-note-pmid8999859-2323. ↑ mwa9yR Mossi, Jónsson Z O, Allen B L, Hardin S H, Hübscher U, mwa9cmwa9gReplication factor C interacts with the C-terminal side of proliferating cell nuclear antigen, in mwa9kJ. Biol. Chem., vol.mwa9o 272, n.mwa9s 3, UNITED STATES, Jan. 1997, pp.mwa9w 1769–76, mwa90DOI:mwa9410.1074/jbc.272.3.1769, mwa98ISSNmwa-a 0021-9258, mwa-gPMIDmwa-k mwa-o8999859.

cite-note-pmid10353443-2424. ↑ mwa-aH van der Kuip, Carius B, Haque S J, Williams B R, Huber C, Fischer T, mwa-emwa-iThe DNA-binding subunit p140 of replication factor C is upregulated in cycling cells and associates with G1 phase cell cycle regulatory proteins, in mwa-mJ. Mol. Med., vol.mwa-q 77, n.mwa-u 4, GERMANY, aprile 1999, pp.mwa-y 386–92, mwa-cDOI:mwa-g10.1007/s001090050365, mwa-kISSNmwa-o 0946-2716, mwbaiPMIDmwbam mwbaq10353443.

cite-note-pmid11022036-2525. ↑ mwbaoN Azam, Vairapandi M, Zhang W, Hoffman B, Liebermann D A, mwbasmwbawInteraction of CR6 (GADD45gamma ) with proliferating cell nuclear antigen impedes negative growth control, in mwba0J. Biol. Chem., vol.mwba4 276, n.mwba8 4, United States, Jan. 2001, pp.mwbba 2766–74, mwbbeDOI:mwbbi10.1074/jbc.M005626200, mwbbmISSNmwbbq 0021-9258, mwbbwPMIDmwbb0 mwbb411022036.

cite-note-pmid10455148-2626. ↑ mwbcqK Nakayama, Hara T, Hibi M, Hirano T, Miyajima A, mwbcumwbcyA novel oncostatin M-inducible gene OIG37 forms a gene family with MyD118 and GADD45 and negatively regulates cell growth, in mwbccJ. Biol. Chem., vol.mwbcg 274, n.mwbck 35, UNITED STATES, agosto 1999, pp.mwbco 24766–72, mwbcsDOI:mwbcw10.1074/jbc.274.35.24766, mwbc0ISSNmwbc4 0021-9258, mwbdyPMIDmwbdc mwbdg10455148.

cite-note-pmid11896603-2727. ↑ mwbd4Takumi Kawabe, Suganuma Masashi, Ando Tomoaki, Kimura Mayumi, Hori Haruna, Okamoto Takashi, mwbd8mwbeaCdc25C interacts with PCNA at G2/M transition, in mwbeeOncogene, vol.mwbei 21, n.mwbem 11, England, marzo 2002, pp.mwbeq 1717–26, mwbeuDOI:mwbey10.1038/sj.onc.1205229, mwbecISSNmwbeg 0950-9232, mwbfaPMIDmwbfe mwbfi11896603.

cite-note-pmid11092888-2828. ↑ mwbfgA Parker, Gu Y, Mahoney W, Lee S H, Singh K K, Lu A L, mwbfkmwbfoHuman homolog of the MutY repair protein (hMYH) physically interacts with proteins involved in long patch DNA base excision repair, in mwbfsJ. Biol. Chem., vol.mwbfw 276, n.mwbf0 8, United States, febbraio 2001, pp.mwbf4 5547–55, mwbf8DOI:mwbga10.1074/jbc.M008463200, mwbgeISSNmwbgi 0021-9258, mwbgoPMIDmwbgs mwbgw11092888.

cite-note-pmid12853968-2929. ↑ mwbhiGhislaine Henneke, Koundrioukoff Stéphane, Hübscher Ulrich, mwbhmmwbhqPhosphorylation of human Fen1 by cyclin-dependent kinase modulates its role in replication fork regulation, in mwbhuOncogene, vol.mwbhy 22, n.mwbhc 28, England, luglio 2003, pp.mwbhg 4301–13, mwbhkDOI:mwbho10.1038/sj.onc.1206606, mwbhsISSNmwbhw 0950-9232, mwbiqPMIDmwbiu mwbiy12853968.

