PCNA, the Maestro of the Replication Fork

DNA methylation patterns and epigenetic memory

Bird, A. (2002) · Genes & Development · doi:10.1101/gad.947102 · Cited by 7,124 · see citing works

Molecular Mechanisms of Mammalian DNA Repair and the DNA Damage Checkpoints

Sancar, A., Lindsey-Boltz, L. A., Ünsal-Kaçmaz, K., & Linn, S. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073723 · Cited by 3,317 · see citing works

RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO

Hoege, C., Pfander, B., Moldovan, G., Pyrowolakis, G., & Jentsch, S. (2002) · Nature · doi:10.1038/nature00991 · Cited by 2,202 · see citing works

DNA Replication in Eukaryotic Cells

Bell, S. P., & Dutta, A. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.110601.135425 · Cited by 2,065 · see citing works

The p21 inhibitor of cyclin-dependent kinases controls DNA replication by interaction with PCNA

Waga, S., Hannon, G. J., Beach, D., & Stillman, B. (1994) · Nature · doi:10.1038/369574a0 · Cited by 1,655 · see citing works

The multifaceted mismatch-repair system

Jiricny, J. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1907 · Cited by 1,375 · see citing works

Human DNA-(Cytosine-5) Methyltransferase-PCNA Complex as a Target for p21 WAF1

Chuang, L. S.-H., Ian, H.-I., Koh, T., Ng, H., Xu, G., & Li, B. F. L. (1997) · Science · doi:10.1126/science.277.5334.1996 · Cited by 902 · see citing works

Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation

Stelter, P., & Ulrich, H. D. (2003) · Nature · doi:10.1038/nature01965 · Cited by 849 · see citing works

Interaction of Human DNA Polymerase η with Monoubiquitinated PCNA

Kannouche, P. L., Wing, J., & Lehmann, A. R. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00259-x · Cited by 845 · see citing works

Structure of the C-Terminal Region of p21WAF1/CIP1 Complexed with Human PCNA

Gulbis, J. M., Kelman, Z., Hurwitz, J., O’Donnell, M. E., & Kuriyan, J. (1996) · Cell · doi:10.1016/s0092-8674(00)81347-1 · Cited by 805 · see citing works

Flexible filaments in a flowing soap film as a model for one-dimensional flags in a two-dimensional wind

Zhang, J., Childress, S., Libchaber, A. J., & Shelley, M. (2000) · Nature · doi:10.1038/35048530 · Cited by 741 · see citing works

The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme

Jentsch, S., McGrath, J. P., & Varshavsky, A. J. (1987) · Nature · doi:10.1038/329131a0 · Cited by 736 · see citing works

Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis.

Bienko, M., Green, C. M., Crosetto, N., Rudolf, F., Zapart, G., Coull, B., Kannouche, P., Wider, G., Peter, M., Lehmann, A. R., et al. (2005) · Science · doi:10.1126/science.1120615 · Cited by 712 · see citing works

Purification and characterization of CAF-I, a human cell factor required for chromatin assembly during DNA replication in vitro

Smith, S. H., & Stillman, B. (1989) · Cell · doi:10.1016/0092-8674(89)90398-x · Cited by 699 · see citing works

SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase

Pfander, B., Moldovan, G., Sacher, M., Hoege, C., & Jentsch, S. (2005) · Nature · doi:10.1038/nature03665 · Cited by 626 · see citing works

Endonucleolytic Function of MutLα in Human Mismatch Repair

Kadyrov, F. A., Dzantiev, L., Constantin, N., & Modrich, P. L. (2006) · Cell · doi:10.1016/j.cell.2006.05.039 · Cited by 626 · see citing works

THE STRUCTURE AND FUNCTION OF SMC AND KLEISIN COMPLEXES

Nasmyth, K., & Haering, C. H. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133219 · Cited by 612 · see citing works

Regulation of monoubiquitinated PCNA by DUB autocleavage

Huang, T. T., Nijman, S. M. B., Mirchandani, K. D., Galardy, P. J., Cohn, M. A., Haas, W., Gygi, S. P., Ploegh, H. L., Bernards, R., & D’Andrea, A. D. (2006) · Nature Cell Biology · doi:10.1038/ncb1378 · Cited by 585 · see citing works

Requirement for PCNA in DNA Mismatch Repair at a Step Preceding DNA Resynthesis

Umar, A., Buermeyer, A. B., Simon, J. A., Thomas, D. C., Clark, A., Liskay, R. M., & Kunkel, T. A. (1996) · Cell · doi:10.1016/s0092-8674(00)81323-9 · Cited by 577 · see citing works

Multiple mechanisms control chromosome integrity after replication fork uncoupling and restart at irreparable UV lesions

Lopes, M., Foiani, M., & Sogo, J. M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2005.11.015 · Cited by 563 · see citing works

CELLULAR DNA REPLICASES: Components and Dynamics at the Replication Fork

Johnson, A. M., & O’Donnell, M. E. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073859 · Cited by 563 · see citing works

The RCAF complex mediates chromatin assembly during DNA replication and repair

Tyler, J. K., Adams, C. R., Chen, S.-R., Kobayashi, R., Kamakaka, R. T., & Kadonaga, J. T. (1999) · Nature · doi:10.1038/990147 · Cited by 555 · see citing works

Direct interaction between DNMT1 and G9a coordinates DNA and histone methylation during replicationPreprint

Estève, P., Chin, H. G., Smallwood, A., Feehery, G. R., Gangisetty, O., Karpf, A. R., Carey, M., & Pradhan, S. (2006) · Genes & Development · doi:10.1101/gad.1463706 · Cited by 539 · see citing works

Rad18 guides polη to replication stalling sites through physical interaction and PCNA monoubiquitination

Watanabe, K., Tateishi, S., Kawasuji, M., Tsurimoto, T., Inoue, H., & Yamaizumi, M. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600383 · Cited by 538 · see citing works

Biochemistry and biology of mammalian DNA methyltransferases

Hermann, A., Gowher, H., & Jeltsch, A. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4201-1 · Cited by 536 · see citing works

Crosstalk between SUMO and Ubiquitin on PCNA Is Mediated by Recruitment of the Helicase Srs2p

Papouli, E., Chen, S., Davies, A. A., Huttner, D., Krejčí, L., Sung, P., & Ulrich, H. D. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.06.001 · Cited by 522 · see citing works

p21WAF1/Cip1: more than a break to the cell cycle?

