During Nucleotide Excision Repair In E. Coli, Which Proteins Identify The Damaged Dna?

PCNA
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4D2G, 1AXC, 1U76, 1U7B, 1UL1, 1VYJ, 1VYM, 1W60, 2ZVK, 2ZVL, 2ZVM, 3P87, 3TBL, 3VKX, 3WGW, 4RJF, 3JA9, 4ZTD, 5IY4, 5E0U, 5E0T, 5E0V
Identifiers
Aliases	PCNA, ATLD2, proliferating cell nuclear antigen
External IDs	OMIM: 176740 MGI: 97503 HomoloGene: 1945 GeneCards: PCNA
Factor location (Homo) Chr. Chromosome 20 (human)[i] Band 20p12.iii Starting time 5,114,953 bp[1] End v,126,626 bp[1]
Factor location (Mouse) Chr. Chromosome 2 (mouse)[two] Ring 2 F2|ii 64.15 cM Start 132,091,082 bp[ii] Terminate 132,095,234 bp[2]
RNA expression blueprint Bgee Top expressed in material anatomical entity bone marrow liver cancellous bone thymus embryo kidney More than reference expression information BioGPS More than reference expression information
Gene ontology Molecular function MutLalpha complex binding identical poly peptide bounden enzyme binding receptor tyrosine kinase bounden Deoxyribonucleic acid binding Deoxyribonucleic acid polymerase binding damaged Dna bounden dinucleotide insertion or deletion bounden Get:0001948 poly peptide binding chromatin binding histone acetyltransferase bounden estrogen receptor binding purine-specific mismatch base pair DNA N-glycosylase activity DNA polymerase processivity factor action Cellular component nucleus replisome nucleoplasm extracellular exosome DNA replication factor C circuitous centrosome PCNA complex nuclear replication fork PCNA-p21 circuitous replication fork nuclear body chromatin Biological process replication fork processing translesion synthesis Deoxyribonucleic acid replication nucleotide-excision repair, DNA gap filling poly peptide sumoylation regulation of DNA replication transcription-coupled nucleotide-excision repair positive regulation of deoxyribonuclease action nucleotide-excision repair, Deoxyribonucleic acid incision error-complimentary translesion synthesis positive regulation of DNA repair regulation of transcription involved in G1/S transition of mitotic cell wheel positive regulation of DNA replication response to lipid heart development DNA mismatch repair cellular response to Dna impairment stimulus mitotic telomere maintenance via semi-bourgeois replication epithelial cell differentiation response to cadmium ion cell population proliferation telomere maintenance fault-prone translesion synthesis cellular response to UV estrous cycle cellular response to hydrogen peroxide response to dexamethasone nucleotide-excision repair, Deoxyribonucleic acid incision, 5'-to lesion liver regeneration response to estradiol response to oxidative stress DNA repair response to L-glutamate Deoxyribonucleic acid damage response, point transduction by p53 class mediator resulting in cell cycle arrest DNA ligation leading strand elongation protein ubiquitination telomere maintenance via semi-conservative replication Become:0022415 viral process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5111	18538
Ensembl	ENSG00000132646	ENSMUSG00000027342
UniProt	P12004	P17918
RefSeq (mRNA)	NM_182649 NM_002592	NM_011045
RefSeq (protein)	NP_002583 NP_872590	NP_035175
Location (UCSC)	Chr 20: five.11 – 5.13 Mb	Chr 2: 132.09 – 132.1 Mb
PubMed search	[iii]	[4]
Wikidata
View/Edit Human being View/Edit Mouse

Cryo-EM structure of the Dna-leap PolD–PCNA processive circuitous

Proliferating cell nuclear antigen (PCNA) is a DNA clamp that acts as a processivity cistron for Deoxyribonucleic acid polymerase δ in eukaryotic cells and is essential for replication. PCNA is a homotrimer and achieves its processivity by encircling the DNA, where it acts as a scaffold to recruit proteins involved in DNA replication, Deoxyribonucleic acid repair, chromatin remodeling and epigenetics.^[5]

Many proteins interact with PCNA via the ii known PCNA-interacting motifs PCNA-interacting peptide (PIP) box^[half-dozen] and AlkB homologue 2 PCNA interacting motif (APIM).^[7] Proteins binding to PCNA via the PIP-box are mainly involved in DNA replication whereas proteins bounden to PCNA via APIM are mainly important in the context of genotoxic stress.^[viii]

Function [edit]

The protein encoded by this cistron is establish in the nucleus and is a cofactor of Deoxyribonucleic acid polymerase delta. The encoded protein acts as a homotrimer and helps increase the processivity of leading strand synthesis during Deoxyribonucleic acid replication. In response to DNA damage, this protein is ubiquitinated and is involved in the RAD6-dependent Dna repair pathway. Two transcript variants encoding the same protein accept been found for this gene. Pseudogenes of this gene accept been described on chromosome 4 and on the X chromosome.^[ix]

Expression in the nucleus during DNA synthesis [edit]

PCNA was originally identified every bit an antigen that is expressed in the nuclei of cells during the Dna synthesis stage of the jail cell cycle.^[10] Part of the poly peptide was sequenced and that sequence was used to allow isolation of a cDNA clone.^[xi] PCNA helps concur Dna polymerase delta (Pol δ) to Deoxyribonucleic acid. PCNA is clamped^[12] to DNA through the activeness of replication factor C (RFC),^[13] which is a heteropentameric fellow member of the AAA+ class of ATPases. Expression of PCNA is under the command of E2F transcription factor-containing complexes.^{[14] [15]}

Part in Deoxyribonucleic acid repair [edit]

Since Dna polymerase epsilon is involved in resynthesis of excised damaged DNA strands during Deoxyribonucleic acid repair, PCNA is important for both DNA synthesis and DNA repair.^{[16] [17]}

PCNA is besides involved in the Deoxyribonucleic acid harm tolerance pathway known as mail service-replication repair (PRR).^[18] In PRR, at that place are two sub-pathways: (1) a translesion pathway, which is carried out past specialised DNA polymerases that are able to incorporate damaged Deoxyribonucleic acid bases into their agile sites (unlike the normal replicative polymerase, which stall), and hence bypass the impairment, and (2) a proposed "template switch" pathway that is idea to involve damage bypass past recruitment of the homologous recombination machinery. PCNA is pivotal to the activation of these pathways and the choice as to which pathway is utilised by the cell. PCNA becomes post-translationally modified past ubiquitin.^[xix] Mono-ubiquitin of lysine number 164 on PCNA activates the translesion synthesis pathway. Extension of this mono-ubiquitin by a non-approved lysine-63-linked poly-ubiquitin concatenation on PCNA^[19] is thought to activate the template switch pathway. Furthermore, sumoylation (by pocket-sized ubiquitin-like modifier, SUMO) of PCNA lysine-164 (and to a lesser extent, lysine-127) inhibits the template switch pathway.^[19] This combative effect occurs because sumoylated PCNA recruits a Deoxyribonucleic acid helicase chosen Srs2,^[xx] which has a part in disrupting Rad51 nucleoprotein filaments central for initiation of homologous recombination.