cite-note-pmid11430825-3030. ↑ mwbiwS Hasan, Stucki M, Hassa P O, Imhof R, Gehrig P, Hunziker P, Hübscher U, Hottiger M O, mwbi0mwbi4Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300, in mwbi8Mol. Cell, vol.mwbja 7, n.mwbje 6, United States, giugno 2001, pp.mwbji 1221–31, mwbjmDOI:mwbjq10.1016/S1097-2765(01)00272-6, mwbjuISSNmwbjy 1097-2765, mwbj4PMIDmwbj8 mwbka11430825.

cite-note-pmid9545252-3131. ↑ mwbkgZ O Jónsson, Hindges R, Hübscher U, mwbkkmwbkoRegulation of DNA replication and repair proteins through interaction with the front side of proliferating cell nuclear antigen, in mwbksEMBO J., vol.mwbkw 17, n.mwbk0 8, ENGLAND, aprile 1998, pp.mwbk4 2412–25, mwbk8DOI:mwbla10.1093/emboj/17.8.2412, mwbleISSNmwbli 0261-4189, mwbloPMCmwbls mwblw1170584, mwbl0PMIDmwbl4 mwbl89545252.

cite-note-pmid9305916-3232. ↑ mwbmuR Gary, Ludwig D L, Cornelius H L, MacInnes M A, Park M S, mwbmymwbmcThe DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21, in mwbmgJ. Biol. Chem., vol.mwbmk 272, n.mwbmo 39, UNITED STATES, settembre 1997, pp.mwbms 24522–9, mwbmwDOI:mwbm010.1074/jbc.272.39.24522, mwbm4ISSNmwbm8 0021-9258, mwbncPMIDmwbng mwbnk9305916.

cite-note-pmid8876181-3333. ↑ mwbn8U Chen, Chen S, Saha P, Dutta A, mwboamwboep21Cip1/Waf1 disrupts the recruitment of human Fen1 by proliferating-cell nuclear antigen into the DNA replication complex, in mwboimwbomProc. Natl. Acad. Sci. U.S.A., vol.mwboq 93, n.mwbou 21, UNITED STATES, ottobre 1996, pp.mwboy 11597–602, mwbocDOI:mwbog10.1073/pnas.93.21.11597, mwbokISSNmwboo 0027-8424, mwbpiPMCmwbpm mwbpq38103, mwbpuPMIDmwbpy mwbpc8876181.

cite-note-pmid11601988-3434. ↑ mwbp0I I Dianova, Bohr V A, Dianov G L, mwbp4mwbp8Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair, in mwbqaBiochemistry, vol.mwbqe 40, n.mwbqi 42, United States, ottobre 2001, pp.mwbqm 12639–44, mwbqqDOI:mwbqu10.1021/bi011117i, mwbqyISSNmwbqc 0006-2960, mwbq8PMIDmwbra mwbre11601988.

cite-note-pmid11313979-3535. ↑ mwbrsP Yu, Huang B, Shen M, Lau C, Chan E, Michel J, Xiong Y, Payan D G, Luo Y, mwbrwmwbr0p15(PAF), a novel PCNA associated factor with increased expression in tumor tissues, in mwbr4Oncogene, vol.mwbr8 20, n.mwbsa 4, England, Jan. 2001, pp.mwbse 484–9, mwbsiDOI:mwbsm10.1038/sj.onc.1204113, mwbsqISSNmwbsu 0950-9232, mwbs0PMIDmwbs4 mwbs811313979.

cite-note-pmid10393198-3636. ↑ mwbtuM Otterlei, Warbrick E, Nagelhus T A, Haug T, Slupphaug G, Akbari M, Aas P A, Steinsbekk K, Bakke O, Krokan H E, mwbtymwbtcPost-replicative base excision repair in replication foci, in mwbtgEMBO J., vol.mwbtk 18, n.mwbto 13, ENGLAND, luglio 1999, pp.mwbts 3834–44, mwbtwDOI:mwbt010.1093/emboj/18.13.3834, mwbt4ISSNmwbt8 0261-4189, mwbucPMCmwbug mwbuk1171460, mwbuoPMIDmwbus mwbuw10393198.

