Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination.

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

EUKARYOTIC TRANSLESION SYNTHESIS DNA POLYMERASES: Specificity of Structure and Function

Prakash, S., Johnson, R. E., & Prakash, L. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133250 · Cited by 999

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

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 434

Specific complex formation between yeast RAD6 and RAD18 proteins: a potential mechanism for targeting RAD6 ubiquitin-conjugating activity to DNA damage sites.Preprint

Bailly, V., Lamb, J., Sung, P., Prakash, S., & Prakash, L. (1994) · Genes & Development · doi:10.1101/gad.8.7.811 · Cited by 321

Yeast DNA Repair Proteins Rad6 and Rad18 Form a Heterodimer That Has Ubiquitin Conjugating, DNA Binding, and ATP Hydrolytic Activities

Bailly, V., Lauder, S., Prakash, S., & Prakash, L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.37.23360 · Cited by 292

Yeast Rad5 Protein Required for Postreplication Repair Has a DNA Helicase Activity Specific for Replication Fork Regression

Blastyák, A., Pintér, L., Unk, I., Prakash, L., Prakash, S., & Haracska, L. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.07.030 · Cited by 285

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

Opposing Effects of Ubiquitin Conjugation and SUMO Modification of PCNA on Replicational Bypass of DNA Lesions in Saccharomyces cerevisiae

Haracska, L., Torres‐Ramos, C. A., Johnson, R. E., Prakash, S., & Prakash, L. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.10.4267-4274.2004 · Cited by 201

Human SHPRH suppresses genomic instability through proliferating cell nuclear antigen polyubiquitination

Motegi, A., Sood, R. B., Moinova, H., Markowitz, S. D., Liu, P. P., & Myung, K. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200606145 · Cited by 199

Cellular Cullin RING Ubiquitin Ligases: Druggable Host Dependency Factors of Cytomegaloviruses

Becker, T., Le‐Trilling, V. T. K., & Trilling, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20071636 · Cited by 30

Mechanisms of direct replication restart at stressed replisomes

Conti, B. A., & Smogorzewska, A. (2020) · DNA repair · doi:10.1016/j.dnarep.2020.102947 · Cited by 34

RAD5a and REV3 function in two alternative pathways of DNA-damage tolerance in Arabidopsis

Wang, S., Wen, R., Shi, X., Lambrecht, A. D., Wang, H., & Xiao, W. (2011) · DNA repair · doi:10.1016/j.dnarep.2011.04.009 · Cited by 31

Rad5, HLTF, and SHPRH: A Fresh View of an Old Story

Elserafy, M., Abugable, A. A., Atteya, R., & El‐Khamisy, S. F. (2018) · Trends in Genetics · doi:10.1016/j.tig.2018.04.006 · Cited by 30

Regulation of HLTF-mediated PCNA polyubiquitination by RFC and PCNA monoubiquitination levels determines choice of damage tolerance pathway

Masuda, Y., Mitsuyuki, S., Kanao, R., Hishiki, A., Hashimoto, H., & Masutani, C. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky943 · Cited by 35

Herpes Simplex Virus Type 2 Inhibits Type I IFN Signaling Mediated by the Novel E3 Ubiquitin Protein Ligase Activity of Viral Protein ICP22

Zhang, M., Fu, M., Li, M., Hu, H., Gong, S., & Hu, Q. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.2000418 · Cited by 30

Helicase-like transcription factor confers radiation resistance in cervical cancer through enhancing the DNA damage repair capacity

Cho, S., Cinghu, S., Yu, J.-R., & Park, W. (2010) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-010-0925-5 · Cited by 29

The levels of p53 govern the hierarchy of DNA damage tolerance pathway usage

Castaño, B. A., Schorer, S., Guo, Y., Calzetta, N. L., Gottifredi, V., Wiesmüller, L., & Biber, S. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae061 · Cited by 29

Ubiquitylation at Stressed Replication Forks: Mechanisms and Functions

Mirsanaye, A. S., Typas, D., & Mailand, N. (2021) · Trends in Cell Biology · doi:10.1016/j.tcb.2021.01.008 · Cited by 28