PCNA-bounden proteins [edit]

PCNA interacts with many proteins.^[21]

• Apoptotic factors
• ATPases
• Base excision repair enzymes
• Cell-cycle regulators
• Chromatin remodeling factor
• Clamp loader
• Cohesin
• DNA ligase
• DNA methyltransferase
• Dna polymerases
• E2 SUMO-conjugating enzyme
• E3 ubiquitin ligases
• Flap endonuclease
• Helicases
• Histone acetyltransferase
• Histone chaperone
• Histone deacetylase
• Mismatch repair enzymes
• NKp44 receptor
• Nucleotide excision repair enzyme
• Poly ADP ribose polymerase
• Procaspases^[22]
• Protein kinases
• Licensing factor
• TCP poly peptide domain
• Topoisomerase

Interactions [edit]

PCNA has been shown to interact with:

• Annexin A2,^[23]
• CAF-1,^{[24] [25] [26]}
• CDC25C,^[27]
• CHTF18,^[23]
• Cyclin D1,^{[28] [29]}
• Cyclin O,^{[23] [30]}
• Cyclin-dependent kinase four,^{[29] [31]}
• Cyclin-dependent kinase inhibitor 1C,^[32]
• DNMT1,^{[33] [34] [35]}
• EP300,^[36]
• Establishment of Sister Chromatid Cohesion 2,^[37]
• Flap structure-specific endonuclease 1,^{[38] [39] [xl] [41] [42] [43] [44]}
• GADD45A,^{[45] [46] [47] [48] [49]}
• GADD45G,^{[50] [51]}
• HDAC1,^[52]
• HUS1,^[53]
• ING1,^[54]
• KCTD13,^[55]
• KIAA0101,^[44]
• Ku70,^{[23] [56]}
• Ku80,^{[23] [56] [57]}
• MCL1,^[58]
• MSH3,^{[23] [59] [sixty]}
• MSH6,^{[23] [59] [60]}
• MUTYH,^[61]
• P21,^{[32] [40] [44] [62] [63] [64] [65] [66]}
• POLD2,^[67]
• POLD3,^{[23] [68]}
• POLDIP2,^[69]
• POLH,^[seventy]
• POLL,^{[71] [72] [73]}
• RFC1,^{[23] [62] [74] [75] [76]}
• RFC2,^{[23] [77] [78]}
• RFC3,^{[23] [79]}
• RFC4,^{[23] [77]}
• RFC5,^{[23] [75] [77]}
• Ubiquitin C^{[80] [81] [82]}
• Werner syndrome ATP-dependent helicase,^{[83] [84]}
• XRCC1,^[85] and
• Y box bounden protein 1.^[86]

Proteins interacting with PCNA via APIM include man AlkB homologue ii, TFIIS-50, TFII-I, Rad51B,^[vii] XPA,^[87] ZRANB3,^[88] and FBH1.^[89]

Uses [edit]

Antibodies against proliferating prison cell nuclear antigen (PCNA) or monoclonal antibiotic termed Ki-67 tin can be used for grading of different neoplasms, due east.grand. astrocytoma. They tin can be of diagnostic and prognostic value. Imaging of the nuclear distribution of PCNA (via antibody labeling) can be used to distinguish betwixt early on, mid and late S phase of the cell cycle.^[90] Notwithstanding, an of import limitation of antibodies is that cells need to exist stock-still leading to potential artifacts.

On the other mitt, the study of the dynamics of replication and repair in living cells tin be done introducing translational fusions of PCNA. To eliminate the demand for transfection and featherbed the problem of difficult to transfect and/or short lived cells, jail cell permeable replication and/or repair markers can be used. These peptides offer the singled-out advantage that can exist used in situ in living tissue and even distinguish cells undergoing replication from cells undergoing repair.^[91]

PCNA is a potential therapeutic target in cancer therapy.^[92]

See also [edit]

• Ki-67 – cellular marker for proliferation
• Transcription

References [edit]