cite-note-pmid9927044-3737. ↑ mwbviT Ise, Nagatani G, Imamura T, Kato K, Takano H, Nomoto M, Izumi H, Ohmori H, Okamoto T, Ohga T, Uchiumi T, Kuwano M, Kohno K, mwbvmTranscription factor Y-box binding protein 1 binds preferentially to cisplatin-modified DNA and interacts with proliferating cell nuclear antigen, in mwbvqCancer Res., vol.mwbvu 59, n.mwbvy 2, UNITED STATES, Jan. 1999, pp.mwbvc 342–6, mwbvgISSNmwbvk 0008-5472, mwbwePMIDmwbwi mwbwm9927044.

cite-note-pmid7908906-3838. ↑ mwbwkS Matsuoka, Yamaguchi M, Matsukage A, mwbwoD-type cyclin-binding regions of proliferating cell nuclear antigen, in mwbwsJ. Biol. Chem., vol.mwbww 269, n.mwbw0 15, UNITED STATES, aprile 1994, pp.mwbw4 11030–6, mwbw8ISSNmwbxa 0021-9258, mwbxgPMIDmwbxk mwbxo7908906.

cite-note-pmid8101826-3939. ↑ mwbyiY Xiong, Zhang H, Beach D, mwbymmwbyqSubunit rearrangement of the cyclin-dependent kinases is associated with cellular transformation, in mwbyuGenes Dev., vol.mwbyy 7, n.mwbyc 8, UNITED STATES, agosto 1993, pp.mwbyg 1572–83, mwbykDOI:mwbyo10.1101/gad.7.8.1572, mwbysISSNmwbyw 0890-9369, mwbzqPMIDmwbzu mwbzy8101826.

cite-note-pmid10888872-4040. ↑ mwbzwM R Rountree, Bachman K E, Baylin S B, mwbz0mwbz4DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci, in mwbz8Nat. Genet., vol.mwbaa 25, n.mwbae 3, UNITED STATES, luglio 2000, pp.mwbai 269–77, mwbamDOI:mwbaq10.1038/77023, mwbauISSNmwbay 1061-4036, mwba4PMIDmwba8 mwbba10888872.

cite-note-pmid12354094-4141. ↑ mwbbyTetsuo Iida, Suetake Isao, Tajima Shoji, Morioka Hiroshi, Ohta Satoshi, Obuse Chikashi, Tsurimoto Toshiki, mwbbcmwbbgPCNA clamp facilitates action of DNA cytosine methyltransferase 1 on hemimethylated DNA, in mwbbkGenes Cells, vol.mwbbo 7, n.mwbbs 10, England, ottobre 2002, pp.mwbbw 997–1007, mwbb0DOI:mwbb410.1046/j.1365-2443.2002.00584.x, mwbb8ISSNmwbca 1356-9597, mwbcgPMIDmwbck mwbco12354094.

cite-note-pmid9302295-4242. ↑ mwbdaL S Chuang, Ian H I, Koh T W, Ng H H, Xu G, Li B F, mwbdemwbdiHuman DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21WAF1, in mwbdmmwbdqScience, vol.mwbdu 277, n.mwbdy 5334, UNITED STATES, settembre 1997, pp.mwbdc 1996–2000, mwbdgDOI:mwbdk10.1126/science.277.5334.1996, mwbdoISSNmwbds 0036-8075, mwbemPMIDmwbeq mwbeu9302295.

cite-note-pmid11929879-4343. ↑ mwbesSnezana Milutinovic, Zhuang Qianli, Szyf Moshe, mwbewmwbe0Proliferating cell nuclear antigen associates with histone deacetylase activity, integrating DNA replication and chromatin modification, in mwbe4J. Biol. Chem., vol.mwbe8 277, n.mwbfa 23, United States, giugno 2002, pp.mwbfe 20974–8, mwbfiDOI:mwbfm10.1074/jbc.M202504200, mwbfqISSNmwbfu 0021-9258, mwbf0PMIDmwbf4 mwbf811929879.

