The DOI matches its Crossref record; 108 of the 110 references it cites were found in a registry or an index.
PCNA, the Maestro of the Replication Fork
Open accessAbstract
Inheritance requires genome duplication, reproduction of chromatin and its epigenetic information, mechanisms to ensure genome integrity, and faithful transmission of the information to progeny. Proliferating cell nuclear antigen (PCNA)-a cofactor of DNA polymerases that encircles DNA-orchestrates several of these functions by recruiting crucial players to the replication fork. Remarkably, many factors that are involved in replication-linked processes interact with a particular face of PCNA and through the same interaction domain, indicating that these interactions do not occur simultaneously during replication. Switching of PCNA partners may be triggered by affinity-driven competition, phosphorylation, proteolysis, and modification of PCNA by ubiquitin and SUMO.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“And, although PCNA is a crucial component of the replication fork during the cell cycle, it also functions in DNA repair.167”
From Census and evaluation of p53 target genes (2017) · cites this paper as [167]
Citations
Cites
1 retracted
Sarraf, S. A., & Stancheva, I. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.06.043 · Cited by 501
RetractedDNA methylation patterns and epigenetic memory
Bird, A. (2002) · Genes & Development · doi:10.1101/gad.947102 · Cited by 7,124
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
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
Self-citationDNA 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
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
The multifaceted mismatch-repair system
Jiricny, J. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1907 · Cited by 1,375
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
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 850
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
Flagged first, then by citations
2 of the 110 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 101–200 of 1,000
Lysine-targeting specificity in ubiquitin and ubiquitin-like modification pathways
Mattiroli, F., & Sixma, T. K. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2792 · Cited by 164
Aflatoxin B1-induced epigenetic alterations: An overview
Dai, Y., Huang, K., Zhang, B., Zhu, L., & Xu, W. (2017) · Food and Chemical Toxicology · doi:10.1016/j.fct.2017.06.034 · Cited by 167
Antiproliferative Effects of Local Anesthetics on Mesenchymal Stem Cells
Lucchinetti, E., Awad, A. E., Rahman, M., Feng, J., Lou, P., Zhang, L., Ionescu, L., Lemieux, H., Thébaud, B., & Zaugg, M. (2012) · Anesthesiology · doi:10.1097/aln.0b013e31824babfe · Cited by 161
Hishiki, A., Hashimoto, H., Hanafusa, T., Kamei, K., Ohashi, E., Shimizu, T., Ohmori, H., & Sato, M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809745200 · Cited by 164
Interactions by disorder – A matter of context
Bugge, K., Brakti, I., Fernandes, C. B., Dreier, J. E., Lundsgaard, J. E., Olsen, J. G., Skriver, K., & Kragelund, B. B. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00110 · Cited by 155
“PCNA has an enormous interactome (Moldovan et al., 2007; Prestel et al., 2019) 1 ), and the APIM motif [KR] (cid:127)(cid:56) 2 [KR] for cytosolic partners (Gilljam et al., 2009; Sebesta et al., 2017).”
BackgroundHuman amniotic epithelial cells improve fertility in an intrauterine adhesion mouse model
Li, B., Zhang, Q., Sun, J., & Lai, D. (2019) · Stem Cell Research & Therapy · doi:10.1186/s13287-019-1368-9 · Cited by 157
SUMO playing tag with ubiquitin
Praefcke, G. J. K., Hofmann, K., & Dohmen, R. J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.09.002 · Cited by 155
The Ubiquitin-Proteasome System Is a Key Component of the SUMO-2/3 Cycle
Schimmel, J., Larsen, K. M., Matić, I., van Hagen, M., Cox, J., Mann, M., Andersen, J., & Vertegaal, A. C. O. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800025-mcp200 · Cited by 155