Dotto, G. P. (2000) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(00)00019-6 · Cited by 474 · see citing works

Mechanisms in Eukaryotic Mismatch Repair

Modrich, P. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.r600022200 · Cited by 459 · see citing works

Cohesion between sister chromatids must be established during DNA replication

Uhlmann, F., & Nasmyth, K. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70463-4 · Cited by 454 · see citing works

Structural analysis of a eukaryotic sliding DNA clamp–clamp loader complex

Bowman, G. D., O’Donnell, M. E., & Kuriyan, J. (2004) · Nature · doi:10.1038/nature02585 · Cited by 451 · see citing works

Two RING finger proteins mediate cooperation between ubiquitin‐conjugating enzymes in DNA repair

Ulrich, H. D., & Jentsch, S. (2000) · The EMBO Journal · doi:10.1093/emboj/19.13.3388 · Cited by 427 · see citing works

Regulation of Early Events in Chromosome Replication

Diffley, J. F. X. (2004) · Current Biology · doi:10.1016/j.cub.2004.09.019 · Cited by 388 · see citing works

Recruitment of DNA methyltransferase I to DNA repair sites

Mortusewicz, O., Schermelleh, L., Walter, J., Cardoso, M. C., & Leonhardt, H. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501034102 · Cited by 380 · see citing works

Trading Places: How Do DNA Polymerases Switch during Translesion DNA Synthesis?

Friedberg, E. C., Lehmann, A. R., & Fuchs, R. P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.03.032 · Cited by 376 · see citing works

Proliferating cell nuclear antigen and p21 are components of multiple cell cycle kinase complexes.

Zhang, H., Xiong, Y., & Beach, D. (1993) · Molecular Biology of the Cell · doi:10.1091/mbc.4.9.897 · Cited by 361 · see citing works

Human DNA ligase I completely encircles and partially unwinds nicked DNA

Pascal, J. M., O’Brien, P., Tomkinson, A. E., & Ellenberger, T. (2004) · Nature · doi:10.1038/nature03082 · Cited by 352 · see citing works

Chromatin Assembly Coupled to DNA Repair: A New Role for Chromatin Assembly Factor I

Gaillard, P.-H. L., Martini, E. M.-D., Kaufman, P. D., Stillman, B., Moustacchi, E., & Almouzni, G. (1996) · Cell · doi:10.1016/s0092-8674(00)80164-6 · Cited by 343 · see citing works

Post‐replicative base excision repair in replication foci

Otterlei, M., Warbrick, E., Nagelhus, T. A., Haug, T., Slupphaug, G., Akbari, M., Aas, P. A., Steinsbekk, K., Bakke, O., & Krokan, H. E. (1999) · The EMBO Journal · doi:10.1093/emboj/18.13.3834 · Cited by 340 · see citing works

DNA Polymerases that Propagate the Eukaryotic DNA Replication Fork

Garg, P., & Burgers, P. (2005) · Critical reviews in biochemistry and molecular biology · doi:10.1080/10409230590935433 · Cited by 336 · see citing works

The PCNA–RFC Families of DNA Clamps and Clamp Loaders

Majka, J., & Burgers, P. (2004) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(04)78006-x · Cited by 328 · see citing works

Tyrosine phosphorylation controls PCNA function through protein stability

Wang, S., Nakajima, Y., Yu, Y. L., Xia, W., Chen, C.-T., Yang, C. C., McIntush, E. W., Li, L., Hawke, D. H., Kobayashi, R., et al. (2006) · Nature Cell Biology · doi:10.1038/ncb1501 · Cited by 322 · see citing works

PCNA connects DNA replication to epigenetic inheritance in yeast

Zhang, Z., Shibahara, K., & Stillman, B. (2000) · Nature · doi:10.1038/35041601 · Cited by 318 · see citing works

PCNA functions as a molecular platform to trigger Cdt1 destruction and prevent re-replication

Arias, E. E., & Walter, J. C. (2005) · Nature Cell Biology · doi:10.1038/ncb1346 · Cited by 314 · see citing works

Heterochromatin Dynamics in Mouse Cells

Murzina, N., Verreault, A., Laue, E., & Stillman, B. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80204-x · Cited by 300 · see citing works

PCNA Controls Establishment of Sister Chromatid Cohesion during S Phase

Moldovan, G., Pfander, B., & Jentsch, S. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.07.007 · Cited by 283 · see citing works

Structural Basis for FEN-1 Substrate Specificity and PCNA-Mediated Activation in DNA Replication and Repair

Chapados, B. R., Hosfield, D. J., Han, S., Qiu, J., Yelent, B., Shen, B., & Tainer, J. A. (2004) · Cell · doi:10.1016/s0092-8674(03)01036-5 · Cited by 279 · see citing works

A small peptide inhibitor of DNA replication defines the site of interaction between the cyclin-dependent kinase inhibitor p21WAF1 and proliferating cell nuclear antigen

Warbrick, E., Lane, D. P., Glover, D. M., & Cox, L. S. (1995) · Current Biology · doi:10.1016/s0960-9822(95)00058-3 · Cited by 278 · see citing works

Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for heterochromatic silencing

Sharp, J. A., Fouts, E. T., Krawitz, D. C., & Kaufman, P. D. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00140-3 · Cited by 262 · see citing works

Gross Chromosomal Rearrangements and Elevated Recombination at an Inducible Site-Specific Replication Fork Barrier

Lambert, S., Watson, A. T., Sheedy, D. M., Martin, B. R., & Carr, A. M. (2005) · Cell · doi:10.1016/j.cell.2005.03.022 · Cited by 261 · see citing works

Regulation of DNA replication and repair proteins through interaction with the front side of proliferating cell nuclear antigen

Jónsson, Z. O., Hindges, R., & Hübscher, U. (1998) · The EMBO Journal · doi:10.1093/emboj/17.8.2412 · Cited by 257 · see citing works

Structural basis for recruitment of human flap endonuclease 1 to PCNA

Sakurai, S., Kitano, K., Yamaguchi, H. Q., Hamada, K., Okada, K., Fukuda, K., Uchida, M., Ohtsuka, E., Morioka, H., & Hakoshima, T. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600519 · Cited by 246 · see citing works

The 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

Gary, R. K., Ludwig, D. L., Cornelius, H. L., MacInnes, M. A., & Park, M. S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.39.24522 · Cited by 239 · see citing works

Ubiquitinated proliferating cell nuclear antigen activates translesion DNA polymerases η and REV1

Garg, P., & Burgers, P. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505949102 · Cited by 236 · see citing works

Human SHPRH is a ubiquitin ligase for Mms2–Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen

Unk, I., Hajdú, I., Fátyol, K., Szakál, B., Blastyák, A., Bermudez, V. P., Hurwitz, J., Prakash, L., Prakash, S., & Haracska, L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608595103 · Cited by 236 · see citing works

A Heterotrimeric PCNA in the Hyperthermophilic Archaeon Sulfolobus solfataricus

Dionne, I., Nookala, R. K., Jackson, S. P., Doherty, A. J., & Bell, S. D. (2003) · Molecular Cell · doi:10.1016/s1097-2765(02)00824-9 · Cited by 228 · see citing works

Replication-Independent Histone Deposition by the HIR Complex and Asf1

Green, E. M., Antczak, A. J., Bailey, A. O., Franco, A. A., Wu, K. J., Yates, J. R., & Kaufman, P. D. (2005) · Current Biology · doi:10.1016/j.cub.2005.10.053 · Cited by 219 · see citing works