cite-note-pmid11593007-4444. ↑ mwbguH He, Tan C K, Downey K M, So A G, mwbgymwbgcA tumor necrosis factor alpha- and interleukin 6-inducible protein that interacts with the small subunit of DNA polymerase delta and proliferating cell nuclear antigen, in mwbggmwbgkProc. Natl. Acad. Sci. U.S.A., vol.mwbgo 98, n.mwbgs 21, United States, ottobre 2001, pp.mwbgw 11979–84, mwbg0DOI:mwbg410.1073/pnas.221452098, mwbg8ISSNmwbha 0027-8424, mwbhgPMCmwbhk mwbho59753, mwbhsPMIDmwbhw mwbh011593007.

cite-note-pmid15107487-4545. ↑ mwbimJinshui Fan, Otterlei Marit, Wong Heng-Kuan, Tomkinson Alan E, Wilson David M, mwbiqmwbiuXRCC1 co-localizes and physically interacts with PCNA, in mwbiyNucleic Acids Res., vol.mwbic 32, n.mwbig 7, England, 2004, pp.mwbik 2193–201, mwbioDOI:mwbis10.1093/nar/gkh556, mwbiwPMCmwbi0 mwbi4407833, mwbi8PMIDmwbja mwbje15107487.

cite-note-pmid8259215-4646. ↑ mwbjcM Serrano, Hannon G J, Beach D, mwbjgmwbjkA new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4, in mwbjomwbjsNature, vol.mwbjw 366, n.mwbj0 6456, ENGLAND, dicembre 1993, pp.mwbj4 704–7, mwbj8DOI:mwbka10.1038/366704a0, mwbkeISSNmwbki 0028-0836, mwbkoPMIDmwbks mwbkw8259207.

cite-note-pmid12393188-4747. ↑ mwbliDiamanto Matheos, Ruiz Marcia T, Price Gerald B, Zannis-Hadjopoulos Maria, mwblmKu antigen, an origin-specific binding protein that associates with replication proteins, is required for mammalian DNA replication, in mwblqBiochim. Biophys. Acta, vol.mwblu 1578, n.mwbly 1-3, Netherlands, ottobre 2002, pp.mwblc 59–72, mwblgISSNmwblk 0006-3002, mwbmePMIDmwbmi mwbmm12393188.

cite-note-pmid11077446-4848. ↑ mwbmkK Komatsu, Wharton W, Hang H, Wu C, Singh S, Lieberman H B, Pledger W J, Wang H G, mwbmomwbmsPCNA interacts with hHus1/hRad9 in response to DNA damage and replication inhibition, in mwbmwOncogene, vol.mwbm0 19, n.mwbm4 46, ENGLAND, novembre 2000, pp.mwbm8 5291–7, mwbnaDOI:mwbne10.1038/sj.onc.1203901, mwbniISSNmwbnm 0950-9232, mwbnsPMIDmwbnw mwbn011077446.

cite-note-pmid7973727-4949. ↑ mwbomM L Smith, Chen I T, Zhan Q, Bae I, Chen C Y, Gilmer T M, Kastan M B, O'Connor P M, Fornace A J, mwboqmwbouInteraction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen, in mwboymwbocScience, vol.mwbog 266, n.mwbok 5189, UNITED STATES, novembre 1994, pp.mwboo 1376–80, mwbosDOI:mwbow10.1126/science.7973727, mwbo0ISSNmwbo4 0036-8075, mwbpyPMIDmwbpc mwbpg7481777.

cite-note-pmid7478510-5050. ↑ mwbp4I T Chen, Smith M L, O'Connor P M, Fornace A J, mwbp8Direct interaction of Gadd45 with PCNA and evidence for competitive interaction of Gadd45 and p21Waf1/Cip1 with PCNA, in mwbqaOncogene, vol.mwbqe 11, n.mwbqi 10, ENGLAND, novembre 1995, pp.mwbqm 1931–7, mwbqqISSNmwbqu 0950-9232, mwbq0PMIDmwbq4 mwbq87478510.