Helicase-Like Transcription Factor (Hltf) Regulates G2/M Transition, Wt1/Gata4/Hif-1a Cardiac Transcription Networks, and Collagen Biogenesis

Helmer, R. A., Martı́nez–Zaguilán, R., Dertien, J. S., Fulford, C., Foreman, O., Peiris, V., & Chilton, B. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080461 · Cited by 30

Role of Helicase-Like Transcription Factor (Hltf) in the G2/M Transition and Apoptosis in Brain

Helmer, R. A., Foreman, O., Dertien, J. S., Panchoo, M., Bhakta, S. M., & Chilton, B. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066799 · Cited by 28

Spatiotemporal regulation of PCNA ubiquitination in damage tolerance pathways

Masuda, Y., & Masutani, C. (2019) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2019.1687420 · Cited by 28

Regulation of PCNA polyubiquitination in human cells

Brun, J., Chiu, R. K., Wouters, B. G., & Gray, D. A. (2010) · BMC Research Notes · doi:10.1186/1756-0500-3-85 · Cited by 27

BRCA1/BARD1 ubiquitinates PCNA in unperturbed conditions to promote continuous DNA synthesis

Salas‐Lloret, D., García‐Rodríguez, N., Soto-Hidalgo, E., González-Vinceiro, L., Espejo-Serrano, C., Giebel, L., Mateos‐Martín, M. L., de Ru, A. H., van Veelen, P. A., Huertas, P., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-48427-6 · Cited by 26

RFWD3 promotes ZRANB3 recruitment to regulate the remodeling of stalled replication forks

Moore, C. E., Yalcindag, S. E., Czeladko, H., Ravindranathan, R., Hanthi, Y. W., Levy, J. C., Sannino, V., Schindler, D., Ciccia, A., Costanzo, V., et al. (2023) · The Journal of Cell Biology · doi:10.1083/jcb.202106022 · Cited by 26

SHPRH regulates rRNA transcription by recognizing the histone code in an mTOR-dependent manner

Lee, D., An, J., Park, Y.-U., Liaw, H., Woodgate, R., Park, J. H., & Myung, K. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1701978114 · Cited by 27

HIV-1 Vpr protein directly loads helicase-like transcription factor (HLTF) onto the CRL4-DCAF1 E3 ubiquitin ligase

Zhou, X., DeLucia, M., Hao, C., Hrecka, K., Monnie, C. M., Skowroński, J., & Ahn, J. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.798801 · Cited by 25

The DNA replication checkpoint prevents PCNA/RFC depletion to protect forks from HLTF-induced collapse in human cells

Bertolin, A. P., Canal, B., Yekezare, M., Early, A. E., Zeng, J., Instrell, R., Howell, M., & Diffley, J. F. X. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.06.002 · Cited by 27

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 26

Role of specialized DNA polymerases in the limitation of replicative stress and DNA damage transmission

Bournique, E., Dall’Osto, M., Hoffmann, J., & Bergoglio, V. (2017) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2017.08.002 · Cited by 26

PARP1 recruits DNA translocases to restrain DNA replication and facilitate DNA repair

Ho, Y.-C., Ku, C.-S., Tsai, S.-S., Shiu, J.-L., Jiang, Y., Miriam, H. E., Zhang, H., Chen, Y., Chiu, W., Chang, S., et al. (2022) · PLoS Genetics · doi:10.1371/journal.pgen.1010545 · Cited by 26

E3 ligases: a ubiquitous link between DNA repair, DNA replication and human disease

Chauhan, A. S., Jhujh, S. S., & Stewart, G. S. (2024) · Biochemical Journal · doi:10.1042/bcj20240124 · Cited by 21

The Role of PCNA Posttranslational Modifications in Translesion Synthesis

Shaheen, M. F., Shanmugam, I., & Hromas, R. (2010) · Journal of Nucleic Acids · doi:10.4061/2010/761217 · Cited by 25