DNA ligase I is recruited to sites of DNA replication by an interaction with proliferating cell nuclear antigen: identification of a common targeting mechanism for the assembly of replication factories

Montecucco, A., Rossi, R., Levin, D. S., Gary, R., Park, M. S., Motycka, T. A., Ciarrocchi, G., Villa, A., Biamonti, G., & Tomkinson, A. E. (1998) · The EMBO Journal · doi:10.1093/emboj/17.13.3786 · Cited by 211 · see citing works

Idling by DNA polymerase δ maintains a ligatable nick during lagging-strand DNA replication

Garg, P., Stith, C. M., Sabouri, N., Johansson, E., & Burgers, P. M. (2004) · Genes & Development · doi:10.1101/gad.1252304 · Cited by 211 · see citing works

Structural and Thermodynamic Analysis of Human PCNA with Peptides Derived from DNA Polymerase-δ p66 Subunit and Flap Endonuclease-1

Bruning, J. B., & Shamoo, Y. (2004) · Structure · doi:10.1016/j.str.2004.09.018 · Cited by 206 · see citing works

The Williams syndrome transcription factor interacts with PCNA to target chromatin remodelling by ISWI to replication foci

Poot, R. A., Bozhenok, L., van den Berg, D. L. C., Steffensen, S., Ferreira, F., Grimaldi, M., Gilbert, N., Ferreira, J. A., & Varga‐Weisz, P. (2004) · Nature Cell Biology · doi:10.1038/ncb1196 · Cited by 203 · see citing works

XRCC1 co-localizes and physically interacts with PCNA

Fan, J. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh556 · Cited by 200 · see citing works

Ubiquitin-Binding Motifs in REV1 Protein Are Required for Its Role in the Tolerance of DNA Damage

Guo, C., Tang, T.-S., Bienko, M., Parker, J. L., Bielen, A. B., Sonoda, E., Takeda, S., Ulrich, H. D., Đikić, I., & Friedberg, E. C. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01118-06 · Cited by 198 · see citing works

Controlling the subcellular localization of DNA polymerases ι and η via interactions with ubiquitin

Plosky, B. S., Vidal, A. E., de Henestrosa, A. R. F., McLenigan, M. P., McDonald, J. P., Mead, S., & Woodgate, R. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601178 · Cited by 196 · see citing works

Transcription coactivator p300 binds PCNA and may have a role in DNA repair synthesis

Hasan, S., Hassa, P. O., Imhof, R., & Hottiger, M. O. (2001) · Nature · doi:10.1038/35066610 · Cited by 177 · see citing works

Chromatin Assembly Factor I Mutants Defective for PCNA Binding Require Asf1/Hir Proteins for Silencing

Krawitz, D. C., Kama, T., & Kaufman, P. D. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.2.614-625.2002 · Cited by 176 · see citing works

The differentiation primary response gene MyD118, related to GADD45, encodes for a nuclear protein which interacts with PCNA and p21WAF1/CIP1.

Vairapandi, M., Balliet, A. G., Fornace, A. J., Hoffman‐Liebermann, B., & Liebermann, D. A. (1996) · PubMed · Cited by 175 · see citing works

Human APE2 protein is mostly localized in the nuclei and to some extent in the mitochondria, while nuclear APE2 is partly associated with proliferating cell nuclear antigen

Tsuchimoto, D. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.11.2349 · Cited by 168 · see citing works

A Role for PCNA Ubiquitination in Immunoglobulin Hypermutation

Arakawa, H., Moldovan, G., Saribasak, H., Saribasak, N. N., Jentsch, S., & Buerstedde, J.-M. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040366 · Cited by 163 · see citing works

Heterochromatin protein 1: don’t judge the book by its cover!

Hediger, F., & Gasser, S. M. (2006) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2006.02.013 · Cited by 160 · see citing works

A Flexible Interface between DNA Ligase and PCNA Supports Conformational Switching and Efficient Ligation of DNA

Pascal, J. M., Tsodikov, O. V., Hura, G. L., Song, W., Cotner‐Gohara, E., Classen, S., Tomkinson, A. E., Tainer, J. A., & Ellenberger, T. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.08.015 · Cited by 160 · see citing works

Homologous regions of Fen1 and p21Cip1 compete for binding to the same site on PCNA: a potential mechanism to co-ordinate DNA replication and repair

Warbrick, E., Lane, D. P., Glover, D. M., & Cox, L. S. (1997) · Oncogene · doi:10.1038/sj.onc.1201072 · Cited by 157 · see citing works

UV-induced binding of ING1 to PCNA regulates the induction of apoptosis

Scott, M. S., Bonnefin, P., Vieyra, D. S., Boisvert, F., Young, D., Bazett‐Jones, D. P., & Riabowol, K. T. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.19.3455 · Cited by 156 · see citing works

ATP Utilization by Yeast Replication Factor C

Gomes, X. V., & Burgers, P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011631200 · Cited by 155 · see citing works

Chromatin assembly: a basic recipe with various flavours

Polo, S. E., & Almouzni, G. (2006) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2006.02.011 · Cited by 150 · see citing works

Comparison of the three-dimensional structures of human, yeast, and oat ubiquitin.

Vijay‐Kumar, S., Bugg, C. E., Wilkinson, K. D., Vierstra, R. D., Hatfield, P. M., & Cook, W. J. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45583-4 · Cited by 138 · see citing works

Ubiquitylation of yeast proliferating cell nuclear antigen and its implications for translesion DNA synthesis

Haracska, L., Unk, I., Prakash, L., & Prakash, S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510924103 · Cited by 136 · see citing works

PCNA clamp facilitates action of DNA cytosine methyltransferase 1 on hemimethylated DNA

Iida, T., Suetake, I., Tajima, S., Morioka, H., Ohta, S., Obuse, C., & Tsurimoto, T. (2002) · Genes to Cells · doi:10.1046/j.1365-2443.2002.00584.x · Cited by 132 · see citing works

A Direct Interaction between Proliferating Cell Nuclear Antigen (PCNA) and Cdk2 Targets PCNA-interacting Proteins for Phosphorylation

Koundrioukoff, S., Jónsson, Z. O., Hasan, S., de Jong, R. N., van der Vliet, P. C., Hottiger, M. O., & Hübscher, U. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001850200 · Cited by 131 · see citing works

Rtt106p is a histone chaperone involved in heterochromatin-mediated silencing

Huang, S., Zhou, H., Katzmann, D., Hochstrasser, M., Atanasova, E., & Zhang, Z. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506176102 · Cited by 130 · see citing works

Replication Protein A-Directed Unloading of PCNA by the Ctf18 Cohesion Establishment Complex

Bylund, G., & Burgers, P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.13.5445-5455.2005 · Cited by 130 · see citing works

L2DTL/CDT2 and PCNA interact with p53 and regulate p53 polyubiquitination and protein stability through MDM2 and CUL4A/DDB1 complexes

