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

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

Atmospheric carbon dioxide concentrations over the past 60 million years

Pearson, P. N., & Palmer, M. R. (2000) · Nature · doi:10.1038/35021000 · Cited by 1,771

The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase η

Masutani, C., Kusumoto, R., Yamada, A., Dohmae, N., Yokoi, M., Yuasa, M., Araki, M., Iwai, S., Takio, K., & Hanaoka, F. (1999) · Nature · doi:10.1038/21447 · Cited by 1,292

The molecular biology of the yeast saccharomyces

Gichner, T. (1982) · Biologia Plantarum · doi:10.1007/bf02909099 · Cited by 1,179

Chromatin Association of Human Origin Recognition Complex, Cdc6, and Minichromosome Maintenance Proteins during the Cell Cycle: Assembly of Prereplication Complexes in Late Mitosis

Méndez, J., & Stillman, B. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.22.8602-8612.2000 · Cited by 923

The Y-Family of DNA Polymerases

Ohmori, H., Friedberg, E. C., Fuchs, R. P., Goodman, M. F., Hanaoka, F., Hinkle, D. C., Kunkel, T. A., Lawrence, C. W., Livneh, Z., Nohmi, T., et al. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00278-7 · Cited by 882

PML regulates p53 acetylation and premature senescence induced by oncogenic Ras

Pearson, M. A., Carbone, R., Sebastiani, C., Cioce, M., Fagioli, M., Saito, S., Higashimoto, Y., Appella, E., Minucci, S., Pandolfi, P. P., et al. (2000) · Nature · doi:10.1038/35018127 · Cited by 868

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

Efficient Bypass of a Thymine-Thymine Dimer by Yeast DNA Polymerase, Polη

Johnson, R. E., Prakash, S., & Prakash, L. (1999) · Science · doi:10.1126/science.283.5404.1001 · Cited by 736

THE BIOLOGY OF THE (6–4) PHOTOPRODUCT

MITCHELL, D. L., & NAIRN, R. S. (1989) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1989.tb05578.x · Cited by 592

The association between RAD18 Arg302Gln polymorphism and the risk of human non-small-cell lung cancer

Kanzaki, H., Ouchida, M., Hanafusa, H., Yamamoto, H., Suzuki, H., Yano, M., Aoe, M., Imai, K., Date, H., Nakachi, K., et al. (2007) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-007-0272-3 · Cited by 12

BRCTx Is a Novel, Highly Conserved RAD18-Interacting Protein

Adams, D. J., van der Weyden, L., Gergely, F. V., Arends, M. J., Ng, B. L., Tannahill, D., Kanaar, R., Markus, M. A., Morris, B. J., & Bradley, A. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.2.779-788.2005 · Cited by 12

Parkin regulates translesion DNA synthesis in response to UV radiation

Zhu, X., Ma, X., Tu, Y., Huang, M., Liu, H., Wang, F., Gong, J., Wang, J., Li, X., Chen, Q., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.16855 · Cited by 12

The TRIM69-MST2 signaling axis regulates centrosome dynamics and chromosome segregation

Wang, Y., Risteski, P., Yang, Y., Chen, H., Droby, G. N., Walens, A., Jayaprakash, D., Troester, M. A., Herring, L. E., Chernoff, J., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad766 · Cited by 11

DNA repair protein Rad18 restricts LINE-1 mobility

Ariumi, Y., Kawano, K., Yasuda-Inoue, M., Kuroki, M., Fukuda, H., Siddiqui, R., Turelli, P., & Tateishi, S. (2018) · Scientific Reports · doi:10.1038/s41598-018-34288-9 · Cited by 13

Structure of PCNA from Drosophila melanogaster

Wang, K., Shi, Z., Zhang, M., & Cheng, D. (2013) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309113004971 · Cited by 11

Non-Canonical CRL4A/4BCDT2 Interacts with RAD18 to Modulate Post Replication Repair and Cell Survival

Sertic, S., Evolvi, C., Tumini, E., Plevani, P., Muzi-Falconi, M., & Rotondo, G. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060000 · Cited by 12

A novel Rad18 function involved in protection of the vertebrate genome after exposure to camptothecin