1. ^ ^{a b c} GRCh38: Ensembl release 89: ENSG00000132646 - Ensembl, May 2022
2. ^ ^{a b c} GRCm38: Ensembl release 89: ENSMUSG00000027342 - Ensembl, May 2022
3. ^ "Human PubMed Reference:". National Center for Biotechnology Data, U.South. National Library of Medicine.
4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ Moldovan GL, Pfander B, Jentsch S (May xviii, 2007). "PCNA, the maestro of the replication fork". Cell. 129 (iv): 665–79. doi:ten.1016/j.cell.2007.05.003. PMID 17512402. S2CID 3547069.
6. ^ Warbrick E (Mar 1998). "PCNA bounden through a conserved motif". BioEssays. 20 (three): 195–9. doi:10.1002/(sici)1521-1878(199803)20:3<195::help-bies2>3.0.co;2-r. PMID 9631646.
7. ^ ^{a b} Gilljam KM, Feyzi East, Aas PA, Sousa MM, Müller R, Vågbø CB, Catterall TC, Liabakk NB, Slupphaug G, Drabløs F, Krokan HE, Otterlei Yard (Sep 7, 2009). "Identification of a novel, widespread, and functionally important PCNA-bounden motif". The Journal of Prison cell Biological science. 186 (5): 645–54. doi:10.1083/jcb.200903138. PMC2742182. PMID 19736315.
8. ^ Mailand N, Gibbs-Seymour I, Bekker-Jensen Due south (May 2022). "Regulation of PCNA-protein interactions for genome stability". Nature Reviews Molecular Prison cell Biology. 14 (v): 269–82. doi:10.1038/nrm3562. PMID 23594953. S2CID 25952152.
9. ^ "Entrez Gene: PCNA proliferating cell nuclear antigen".
10. ^ Leonardi Due east, Girlando S, Serio G, Mauri FA, Perrone M, Scampini Due south, Dalla Palma P, Barbareschi M (1992). "PCNA and Ki67 expression in breast carcinoma: correlations with clinical and biological variables". J. Clin. Pathol. 45 (5): 416–419. doi:10.1136/jcp.45.five.416. PMC495304. PMID 1350788.
11. ^ Matsumoto 1000, Moriuchi T, Koji T, Nakane PK (1987). "Molecular cloning of cDNA coding for rat proliferating cell nuclear antigen (PCNA)/cyclin". EMBO J. 6 (3): 637–42. doi:ten.1002/j.1460-2075.1987.tb04802.x. PMC553445. PMID 2884104.
12. ^ Bowman GD, O'Donnell M, Kuriyan J (2004). "Structural analysis of a eukaryotic sliding DNA clench-clamp loader complex". Nature. 429 (6993): 724–730. Bibcode:2004Natur.429..724B. doi:10.1038/nature02585. PMID 15201901. S2CID 4346799.
13. ^ Zhang G, Gibbs Due east, Kelman Z, O'Donnell K, Hurwitz J (1999). "Studies on the interactions between human replication factor C and human proliferating prison cell nuclear antigen". Proc. Natl. Acad. Sci. U.S.A. 96 (5): 1869–1874. Bibcode:1999PNAS...96.1869Z. doi:10.1073/pnas.96.5.1869. PMC26703. PMID 10051561.
14. ^ Egelkrout EM, Mariconti L, Settlage SB, Cella R, Robertson D, Hanley-Bowdoin L (2002). "Two E2F elements regulate the proliferating cell nuclear antigen promoter differently during foliage development". Establish Cell. 14 (12): 3225–3236. doi:10.1105/tpc.006403. PMC151214. PMID 12468739.
15. ^ Nikolai BC, Lanz RB, York B, Dasgupta S, Mitsiades N, Creighton CJ, Tsimelzon A, Hilsenbeck SG, Lonard DM, Smith CL, O'Malley BW (15 March 2022). "HER2 Signaling Drives Deoxyribonucleic acid Anabolism and Proliferation through SRC-iii Phosphorylation and E2F1-Regulated Genes". Cancer Res. 76 (6): 1463–75. doi:10.1158/0008-5472.CAN-15-2383. PMC4794399. PMID 26833126.
16. ^ Shivji KK, Kenny MK, Wood RD (April 1992). "Proliferating cell nuclear antigen is required for DNA excision repair". Cell. 69 (2): 367–74. doi:ten.1016/0092-8674(92)90416-A. PMID 1348971. S2CID 12260457.
17. ^ Essers J, Theil AF, Baldeyron C, van Cappellen WA, Houtsmuller AB, Kanaar R, Vermeulen Westward (2005). "Nuclear dynamics of PCNA in DNA replication and repair". Mol. Cell. Biol. 25 (21): 9350–9359. doi:10.1128/MCB.25.21.9350-9359.2005. PMC1265825. PMID 16227586.
18. ^ Lehmann AR, Fuchs RP (Dec 2006). "Gaps and forks in Dna replication: Rediscovering old models" (PDF). Deoxyribonucleic acid Repair (Amst.). 5 (12): 1495–1498. doi:10.1016/j.dnarep.2006.07.002. PMID 16956796.
19. ^ ^{a b c} Hoege C, Pfander B, Moldovan GL, Pyrowolakis G, Jentsch S (September 2002). "RAD6-dependent Dna repair is linked to modification of PCNA by ubiquitin and SUMO". Nature. 419 (6903): 135–141. Bibcode:2002Natur.419..135H. doi:ten.1038/nature00991. PMID 12226657. S2CID 205209495.
20. ^ Pfander B, Moldovan GL, Sacher K, Hoege C, Jentsch S (July 2005). "SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase". Nature. 436 (7049): 428–33. Bibcode:2005Natur.436..428P. doi:x.1038/nature03665. PMID 15931174. S2CID 4316517.
21. ^ Moldovan GL, Pfander B, Jentsch Due south (2007). "PCNA, the maestro of the replication fork". Cell. 129 (4): 665–679. doi:x.1016/j.cell.2007.05.003. PMID 17512402. S2CID 3547069.
22. ^ Witko-Sarsat Five, Mocek J, Bouayad D, Tamassia Northward, Ribeil JA, Candalh C, Davezac North, Reuter N, Mouthon L, Hermine O, Pederzoli-Ribeil M, Cassatella MA (Nov 22, 2010). "Proliferating jail cell nuclear antigen acts as a cytoplasmic platform decision-making human neutrophil survival". The Periodical of Experimental Medicine. 207 (12): 2631–45. doi:10.1084/jem.20092241. PMC2989777. PMID 20975039.