Banks, D., Wu, M., Higa, L. A., Gavrilova, N., Quan, J., Ye, T., Kobayashi, R., Sun, H., & Zhang, H. (2006) · Cell Cycle · doi:10.4161/cc.5.15.3150 · Cited by 127 · see citing works

Regulation of alternative replication bypass pathways at stalled replication forks and its effects on genome stability: a yeast model

Barbour, L., & Xiao, W. (2003) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2003.08.014 · Cited by 125 · see citing works

The histone chaperone Asf1 at the crossroads of chromatin and DNA checkpoint pathways

Mousson, F., Ochsenbein, F., & Mann, C. (2006) · Chromosoma · doi:10.1007/s00412-006-0087-z · Cited by 121 · see citing works

Growth inhibition by CDK-cyclin and PCNA binding domains of p21 occurs by distinct mechanisms and is regulated by ubiquitin-proteasome pathway

Rousseau, D. L., Cannella, D., Boulaire, J., FITZGERALD, P. J., Fotedar, A., & Fotedar, R. (1999) · Oncogene · doi:10.1038/sj.onc.1202681 · Cited by 116 · see citing works

The 9-1-1 Checkpoint Clamp Physically Interacts with Polζ and Is Partially Required for Spontaneous Polζ-dependent Mutagenesis in Saccharomyces cerevisiae

Sabbioneda, S., Minesinger, B. K., Giannattasio, M., Plevani, P., Muzi-Falconi, M., & Jinks-Robertson, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507638200 · Cited by 116 · see citing works

Mediation of Proliferating Cell Nuclear Antigen (PCNA)-dependent DNA Replication through a Conserved p21Cip1-like PCNA-binding Motif Present in the Third Subunit of Human DNA Polymerase δ

Ducoux‐Petit, M., Urbach, S., Baldacci, G., Hübscher, U., Koundrioukoff, S., Christensen, J. F., & Hughes, P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106990200 · Cited by 112 · see citing works

Phosphorylation of human Fen1 by cyclin-dependent kinase modulates its role in replication fork regulation

Henneke, G., Koundrioukoff, S., & Hübscher, U. (2003) · Oncogene · doi:10.1038/sj.onc.1206606 · Cited by 109 · see citing works

Proliferating Cell Nuclear Antigen Associates with Histone Deacetylase Activity, Integrating DNA Replication and Chromatin Modification

Milutinovic, S., Zhuang, Q., & Moshe Szyf, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202504200 · Cited by 105 · see citing works

DNA Ligase I and Proliferating Cell Nuclear Antigen Form a Functional Complex

Tom, S., Henricksen, L. A., Park, M. S., & Bambara, R. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101673200 · Cited by 104 · see citing works

Interaction of CR6 (GADD45γ) with Proliferating Cell Nuclear Antigen Impedes Negative Growth Control

Azam, N., Vairapandi, M., Zhang, W., Hoffman‐Liebermann, B., & Liebermann, D. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m005626200 · Cited by 99 · see citing works

Human 3-Methyladenine-DNA Glycosylase: Effect of Sequence Context on Excision, Association with PCNA, and Stimulation by AP Endonuclease

Xia, L., Li, Z., Lee, H., Bates, S., Federico, L., Shen, B., & O'Connor, T. R. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.01.014 · Cited by 97 · see citing works

Analysis of Interactions Between Mismatch Repair Initiation Factors and the Replication Processivity Factor PCNA

Lee, S. D., & Alani, E. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.10.059 · Cited by 96 · see citing works

A Novel PCNA-Binding Motif Identified by the Panning of a Random Peptide Display Library

Xu, H., Zhang, P., Liu, L., & Lee, M. (2001) · Biochemistry · doi:10.1021/bi010103+ · Cited by 96 · see citing works

Ubiquitin/SUMO modification of PCNA promotes replication fork progression in Xenopus laevis egg extracts

Leach, C. A., & Michael, W. M. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200508100 · Cited by 93 · see citing works

9-1-1 Complex Involvement in DNA Repair: Evidence that DNA Damage Detection Machinery Participates in DNA Repair

Helt, C. E., Wang, W., Keng, P. C., & Bambara, R. A. (2005) · Cell Cycle · doi:10.4161/cc.4.4.1598 · Cited by 90 · see citing works

Growth inhibition by CDK-cyclin and PCNA binding domains of p21 occurs by distinct mechanisms and is regulated by ubiquitin-proteasome pathway

Rousseau, D. L., Cannella, D., Boulaire, J., FITZGERALD, P. J., Fotedar, A., & Fotedar, R. (1999) · Oncogene · doi:10.1038/sj.onc.1202686 · Cited by 84 · see citing works

Mechanism of Proliferating Cell Nuclear Antigen Clamp Opening by Replication Factor C

Yao, N. Y., Johnson, A. M., Bowman, G. D., Kuriyan, J., & O’Donnell, M. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601273200 · Cited by 81 · see citing works

Functional sites of human PCNA which interact with p21 (Cip1/Waf1), DNA polymerase δ and replication factor C

Oku, T., Ikeda, S., Sasaki, H., Fukuda, K., Morioka, H., Ohtsuka, E., Yoshikawa, H., & Tsurimoto, T. (1998) · Genes to Cells · doi:10.1046/j.1365-2443.1998.00199.x · Cited by 77 · see citing works

Role of Saccharomyces cerevisiae Chromatin Assembly Factor-I in Repair of Ultraviolet Radiation Damage in Vivo

Game, J. C., & Kaufman, P. D. (1999) · Genetics · doi:10.1093/genetics/151.2.485 · Cited by 76 · see citing works

Stimulation of 3′→5′ Exonuclease and 3′-Phosphodiesterase Activities of Yeast Apn2 by Proliferating Cell Nuclear Antigen

Unk, I., Haracska, L., Gomes, X. V., Burgers, P., Prakash, L., & Prakash, S. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.18.6480-6486.2002 · Cited by 62 · see citing works

Physical and functional interaction of human nuclear uracil-DNA glycosylase with proliferating cell nuclear antigen

Ko, R., & Bennett, S. E. (2005) · DNA repair · doi:10.1016/j.dnarep.2005.08.006 · Cited by 59 · see citing works

Crystallization of Proliferating Cell Nuclear Antigen (PCNA) from Saccharomyces cerevisiae

Krishna, T. S. R., Fenyö, D., Kong, X., Gary, S. L., Chait, B. T., Burgers, P., & Kuriyan, J. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1495 · Cited by 45 · see citing works

Solution structure of a yeast ubiquitin‐like protein Smt3: The role of structurally less defined sequences in protein–protein recognitions

Sheng, W., & Liao, X. (2002) · Protein Science · doi:10.1110/ps.0201602 · Cited by 44 · see citing works

Human NTH1 physically interacts with p53 and proliferating cell nuclear antigen

Oyama, M., Wakasugi, M., Hama, T., Hashidume, H., Iwakami, Y., Imai, R., Hoshino, S., Morioka, H., Ishigaki, Y., Nikaido, O., et al. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.06.136 · Cited by 37 · see citing works

Trading Places: How Do DNA Polymerases Switch during Translesion DNA Synthesis?