Exploring the multiple roles of guardian of the genome: P53
Feroz, W., & Sheikh, A. M. A. (2020) · Egyptian Journal of Medical Human Genetics · doi:10.1186/s43042-020-00089-x · Cited by 172
The Ino80 chromatin-remodeling enzyme regulates replisome function and stability
Papamichos‐Chronakis, M., & Peterson, C. L. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1413 · Cited by 162
Asharani, P. V., Sethu, S., Lim, H. K., Balaji, G., Valiyaveettil, S., & Hande, M. P. (2012) · Genome Integrity · doi:10.1186/2041-9414-3-2 · Cited by 151
DNA damage tolerance by recombination: Molecular pathways and DNA structures
Branzei, D., & Szakál, B. (2016) · DNA repair · doi:10.1016/j.dnarep.2016.05.008 · Cited by 154
Multiple degradation pathways regulate versatile CIP/KIP CDK inhibitors
Starostina, N. G., & Kipreos, E. T. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.10.004 · Cited by 147
More forks on the road to replication stress recovery
Allen, C., Ashley, A. K., Hromas, R., & Nickoloff, J. A. (2011) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjq049 · Cited by 152
An Overview on Chemical Aspects and Potential Health Benefits of Limonoids and Their Derivatives
Tundis, R., Loizzo, M. R., & Menichini, F. (2012) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2011.581400 · Cited by 145
Ubiquitin-binding domains and their role in the DNA damage response
Hofmann, K. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.01.003 · Cited by 142
Abbas, T., & Dutta, A. (2011) · Cell Cycle · doi:10.4161/cc.10.2.14530 · Cited by 147
Park, J. M., Yang, S. W., Yu, K. R., Ka, S. H., Lee, S. W., Seol, J. H., Jeon, Y. J., & Chung, C. H. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.031 · Cited by 144
PCNA Is Required for Initiation of Recombination-Associated DNA Synthesis by DNA Polymerase δ
Li, X., Stith, C. M. W., Burgers, P., & Heyer, W. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.036 · Cited by 140
Punchihewa, C., Inoue, A., Hishiki, A., Fujikawa, Y., Connelly, M., Evison, B., Shao, Y., Heath, R., Kuraoka, I., Rodrigues, P., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.353201 · Cited by 135
Proliferating Cell Nuclear Antigen Uses Two Distinct Modes to Move along DNA
Kochaniak, A. B., Habuchi, S., Loparo, J. J., Chang, D. J., Cimprich, K. A., Walter, J. C., & van Oijen, A. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.008706 · Cited by 138
Spartan/C1orf124, a Reader of PCNA Ubiquitylation and a Regulator of UV-Induced DNA Damage Response
Centore, R. C., Yazinski, S. A., Tse, A., & Zou, L. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.020 · Cited by 142
ATAD5 regulates the lifespan of DNA replication factories by modulating PCNA level on the chromatin
Lee, K., Fu, H., Aladjem, M. I., & Myung, K. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201206084 · Cited by 138
PCNA Ubiquitination Is Important, But Not Essential for Translesion DNA Synthesis in Mammalian Cells
Hendel, A., Krijger, P. H. L., Diamant, N., Goren, Z., Langerak, P., Kim, J., Reißner, T., Lee, K.-Y., Geacintov, N. E., Carell, T., et al. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002262 · Cited by 132
Chemically ubiquitylated PCNA as a probe for eukaryotic translesion DNA synthesis
Chen, J., Ai, Y., Wang, J., Haracska, L., & Zhuang, Z. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.316 · Cited by 138
Regulation of Rev1 by the Fanconi anemia core complex
Kim, H., Yang, K., Dejsuphong, D., & D’Andrea, A. D. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2222 · Cited by 143
Ubiquitin pathways in neurodegenerative disease
Atkin, G., & Paulson, H. L. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00063 · Cited by 140
Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2
Armstrong, A. A., Mohideen, F., & Lima, C. D. (2012) · Nature · doi:10.1038/nature10883 · Cited by 140