Yoshimura, A., Nishino, K., Takezawa, J., Tada, S., Kobayashi, T., Sonoda, E., Kawamoto, T., Takeda, S., Ishii, Y., Yamada, K., et al. (2006) · DNA repair · doi:10.1016/j.dnarep.2006.05.045 · Cited by 11

Phosphorylation of human INO80 is involved in DNA damage tolerance

Kato, D., Waki, M., Umezawa, M., Aoki, Y., Utsugi, T., Ohtsu, M., & Murakami, Y. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.11.134 · Cited by 11

RAD18–BRCTx interaction is required for efficient repair of UV-induced DNA damage

Liu, T., Chen, H., Kim, H., Huen, M. S. Y., Chen, J., & Huang, J. (2011) · DNA repair · doi:10.1016/j.dnarep.2011.10.012 · Cited by 11

Elevated MSH2 MSH3 expression interferes with DNA metabolism in vivo

Medina‐Rivera, M., Phelps, S. E., Sridharan, M., Becker, J. T., Lamb, N. A., Kumar, C., Sutton, M. D., Bielinsky, A., Balakrishnan, L., & Surtees, J. A. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad934 · Cited by 10

Ubiquitin and Ubiquitin-Like Proteins Are Essential Regulators of DNA Damage Bypass

Wilkinson, N. A., Mnuskin, K. S., Ashton, N. W., & Woodgate, R. (2020) · Cancers · doi:10.3390/cancers12102848 · Cited by 10

Functional hierarchy of PCNA‐interacting motifs in DNA processing enzymes

Hamdan, S. M., & Biasio, A. D. (2023) · BioEssays · doi:10.1002/bies.202300020 · Cited by 10

Rev1, Rev3, or Rev7 siRNA Abolishes Ultraviolet Light‐Induced Translesion Replication in HeLa Cells: A Comprehensive Study Using Alkaline Sucrose Density Gradient Sedimentation

Takezawa, J., Ishimi, Y., Aiba, N., & Yamada, K. (2010) · Journal of Nucleic Acids · doi:10.4061/2010/750296 · Cited by 10

Translesion DNA synthesis-driven mutagenesis in very early embryogenesis of fast cleaving embryos

Furno, E. L., Busseau, I., Aze, A., Lorenzi, C., Saghira, C., Danzi, M. C., Zuchner, S. L., & Maiorano, D. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab1223 · Cited by 9

A novel ubiquitin binding mode in the S. cerevisiae translesion synthesisDNA polymerase η

Ai, Y., Wang, J., Johnson, R. E., Haracska, L., Prakash, L., & Zhuang, Z. (2011) · Molecular BioSystems · doi:10.1039/c0mb00355g · Cited by 10

Xeroderma Pigmentosum Variant, XP-V: Its Product and Biological Roles

Masutani, C., Hanaoka, F., & Ahmad, S. (2008) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-09599-8_10 · Cited by 10

Implications of Translesion DNA Synthesis Polymerases on Genomic Stability and Human Health

Venkadakrishnan, J., Lahane, G. P., Dhar, A., Xiao, W., Bhat, K. M., Pandita, T. K., & Bhat, A. (2023) · Molecular and Cellular Biology · doi:10.1080/10985549.2023.2224199 · Cited by 10

Ubiquitination of the histone variant mH2A1.2 prevents toxic RAD18 accumulation at a subset of genomic loci upon replication stress

Galloy, M., Blondeau, A., Vion, É., Kim, D., Bakker, C., Gaggioli, V., THOMAS, M. L., Lavoie, É. G., Marois, I., Monterroso, A. D. D., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.07.013 · Cited by 8

Monoubiquitination of KRAS at Lysine104 and Lysine147 Modulates Its Dynamics and Interaction with Partner Proteins

Nair, V. V., Yin, G., Zhang, J., Hancock, J. F., Campbell, S. L., & Gorfe, A. A. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c01062 · Cited by 9

Evidence for a Rad18-Independent Frameshift Mutagenesis Pathway in Human Cell-Free Extracts

Janel‐Bintz, R., Wagner, J. E., Haracska, L., Mah-Becherel, M. C.-M., Bichara, M., Fuchs, R. P., & Cordonnier, A. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036004 · Cited by 9

Molecular Determinants of Polyubiquitin Recognition by Continuous Ubiquitin-Binding Domains of Rad18