cite-note-pmid10828065-5151. ↑ mwbruM Vairapandi, Azam N, Balliet A G, Hoffman B, Liebermann D A, mwbrymwbrcCharacterization of MyD118, Gadd45, and proliferating cell nuclear antigen (PCNA) interacting domains. PCNA impedes MyD118 AND Gadd45-mediated negative growth control, in mwbrgJ. Biol. Chem., vol.mwbrk 275, n.mwbro 22, UNITED STATES, giugno 2000, pp.mwbrs 16810–9, mwbrwDOI:mwbr010.1074/jbc.275.22.16810, mwbr4ISSNmwbr8 0021-9258, mwbscPMIDmwbsg mwbsk10828065.

cite-note-pmid7784094-5252. ↑ mwbs8P A Hall, Kearsey J M, Coates P J, Norman D G, Warbrick E, Cox L S, mwbtaCharacterisation of the interaction between PCNA and Gadd45, in mwbteOncogene, vol.mwbti 10, n.mwbtm 12, ENGLAND, giugno 1995, pp.mwbtq 2427–33, mwbtuISSNmwbty 0950-9232, mwbt4PMIDmwbt8 mwbua7784094.

cite-note-pmid10973963-5353. ↑ mwbuyQ Yang, Manicone A, Coursen J D, Linke S P, Nagashima M, Forgues M, Wang X W, mwbucmwbugIdentification of a functional domain in a GADD45-mediated G2/M checkpoint, in mwbukJ. Biol. Chem., vol.mwbuo 275, n.mwbus 47, UNITED STATES, novembre 2000, pp.mwbuw 36892–8, mwbu0DOI:mwbu410.1074/jbc.M005319200, mwbu8ISSNmwbva 0021-9258, mwbvgPMIDmwbvk mwbvo10973963.

cite-note-pmid11986310-5454. ↑ mwbwaXiaoqing Lu, Tan Cheng-Keat, Zhou Jin-Qiu, You Min, Carastro L Michael, Downey Kathleen M, So Antero G, mwbwemwbwiDirect interaction of proliferating cell nuclear antigen with the small subunit of DNA polymerase delta, in mwbwmJ. Biol. Chem., vol.mwbwq 277, n.mwbwu 27, United States, luglio 2002, pp.mwbwy 24340–5, mwbwcDOI:mwbwg10.1074/jbc.M200065200, mwbwkISSNmwbwo 0021-9258, mwbxiPMIDmwbxm mwbxq11986310.

cite-note-pmid11682605-5555. ↑ mwbxoM Scott, Bonnefin P, Vieyra D, Boisvert F M, Young D, Bazett-Jones D P, Riabowol K, mwbxsUV-induced binding of ING1 to PCNA regulates the induction of apoptosis, in mwbxwJ. Cell. Sci., vol.mwbx0 114, Pt 19, England, ottobre 2001, pp.mwbx4 3455–62, mwbx8ISSNmwbya 0021-9533, mwbygPMIDmwbyk mwbyo11682605.

cite-note-pmid11585903-5656. ↑ mwbzaL Haracska, Johnson R E, Unk I, Phillips B, Hurwitz J, Prakash L, Prakash S, mwbzemwbziPhysical and functional interactions of human DNA polymerase eta with PCNA, in mwbzmMol. Cell. Biol., vol.mwbzq 21, n.mwbzu 21, United States, novembre 2001, pp.mwbzy 7199–206, mwbzcDOI:mwbzg10.1128/MCB.21.21.7199-7206.2001, mwbzkISSNmwbzo 0270-7306, mwb0iPMCmwb0m mwb0q99895, mwb0uPMIDmwb0y mwb0c11585903.