Friedberg, E. C., Lehmann, A. R., & Fuchs, R. P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.06.003 · Cited by 34 · see citing works

Distinct pools of proliferating cell nuclear antigen associated to DNA replication sites interact with the p125 subunit of DNA polymerase δ or DNA ligase I

Riva, F., Savio, M., Cazzalini, O., Stivala, L. A., Scovassi, A. I., Cox, L. S., Ducommun, B., & Prosperi, E. (2003) · Experimental Cell Research · doi:10.1016/j.yexcr.2003.10.025 · Cited by 28 · see citing works

Proliferating Cell Nuclear Antigen Recruits Cyclin-dependent Kinase Inhibitor Xic1 to DNA and Couples Its Proteolysis to DNA Polymerase Switching

Chuang, L.-C., & Yew, P. R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506429200 · Cited by 26 · see citing works

The DNA Damage Response: Making It Safe to Play with Knives

Ciccia, A., & Elledge, S. J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.019 · Cited by 4,368 · see citing works

The ubiquitin code

Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679 · see citing works

p21 in cancer: Intricate networks and multiple activities

Abbas, T., & Dutta, A. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2657 · Cited by 2,712 · see citing works

The DNA Damage Response: Ten Years After

Harper, J. W., & Elledge, S. J. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.11.015 · Cited by 1,705 · see citing works

The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition

Gareau, J. R., & Lima, C. D. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3011 · Cited by 1,106 · see citing works

Census and evaluation of p53 target genes

Fischer, M. (2017) · Oncogene · doi:10.1038/onc.2016.502 · Cited by 971 · see citing works

Epigenetic inheritance during the cell cycle

Probst, A. V., Dunleavy, E. M., & Almouzni, G. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2640 · Cited by 793 · see citing works

Structure of replicating SARS-CoV-2 polymerase

Hillen, H. S., Kokić, G., Farnung, L., Dienemann, C., Tegunov, D., & Cramer, P. (2020) · Nature · doi:10.1038/s41586-020-2368-8 · Cited by 795 · see citing works

Proliferating cell nuclear antigen (PCNA): a key factor in DNA replication and cell cycle regulation

Strzałka, W., & Ziemienowicz, A. (2010) · Annals of Botany · doi:10.1093/aob/mcq243 · Cited by 789 · see citing works

Chromatin structure and the inheritance of epigenetic information

Margueron, R., & Reinberg, D. (2010) · Nature Reviews Genetics · doi:10.1038/nrg2752 · Cited by 733 · see citing works

The emerging complexity of protein ubiquitination

Komander, D. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370937 · Cited by 821 · see citing works

A model for transmission of the H3K27me3 epigenetic mark

Hansen, K. H., Bracken, A. P., Pasini, D., Dietrich, N., Gehani, S. S., Monrad, A., Rappsilber, J., Lerdrup, M., & Helin, K. (2008) · Nature Cell Biology · doi:10.1038/ncb1787 · Cited by 720 · see citing works

Y-family DNA polymerases and their role in tolerance of cellular DNA damage

Sale, J. E., Lehmann, A. R., & Woodgate, R. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3289 · Cited by 665 · see citing works

Murine features of neurogenesis in the human hippocampus across the lifespan from 0 to 100 years

Knoth, R., Singec, I., Ditter, M., Pantazis, G., Capetian, P., Meyer, R. P., Horvat, V., Volk, B., & Kempermann, G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008809 · Cited by 650 · see citing works

Most Random Gene Expression Signatures Are Significantly Associated with Breast Cancer Outcome

Venet, D., Dumont, J. E., & Detours, V. (2011) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002240 · Cited by 594 · see citing works

How the Fanconi Anemia Pathway Guards the Genome

Moldovan, G., & D’Andrea, A. D. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102108-134222 · Cited by 586 · see citing works

Rad51 protects nascent DNA from Mre11-dependent degradation and promotes continuous DNA synthesis

Hashimoto, Y., Chaudhuri, A. R., Lopes, M., & Costanzo, V. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1927 · Cited by 537 · see citing works

Principles of ubiquitin and SUMO modifications in DNA repair

Bergink, S., & Jentsch, S. (2009) · Nature · doi:10.1038/nature07963 · Cited by 525 · see citing works

Regulation of DNA cross-link repair by the Fanconi anemia/BRCA pathwayPreprint

Kim, H., & D’Andrea, A. D. (2012) · Genes & Development · doi:10.1101/gad.195248.112 · Cited by 510 · see citing works

The Biochemistry of Somatic Hypermutation

Peled, J. U., Kuang, F. L., Iglesias-Ussel, M. D., Roa, S., Kalis, S. L., Goodman, M. F., & Scharff, M. D. (2008) · Annual Review of Immunology · doi:10.1146/annurev.immunol.26.021607.090236 · Cited by 460 · see citing works

Multiple roles of the cell cycle inhibitor p21CDKN1A in the DNA damage response

Cazzalini, O., Scovassi, A. I., Savio, M., Stivala, L. A., & Prosperi, E. (2010) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2010.01.009 · Cited by 430 · see citing works

The Ubiquitin–Proteasome System of Saccharomyces cerevisiae

Finley, D. J., Ulrich, H. D., Sommer, T., & Kaiser, P. (2012) · Genetics · doi:10.1534/genetics.112.140467 · Cited by 427 · see citing works

Examination of the expanding pathways for the regulation of p21 expression and activity

Jung, Y.-S., Qian, Y., & Chen, X. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.01.013 · Cited by 418 · see citing works

CRL4s: the CUL4-RING E3 ubiquitin ligases

Jackson, S., & Xiong, Y. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.07.002 · Cited by 410 · see citing works

DNA damage during S-phase mediates the proliferation-quiescence decision in the subsequent G1 via p21 expression

Barr, A. R., Cooper, S., Heldt, F. S., Butera, F., Stoy, H., Mansfeld, J., Novák, B., & Bakal, C. (2017) · Nature Communications · doi:10.1038/ncomms14728 · Cited by 403 · see citing works

Three DNA polymerases, recruited by different mechanisms, carry out NER repair synthesis in human cells

Ogi, T., Limsirichaikul, S., Overmeer, R. M., Volker, M., Takenaka, K., Cloney, R., Nakazawa, Y., Niimi, A., Miki, Y., Jaspers, N. G., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.009 · Cited by 392 · see citing works

The Replication Checkpoint Prevents Two Types of Fork Collapse without Regulating Replisome Stability

Dungrawala, H., Rose, K. L., Bhat, K. P., Mohni, K. N., Glick, G. G., Couch, F. B., & Cortez, D. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.030 · Cited by 376 · see citing works

What a difference a decade makes: Insights into translesion DNA synthesis

Yang, W., & Woodgate, R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0704219104 · Cited by 377 · see citing works

Regulation of PCNA–protein interactions for genome stability

Mailand, N., Gibbs‐Seymour, I., & Bekker‐Jensen, S. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3562 · Cited by 375 · see citing works