Thach, T. T., Lee, N., Shin, D. H., Han, S., Kim, G., Kim, H., & Lee, S. (2015) · Biochemistry · doi:10.1021/bi5012546 · Cited by 11

Aberrant C-terminal domain of polymerase η targets the functional enzyme to the proteosomal degradation pathway

Ahmed‐Seghir, S., Pouvelle, C., Despras, E., Cordonnier, A. M., Sarasin, A. R., & Kannouche, P. L. (2015) · DNA repair · doi:10.1016/j.dnarep.2015.02.017 · Cited by 9

Nontranscriptional Function of FOXO1/DAF-16 Contributes to Translesion DNA Synthesis

Daitoku, H., Kaneko, Y., Yoshimochi, K., Matsumoto, K., Araoi, S., Sakamaki, J.-I., Takahashi, Y., & Fukamizu, A. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00265-16 · Cited by 10

Control of PCNA deubiquitylation in yeast

Gallego-Sánchez, A., Conde, F., San-Segundo, P. A., & Bueno, A. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380104 · Cited by 9

Role of budding yeast Rad18 in repair of HO-induced double-strand breaks

Hirano, Y., Reddy, J., & Sugimoto, K. (2008) · DNA repair · doi:10.1016/j.dnarep.2008.08.013 · Cited by 9

Structural mechanisms of SLF1 interactions with Histone H4 and RAD18 at the stalled replication fork

Ryder, E. L., Nasir, N., Durgan, A. E. O., Jenkyn-Bedford, M., Tye, S., Zhang, X., & Wu, Q. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae831 · Cited by 8

RAD18-catalysed formation of ubiquitination intermediate mimic of proliferating cell nuclear antigen PCNA

Zhang, L., Deng, Z., Du, Y., Xu, Z., Zhang, T., Tong, Z., Ai, H., Liang, L., & Liu, L. (2024) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2024.118016 · Cited by 8

MicroRNA-379-5p attenuates cancer stem cells and reduces cisplatin resistance in ovarian cancer by regulating RAD18/Polη axis

Shukla, D., Mishra, S., Mandal, T., Charan, M., Verma, A. K., Khan, M. M. A., Chatterjee, N., Dixit, A. K., Ganesan, S. K., Ganju, R. K., et al. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07430-5 · Cited by 8

Yeast DNA polymerase η possesses two PIP-like motifs that bind PCNA and Rad6-Rad18 with different specificities

Ripley, B. M., Reusch, D. T., & Washington, M. T. (2020) · DNA repair · doi:10.1016/j.dnarep.2020.102968 · Cited by 10

Enzymatic Processing of DNA–Protein Crosslinks

Essawy, M. M., & Campbell, C. (2024) · Genes · doi:10.3390/genes15010085 · Cited by 8

Replisome components—Post-translational modifications and their effects

Zech, J., & Dalgaard, J. Z. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.03.026 · Cited by 8

A RAD18–UBC13–PALB2–RNF168 axis mediates replication fork recovery in BRCA1-deficient cancer cells

Cybulla, E., Wallace, S., Meroni, A., Jackson, J., Agashe, S., Tennakoon, M., Limbu, M., Quinet, A., Lomonosova, E. E., Noia, H. M., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae563 · Cited by 11

The role of the DNA damage checkpoint in regulation of translesion DNA synthesis

Koren, A. (2007) · Mutagenesis · doi:10.1093/mutage/gem003 · Cited by 8

Arsenite‐induced changes in hepatic protein abundance in cynomolgus monkeys ( Macaca fascicularis )

Kim, S.-H., Lee, S. H., Lee, S.-W., Park, J., & Ryu, D. (2014) · PROTEOMICS · doi:10.1002/pmic.201300509 · Cited by 7

The Multiple Roles of Ubiquitylation in Regulating Challenged DNA Replication

Villa‐Hernández, S., Bueno, A., & Bermejo, R. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-6955-0_18 · Cited by 7

RAD18 mediates DNA double-strand break-induced ubiquitination of chromatin protein

Mustofa, M. K., Tanoue, Y., Chirifu, M., Shimasaki, T., Tateishi, C., Nakamura, T., & Tateishi, S. (2021) · The Journal of Biochemistry · doi:10.1093/jb/mvab010 · Cited by 10