CDKN1C mutation affecting the PCNA-binding domain as a cause of familial Russell Silver syndrome
Brioude, F., Petit, I., Blaise, A., Praz, F., Rossignol, S., Jule, M. L., Thibaud, N., Faussat, A., Tauber, M., Bouc, Y. L., et al. (2013) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2013-101691 · Cited by 134
Lee, K., Yang, K., Cohn, M. A., Sikdar, N., D’Andrea, A. D., & Myung, K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.092544 · Cited by 134
Kumar, G. H., Priyadarsini, R. V., Vinothini, G., Letchoumy, P. V., & Nagini, S. (2009) · Investigational New Drugs · doi:10.1007/s10637-009-9263-3 · Cited by 131
Tang, S.-W., Chang, W.-H., Su, Y.-C., Chen, Y., Lai, Y.-H., Wu, P.-T., Hsu, C., Lin, W., Lai, M., & Lin, J. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.07.038 · Cited by 131
PARG is recruited to DNA damage sites through poly(ADP-ribose)- and PCNA-dependent mechanisms
Mortusewicz, O., Fouquerel, E., Amé, J., Leonhardt, H., & Schreiber, V. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr099 · Cited by 130
Chemistry and Biology of the Ubiquitin Signal
Spasser, L., & Brik, A. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201200020 · Cited by 132
APOBEC3A and APOBEC3B Activities Render Cancer Cells Susceptible to ATR Inhibition
Buisson, R., Lawrence, M. S., Benes, C. H., & Zou, L. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-3389 · Cited by 132
Yunus, A. A., & Lima, C. D. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.07.013 · Cited by 129
SET8 is degraded via PCNA-coupled CRL4(CDT2) ubiquitylation in S phase and after UV irradiation
Jørgensen, S., Eskildsen, M., Fugger, K., Hansen, L., Larsen, M. S. Y., Kousholt, A. N., Syljuåsen, R. G., Trelle, M. B., Jensen, O. N., Helin, K., et al. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201009076 · Cited by 128
SUMO Modification Regulates BLM and RAD51 Interaction at Damaged Replication Forks
Ouyang, K. J., Woo, L. L., Zhu, J., Huo, D., Matunis, M. J., & Ellis, N. A. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000252 · Cited by 128
Cytokinins Are Initial Targets of Light in the Control of Bud Outgrowth
Roman, H., Girault, T., Barbier, F. F., Péron, T., Brouard, N., Pěnčík, A., Novák, O., Vian, A., Sakr, S., Lothier, J., et al. (2016) · PLANT PHYSIOLOGY · doi:10.1104/pp.16.00530 · Cited by 125
Huen, M. S. Y., Sy, S. M.-H., van Deursen, J. M., & Chen, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.c700242200 · Cited by 129
Histone H3 Lysine 56 Methylation Regulates DNA Replication through Its Interaction with PCNA
Yu, Y., Song, C., Zhang, Q., DiMaggio, P. A., Garcia, B. A., York, A. G., Carey, M., & Grunstein, M. R. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.01.019 · Cited by 132
Bianchini, A., Loiarro, M., Bielli, P., Busà, R., Paronetto, M. P., Loreni, F., Geremia, R., & Sette, C. (2008) · Carcinogenesis · doi:10.1093/carcin/bgn221 · Cited by 130
Anderson, D. D., Woeller, C. F., Chiang, E. I., Shane, B., & Stover, P. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.333120 · Cited by 124
Regulating neutrophil apoptosis: new players enter the game
Witko‐Sarsat, V., Pederzoli-Ribeil, M., Hirsch, E., Sozzani, S., & Cassatella, M. A. (2011) · Trends in Immunology · doi:10.1016/j.it.2011.01.001 · Cited by 124
Hara, K., Hashimoto, H., Murakumo, Y., Kobayashi, S., Kogame, T., Unzai, S., Akashi, S., Takeda, S., Shimizu, T., & Sato, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.092403 · Cited by 123
Functional Analysis of the Replication Fork Proteome Identifies BET Proteins as PCNA Regulators
Wessel, S. R., Mohni, K. N., Luzwick, J. W., Dungrawala, H., & Cortez, D. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.051 · Cited by 120
Yin, H., Zhang, X., Liu, J., Wang, Y., He, J., Yang, T., Hong, X., Yang, Q., & Gong, Z. (2009) · The Plant Cell · doi:10.1105/tpc.108.061549 · Cited by 126