Chromatin Dynamics During DNA Replication and Uncharacterized Replication Factors determined by Nascent Chromatin Capture (NCC) Proteomics

Alabert, C., Bukowski-Wills, J.-C., Lee, S.-B., Kustatscher, G., Nakamura, K., Alves, F. D. L., Ménard, P., Mejlvang, J., Rappsilber, J., & Groth, A. (2014) · Nature Cell Biology · doi:10.1038/ncb2918 · Cited by 334 · see citing works

Forging Ahead through Darkness: PCNA, Still the Principal Conductor at the Replication Fork

Choe, K. N., & Moldovan, G.-L. (2017) · Molecular Cell · doi:10.1016/j.molcel.2016.12.020 · Cited by 325 · see citing works

Damage to dopaminergic neurons by oxidative stress in Parkinson's disease (Review)

Guo, J., Zhao, X., Li, Y., Li, G., & Liu, X. (2018) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2018.3406 · Cited by 347 · see citing works

DNA polymerases and human disease

Loeb, L. A., & Monnat, R. J. (2008) · Nature Reviews Genetics · doi:10.1038/nrg2345 · Cited by 316 · see citing works

Mechanisms that regulate localization of a DNA double-strand break to the nuclear peripheryPreprint

Oza, P., Jaspersen, S. L., Miele, A., Dekker, J., & Peterson, C. L. (2009) · Genes & Development · doi:10.1101/gad.1782209 · Cited by 314 · see citing works

Base excision DNA repair

Zharkov, D. O. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-7543-2 · Cited by 314 · see citing works

Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks.

Motegi, A., Liaw, H.-J., Lee, K.-Y., Roest, H. P., Maas, A., Wu, X., Moinova, H., Markowitz, S. D., Ding, H., Hoeijmakers, J. H. J., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805685105 · Cited by 304 · see citing works

The Many Roles of PCNA in Eukaryotic DNA Replication

Boehm, E. M., Gildenberg, M. S., & Washington, M. T. (2016) · The Enzymes · doi:10.1016/bs.enz.2016.03.003 · Cited by 297 · see citing works

Polyubiquitinated PCNA Recruits the ZRANB3 Translocase to Maintain Genomic Integrity after Replication Stress

Ciccia, A., Nimonkar, A. V., Hu, Y., Hajdú, I., Achar, Y. J., Izhar, L., Petit, S. A., Adamson, B., Yoon, J. C., Kowalczykowski, S. C., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.024 · Cited by 293 · see citing works

The RAD6 DNA damage tolerance pathway operates uncoupled from the replication fork and is functional beyond S phase

Karras, G. I., & Jentsch, S. (2010) · Cell · doi:10.1016/j.cell.2010.02.028 · Cited by 282 · see citing works

PCNA: a silent housekeeper or a potential therapeutic target?

Wang, S.-C. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.02.004 · Cited by 285 · see citing works

Human PCNA Structure, Function and Interactions

Magaña, A. G., & Blanco, F. J. (2020) · Biomolecules · doi:10.3390/biom10040570 · Cited by 288 · see citing works

Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass

Povlsen, L. K., Beli, P., Wagner, S., Poulsen, S. L., Sylvestersen, K. B., Poulsen, J. W., Nielsen, M. L., Bekker‐Jensen, S., Mailand, N., & Choudhary, C. (2012) · Nature Cell Biology · doi:10.1038/ncb2579 · Cited by 287 · see citing works

ELM—the eukaryotic linear motif resource in 2020

Kumar, M., Gouw, M., Michael, S., Sámano‐Sánchez, H., Pancsa, R., Glavina, J., Diakogianni, A., Alvarado-Valverde, J., Bukirova, D., Čalyševa, J., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz1030 · Cited by 278 · see citing works

CRL4Cdt2 Regulates Cell Proliferation and Histone Gene Expression by Targeting PR-Set7/Set8 for Degradation

Abbas, T., Shibata, E., Park, J.-H., Jha, S., Karnani, N., & Dutta, A. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.014 · Cited by 280 · see citing works

The Elg1 replication factor C-like complex functions in PCNA unloading during DNA replication

Kubota, T., Nishimura, K., Kanemaki, M. T., & Donaldson, A. D. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.02.012 · Cited by 279 · see citing works

Circadian molecular clocks and cancer

Kelleher, F. C., Rao, A. D., & Maguire, A. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.09.040 · Cited by 276 · see citing works

Molecular Mechanisms of Somatic Hypermutation and Class Switch Recombination

Methot, S. P., & Noia, J. M. D. (2016) · Advances in immunology · doi:10.1016/bs.ai.2016.11.002 · Cited by 253 · see citing works

V(D)J recombination, somatic hypermutation and class switch recombination of immunoglobulins: mechanism and regulation

Chi, X., Li, Y., & Qiu, X. (2020) · Immunology · doi:10.1111/imm.13176 · Cited by 257 · see citing works

Rescuing Stalled or Damaged Replication ForksPreprint

Yeeles, J. T. P., Poli, J., Marians, K. J., & Pasero, P. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012815 · Cited by 253 · see citing works

Translesion DNA polymerases in eukaryotes: what makes them tick?

Vaisman, A., & Woodgate, R. (2017) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2017.1291576 · Cited by 247 · see citing works

Replication-Coupled DNA Repair

Cortez, D. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.04.027 · Cited by 248 · see citing works

Terminal Deoxynucleotidyl Transferase: The Story of a Misguided DNA Polymerase

Motea, E., & Berdis, A. (2009) · Biochimica et Biophysica Acta · doi:10.1016/j.bbapap.2009.06.030 · Cited by 222 · see citing works

Identification of Proteins at Active, Stalled, and Collapsed Replication Forks Using Isolation of Proteins on Nascent DNA (iPOND) Coupled with Mass Spectrometry

Sirbu, B. M., McDonald, W. H., Dungrawala, H., Badu-Nkansah, A., Kavanaugh, G. M., Chen, Y., Tabb, D. L., & Cortez, D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.511337 · Cited by 246 · see citing works

Regulation of the Histone H4 Monomethylase PR-Set7 by CRL4Cdt2-Mediated PCNA-Dependent Degradation during DNA Damage

Oda, H., Hübner, M. R., Beck, D. B., Vermeulen, M., Hurwitz, J., Spector, D. L., & Reinberg, D. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.011 · Cited by 247 · see citing works

TrxG and PcG Proteins but Not Methylated Histones Remain Associated with DNA through Replication

Petruk, S., Sedkov, Y., Johnston, D. M., Hodgson, J. W., Black, K. L., Kovermann, S. K., Beck, S., Canaani, E., Brock, H. W., & Mazo, A. (2012) · Cell · doi:10.1016/j.cell.2012.06.046 · Cited by 246 · see citing works

Phytochrome regulation of branching in Arabidopsis

Finlayson, S. A., Krishnareddy, S. R., Kebrom, T. H., & Casal, J. J. (2010) · Plant Physiology · doi:10.1104/pp.109.148833 · Cited by 240 · see citing works