23. ^ ^{a b c d e f thou h i j k l thousand} Ohta S, Shiomi Y, Sugimoto Grand, Obuse C, Tsurimoto T (October 2002). "A proteomics arroyo to identify proliferating cell nuclear antigen (PCNA)-binding proteins in human cell lysates. Identification of the human CHL12/RFCs2-v complex as a novel PCNA-binding protein". J. Biol. Chem. 277 (43): 40362–vii. doi:10.1074/jbc.M206194200. PMID 12171929.
24. ^ Zhang G, Gao Y, Li J, Burgess R, Han J, Liang H, Zhang Z, Liu Y (June 2022). "A Dna binding winged helix domain in CAF-i functions with PCNA to stabilize CAF-1 at replication forks". Nucleic Acids Research. 44 (11): 5083–94. doi:x.1093/nar/gkw106. PMC4914081. PMID 26908650.
25. ^ Moggs JG, Grandi P, Quivy JP, Jónsson ZO, Hübscher U, Becker PB, Almouzni Yard (February 2000). "A CAF-1-PCNA-mediated chromatin assembly pathway triggered by sensing Dna damage". Molecular and Cellular Biological science. xx (4): 1206–xviii. doi:10.1128/mcb.xx.4.1206-1218.2000. PMC85246. PMID 10648606.
26. ^ Rolef Ben-Shahar T, Castillo AG, Osborne MJ, Borden KL, Kornblatt J, Verreault A (December 2009). "Two fundamentally distinct PCNA interaction peptides contribute to chromatin assembly factor ane office". Molecular and Cellular Biology. 29 (24): 6353–65. doi:10.1128/MCB.01051-09. PMC2786881. PMID 19822659.
27. ^ Kawabe T, Suganuma Yard, Ando T, Kimura Yard, Hori H, Okamoto T (March 2002). "Cdc25C interacts with PCNA at G2/Thou transition". Oncogene. 21 (11): 1717–26. doi:10.1038/sj.onc.1205229. PMID 11896603.
28. ^ Matsuoka S, Yamaguchi 1000, Matsukage A (April 1994). "D-blazon cyclin-bounden regions of proliferating jail cell nuclear antigen". J. Biol. Chem. 269 (xv): 11030–six. doi:10.1016/S0021-9258(19)78087-9. PMID 7908906.
29. ^ ^{a b} Xiong Y, Zhang H, Embankment D (Baronial 1993). "Subunit rearrangement of the cyclin-dependent kinases is associated with cellular transformation". Genes Dev. 7 (viii): 1572–83. doi:10.1101/gad.7.viii.1572. PMID 8101826.
30. ^ Otterlei Grand, Warbrick East, Nagelhus TA, Haug T, Slupphaug Yard, Akbari 1000, Aas PA, Steinsbekk K, Bakke O, Krokan HE (July 1999). "Postal service-replicative base excision repair in replication foci". EMBO J. 18 (13): 3834–44. doi:10.1093/emboj/18.13.3834. PMC1171460. PMID 10393198.
31. ^ Serrano M, Hannon GJ, Beach D (Dec 1993). "A new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4". Nature. 366 (6456): 704–seven. Bibcode:1993Natur.366..704S. doi:10.1038/366704a0. PMID 8259215. S2CID 4368128.
32. ^ ^{a b} Watanabe H, Pan ZQ, Schreiber-Agus N, DePinho RA, Hurwitz J, Xiong Y (February 1998). "Suppression of prison cell transformation by the cyclin-dependent kinase inhibitor p57KIP2 requires binding to proliferating cell nuclear antigen". Proc. Natl. Acad. Sci. U.S.A. 95 (iv): 1392–7. Bibcode:1998PNAS...95.1392W. doi:ten.1073/pnas.95.4.1392. PMC19016. PMID 9465025.
33. ^ Rountree MR, Bachman KE, Baylin SB (July 2000). "DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci". Nat. Genet. 25 (3): 269–77. doi:10.1038/77023. PMID 10888872. S2CID 26149386.
34. ^ Iida T, Suetake I, Tajima S, Morioka H, Ohta Due south, Obuse C, Tsurimoto T (Oct 2002). "PCNA clamp facilitates activity of Deoxyribonucleic acid cytosine methyltransferase 1 on hemimethylated DNA". Genes Cells. 7 (x): 997–1007. doi:x.1046/j.1365-2443.2002.00584.ten. PMID 12354094. S2CID 25310911.
35. ^ Chuang LS, Ian Hi, Koh TW, Ng HH, Xu G, Li BF (September 1997). "Human DNA-(cytosine-v) methyltransferase-PCNA circuitous as a target for p21WAF1". Scientific discipline. 277 (5334): 1996–2000. doi:ten.1126/science.277.5334.1996. PMID 9302295.
36. ^ Hasan Southward, Hassa PO, Imhof R, Hottiger MO (March 2001). "Transcription coactivator p300 binds PCNA and may take a role in DNA repair synthesis". Nature. 410 (6826): 387–91. Bibcode:2001Natur.410..387H. doi:10.1038/35066610. PMID 11268218. S2CID 2129847.
37. ^ Bender D, De Silva E, Chen J, Poss A, Gawey L, Rulon Z, Rankin, S (December 2022). "Multivalent interaction of ESCO2 with replication machinery is required for sister chromatid cohesion in vertebrates". Proc. Natl. Acad. Sci. U.s.a.A. 117 (ii): 1081–1089. doi:x.1073/pnas.1911936117. PMC6969535. PMID 31879348.
38. ^ Henneke G, Koundrioukoff S, Hübscher U (July 2003). "Phosphorylation of human being Fen1 by cyclin-dependent kinase modulates its role in replication fork regulation". Oncogene. 22 (28): 4301–13. doi:10.1038/sj.onc.1206606. PMID 12853968.
39. ^ Hasan Southward, Stucki Grand, Hassa PO, Imhof R, Gehrig P, Hunziker P, Hübscher U, Hottiger MO (June 2001). "Regulation of human flap endonuclease-1 action by acetylation through the transcriptional coactivator p300". Mol. Cell. 7 (6): 1221–31. doi:10.1016/s1097-2765(01)00272-six. PMID 11430825.
40. ^ ^{a b} Jónsson ZO, Hindges R, Hübscher U (April 1998). "Regulation of Deoxyribonucleic acid replication and repair proteins through interaction with the front side of proliferating prison cell nuclear antigen". EMBO J. 17 (8): 2412–25. doi:x.1093/emboj/17.eight.2412. PMC1170584. PMID 9545252.