Regulation of various DNA repair pathways by E3 ubiquitin ligases

Natarajan, C., & Takeda, K. (2017) · Journal of Cancer Research and Therapeutics · doi:10.4103/0973-1482.204879 · Cited by 25

Rad5 dysregulation drives hyperactive recombination at replication forks resulting in cisplatin sensitivity and genome instability

Bryant, E. E., Šunjevarić, I., Berchowitz, L. E., Rothstein, R. J., & Reid, R. J. D. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz631 · Cited by 23

Inflammatory Gene Regulatory Networks in Amnion Cells Following Cytokine Stimulation: Translational Systems Approach to Modeling Human Parturition

Li, R., Ackerman, W. E., Summerfield, T. L. S., Yu, L., Gulati, P., Zhang, J., Huang, K., Romero, R. J., & Kniss, D. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020560 · Cited by 23

LINC01088 prevents ferroptosis in glioblastoma by enhancing SLC7A11 via HLTF/USP7 axis

Zhou, Y., Zhao, Z. W., Cheng, J., Nie, C., Xiao, D., Wu, Z., Yu, H., Zheng, J., Wang, X., & Jiang, X. (2025) · Clinical and Translational Medicine · doi:10.1002/ctm2.70257 · Cited by 22

Error‐free DNA damage tolerance pathway is facilitated by the Irc5 translocase through cohesin

Litwin, I., Bakowski, T., Szakál, B., Pilarczyk, E., Maciaszczyk-Dziubińska, E., Branzei, D., & Wysocki, R. (2018) · The EMBO Journal · doi:10.15252/embj.201798732 · Cited by 23

FANCD2-dependent mitotic DNA synthesis relies on PCNA K164 ubiquitination

Leung, W., Baxley, R. M., Traband, E. L., Chang, Y., Rogers, C. B., Wang, L., Durrett, W., Bromley, K., Fiedorowicz, L., Thakar, T., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113523 · Cited by 21

Regulation of Mammalian DNA Replication via the Ubiquitin-Proteasome System

Abbas, T., & Dutta, A. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-6955-0_19 · Cited by 23

Post-replication repair: Rad5/HLTF regulation, activity on undamaged templates, and relationship to cancer

Gallo, D., & Brown, G. W. (2019) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2019.1651817 · Cited by 21

The RecQ‐like helicase HRQ1 is involved in DNA crosslink repair in Arabidopsis in a common pathway with the Fanconi anemia‐associated nuclease FAN1 and the postreplicative repair ATPase RAD5A

Röhrig, S., Dorn, A., Enderle, J., Schindele, A., Herrmann, N. J., Knoll, A., & Puchta, H. (2018) · New Phytologist · doi:10.1111/nph.15109 · Cited by 21

PRIMPOL ensures robust handoff between on-the-fly and post-replicative DNA lesion bypass

Mellor, C., Nassar, J., Šviković, S., & Sale, J. E. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad1054 · Cited by 20

Ubiquitylation at the Fork: Making and Breaking Chains to Complete DNA Replication

Yates, M., & Maréchal, A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19102909 · Cited by 19

Balancing self-renewal against genome preservation in stem cells: How do they manage to have the cake and eat it too?

Tsai, R. Y. L. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2152-y · Cited by 20

Chronic treatment with cisplatin induces replication-dependent sister chromatid recombination to confer cisplatin-resistant phenotype in nasopharyngeal carcinoma

Su, W., Hsu, S.-H., Wu, C.-K., Chang, S., Lin, Y.-J., Yang, W., Hung, J., Chiu, W., Tzeng, S., Tseng, Y., et al. (2014) · Oncotarget · doi:10.18632/oncotarget.2210 · Cited by 20

The DNA translocase RAD 5A acts independently of the other main DNA repair pathways, and requires both its ATP ase and RING domain for activity in Arabidopsis thaliana

Klemm, T., Mannuß, A., Kobbe, D., Knoll, A., Trapp, O., Dorn, A., & Puchta, H. (2017) · The Plant Journal · doi:10.1111/tpj.13602 · Cited by 19