cite-note-pmid12522211-5757. ↑ mwb00Li Liu, Rodriguez-Belmonte Esther M, Mazloum Nayef, Xie Bin, Lee Marietta Y W T, mwb04mwb08Identification of a novel protein, PDIP38, that interacts with the p50 subunit of DNA polymerase delta and proliferating cell nuclear antigen, in mwb1aJ. Biol. Chem., vol.mwb1e 278, n.mwb1i 12, United States, marzo 2003, pp.mwb1m 10041–7, mwb1qDOI:mwb1u10.1074/jbc.M208694200, mwb1yISSNmwb1c 0021-9258, mwb18PMIDmwb2a mwb2e12522211.

cite-note-pmid11268218-5858. ↑ mwb2cS Hasan, Hassa P O, Imhof R, Hottiger M O, mwb2gmwb2kTranscription coactivator p300 binds PCNA and may have a role in DNA repair synthesis, in mwb2omwb2sNature, vol.mwb2w 410, n.mwb20 6826, England, marzo 2001, pp.mwb24 387–91, mwb28DOI:mwb3a10.1038/35066610, mwb3eISSNmwb3i 0028-0836, mwb3oPMIDmwb3s mwb3w11268218.

cite-note-pmid10978339-5959. ↑ mwb4iK Fujise, Zhang D, Liu J, Yeh E T, mwb4mmwb4qRegulation of apoptosis and cell cycle progression by MCL1. Differential role of proliferating cell nuclear antigen, in mwb4uJ. Biol. Chem., vol.mwb4y 275, n.mwb4c 50, UNITED STATES, dicembre 2000, pp.mwb4g 39458–65, mwb4kDOI:mwb4o10.1074/jbc.M006626200, mwb4sISSNmwb4w 0021-9258, mwb5qPMIDmwb5u mwb5y10978339.

cite-note-pmid11595739-6060. ↑ mwb5wM Ducoux, Urbach S, Baldacci G, Hübscher U, Koundrioukoff S, Christensen J, Hughes P, mwb50mwb54Mediation of proliferating cell nuclear antigen (PCNA)-dependent DNA replication through a conserved p21(Cip1)-like PCNA-binding motif present in the third subunit of human DNA polymerase delta, in mwb58J. Biol. Chem., vol.mwb6a 276, n.mwb6e 52, United States, dicembre 2001, pp.mwb6i 49258–66, mwb6mDOI:mwb6q10.1074/jbc.M106990200, mwb6uISSNmwb6y 0021-9258, mwb64PMIDmwb68 mwb7a11595739.

cite-note-pmid9465025-6161. ↑ mwb7gH Watanabe, Pan Z Q, Schreiber-Agus N, DePinho R A, Hurwitz J, Xiong Y, mwb7kmwb7oSuppression of cell transformation by the cyclin-dependent kinase inhibitor p57KIP2 requires binding to proliferating cell nuclear antigen, in mwb7smwb7wProc. Natl. Acad. Sci. U.S.A., vol.mwb70 95, n.mwb74 4, UNITED STATES, febbraio 1998, pp.mwb78 1392–7, mwb8aDOI:mwb8e10.1073/pnas.95.4.1392, mwb8iISSNmwb8m 0027-8424, mwb8sPMCmwb8w mwb8019016, mwb84PMIDmwb88 mwb9a9465025.

cite-note-pmid11784855-6262. ↑ mwb9yLajos Haracska, Unk Ildiko, Johnson Robert E, Phillips Barbara B, Hurwitz Jerard, Prakash Louise, Prakash Satya, mwb9cmwb9gStimulation of DNA synthesis activity of human DNA polymerase kappa by PCNA, in mwb9kMol. Cell. Biol., vol.mwb9o 22, n.mwb9s 3, United States, febbraio 2002, pp.mwb9w 784–91, mwb90DOI:mwb9410.1128/MCB.22.3.784-791.2002, mwb98ISSNmwb-a 0270-7306, mwb-gPMCmwb-k mwb-o133560, mwb-sPMIDmwb-w mwb-011784855.