41. ^ Gary R, Ludwig DL, Cornelius HL, MacInnes MA, Park MS (September 1997). "The Deoxyribonucleic acid repair endonuclease XPG binds to proliferating prison cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-one and cyclin-dependent kinase inhibitor p21". J. Biol. Chem. 272 (39): 24522–ix. doi:10.1074/jbc.272.39.24522. PMID 9305916.
42. ^ Chen U, Chen Southward, Saha P, Dutta A (October 1996). "p21Cip1/Waf1 disrupts the recruitment of human Fen1 by proliferating-cell nuclear antigen into the Deoxyribonucleic acid replication circuitous". Proc. Natl. Acad. Sci. U.S.A. 93 (21): 11597–602. Bibcode:1996PNAS...9311597C. doi:10.1073/pnas.93.21.11597. PMC38103. PMID 8876181.
43. ^ Dianova II, Bohr VA, Dianov GL (October 2001). "Interaction of human AP endonuclease i with flap endonuclease i and proliferating cell nuclear antigen involved in long-patch base of operations excision repair". Biochemistry. twoscore (42): 12639–44. doi:ten.1021/bi011117i. PMID 11601988.
44. ^ ^{a b c} Yu P, Huang B, Shen M, Lau C, Chan E, Michel J, Xiong Y, Payan DG, Luo Y (Jan 2001). "p15(PAF), a novel PCNA associated factor with increased expression in tumor tissues". Oncogene. 20 (4): 484–9. doi:10.1038/sj.onc.1204113. PMID 11313979.
45. ^ Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ (November 1994). "Interaction of the p53-regulated poly peptide Gadd45 with proliferating prison cell nuclear antigen". Science (Submitted manuscript). 266 (5189): 1376–fourscore. Bibcode:1994Sci...266.1376S. doi:x.1126/science.7973727. PMID 7973727.
46. ^ Chen It, Smith ML, O'Connor PM, Fornace AJ (November 1995). "Direct interaction of Gadd45 with PCNA and evidence for competitive interaction of Gadd45 and p21Waf1/Cip1 with PCNA". Oncogene. eleven (10): 1931–7. PMID 7478510.
47. ^ Vairapandi 1000, Azam N, Balliet AG, Hoffman B, Liebermann DA (June 2000). "Characterization of MyD118, Gadd45, and proliferating cell nuclear antigen (PCNA) interacting domains. PCNA impedes MyD118 AND Gadd45-mediated negative growth control". J. Biol. Chem. 275 (22): 16810–9. doi:10.1074/jbc.275.22.16810. PMID 10828065.
48. ^ Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick East, Cox LS (June 1995). "Characterisation of the interaction betwixt PCNA and Gadd45". Oncogene. 10 (12): 2427–33. PMID 7784094.
49. ^ Yang Q, Manicone A, Coursen JD, Linke SP, Nagashima M, Forgues Thou, Wang XW (Nov 2000). "Identification of a functional domain in a GADD45-mediated G2/Thousand checkpoint". J. Biol. Chem. 275 (47): 36892–8. doi:x.1074/jbc.M005319200. PMID 10973963.
50. ^ Azam N, Vairapandi Grand, Zhang W, Hoffman B, Liebermann DA (Jan 2001). "Interaction of CR6 (GADD45gamma ) with proliferating jail cell nuclear antigen impedes negative growth command". J. Biol. Chem. 276 (4): 2766–74. doi:10.1074/jbc.M005626200. PMID 11022036.
51. ^ Nakayama K, Hara T, Hibi Thou, Hirano T, Miyajima A (Baronial 1999). "A novel oncostatin M-inducible cistron OIG37 forms a gene family with MyD118 and GADD45 and negatively regulates prison cell growth". J. Biol. Chem. 274 (35): 24766–72. doi:ten.1074/jbc.274.35.24766. PMID 10455148.
52. ^ Milutinovic S, Zhuang Q, Szyf K (June 2002). "Proliferating cell nuclear antigen associates with histone deacetylase activity, integrating Dna replication and chromatin modification". J. Biol. Chem. 277 (23): 20974–8. doi:x.1074/jbc.M202504200. PMID 11929879.
53. ^ Komatsu K, Wharton Due west, Hang H, Wu C, Singh S, Lieberman HB, Pledger WJ, Wang HG (Nov 2000). "PCNA interacts with hHus1/hRad9 in response to DNA impairment and replication inhibition". Oncogene. xix (46): 5291–7. doi:10.1038/sj.onc.1203901. PMID 11077446.
54. ^ Scott Thousand, Bonnefin P, Vieyra D, Boisvert FM, Young D, Bazett-Jones DP, Riabowol K (October 2001). "UV-induced binding of ING1 to PCNA regulates the consecration of apoptosis". J. Prison cell Sci. 114 (Pt 19): 3455–62. doi:10.1242/jcs.114.nineteen.3455. PMID 11682605.
55. ^ He H, Tan CK, Downey KM, So AG (October 2001). "A tumor necrosis factor alpha- and interleukin half dozen-inducible protein that interacts with the minor subunit of Deoxyribonucleic acid polymerase delta and proliferating cell nuclear antigen". Proc. Natl. Acad. Sci. U.s.A. 98 (21): 11979–84. Bibcode:2001PNAS...9811979H. doi:10.1073/pnas.221452098. PMC59753. PMID 11593007.
56. ^ ^{a b} Balajee Every bit, Geard CR (March 2001). "Chromatin-bound PCNA complex formation triggered past DNA damage occurs independent of the ATM gene product in human cells". Nucleic Acids Res. 29 (6): 1341–51. doi:10.1093/nar/29.6.1341. PMC29758. PMID 11239001.
57. ^ Matheos D, Ruiz MT, Price GB, Zannis-Hadjopoulos 1000 (October 2002). "Ku antigen, an origin-specific binding protein that assembly with replication proteins, is required for mammalian DNA replication". Biochim. Biophys. Acta. 1578 (1–3): 59–72. doi:ten.1016/s0167-4781(02)00497-9. PMID 12393188.
58. ^ Fujise K, Zhang D, Liu J, Yeh ET (December 2000). "Regulation of apoptosis and cell cycle progression by MCL1. Differential role of proliferating cell nuclear antigen". J. Biol. Chem. 275 (50): 39458–65. doi:10.1074/jbc.M006626200. PMID 10978339.