Identification of Neurensin-2 as a novel modulator of emotional behavior

Umschweif, G., Medrihan, L., Guillén-Samander, A., Wang, W., Sagi, Y., & Greengard, P. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01058-5 · Cited by 18

Protein Degradation Pathways Regulate the Functions of Helicases in the DNA Damage Response and Maintenance of Genomic Stability

Sommers, J. A., Suhasini, A. N., & Brosh, R. M. (2015) · Biomolecules · doi:10.3390/biom5020590 · Cited by 19

A genetic study based on PCNA-ubiquitin fusions reveals no requirement for PCNA polyubiquitylation in DNA damage tolerance

Gervai, J. Z., Gálicza, J., Szeltner, Z., Zámborszky, J., & Szüts, D. (2017) · DNA repair · doi:10.1016/j.dnarep.2017.04.003 · Cited by 20

Helicase-like transcription factor exhibits increased expression and altered intracellular distribution during tumor progression in hypopharyngeal and laryngeal squamous cell carcinomas

Capouillez, A., Decaestecker, C., Filleul, O., Chevalier, D., Coppée, F., Leroy, X., Belayew, A., & Saussez, S. (2008) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/s00428-008-0675-9 · Cited by 18

Solution NMR structure of the HLTF HIRAN domain: a conserved module in SWI2/SNF2 DNA damage tolerance proteins

Korzhnev, D. M., Neculai, D., Dhe‐Paganon, S., Arrowsmith, C. H., & Bezsonova, I. (2016) · Journal of Biomolecular NMR · doi:10.1007/s10858-016-0070-9 · Cited by 19

TonEBP Regulates PCNA Polyubiquitination in Response to DNA Damage through Interaction with SHPRH and USP1

Kang, H. J., Park, H., Yoo, E. J., Lee, J. H., Choi, S. Y., Lee‐Kwon, W., Lee, K., Hur, J., Seo, J. K., Ra, J. S., et al. (2019) · iScience · doi:10.1016/j.isci.2019.07.021 · Cited by 16

Translesion Synthesis of 2′-Deoxyguanosine Lesions by Eukaryotic DNA Polymerases

Basu, A. K., Pande, P., & Bose, A. (2016) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.6b00285 · Cited by 17

Ubiquitin-PCNA fusion as a mimic for mono-ubiquitinated PCNA in Schizosaccharomyces pombe

Ramasubramanyan, S., Coulon, S., Fuchs, R. P., Lehmann, A. R., & Green, C. (2010) · DNA repair · doi:10.1016/j.dnarep.2010.03.015 · Cited by 16

Replicating Damaged DNA in EukaryotesPreprint

Chatterjee, N., & Siede, W. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a019836 · Cited by 17

A comprehensive genetic catalog of human double-strand break repair

de Alba, E. L., Salguero, I., Giménez-Llorente, D., Montes-Torres, J., Fernández-Sanromán, Á., Casajús-Pelegay, E., Terrón-Bautista, J., González, J. B., Bernal, J. A., Macintyre, G., et al. (2025) · Science · doi:10.1126/science.adr5048 · Cited by 14

Zebrafish Mms2 promotes K63-linked polyubiquitination and is involved in p53-mediated DNA-damage response

Wen, R., Li, J., Xu, X., Cui, Z., & Xiao, W. (2011) · DNA repair · doi:10.1016/j.dnarep.2011.10.015 · Cited by 15

Ubiquitin-dependent regulation of translesion polymerases

Chun, A. C. S., & Jin, D. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380110 · Cited by 15

At RAD 5A is a DNA translocase harboring a HIRAN domain which confers binding to branched DNA structures and is required for DNA repair in vivo

Kobbe, D., Kahles, A., Walter, M., Klemm, T., Mannuß, A., Knoll, A., Focke, M., & Puchta, H. (2016) · The Plant Journal · doi:10.1111/tpj.13283 · Cited by 15

A germline HLTF mutation in familial MDS induces DNA damage accumulation through impaired PCNA polyubiquitination