BRCA1 Is Required for Postreplication Repair after UV-Induced DNA Damage
Pathania, S., Nguyen, J., Hill, S. J., Scully, R., Adelmant, G., Marto, J. A., Feunteun, J., & Livingston, D. M. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.09.002 · Cited by 125
Yuan, J., Ghosal, G., & Chen, J. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.025 · Cited by 120
Intercellular communication of cellular stress monitored by γ-H2AX induction
Dickey, J. S., Baird, B. J., Redon, C. E., Sokolov, M. V., Sedelnikova, O. A., & Bonner, W. M. (2009) · Carcinogenesis · doi:10.1093/carcin/bgp192 · Cited by 125
Tsai, J. M., Sinha, R., Seita, J., Fernhoff, N. B., Christ, S., Koopmans, T., Krampitz, G. W., McKenna, K. M., Xing, L., Sandholzer, M., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aan6735 · Cited by 121
Hayashi, T., Shibata, N., Okumura, R., Kudome, T., Nishimura, O., Tarui, H., & Agata, K. (2010) · Development Growth & Differentiation · doi:10.1111/j.1440-169x.2009.01157.x · Cited by 119
CREBBP and p300 lysine acetyl transferases in the DNA damage response
Dutto, I., Scalera, C., & Prosperi, E. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2717-4 · Cited by 118
Ha, K., Lee, G. E., Palii, S. S., Brown, K. D., Takeda, Y., Liu, K., Bhalla, K. N., & Robertson, K. D. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq451 · Cited by 127
ZRANB3 is a structure-specific ATP-dependent endonuclease involved in replication stress responsePreprint
Weston, R., Peeters, H. J. M., & Ahel, D. (2012) · Genes & Development · doi:10.1101/gad.193516.112 · Cited by 123
An 8-oxo-guanine repair pathway coordinated by MUTYH glycosylase and DNA polymerase λ
van Loon, B., & Hübscher, U. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907280106 · Cited by 119
The Intra-S Checkpoint Responses to DNA Damage
Iyer, D., & Rhind, N. (2017) · Genes · doi:10.3390/genes8020074 · Cited by 131
Fanconi Anemia Signaling and Cancer
Nepal, M. K., Che, R., Zhang, J., Ma, C., & Fei, P. (2017) · Trends in cancer · doi:10.1016/j.trecan.2017.10.005 · Cited by 125
Tundo, G. R., Sbardella, D., Santoro, A. M., Coletta, A., Oddone, F., Grasso, G., Milardi, D., Lacal, P. M., Marini, S., Purrello, R., et al. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107579 · Cited by 120
Kubota, T., Katou, Y., Nakato, R., Shirahige, K., & Donaldson, A. D. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.06.066 · Cited by 110
A Chemical and Kinetic Perspective on Base Excision Repair of DNA
Schermerhorn, K. M., & Delaney, S. (2014) · Accounts of Chemical Research · doi:10.1021/ar400275a · Cited by 115
Diabetic ferroptosis plays an important role in triggering on inflammation in diabetic wound
Li, S., Li, Y., Wu, Z., Wu, Z., & Fang, H. (2021) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00042.2021 · Cited by 121
Berdis, A. J. (2009) · Chemical Reviews · doi:10.1021/cr800530b · Cited by 113
Roa, S., Avdievich, E., Peled, J. U., MacCarthy, T., Werling, U., Kuang, F. L., Kan, R., Zhao, C., Bergman, A., Cohen, P. E., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808182105 · Cited by 113
Diamant, N., Hendel, A., Vered, I., Carell, T., Reißner, T., de Wind, N., Geacinov, N., & Livneh, Z. (2012) · Nucleic Acids Research · doi:10.1093/nar/gkr596 · Cited by 109
The PCNA interaction motifs revisited: thinking outside the PIP-box
Prestel, A., Wichmann, N., Martins, J. M. D. S., Marabini, R., Kassem, N., Broendum, S. S., Otterlei, M., Nielsen, O., Willemoës, M., Ploug, M., et al. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03150-0 · Cited by 112
Chk1 and Claspin potentiate PCNA ubiquitination
Yang, X. H., Shiotani, B., Classon, M., & Zou, L. (2008) · Genes & Development · doi:10.1101/gad.1632808 · Cited by 111
Pal, H. C., Sharma, S., Strickland, L. R., Agarwal, J., Athar, M., Elmets, C. A., & Afaq, F. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077270 · Cited by 111
Regulation of PCNA cycling on replicating DNA by RFC and RFC-like complexes