59. ^ ^{a b} Kleczkowska HE, Marra Yard, Lettieri T, Jiricny J (March 2001). "hMSH3 and hMSH6 interact with PCNA and colocalize with information technology to replication foci". Genes Dev. 15 (6): 724–36. doi:x.1101/gad.191201. PMC312660. PMID 11274057.
60. ^ ^{a b} Clark AB, Valle F, Drotschmann G, Gary RK, Kunkel TA (November 2000). "Functional interaction of proliferating cell nuclear antigen with MSH2-MSH6 and MSH2-MSH3 complexes". J. Biol. Chem. 275 (47): 36498–501. doi:10.1074/jbc.C000513200. PMID 11005803.
61. ^ Parker A, Gu Y, Mahoney W, Lee SH, Singh KK, Lu AL (Feb 2001). "Human being homolog of the MutY repair protein (hMYH) physically interacts with proteins involved in long patch DNA base excision repair". J. Biol. Chem. 276 (8): 5547–55. doi:x.1074/jbc.M008463200. PMID 11092888.
62. ^ ^{a b} Fotedar R, Mossi R, Fitzgerald P, Rousselle T, Maga Yard, Brickner H, Messier H, Kasibhatla S, Hübscher U, Fotedar A (Baronial 1996). "A conserved domain of the large subunit of replication factor C binds PCNA and acts like a dominant negative inhibitor of Deoxyribonucleic acid replication in mammalian cells". EMBO J. 15 (16): 4423–33. doi:10.1002/j.1460-2075.1996.tb00815.ten. PMC452166. PMID 8861969.
63. ^ Rual JF, Venkatesan Chiliad, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze 1000, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem Grand, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin Yard, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human poly peptide-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
64. ^ Frouin I, Maga G, Denegri Chiliad, Riva F, Savio K, Spadari S, Prosperi Eastward, Scovassi AI (October 2003). "Human being proliferating jail cell nuclear antigen, poly(ADP-ribose) polymerase-1, and p21waf1/cip1. A dynamic exchange of partners". J. Biol. Chem. 278 (41): 39265–viii. doi:10.1074/jbc.C300098200. PMID 12930846.
65. ^ Gulbis JM, Kelman Z, Hurwitz J, O'Donnell 1000, Kuriyan J (October 1996). "Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA". Cell. 87 (2): 297–306. doi:x.1016/s0092-8674(00)81347-1. PMID 8861913. S2CID 17461501.
66. ^ Touitou R, Richardson J, Bose Due south, Nakanishi M, Rivett J, Allday MJ (May 2001). "A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome". EMBO J. 20 (ten): 2367–75. doi:10.1093/emboj/20.x.2367. PMC125454. PMID 11350925.
67. ^ Lu X, Tan CK, Zhou JQ, You 1000, Carastro LM, Downey KM, And so AG (July 2002). "Direct interaction of proliferating cell nuclear antigen with the pocket-size subunit of DNA polymerase delta". J. Biol. Chem. 277 (27): 24340–5. doi:10.1074/jbc.M200065200. PMID 11986310.
68. ^ Ducoux M, Urbach S, Baldacci G, Hübscher U, Koundrioukoff South, Christensen J, Hughes P (December 2001). "Mediation of proliferating jail cell nuclear antigen (PCNA)-dependent DNA replication through a conserved p21(Cip1)-like PCNA-binding motif present in the tertiary subunit of human DNA polymerase delta". J. Biol. Chem. 276 (52): 49258–66. doi:10.1074/jbc.M106990200. PMID 11595739.
69. ^ Liu L, Rodriguez-Belmonte EM, Mazloum N, Xie B, Lee MY (March 2003). "Identification of a novel protein, PDIP38, that interacts with the p50 subunit of Dna polymerase delta and proliferating cell nuclear antigen". J. Biol. Chem. 278 (12): 10041–7. doi:10.1074/jbc.M208694200. PMID 12522211.
70. ^ Haracska L, Johnson RE, Unk I, Phillips B, Hurwitz J, Prakash 50, Prakash Due south (Nov 2001). "Concrete and functional interactions of human being Dna polymerase eta with PCNA". Mol. Jail cell. Biol. 21 (21): 7199–206. doi:10.1128/MCB.21.21.7199-7206.2001. PMC99895. PMID 11585903.
71. ^ Haracska L, Unk I, Johnson RE, Phillips BB, Hurwitz J, Prakash L, Prakash S (Feb 2002). "Stimulation of DNA synthesis action of homo Deoxyribonucleic acid polymerase kappa by PCNA". Mol. Cell. Biol. 22 (3): 784–91. doi:10.1128/mcb.22.3.784-791.2002. PMC133560. PMID 11784855.
72. ^ Maga G, Villani G, Ramadan Yard, Shevelev I, Tanguy Le Gac N, Blanco L, Blanca Grand, Spadari South, Hübscher U (Dec 2002). "Homo DNA polymerase lambda functionally and physically interacts with proliferating cell nuclear antigen in normal and translesion DNA synthesis". J. Biol. Chem. 277 (50): 48434–40. doi:10.1074/jbc.M206889200. PMID 12368291.
73. ^ Shimazaki N, Yoshida Grand, Kobayashi T, Toji S, Tamai K, Koiwai O (July 2002). "Over-expression of human Dna polymerase lambda in Eastward. coli and characterization of the recombinant enzyme". Genes Cells. 7 (seven): 639–51. doi:10.1046/j.1365-2443.2002.00547.x. PMID 12081642. S2CID 29714829.
74. ^ Maruyama T, Farina A, Dey A, Cheong J, Bermudez VP, Tamura T, Sciortino S, Shuman J, Hurwitz J, Ozato K (September 2002). "A Mammalian bromodomain protein, brd4, interacts with replication gene C and inhibits progression to Due south phase". Mol. Jail cell. Biol. 22 (eighteen): 6509–20. doi:10.1128/mcb.22.18.6509-6520.2002. PMC135621. PMID 12192049.
75. ^ ^{a b} Mossi R, Jónsson ZO, Allen BL, Hardin SH, Hübscher U (January 1997). "Replication factor C interacts with the C-terminal side of proliferating prison cell nuclear antigen". J. Biol. Chem. 272 (3): 1769–76. doi:10.1074/jbc.272.3.1769. PMID 8999859.