Impacts of arsenic on Rad18 and translesion synthesis

Volk, L. B., Cooper, K. L., Jiang, T., Paffett, M. L., & Hudson, L. G. (2022) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2022.116230 · Cited by 7

RAD18 and associated proteins are immobilized in nuclear foci in human cells entering S-phase with ultraviolet light-induced damage

Watson, N. B., Nelson, E., Digman, M. A., Thornburg, J. M., Alphenaar, B., & McGregor, W. G. (2008) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2008.09.006 · Cited by 8

Multiple interaction nodes define the postreplication repair response to UV‐induced DNA damage that is defective in melanomas and correlated with UV signature mutation load

Pavey, S. J., Pinder, A., Fernando, W., D’Arcy, N., Matigian, N., Škalamera, D., Cao, K. L., Loo, D., Hill, M. M. C., Stark, M. S., et al. (2019) · Molecular Oncology · doi:10.1002/1878-0261.12601 · Cited by 6

The fanconi anemia pathway promotes homologous recombination repair in DT40 cell line

Takata, M., Yamamoto, K., Matsushita, N., Kitao, H., Hirano, S., & Ishaiai, M. (2006) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4020-4896-8_17 · Cited by 7

Human TLS DNA polymerase: saviors or threats under replication stress?

Rajpurohit, Y. S., Lal, M., Sharma, D. K., & Soni, I. (2025) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-025-05291-2 · Cited by 6

Hypoxia-dependent recruitment of error-prone DNA polymerases to genome replication

Yehuda, R., Dromi, I., Levin, Y., Carell, T., Geacintov, N. E., & Livneh, Z. (2024) · Oncogene · doi:10.1038/s41388-024-03192-0 · Cited by 6

Exploring RAD18-dependent replication of damaged DNA and discontinuities: A collection of advanced tools

Mórocz, M., Qorri, E., Pekker, E., Tick, G., & Haracska, L. (2023) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2023.12.001 · Cited by 7

PCNA Ubiquitylation: Instructive or Permissive to DNA Damage Tolerance Pathways?

Che, J., Hong, X., & Rao, H. (2021) · Biomolecules · doi:10.3390/biom11101543 · Cited by 6

Translesion Synthesis And Errorprone Polymerases

Green, C., & Lehmann, A. R. (2006) · Springer eBooks · doi:10.1007/1-4020-3764-3_7 · Cited by 6

Fanconi anemia: genetic analysis of a human disease using chicken system

Takata, M., Kitao, H., & Ishiai, M. (2007) · Cytogenetic and Genome Research · doi:10.1159/000103197 · Cited by 6

Canonical and Non-Canonical Roles of Human DNA Polymerase η

Bedaiwi, S., Usmani, A., & Carty, M. P. (2024) · Genes · doi:10.3390/genes15101271 · Cited by 6

The RING finger E3 ligase RNF25 protects DNA replication forks independently of its canonical roles in ubiquitin signaling

Chiou, L. F., Droby, G. N., Jayaprakash, D., Anand, J. R., Zhang, X., Yang, Y., Mills, C. A., Webb, T. S., Barker, N. K., Xie, J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-62368-8 · Cited by 5

Complex roles for proliferating cell nuclear antigen in restricting human cytomegalovirus replication

Longmire, P., Daigle, O., Zeltzer, S., Lee, M., Svoboda, M., Padilla‐Rodriguez, M., Bobak, C. A., Bosco, G., & Goodrum, F. D. (2025) · mBio · doi:10.1128/mbio.00450-25 · Cited by 5

Bypass DNA Polymerases

Choi, J., Eoff, R. L., & Guengerich, F. P. (2010) · Humana Press eBooks · doi:10.1007/978-1-61737-995-6_16 · Cited by 5

Detection of endogenous translesion DNA synthesis in single mammalian cells

Egger, T., Aze, A., & Maiorano, D. (2023) · Cell Reports Methods · doi:10.1016/j.crmeth.2023.100501 · Cited by 7

Establishment of a Method for Analyzing Translesion DNA Synthesis across a Single Bulky Adduct in Human Cells

Sawai, T., Kawanishi, M., Takamura‐Enya, T., & Yagi, T. (2009) · Genes and Environment · doi:10.3123/jemsge.31.24 · Cited by 5