Takaoka, K., Kawazu, M., Koya, J., Yoshimi, A., Masamoto, Y., Maki, H., Toya, T., Kobayashi, T., Nannya, Y., Arai, S., et al. (2019) · Leukemia · doi:10.1038/s41375-019-0385-0 · Cited by 15

Posttranslational Regulation of Human DNA Polymerase ι

McIntyre, J., McLenigan, M. P., Frank, E. G., Dai, X., Yang, W., Wang, Y., & Woodgate, R. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.675769 · Cited by 15

PCNA-Ub polyubiquitination inhibits cell proliferation and induces cell-cycle checkpoints

Qin, Z., Bai, Z., Sun, Y. J., Niu, X., & Xiao, W. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1245247 · Cited by 16

Multilevel structure–activity profiling reveals multiple green tea compound families that each modulate ubiquitin-activating enzyme and ubiquitination by a distinct mechanism

Fenteany, G., Gaur, P., Hegedűs, L., Dudás, K., Kiss, E., Wéber, E., Hackler, L., Martinek, T. A., Puskás, L. G., & Haracska, L. (2019) · Scientific Reports · doi:10.1038/s41598-019-48888-6 · Cited by 14

Structural aspects of multi-domain RING/Ubox E3 ligases in DNA repair

Hibbert, R. G., Mattiroli, F., & Sixma, T. K. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.01.014 · Cited by 15

The HLTF–PARP1 interaction in the progression and stability of damaged replication forks caused by methyl methanesulfonate

Shiu, J.-L., Wu, C.-K., Chang, S., Sun, Y.-J., Chen, Y., Lai, C., Chiu, W., Chang, W., Myung, K., Su, W., et al. (2020) · Oncogenesis · doi:10.1038/s41389-020-00289-5 · Cited by 15

Targeting proliferating cell nuclear antigen (PCNA) for cancer therapy

Søgaard, C. K., & Otterlei, M. (2024) · Advances in pharmacology · doi:10.1016/bs.apha.2024.04.002 · Cited by 14

Polyubiquitinated PCNA triggers SLX4-mediated break-induced replication in alternative lengthening of telomeres (ALT) cancer cells

Kim, S., Park, S. H., Kang, N., Ra, J. S., Myung, K., & Lee, K. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae785 · Cited by 14

Regulation of double-stranded DNA gap repair by the RAD6 pathway

Moertl, S., Karras, G. I., Wismüller, T., Ahne, F., & Eckardt‐Schupp, F. (2008) · DNA repair · doi:10.1016/j.dnarep.2008.07.016 · Cited by 14

The Human RAD5 Homologs, HLTF and SHPRH, Have Separate Functions in DNA Damage Tolerance Dependent on the DNA Lesion Type

Seelinger, M., Søgaard, C. K., & Otterlei, M. (2020) · Biomolecules · doi:10.3390/biom10030463 · Cited by 14

Intrinsic Immune Mechanisms Restricting Human Cytomegalovirus Replication

Schilling, E.-M., Scherer, M., & Stamminger, T. (2021) · Viruses · doi:10.3390/v13020179 · Cited by 14

USP1/UAF1 targets polyubiquitinated PCNA with an exo-cleavage mechanism that can temporarily enrich for monoubiquitinated PCNA

Keijzer, N., Sakoltchik, J., Majumder, K., van Lil, N., Oualid, F. E., Fish, A., & Sixma, T. K. (2025) · Nature Communications · doi:10.1038/s41467-025-61768-0 · Cited by 16

Helicase-like transcription factor-deletion from the tumor microenvironment in a cell line-derived xenograft model of colorectal cancer reprogrammed the human transcriptome-S-nitroso-proteome to promote inflammation and redirect metastasis

Helmer, R. A., Martı́nez–Zaguilán, R., Kaur, G., Smith, L. A., Dufour, J. M., & Chilton, B. S. (2021) · PLoS ONE · doi:10.1371/journal.pone.0251132 · Cited by 13

A PIAS-ed view of DNA double strand break repair focuses on SUMO

Zlatanou, A., & Stewart, G. S. (2010) · DNA repair · doi:10.1016/j.dnarep.2010.02.003 · Cited by 13