76. ^ van der Kuip H, Carius B, Haque SJ, Williams BR, Huber C, Fischer T (April 1999). "The DNA-binding subunit p140 of replication cistron C is upregulated in cycling cells and associates with G1 stage cell bike regulatory proteins". J. Mol. Med. 77 (4): 386–92. doi:ten.1007/s001090050365. PMID 10353443. S2CID 22183443.
77. ^ ^{a b c} Cai J, Gibbs East, Uhlmann F, Phillips B, Yao N, O'Donnell M, Hurwitz J (July 1997). "A circuitous consisting of human replication factor C p40, p37, and p36 subunits is a Deoxyribonucleic acid-dependent ATPase and an intermediate in the assembly of the holoenzyme". J. Biol. Chem. 272 (30): 18974–81. doi:ten.1074/jbc.272.30.18974. PMID 9228079.
78. ^ Pan ZQ, Chen G, Hurwitz J (January 1993). "The subunits of activator one (replication factor C) carry out multiple functions essential for proliferating-cell nuclear antigen-dependent Dna synthesis". Proc. Natl. Acad. Sci. UsA. ninety (one): half dozen–10. Bibcode:1993PNAS...90....6P. doi:ten.1073/pnas.ninety.1.6. PMC45588. PMID 8093561.
79. ^ Merkle CJ, Karnitz LM, Henry-Sánchez JT, Chen J (August 2003). "Cloning and characterization of hCTF18, hCTF8, and hDCC1. Homo homologs of a Saccharomyces cerevisiae complex involved in sister chromatid cohesion institution". J. Biol. Chem. 278 (32): 30051–6. doi:10.1074/jbc.M211591200. PMID 12766176.
80. ^ Motegi A, Liaw HJ, Lee KY, Roest HP, Maas A, Wu X, Moinova H, Markowitz SD, Ding H, Hoeijmakers JH, Myung Thousand (Baronial 2008). "Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks". Proc. Natl. Acad. Sci. U.Southward.A. 105 (34): 12411–vi. Bibcode:2008PNAS..10512411M. doi:10.1073/pnas.0805685105. PMC2518831. PMID 18719106.
81. ^ Unk I, Hajdú I, Fátyol K, Hurwitz J, Yoon JH, Prakash L, Prakash S, Haracska Fifty (March 2008). "Human HLTF functions every bit a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination". Proc. Natl. Acad. Sci. UsA. 105 (10): 3768–73. Bibcode:2008PNAS..105.3768U. doi:10.1073/pnas.0800563105. PMC2268824. PMID 18316726.
82. ^ Brun J, Chiu R, Lockhart One thousand, Xiao Westward, Wouters BG, Gray DA (2008). "hMMS2 serves a redundant role in man PCNA polyubiquitination". BMC Mol. Biol. ix: 24. doi:ten.1186/1471-2199-nine-24. PMC2263069. PMID 18284681.
83. ^ Rodríguez-López AM, Jackson DA, Nehlin JO, Iborra F, Warren AV, Cox LS (Feb 2003). "Characterisation of the interaction between WRN, the helicase/exonuclease defective in progeroid Werner's syndrome, and an essential replication factor, PCNA". Mech. Ageing Dev. 124 (2): 167–74. doi:10.1016/s0047-6374(02)00131-8. PMID 12633936. S2CID 37287691.
84. ^ Huang S, Beresten S, Li B, Oshima J, Ellis NA, Campisi J (June 2000). "Label of the human and mouse WRN three'-->5' exonuclease". Nucleic Acids Res. 28 (12): 2396–405. doi:ten.1093/nar/28.12.2396. PMC102739. PMID 10871373.
85. ^ Fan J, Otterlei Thou, Wong HK, Tomkinson AE, Wilson DM (2004). "XRCC1 co-localizes and physically interacts with PCNA". Nucleic Acids Res. 32 (vii): 2193–201. doi:10.1093/nar/gkh556. PMC407833. PMID 15107487.
86. ^ Ise T, Nagatani G, Imamura T, Kato M, Takano H, Nomoto M, Izumi H, Ohmori H, Okamoto T, Ohga T, Uchiumi T, Kuwano Thousand, Kohno Thousand (January 1999). "Transcription factor Y-box binding protein 1 binds preferentially to cisplatin-modified Dna and interacts with proliferating cell nuclear antigen". Cancer Res. 59 (2): 342–6. PMID 9927044.
87. ^ Gilljam KM, Müller R, Liabakk NB, Otterlei M (2012). "Nucleotide excision repair is associated with the replisome and its efficiency depends on a direct interaction betwixt XPA and PCNA". PLOS I. 7 (xi): e49199. Bibcode:2012PLoSO...749199G. doi:10.1371/periodical.pone.0049199. PMC3496702. PMID 23152873.
88. ^ Ciccia A, Nimonkar AV, Hu Y, Hajdu I, Achar YJ, Izhar L, Petit SA, Adamson B, Yoon JC, Kowalczykowski SC, Livingston DM, Haracska L, Elledge SJ (Aug 10, 2022). "Polyubiquitinated PCNA recruits the ZRANB3 translocase to maintain genomic integrity after replication stress". Molecular Cell. 47 (3): 396–409. doi:10.1016/j.molcel.2012.05.024. PMC3613862. PMID 22704558.
89. ^ Bacquin A, Pouvelle C, Siaud N, Perderiset M, Salomé-Desnoulez S, Tellier-Lebegue C, Lopez B, Charbonnier JB, Kannouche PL (Jul 2022). "The helicase FBH1 is tightly regulated by PCNA via CRL4(Cdt2)-mediated proteolysis in human cells". Nucleic Acids Research. 41 (xiii): 6501–13. doi:10.1093/nar/gkt397. PMC3711418. PMID 23677613.
90. ^ Schönenberger F, Deutzmann A, Ferrando-May East, Merhof D (29 May 2022). "Bigotry of cell cycle phases in PCNA-immunolabeled cells". BMC Bioinform. xvi (180): 180. doi:x.1186/s12859-015-0618-9. PMC4448323. PMID 26022740.
91. ^ Herce HD, Rajan Grand, Lättig-Tünnemann G, Fillies M, Cardoso MC (three September 2022). "A novel jail cell permeable Dna replication and repair mark". Nucleus (Austin, Tex.). 5 (6): 590–600. doi:10.4161/nucl.36290. PMC4615156. PMID 25484186.
92. ^ Wang SC (April 2022). "PCNA: a silent housekeeper or a potential therapeutic target?". Trends in Pharmacological Sciences. 35 (4): 178–186. doi:10.1016/j.tips.2014.02.004. PMID 24655521.