Ubiquitylation of Terminal Deoxynucleotidyltransferase Inhibits Its Activity

Maezawa, S., Fukushima, R., Matsushita, T., Tomoyoshi, K., Takagaki, Y., Nishiyama, Y., Ando, S., Matsumoto, T., Kouda, K., Hayano, T., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039511 · Cited by 5

Mutation analysis of Rad18 in human cancer cell lines and non small cell lung cancer tissues

Nakamura, T., Ishikawa, S., Koga, Y., Nagai, Y., Imamura, Y., Ikeda, K., Mori, T., Nomori, H., & Baba, H. (2009) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/1756-9966-28-106 · Cited by 5

Biological and Physicochemical Functions of Ubiquitylation Revealed by Synthetic Chemistry Approaches

Morimoto, D., Walinda, E., Sugase, K., & Shirakawa, M. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061145 · Cited by 5

The Ubiquitin-Proteasome System and DNA Repair

Christine, A. K., Emily, C., Raha, S., Paunesku, T., & Gayle, E. (2011) · InTech eBooks · doi:10.5772/24431 · Cited by 5

Role of ubiquitination in the DNA damage response: proteomic analysis to identify new DNA-damage-induced ubiquitinated proteins

Selvarajah, J., & Moumen, A. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380087 · Cited by 6

The Zn-finger of Saccharomyces cerevisiae Rad18 and its adjacent region mediate interaction with Rad5

Frittmann, O., Gali, V. K., Halmai, M., Tóth, R., Györfy, Z., Bálint, É., & Unk, I. (2021) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkab041 · Cited by 4

Chemosensitizing effect of neferine on cisplatin-resistant colorectal cancer: Identification of potential candidate genes and pathways through whole transcriptome profiling

Somasundram, B., Manogaran, P., Vasudevan, M., & Viswanadha, V. P. (2022) · Phytomedicine Plus · doi:10.1016/j.phyplu.2022.100299 · Cited by 4

DNA Sequence Specificity Reveals a Role of the HLTF HIRAN Domain in the Recognition of Trinucleotide Repeats

Dusek, C. O., Dash, R. C., McPherson, K. S., Calhoun, J. T., Bezsonova, I., Korzhnev, D. M., & Hadden, M. K. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00027 · Cited by 4

Adaptive use of error‐prone DNA polymerases provides flexibility in genome replication during tumorigenesis

Bainbridge, L. J., & Daigaku, Y. (2024) · Cancer Science · doi:10.1111/cas.16188 · Cited by 5

Analysis of DNA replication damage bypass and its role in immunoglobulin repertoire development

Sale, J. E., Ross, A.-L., & Simpson, L. J. (2006) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4020-4896-8_16 · Cited by 4

Roadworks of DNA Damage Bypass during and after Replication

Daigaku, Y. (2012) · Genes and Environment · doi:10.3123/jemsge.34.77 · Cited by 5

One stone, two birds

Zhang, H., & Yu, D. S. (2012) · Cell Cycle · doi:10.4161/cc.21068 · Cited by 4

The Reparative DNA Polymerase Polη Plays a Key Role in Mutagenesis at Low Doses of UV Radiation in Yeast Saccharomyces cerevisiae

Alekseeva, E. A., Evstyukhina, T. А., Скобелева, И. И., Peshekhonov, V. T., & Королев, В. Г. (2024) · Russian Journal of Genetics · doi:10.1134/s1022795424701199 · Cited by 3

Human cytomegalovirus regulates host DNA repair machinery for viral genome integrity

Longmire, P., Zeltzer, S., Zarrella, K., Daigle, O., Svoboda, M., Reitsma, J. M., Terhune, S. S., Bobak, C. A., Bosco, G., & Goodrum, F. D. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1445 · Cited by 3

Chapter 6 Application of New Methods for Detection of DNA Damage and Repair

Svetlova, M., Solovjeva, L. V., & Tomilin, N. (2009) · International review of cytology · doi:10.1016/s1937-6448(09)77006-6 · Cited by 4

Translesion DNA Synthesis and Damage Tolerance Pathways

Masuda, Y., Hanaoka, F., & Masutani, C. (2016) · Springer eBooks · doi:10.1007/978-4-431-55873-6_11 · Cited by 3