Analysis of SHPRH functions in DNA repair and immunoglobulin diversification

Tomi, N.-S., Davari, K., Grotzky, D., Loos, F., Böttcher, K., Frankenberger, S., & Jungnickel, B. (2014) · DNA repair · doi:10.1016/j.dnarep.2014.09.010 · Cited by 12

Helicase-like transcription factor: a new marker of well-differentiated thyroid cancers

Arcolia, V., Paci, P., Dhont, L., Chantrain, G., Sirtaine, N., Decaestecker, C., Remmelink, M., Belayew, A., & Saussez, S. (2014) · BMC Cancer · doi:10.1186/1471-2407-14-492 · Cited by 12

Rad5 and Its Human Homologs, HLTF and SHPRH, Are Novel Interactors of Mismatch Repair

Miller, A. K., Mao, G., Knicely, B. G., Daniels, H. G., Rahal, C. M., Putnam, C. D., Kolodner, R. D., & Goellner, E. M. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.843121 · Cited by 11

Small-molecule activators specific to adenine base editors through blocking the canonical TGF-β pathway

Yang, Y., Zhang, C., Song, Y., Li, Y., Li, P., Huang, M., Meng, F., & Zhang, M. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac742 · Cited by 11

The fork remodeler helicase-like transcription factor in cancer development: all at once

Waheed, Y., Mojumdar, A., Shafiq, M., de Marco, A., & March, M. D. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167280 · Cited by 11

Structure of HIRAN domain of human HLTF bound to duplex DNA provides structural basis for DNA unwinding to initiate replication fork regression

Hishiki, A., Sato, M., & Hashimoto, H. (2020) · The Journal of Biochemistry · doi:10.1093/jb/mvaa008 · Cited by 11

The Role of Ubiquitination and SUMOylation in DNA Replication

Abbas, T. (2020) · Current Issues in Molecular Biology · doi:10.21775/cimb.040.189 · Cited by 9

Arginine shortage induces replication stress and confers genotoxic resistance by inhibiting histone H4 translation and promoting PCNA ubiquitination

Wang, Y.-C., Kelso, A. A., Karamafrooz, A., Chen, Y., Chen, W., Cheng, C.-T., Qi, Y., Gu, L., Malkas, L. H., Taglialatela, A., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112296 · Cited by 9

The SWI/SNF-related protein SMARCA3 is a histone H3K23 ubiquitin ligase that regulates H3K9me3 in cancer

Akano, I., Hebert, J. M., Tiedemann, R. L., Gao, Q., Xiao, Y. F., Prescott, N. A., Liu, Y., Tan, K. S., Bastle, R. M., Ramakrishnan, A., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.06.020 · Cited by 10

RFWD3 and translesion DNA polymerases contribute to PCNA modification–dependent DNA damage tolerance

Kanao, R., Kawai, H., Taniguchi, T., Takata, M., & Masutani, C. (2022) · Life Science Alliance · doi:10.26508/lsa.202201584 · Cited by 9

Robust high-throughput assays to assess discrete steps in ubiquitination and related cascades

Fenteany, G., Gaur, P., Sharma, G., Pintér, L., Kiss, E., & Haracska, L. (2020) · BMC Molecular and Cell Biology · doi:10.1186/s12860-020-00262-5 · Cited by 9

A series of xanthenes inhibiting Rad6 function and Rad6-Rad18 interaction in the PCNA ubiquitination cascade

Fenteany, G., Sharma, G., Gaur, P., Borics, A., Wéber, E., Kiss, E., & Haracska, L. (2022) · iScience · doi:10.1016/j.isci.2022.104053 · Cited by 9

Degradation of helicase-like transcription factor (HLTF) by β-TrCP promotes hepatocarcinogenesis via activation of the p62/mTOR axis

Tan, Y., Wu, D., Liu, Z., Yu, H., Zheng, X., Lin, X., Bie, P., Zhang, L.-D., & Xie, C. (2023) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjad012 · Cited by 9

Visualisation of PCNA Monoubiquitination In Vivo by Single Pass Spectral Imaging FRET Microscopy