Further reading [edit]

• Prosperi Due east (1998). "Multiple roles of the proliferating prison cell nuclear antigen: DNA replication, repair and cell cycle control". Progress in Cell Bicycle Research. Vol. 3. pp. 193–210. doi:10.1007/978-1-4615-5371-7_15. ISBN978-1-4613-7451-0. PMID 9552415.
• Miura M (1999). "Detection of chromatin-bound PCNA in mammalian cells and its utilise to study DNA excision repair". J. Radiat. Res. forty (1): 1–12. Bibcode:1999JRadR..40....1M. doi:10.1269/jrr.40.1. PMID 10408173.
• Chen K, Pan ZQ, Hurwitz J (1992). "Sequence and expression in Escherichia coli of the 40-kDa subunit of activator 1 (replication factor C) of HeLa cells". Proc. Natl. Acad. Sci. U.S.A. 89 (7): 2516–2520. Bibcode:1992PNAS...89.2516C. doi:10.1073/pnas.89.7.2516. PMC48692. PMID 1313560.
• Kemeny MM, Alava G, Oliver JM (1993). "Improving responses in hepatomas with circadian-patterned hepatic artery infusions of recombinant interleukin-2". J. Immunother. 12 (4): 219–223. doi:10.1097/00002371-199211000-00001. PMID 1477073.
• Morris GF, Mathews MB (1990). "Assay of the proliferating jail cell nuclear antigen promoter and its response to adenovirus early region 1". J. Biol. Chem. 265 (27): 16116–25. doi:ten.1016/S0021-9258(17)46196-5. PMID 1975809.
• Webb G, Parsons P, Chenevix-Trench G (1991). "Localization of the gene for human proliferating nuclear antigen/cyclin by in situ hybridization". Hum. Genet. 86 (i): 84–half-dozen. doi:x.1007/bf00205180. PMID 1979311. S2CID 27107553.
• Travali S, Ku DH, Rizzo MG, Ottavio L, Baserga R, Calabretta B (1989). "Structure of the human being gene for the proliferating cell nuclear antigen". J. Biol. Chem. 264 (13): 7466–72. doi:x.1016/S0021-9258(18)83257-4. PMID 2565339.
• Ku DH, Travali S, Calabretta B, Huebner Thousand, Baserga R (1989). "Human being factor for proliferating cell nuclear antigen has pseudogenes and localizes to chromosome 20". Somat. Cell Mol. Genet. 15 (iv): 297–307. doi:x.1007/BF01534969. PMID 2569765. S2CID 27217843.
• Prelich G, Kostura M, Marshak DR, Mathews MB, Stillman B (1987). "The prison cell-bicycle regulated proliferating cell nuclear antigen is required for SV40 Deoxyribonucleic acid replication in vitro". Nature. 326 (6112): 471–5. Bibcode:1987Natur.326..471P. doi:10.1038/326471a0. PMID 2882422. S2CID 4336365.
• Almendral JM, Huebsch D, Blundell PA, Macdonald-Bravo H, Bravo R (1987). "Cloning and sequence of the human nuclear poly peptide cyclin: homology with Deoxyribonucleic acid-binding proteins". Proc. Natl. Acad. Sci. U.S.A. 84 (vi): 1575–nine. Bibcode:1987PNAS...84.1575A. doi:10.1073/pnas.84.half dozen.1575. PMC304478. PMID 2882507.
• Chen IT, Smith ML, O'Connor PM, Fornace AJ (1995). "Direct interaction of Gadd45 with PCNA and testify for competitive interaction of Gadd45 and p21Waf1/Cip1 with PCNA". Oncogene. 11 (10): 1931–7. PMID 7478510.
• Li X, Li J, Harrington J, Lieber MR, Burgers PM (1995). "Lagging strand Deoxyribonucleic acid synthesis at the eukaryotic replication fork involves binding and stimulation of FEN-1 by proliferating jail cell nuclear antigen". J. Biol. Chem. 270 (38): 22109–12. doi:10.1074/jbc.270.38.22109. PMID 7673186.
• Fukuda K, Morioka H, Imajou S, Ikeda Due south, Ohtsuka E, Tsurimoto T (1995). "Structure-part relationship of the eukaryotic DNA replication cistron, proliferating cell nuclear antigen". J. Biol. Chem. 270 (38): 22527–34. doi:10.1074/jbc.270.38.22527. PMID 7673244.
• Warbrick E, Lane DP, Glover DM, Cox LS (1995). "A pocket-sized peptide inhibitor of DNA replication defines the site of interaction between the cyclin-dependent kinase inhibitor p21WAF1 and proliferating cell nuclear antigen". Curr. Biol. 5 (3): 275–282. doi:10.1016/S0960-9822(95)00058-3. PMID 7780738. S2CID 1559243.
• Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick East, Cox LS (1995). "Characterisation of the interaction betwixt PCNA and Gadd45". Oncogene. 10 (12): 2427–33. PMID 7784094.
• Kato S, Sekine Southward, Oh SW, Kim NS, Umezawa Y, Abe N, Yokoyama-Kobayashi M, Aoki T (1995). "Structure of a man full-length cDNA banking company". Gene. 150 (ii): 243–50. doi:x.1016/0378-1119(94)90433-2. PMID 7821789.
• Matsuoka Due south, Yamaguchi Thou, Matsukage A (1994). "D-type cyclin-binding regions of proliferating cell nuclear antigen". J. Biol. Chem. 269 (15): 11030–6. doi:10.1016/S0021-9258(19)78087-nine. PMID 7908906.
• Szepesi A, Gelfand EW, Lucas JJ (1994). "Clan of proliferating jail cell nuclear antigen with cyclin-dependent kinases and cyclins in normal and transformed human T lymphocytes". Blood. 84 (10): 3413–21. doi:10.1182/blood.V84.ten.3413.3413. PMID 7949095.
• Smith ML, Chen Information technology, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ (1994). "Interaction of the p53-regulated poly peptide Gadd45 with proliferating cell nuclear antigen". Science (Submitted manuscript). 266 (5189): 1376–80. Bibcode:1994Sci...266.1376S. doi:10.1126/science.7973727. PMID 7973727.
• Pan ZQ, Chen Yard, Hurwitz J (1993). "The subunits of activator ane (replication factor C) carry out multiple functions essential for proliferating-cell nuclear antigen-dependent Dna synthesis". Proc. Natl. Acad. Sci. U.South.A. 90 (one): 6–ten. Bibcode:1993PNAS...90....6P. doi:10.1073/pnas.ninety.i.half dozen. PMC45588. PMID 8093561.

External links [edit]

• PCNA at the US National Library of Medicine Medical Field of study Headings (MeSH)
• "ANA: Cell bike related (Mitotic): PCNA type one and blazon two Antibody Patterns". Antibody Patterns.com. Retrieved 2008-04-15 .
• Dan Krotz. "Structure of a clench–loader complex". Avant-garde Light Source News. Lawrence Berkeley National Laboratory. Retrieved 2008-04-15 .
• "Picture show showing a model of clamp loading of PCNA onto DNA". Pubmed Central. ^{[ permanent dead link ]}
• Overview of all the structural information bachelor in the PDB for UniProt: P12004 (Proliferating prison cell nuclear antigen) at the PDBe-KB.

During Nucleotide Excision Repair In E. Coli, Which Proteins Identify The Damaged Dna?,

Source: https://en.wikipedia.org/wiki/Proliferating_cell_nuclear_antigen

Posted by: hernandezbourponshave.blogspot.com

Share this post