DNA polymerase η is a substrate for calpain: A possible mechanism for pol η retention in UV induced replication foci

Nettersheim, J.-A., Janel‐Bintz, R., Kühn, L., & Cordonnier, A. M. (2021) · Journal of Cell Science · doi:10.1242/jcs.258637 · Cited by 4

Mechanistic Insights into the Multiple Activities of the Rad5 Family of Enzymes

Shen, M., Huang, W., Qiu, F., Niu, H., & Xiang, S. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167581 · Cited by 3

Role of tyrosine residue (Y213) in nuclear retention of PCNA1 in human malaria parasite Plasmodium falciparum

Banu, K., Mitra, P., Subbarao, N., & Dhar, S. K. (2018) · FEMS Microbiology Letters · doi:10.1093/femsle/fny182 · Cited by 3

DNA Damage Tolerance and Mutagenesis in Eukaryotic Cells

(2014) · ASM Press eBooks · doi:10.1128/9781555816704.ch17 · Cited by 3

A ubiquitin-specific, proximity-based labeling approach for the identification of ubiquitin ligase substratesPreprint

Mukhopadyay, U., Levantovsky, S., Gharbi, S., Stein, F., Behrends, C., & Bhogaraju, S. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.04.556194 · Cited by 3

Roles of RAD18 in DNA replication and post-replication repair (PRR)

Kovalchuk, I. (2021) · Elsevier eBooks · doi:10.1016/b978-0-323-85679-9.00016-7 · Cited by 2

PCNA Ser46-Leu47 residues are crucial in preserving genomic integrity

Kim, S., Kim, Y., Kim, Y., Yoon, S., Lee, K., Lee, Y., Kang, S., Myung, K., & Oh, C. (2023) · PLoS ONE · doi:10.1371/journal.pone.0285337 · Cited by 3

Ubiquitin protease Ubp1 cooperates with Ubp10 and Ubp12 to revert lysine-164 PCNA ubiquitylation at replication forks

Zamarreño, J., Rodríguez, S., Muñoz, S., Bueno, A., & Sacristán, M. P. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf076 · Cited by 3

Identification of a PCNA-binding motif in human translesion DNA polymerase REV1 and structural basis of its interaction with PCNA

Hishiki, A., Hoshino, N., Okawara, K., Fuchigami, S., Hara, K., & Hashimoto, H. (2025) · The Journal of Biochemistry · doi:10.1093/jb/mvaf054 · Cited by 2

Roles of RAD18 in DNA Replication and Postreplication Repair

Vaziri, C., Tateishi, S., Mutter‐Rottmayer, E., & Gao, Y. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-803309-8.00016-1 · Cited by 2

Complex repeat structure promotes hyper-amplification and amplicon evolution through rolling-circle replication

Watanabe, T., Tanaka, H., & Horiuchi, T. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky275 · Cited by 2

Human DNA polymerase q activity and translocation is regulated by phosphorylation

Chena, Y.-W., & Choua, K.-M. (2016) · Cited by 2

Cellular Responses to DNA Damage

Klapacz, J., & Gollapudi, B. B. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.95611-3 · Cited by 2

Ubiquitin and Fanconi Anemia

Drikos, I. G., & Sachinidis, A. G. (2018) · InTech eBooks · doi:10.5772/intechopen.77123 · Cited by 2

DNA damage tolerance in mammalian cells

Andersen, P. L. (2009) · University Library - University of Saskatchewan (University of Saskatchewan) · Cited by 2

Cryo-EM structure of Pol κ−DNA−PCNA holoenzyme and implications for polymerase switching in DNA lesion bypassPreprint

Lancey, C., Tehseen, M., Takahashi, M., Sobhy, M. A., Ragan, T. J., Crehuet, R., Hamdan, S. M., & Biasio, A. D. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.10.196956 · Cited by 2

The RING Finger E3 Ligase RNF25 Protects DNA Replication Forks Independently of its Canonical Roles in Ubiquitin SignalingPreprint

Chiou, L. F., Jayaprakash, D., Droby, G. N., Zhang, X., Yang, Y., Mills, C. A., Webb, T. S., Barker, N. K., Wu, D., Herring, L. E., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.09.632184 · Cited by 2