The CRL4^Cdt2 ubiquitin ligase targets the degradation of p21^Cip1 to control replication licensing

Kim, Y., Starostina, N. G., & Kipreos, E. T. (2008) · Genes & Development · doi:10.1101/gad.1703708 · Cited by 240 · see citing works

Herpes Simplex Viruses: Mechanisms of DNA ReplicationPreprint

Weller, S. K., & Coen, D. M. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013011 · Cited by 239 · see citing works

SUMO-targeted ubiquitin ligases

Sriramachandran, A. M., & Dohmen, R. J. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.08.022 · Cited by 241 · see citing works

Biology of the cell cycle inhibitor p21CDKN1A: molecular mechanisms and relevance in chemical toxicology

Dutto, I., Tillhon, M., Cazzalini, O., Stivala, L. A., & Prosperi, E. (2014) · Archives of Toxicology · doi:10.1007/s00204-014-1430-4 · Cited by 235 · see citing works

Inhibition of Homologous Recombination by the PCNA-Interacting Protein PARI

Moldovan, G., Dejsuphong, D., Petalcorin, M. I. R., Hofmann, K., Takeda, S., Boulton, S. J., & D’Andrea, A. D. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.11.010 · Cited by 232 · see citing works

DNA Repair Mechanisms and the Bypass of DNA Damage in Saccharomyces cerevisiae

Boiteux, S., & Jinks-Robertson, S. (2013) · Genetics · doi:10.1534/genetics.112.145219 · Cited by 227 · see citing works

Proliferating cell nuclear antigen: a proteomics view

Naryzhny, S. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8305-x · Cited by 229 · see citing works

The ubiquitous role of ubiquitin in the DNA damage response

Al-Hakim, A., Escribano‐Diaz, C., Landry, M.-C., O’Donnell, L., Panier, S., Szilard, R. K., & Durocher, D. (2010) · DNA repair · doi:10.1016/j.dnarep.2010.09.011 · Cited by 224 · see citing works

The Role of the Cyclin Dependent Kinase Inhibitor p21cip1/waf1 in Targeting Cancer: Molecular Mechanisms and Novel Therapeutics

Bitar, S. A., & Gali‐Muhtasib, H. U. (2019) · Cancers · doi:10.3390/cancers11101475 · Cited by 224 · see citing works

Mechanism of CRL4Cdt2, a PCNA-dependent E3 ubiquitin ligasePreprint

Havens, C. G., & Walter, J. C. (2011) · Genes & Development · doi:10.1101/gad.2068611 · Cited by 223 · see citing works

A DNA Damage Response Screen Identifies RHINO, a 9-1-1 and TopBP1 Interacting Protein Required for ATR Signaling

Cotta‐Ramusino, C., McDonald, E. R., Hurov, K. E., Sowa, M. E., Harper, J. W., & Elledge, S. J. (2011) · Science · doi:10.1126/science.1203430 · Cited by 221 · see citing works

Histone Lysine Methyltransferase SETD8 Promotes Carcinogenesis by Deregulating PCNA Expression

Takawa, M., Cho, H., Hayami, S., Toyokawa, G., Kogure, M., Yamane, Y., Iwai, Y., Maejima, K., Ueda, K., Masuda, A., et al. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-3701 · Cited by 212 · see citing works

Glutathione-Scavenging Poly(disulfide amide) Nanoparticles for the Effective Delivery of Pt(IV) Prodrugs and Reversal of Cisplatin Resistance

Ling, X., Chen, X., Riddell, I. A., Tao, W., Wang, J., Hollett, G., Lippard, S. J., Farokhzad, O. C., Shi, J., & Wu, J. (2018) · Nano Letters · doi:10.1021/acs.nanolett.8b01924 · Cited by 209 · see citing works

Reshaping the Endogenous Electric Field to Boost Wound Repair via Electrogenerative Dressing

Luo, R., Liang, Y., Yang, J., Feng, H., Chen, Y., Jiang, X., Zhang, Z., Liu, J., Bai, Y., Xue, J., et al. (2023) · Advanced Materials · doi:10.1002/adma.202208395 · Cited by 208 · see citing works

DNA damage tolerance: when it's OK to make mistakes

Chang, D. J., & Cimprich, K. A. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.139 · Cited by 203 · see citing works

Eukaryotic DNA damage tolerance and translesion synthesis through covalent modifications of PCNA

Andersen, P. L., Xu, F., & Xiao, W. (2007) · Cell Research · doi:10.1038/cr.2007.114 · Cited by 204 · see citing works

DNA damage tolerance: a double-edged sword guarding the genome.

Ghosal, G., & Chen, J. (2013) · PubMed · doi:10.3978/j.issn.2218-676x.2013.04.01 · Cited by 204 · see citing works

Regulation of heterochromatic DNA replication by histone H3 lysine 27 methyltransferases

Jacob, Y., Stroud, H., LeBlanc, C., Feng, S., Zhuo, L., Caro, E., Hassel, C. A., Gutiérrez, C., Michaels, S. D., & Jacobsen, S. E. (2010) · Nature · doi:10.1038/nature09290 · Cited by 198 · see citing works

DNA Damage and P53-Mediated Growth Arrest in Human Cells Treated with Platinum Nanoparticles

Asharani, P. V., Xinyi, N., Hande, M. P., & Valiyaveettil, S. (2009) · Nanomedicine · doi:10.2217/nnm.09.85 · Cited by 198 · see citing works

Strand-Specific Analysis Shows Protein Binding at Replication Forks and PCNA Unloading from Lagging Strands when Forks Stall

Yu, C., Gan, H., Han, J., Zhou, Z.-X., Jia, S., Chabes, A., Farrugia, G., Ördög, T., & Zhang, Z. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.09.017 · Cited by 190 · see citing works

DNA mismatch repair and its many roles in eukaryotic cells

Liu, D., Keijzers, G., & Rasmussen, L. J. (2017) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2017.07.001 · Cited by 192 · see citing works

H19 lncRNA alters stromal cell growth via IGF signaling in the endometrium of women with endometriosis

Ghazal, S., McKinnon, B. D., Zhou, J., Mueller, M., Men, Y., Yang, L., Mueller, M. D., Flannery, C. A., Huang, Y., & Taylor, H. S. (2015) · EMBO Molecular Medicine · doi:10.15252/emmm.201505245 · Cited by 193 · see citing works

DNA Mismatch Repair in Eukaryotes and Bacteria

Fukui, K. (2010) · Journal of Nucleic Acids · doi:10.4061/2010/260512 · Cited by 192 · see citing works

Cellular responses to DNA double-strand breaks after low-dose γ-irradiation

Asaithamby, A., & Chen, D. J. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp237 · Cited by 190 · see citing works

Maintenance of Silent Chromatin through Replication Requires SWI/SNF-like Chromatin Remodeler SMARCAD1