Kang, M.-S., Ryu, E., Lee, S.-W., Park, J., Ha, N. Y., Ra, J. S., Kim, Y. J., Kim, J., Abdel‐Rahman, M. H., Park, S. H., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10376-w · Cited by 111
Kumar, G. H., Mohan, K. V. P. C., Rao, A. J., & Nagini, S. (2008) · Investigational New Drugs · doi:10.1007/s10637-008-9170-z · Cited by 110
Dieckman, L. M., Freudenthal, B., & Washington, M. T. (2012) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-4572-8_15 · Cited by 114
Capturing a substrate in an activated RING E3/E2–SUMO complex
Streich Jr, F. C., & Lima, C. D. (2016) · Nature · doi:10.1038/nature19071 · Cited by 108
Nicolae, C. M., Aho, E. R., Vlahos, A. H. S., Choe, K. N., De, S., Karras, G. I., & Moldovan, G. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.556340 · Cited by 109
Self-citationCBP and p300 acetylate PCNA to link its degradation with nucleotide excision repair synthesis
Cazzalini, O., Sommatis, S., Tillhon, M., Dutto, I., Bachi, A., Rapp, A. W., Nardò, T., Scovassi, A. I., Necchi, D., Cardoso, M. C., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku533 · Cited by 106
Mechanistic analysis of PCNA poly‐ubiquitylation by the ubiquitin protein ligases Rad18 and Rad5
Parker, J. L., & Ulrich, H. D. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.303 · Cited by 106
Manikandan, P., Letchoumy, P. V., Gopalakrishnan, M., & Nagini, S. (2008) · Food and Chemical Toxicology · doi:10.1016/j.fct.2008.03.013 · Cited by 106
APE2 is required for ATR-Chk1 checkpoint activation in response to oxidative stress
Willis, J., Patel, Y., Lentz, B. L., & Yan, S. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301445110 · Cited by 100
Elg1, an alternative subunit of the RFC clamp loader, preferentially interacts with SUMOylated PCNA
Parnas, O., Zipin‐Roitman, A., Pfander, B., Liefshitz, B., Mazor, Y., Ben‐Aroya, S., Jentsch, S., & Kupiec, M. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.128 · Cited by 106
Self-citationMorita, R., Nakane, S., Shimada, A., Inoue, M., Iino, H., Wakamatsu, T., Fukui, K., Nakagawa, N., Masui, R., & Kuramitsu, S. (2010) · Journal of Nucleic Acids · doi:10.4061/2010/179594 · Cited by 117
Role of SUMO modification of human PCNA at stalled replication fork
Gali, H., Juhász, S., Mórocz, M., Hajdú, I., Fátyol, K., Szukacsov, V., Burkovics, P., & Haracska, L. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks256 · Cited by 103
DNA Polymerase POLN Participates in Cross-Link Repair and Homologous Recombination
Moldovan, G., Madhavan, M. V., Mirchandani, K. D., McCaffrey, R. M., Vinciguerra, P., & D’Andrea, A. D. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01124-09 · Cited by 103
Self-citationXiong, F., Ling, X., Chen, X., Chen, J., Tan, J., Cao, W., Ge, L., Ma, M., & Wu, J. (2019) · Nano Letters · doi:10.1021/acs.nanolett.9b00824 · Cited by 103
Leman, A. R., & Noguchi, E. (2013) · Genes · doi:10.3390/genes4010001 · Cited by 102
Molecular Carcinogenesis of Canine Mammary Tumors
Klopfleisch, R., von Euler, H., Sarli, G., Pinho, S. S., Gärtner, F., & Gruber, A. D. (2010) · Veterinary Pathology · doi:10.1177/0300985810390826 · Cited by 107
Mazumder, S., Higgins, P. J., & Samarakoon, R. (2023) · Cancers · doi:10.3390/cancers15041316 · Cited by 118
Structural Basis of Recruitment of DNA Polymerase ζ by Interaction between REV1 and REV7 Proteins
Kikuchi, S., Hara, K., Shimizu, T., Sato, M., & Hashimoto, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.396838 · Cited by 103
Müller, R., Misund, K., Holien, T., Bachke, S., Gilljam, K. M., Våtsveen, T. K., Rø, T. B., Bellacchio, E., Sundan, A., & Otterlei, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0070430 · Cited by 103
Identification of a novel REV1‐interacting motif necessary for DNA polymerase κ function
Ohashi, E., Hanafusa, T., Kamei, K., Song, I. Y., Tomida, J., Hashimoto, H., Vaziri, C., & Ohmori, H. (2009) · Genes to Cells · doi:10.1111/j.1365-2443.2008.01255.x · Cited by 103