Development of Next Generation Cell-Permeable Peptide Inhibitors for the Oncological Target MAGE-A4

Lim, J., Chiou, L. F., Novy, B., Chow, E. J., Norris-Drouin, J. L., Hardy, P. B., Popov, K., Vaziri, C., Bowers, A. A., & Pearce, K. H. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01540 · Cited by 1

Regulation of BACH1/FANCJ Function in DNA Damage Repair: A Dissertation

Xie, J. (2009) · eScholarship@UMassChan · doi:10.13028/95cm-wn54 · Cited by 1

p21 is dispensable for AID-mediated class switch recombination and mutagenesis of immunoglobulin genes during somatic hypermutation

Shansab, M., & Selsing, E. (2011) · Molecular Immunology · doi:10.1016/j.molimm.2011.01.004 · Cited by 1

RAD18 gene product of yeast Saccharomyces cerevisiae controls mutagenesis induced by hydrogen peroxide

Кожина, Т. Н., & Королев, В. Г. (2012) · Russian Journal of Genetics · doi:10.1134/s1022795412010127 · Cited by 1

CTF18 interacts with replication protein A in response to replication stress

Kaneko, Y., Daitoku, H., Komeno, C., & Fukamizu, A. (2016) · Molecular Medicine Reports · doi:10.3892/mmr.2016.5262 · Cited by 1

Theoretical analysis of transcription process with polymerase stalling

Li, J., & Zhang, Y. (2015) · Physical Review E · doi:10.1103/physreve.91.052713 · Cited by 1

Polymerases ε and ∂ repair dysfunctional telomeres facilitated by salt

Ivanova, I. G., & Maringele, L. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw071 · Cited by 1

The interaction between ubiquitin and yeast polymerase η C terminus does not require the UBZ domain

Duong, P. T. M., Bui, A. T. N., Kim, S., Park, H., Seo, Y., & Choi, B. (2020) · FEBS Letters · doi:10.1002/1873-3468.13783 · Cited by 1

Determination of DNA lesion bypass using a ChIP-based assay

Wu, D., Banerjee, A. T., Cai, S., Li, N., Han, C., Bai, X., Zhang, J., & Wang, Q. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103230 · Cited by 2

Interplay and Quality Control of DNA Damage Repair Mechanisms

Eppink, B., Essers, J., & Kanaar, R. (2011) · Wiley eBooks · doi:10.1002/9783527639991.ch16 · Cited by 1

Replication forks and replication checkpoints in repair

Branzei, D., & Foiani, M. (2007) · Springer eBooks · doi:10.1007/4735_2006_0200 · Cited by 1

TENT4A non-canonical poly(A) polymerase regulates DNA-damage tolerance via multiple pathways which are mutated in endometrial cancerPreprint

Swain, U., Friedlander, G., Sehrawat, U., Sarusi-Portuguez, A., Rotkopf, R., Ebert, C., Paz-Elizur, T., Dikstein, R., Carell, T., Geacintov, N. E., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.03.409367 · Cited by 1

Rad18 suppresses the late step of human immunodeficiency virus type 1 replicationPreprint

Ariumi, Y., Zou, C., Fukuda, H., Tateishi, S., Miyagi, E., & Strebel, K. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.26.690725 · Cited by 1

Characterization of the Ubc13-Mms2 Lysine-63-linked ubiquitin conjugating complex

Pastushok, L. (2006) · University Library - University of Saskatchewan (University of Saskatchewan)

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

Interaction of Human DNA polymerase h with monoubiquitinated PCNA; a possible mechanism for the polymerase switch in response to DNA damage

(16043672), P. L. K., (15445256), J. W., & (4461370), A. L. (2004) · Figshare

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Durando, M., Tateishi, S., & Vaziri, C. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt016 · Cited by 91

DNA polymerase η lacking the ubiquitin-binding domain promotes replicative lesion bypass in humans cells

Acharya, N., Yoon, J. H., Hurwitz, J., Prakash, L., & Prakash, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1005492107 · Cited by 42

Rad6/Rad18 Competes with DNA Polymerases η and δ for PCNA Encircling DNA

Li, M., Larsen, L., & Hedglin, M. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00938 · Cited by 13