cite-note-pmid12368291-6363. ↑ mwb-mGiovanni Maga, Villani Giuseppe, Ramadan Kristijan, Shevelev Igor, Tanguy Le Gac Nicolas, Blanco Luis, Blanca Giuseppina, Spadari Silvio, Hübscher Ulrich, mwb-qmwb-uHuman DNA polymerase lambda functionally and physically interacts with proliferating cell nuclear antigen in normal and translesion DNA synthesis, in mwb-yJ. Biol. Chem., vol.mwb-c 277, n.mwb-g 50, United States, dicembre 2002, pp.mwb-k 48434–40, mwb-oDOI:mwb-s10.1074/jbc.M206889200, mwb-wISSNmwb-0 0021-9258, mwcauPMIDmwcay mwcac12368291.

cite-note-pmid12081642-6464. ↑ mwca0Noriko Shimazaki, Yoshida Kenta, Kobayashi Toshiko, Toji Shingo, Tamai Katsuyuki, Koiwai Osamu, mwca4Over-expression of human DNA polymerase lambda in E. coli and characterization of the recombinant enzyme, in mwca8Genes Cells, vol.mwcba 7, n.mwcbe 7, England, luglio 2002, pp.mwcbi 639–51, mwcbmISSNmwcbq 1356-9597, mwcbwPMIDmwcb0 mwcb412081642.

cite-note-pmid18719106-6565. ↑ mwccqAkira Motegi, Liaw Hung-Jiun, Lee Kyoo-Young, Roest Henk P, Maas Alex, Wu Xiaoli, Moinova Helen, Markowitz Sanford D, Ding Hao, Hoeijmakers Jan H J, Myung Kyungjae, mwccumwccyPolyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks, in mwcccmwccgProc. Natl. Acad. Sci. U.S.A., vol.mwcck 105, n.mwcco 34, United States, agosto 2008, pp.mwccs 12411–6, mwccwDOI:mwcc010.1073/pnas.0805685105, mwcc4PMCmwcc8 mwcda2518831, mwcdePMIDmwcdi mwcdm18719106.

cite-note-pmid18316726-6666. ↑ mwcdkIldiko Unk, Hajdú Ildikó, Fátyol Károly, Hurwitz Jerard, Yoon Jung-Hoon, Prakash Louise, Prakash Satya, Haracska Lajos, mwcdomwcdsHuman HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination, in mwcdwmwcd0Proc. Natl. Acad. Sci. U.S.A., vol.mwcd4 105, n.mwcd8 10, United States, marzo 2008, pp.mwcea 3768–73, mwceeDOI:mwcei10.1073/pnas.0800563105, mwcemPMCmwceq mwceu2268824, mwceyPMIDmwcec mwceg18316726.

cite-note-pmid18284681-6767. ↑ mwce4Jan Brun, Chiu Roland, Lockhart Katherine, Xiao Wei, Wouters Bradly G, Gray Douglas A, mwce8mwcfahMMS2 serves a redundant role in human PCNA polyubiquitination, in mwcfeBMC Mol. Biol., vol.mwcfi 9, England, 2008, p.mwcfm 24, mwcfqDOI:mwcfu10.1186/1471-2199-9-24, mwcfyPMCmwcfc mwcfg2263069, mwcfkPMIDmwcfo mwcfs18284681.

cite-note-pmid16189514-6868. ↑ mwcgeJean-François Rual, Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc, mwcgimwcgmTowards a proteome-scale map of the human protein-protein interaction network, in mwcgqmwcguNature, vol.mwcgy 437, n.mwcgc 7062, England, ottobre 2005, pp.mwcgg 1173–8, mwcgkDOI:mwcgo10.1038/nature04209, mwcgsPMIDmwcgw mwcg016189514.

cite-note-pmid12930846-6969. ↑ mwchmIsabelle Frouin, Maga Giovanni, Denegri Marco, Riva Federica, Savio Monica, Spadari Silvio, Prosperi Ennio, Scovassi A Ivana, mwchqmwchuHuman proliferating cell nuclear antigen, poly(ADP-ribose) polymerase-1, and p21waf1/cip1. A dynamic exchange of partners, in mwchyJ. Biol. Chem., vol.mwchc 278, n.mwchg 41, United States, ottobre 2003, pp.mwchk 39265–8, mwchoDOI:mwchs10.1074/jbc.C300098200, mwchwISSNmwch0 0021-9258, mwciuPMIDmwciy mwcic12930846.

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