Rowbotham, S. P., Barki‐Celli, L., Neves‐Costa, A., Santos, F., Dean, W., Hawkes, N. A., Choudhary, P., Will, W. R., Webster, J. A., Oxley, D., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.036 · Cited by 186 · see citing works

3D printing of biomaterials with mussel-inspired nanostructures for tumor therapy and tissue regeneration

Ma, H., Luo, J., Sun, Z., Xia, L., Shi, M., Liu, M., Chang, J., & Wu, C. (2016) · Biomaterials · doi:10.1016/j.biomaterials.2016.10.005 · Cited by 189 · see citing works

Chitosan/TiO 2 composite membrane improves proliferation and survival of L929 fibroblast cells: Application in wound dressing and skin regeneration

Behera, S. S., Das, U., Kumar, A., Bissoyi, A., & Singh, A. K. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.02.017 · Cited by 187 · see citing works

Molecular Markers for Breast Cancer: Prediction on Tumor Behavior

Hirata, B. K. B., Oda, J. M. M., Guembarovski, R. L., Ariza, C. B., de Oliveira, C. E. C., & Watanabe, M. A. E. (2014) · Disease Markers · doi:10.1155/2014/513158 · Cited by 184 · see citing works

Wolbachia-Mediated Cytoplasmic Incompatibility Is Associated with Impaired Histone Deposition in the Male Pronucleus

Landmann, F., Orsi, G. A., Loppin, B., & Sullivan, W. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000343 · Cited by 184 · see citing works

Targeting Proliferating Cell Nuclear Antigen (PCNA) as an Effective Strategy to Inhibit Tumor Cell Proliferation

Cardano, M., Tribioli, C., & Prosperi, E. (2020) · Current Cancer Drug Targets · doi:10.2174/1568009620666200115162814 · Cited by 187 · see citing works

Break-induced replication requires all essential DNA replication factors except those specific for pre-RC assemblyPreprint

Lydeard, J. R., Lipkin-Moore, Z., Sheu, Y.-J., Stillman, B., Burgers, P., & Haber, J. E. (2010) · Genes & Development · doi:10.1101/gad.1922610 · Cited by 181 · see citing works

Three-dimensional super-resolution microscopy of the inactive X chromosome territory reveals a collapse of its active nuclear compartment harboring distinct Xist RNA foci

Smeets, D., Markaki, Y., Schmid, V. J., Kraus, F., Tattermusch, A., Cerase, A., Sterr, M., Fiedler, S., Demmerle, J., Popken, J., et al. (2014) · Epigenetics & Chromatin · doi:10.1186/1756-8935-7-8 · Cited by 177 · see citing works

Docking of a Specialized PIP Box onto Chromatin-Bound PCNA Creates a Degron for the Ubiquitin Ligase CRL4Cdt2

Havens, C. G., & Walter, J. C. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.05.012 · Cited by 178 · see citing works

Oligonucleotide/oligosaccharide-binding fold proteins: a growing family of genome guardians

Flynn, R. L., & Zou, L. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2010.488216 · Cited by 178 · see citing works

Tissue Biomarkers for Prognosis in Cutaneous Melanoma: A Systematic Review and Meta-analysis

Rothberg, B. E. G., Bracken, M. B., & Rimm, D. L. (2009) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djp038 · Cited by 180 · see citing works

A Systematic Analysis of Factors Localized to Damaged Chromatin Reveals PARP-Dependent Recruitment of Transcription Factors

Izhar, L., Adamson, B., Ciccia, A., Lewis, J., Vaites, L. P., Leng, Y., Liang, A. C. T., Westbrook, T. F., Harper, J. W., & Elledge, S. J. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.053 · Cited by 178 · see citing works

Silibinin Inhibits Colorectal Cancer Growth by Inhibiting Tumor Cell Proliferation and Angiogenesis

Singh, R. P., Gu, M., & Agarwal, R. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-6247 · Cited by 177 · see citing works

Proliferating cell nuclear antigen acts as a cytoplasmic platform controlling human neutrophil survival

Witko‐Sarsat, V., Mocek, J., Bouayad, D., Tamassia, N., Ribeil, J., Candalh, C., Davezac, N., Reuter, N., Mouthon, L., Hermine, O., et al. (2010) · The Journal of Experimental Medicine · doi:10.1084/jem.20092241 · Cited by 173 · see citing works

DVC1 (C1orf124) is a DNA damage–targeting p97 adaptor that promotes ubiquitin-dependent responses to replication blocks

Mosbech, A., Gibbs‐Seymour, I., Kagias, K., Thorslund, T., Beli, P., Povlsen, L. K., Nielsen, S. V., Smedegaard, S. B., Sedgwick, G. G., Lukas, C., et al. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2395 · Cited by 170 · see citing works

bioPROTACs as versatile modulators of intracellular therapeutic targets including proliferating cell nuclear antigen (PCNA)

Lim, S., Khoo, R., Peh, K. M., Teo, J., Chang, S. C., Ng, S., Beilhartz, G. L., Melnyk, R. A., Johannes, C. W., Brown, C. J., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1920251117 · Cited by 170 · see citing works

H2AX Is Required for Cell Cycle Arrest via the p53/p21 Pathway

Fragkos, M., Jurvansuu, J., & Beard, P. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01830-08 · Cited by 170 · see citing works

Regulating post-translational modifications of the eukaryotic replication clamp PCNA

Ulrich, H. D. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.01.006 · Cited by 167 · see citing works

Identification of a novel, widespread, and functionally important PCNA-binding motif

Gilljam, K. M., Feyzi, E., Aas, P. A., de Sousa, M. M. L., Müller, R., Vågbø, C. B., Catterall, T., Liabakk, N., Slupphaug, G., Drabløs, F., et al. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200903138 · Cited by 169 · see citing works

LncRNA PCNAP1 modulates hepatitis B virus replication and enhances tumor growth of liver cancer

Feng, J., Yang, G., Liu, Y., Gao, Y., Zhao, M., Bu, Y., Yuan, H., Yuan, Y., Yun, H., Sun, M., et al. (2019) · Theranostics · doi:10.7150/thno.34273 · Cited by 168 · see citing works

Forging Ahead through Darkness: PCNA, Still the Principal Conductor at the Replication Fork

Choe, K. N., & Moldovan, G.-L. (2017) · Molecular Cell · doi:10.1016/j.molcel.2016.12.020 · Cited by 325 · see citing works

Ub‐family modifications at the replication fork: Regulating PCNA‐interacting components

Kirchmaier, A. L. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.08.008 · Cited by 24 · see citing works

The Many Roles of PCNA in Eukaryotic DNA Replication

Boehm, E. M., Gildenberg, M. S., & Washington, M. T. (2016) · The Enzymes · doi:10.1016/bs.enz.2016.03.003 · Cited by 297 · see citing works

3 PCNA and DNA replication (I)

Görisch, S. M., & Cardoso, M. C. (2015)

The fellowship of the rings: distinct pools of proliferating cell nuclear antigen trimer at work

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