Endogenous DNA replication stress results in expansion of dNTP pools and a mutator phenotype
Davidson, M. B., Katou, Y., Keszthelyi, A., Sing, T. L., Xia, T., Ou, J., Vaisica, J. A., Thevakumaran, N., Marjavaara, L., Myers, C. L., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2011.485 · Cited by 107
The Multifaceted Roles of Ku70/80
Zahid, S., Dahan, M. S. E., Iehl, F., Varela, P. F., Du, M. L., Ropars, V., & Charbonnier, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22084134 · Cited by 108
Cell-based therapy in thin endometrium and Asherman syndrome
Gharibeh, N., Maleki, L. A., Madani, J., Pourakbari, R., Yousefi, M., & Heris, J. A. (2022) · Stem Cell Research & Therapy · doi:10.1186/s13287-021-02698-8 · Cited by 101
Tan, Z., Wortman, M. D., McKillip, K. D., Seibel, W. L., Evelyn, C. R., Smith, S. J., Malkas, L. H., Zheng, Y., Lu, S., & Dong, Z. (2012) · Molecular Pharmacology · doi:10.1124/mol.112.077735 · Cited by 101
Reverse the curse—the role of deubiquitination in cell cycle control
Song, L., & Rapé, M. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.01.012 · Cited by 101
T Cells Localize with Proliferating Smooth Muscle α-Actin+ Cell Compartments in Asthma
Ramos‐Barbón, D., Fraga-Iriso, R., Brienza, N. S., Montero-Martínez, C., Verea-Hernando, H., Olivenstein, R., Lemière, C., Ernst, P., Hamid, Q. A., & Martin, J. G. (2010) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200905-0745oc · Cited by 107
KSHV Genome Replication and Maintenance
Purushothaman, P., Dabral, P., Gupta, N., Sarkar, R., & Verma, S. C. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.00054 · Cited by 101
Mechanisms of DNA Damage Tolerance: Post-Translational Regulation of PCNA
Leung, W., Baxley, R. M., Moldovan, G., & Bielinsky, A. (2018) · Genes · doi:10.3390/genes10010010 · Cited by 100
Self-citationRegulated Proteolysis of DNA Polymerase η during the DNA-Damage Response in C. elegans
Kim, S.-H., & Michael, W. M. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.11.016 · Cited by 99
Zaidi, I. W., Rabut, G. E. E., Poveda, A., Scheel, H., Malmström, J. A., Ulrich, H. D., Hofmann, K., Pasero, P., Peter, M., & Luke, B. (2008) · EMBO Reports · doi:10.1038/embor.2008.155 · Cited by 101
Biasio, A. D., de Opakua, A. I., Mortuza, G. B., Molina, R., Cordeiro, T. N., Castillo, F., Villate, M., Merino, N., Delgado, S., Gil‐Carton, D., et al. (2015) · Nature Communications · doi:10.1038/ncomms7439 · Cited by 98
Repair of naturally occurring mismatches can induce mutations in flanking DNA
Chen, J., Miller, B., & Furano, A. V. (2014) · eLife · doi:10.7554/elife.02001 · Cited by 99
Metadata
- Authors
- Moldovan, G.-L., Pfander, B., & Jentsch, S.
- Affiliations
- Harvard University (US)
- Cancer Research UK (GB)
- Max Planck Institute of Biochemistry (DE)
- Corresponding author
- Jentsch, Stefan
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2007-05
- Volume
- 129
- Issue
- 4
- Pages
- 665-679
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2072747624
- Cited by
- 1,796
- References
- 110
- Citations by year
- 2026: 53 · 2025: 70 · 2024: 77 · 2023: 84 · 2022: 80 · 2021: 86 · 2020: 87 · 2019: 97 · 2018: 87 · 2017: 111 · 2016: 113 · 2015: 92 · 2014: 113 · 2013: 106 · 2012: 125
- FWCI
- 8.35
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 2269 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- proliferating cell nuclear antigen, PCNA, DNA replication, replication fork, genome stability, epigenetic inheritance, whole-genome duplication, protein-protein interaction, phosphorylation, ubiquitination, SUMOylation, proteolysis, chromatin inheritance
- MeSH terms
- Animals, DNA-Directed DNA Polymerase, DNA Repair, DNA Replication, DNA-Binding Proteins, Humans, S Phase, Cell Cycle Proteins, Proliferating Cell Nuclear Antigen, Genomic Instability, Epigenesis, Genetic
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review