Batters, C., Zhu, H., & Sale, J. E. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009008 · Cited by 9

Expression of the helicase-like transcription factor and its variants during carcinogenesis of the uterine cervix: implications for tumour progression

Capouillez, A., Noël, J., Arafa, M., Arcolia, V., Mouallif, M., Guénin, S., Delvenne, P., Belayew, A., & Saussez, S. (2011) · Histopathology · doi:10.1111/j.1365-2559.2011.03843.x · Cited by 9

Both RAD5-dependent and independent pathways are involved in DNA damage-associated sister chromatid exchange in budding yeast

Fasullo, M., & Sun, M. (2017) · Global Medical Genetics · doi:10.3934/genet.2017.2.84 · Cited by 9

Unique Interactome Network Signatures for Peroxisome Proliferator-activated Receptor Gamma (PPARγ) Modulation by Functional Selective Ligands

Lam, V. Q., Zheng, J., & Griffin, P. R. (2017) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra117.000308 · Cited by 8

ATAD5 functions as a regulatory platform for Ub–PCNA deubiquitination

Ryu, E., Yoo, J., Kang, M.-S., Ha, N. Y., Jang, Y., Kim, J., Kim, Y., Kim, B., Kim, S., Myung, K., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2315759121 · Cited by 7

Structure of the HLTF HIRAN domain and its functional implications in regression of a stalled replication fork

Hishiki, A., Sato, M., & Hashimoto, H. (2020) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798320008074 · Cited by 7

Coordinated Cut and Bypass: Replication of Interstrand Crosslink-Containing DNA

Li, Q., Dudás, K., Tick, G., & Haracska, L. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.699966 · Cited by 8

Modulation of Gene Silencing by Cdc7p via H4 K16 Acetylation and Phosphorylation of Chromatin Assembly Factor CAF-1 in Saccharomyces cerevisiae

Young, T. J., Cui, Y., Irudayaraj, J., & Kirchmaier, A. L. (2019) · Genetics · doi:10.1534/genetics.118.301858 · Cited by 8

The Rad5 Helicase and RING Domains Contribute to Genome Stability through their Independent Catalytic Activities

Tóth, R., Balogh, D., Pintér, L., Jaksa, G., Szeplaki, B., Graf, A., Györfy, Z., Enyedi, M. Z., Kiss, E., Haracska, L., et al. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167437 · Cited by 7

Just bypass it: mechanisms of DNA damage tolerance

Minocha, S., Oliva-Santiago, M., Gadi, S. A., & Duxin, J. P. (2025) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2025.07.004 · Cited by 8

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

Rad5 participates in lesion bypass through its Rev1-binding and ubiquitin ligase domains, but not through its helicase function

Masłowska, K. H., & Pagès, V. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1062027 · 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

Replication stress responses in human lymphocytes change sex-specifically during aging

Rall-Scharpf, M., Schlotter, D., Koch, P., Szafranski, K., Groth, M., Sahm, A., Biber, S., Castaño, B. A., Heitmeir, B., Zengerling, F., et al. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf498 · Cited by 4

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

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

Upregulation of helicase-like transcription factor predicts poor prognosis and facilitates hepatocellular carcinoma progression

Cen, X., Lu, Y., Lü, J., Zhan, P., Cheng, Y., Luo, C., Liu, J., Xie, C., & Wang, F. (2023) · Human Cell · doi:10.1007/s13577-023-00917-3 · Cited by 4

Crystallographic study of a novel DNA-binding domain of human HLTF involved in the template-switching pathway to avoid the replication arrest caused by DNA damage

Ikegaya, Y., Hara, K., Hishiki, A., Yokoyama, H., & Hashimoto, H. (2015) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x15005907 · Cited by 4

REV1 coordinates a multi-faceted tolerance response to DNA alkylation damage and prevents chromosome shattering in Drosophila melanogaster

Khodaverdian, V. Y., Sano, T., Maggs, L. R., Tomarchio, G., Dias, A., Clairmont, C., Tran, M., & McVey, M. (2024) · PLoS Genetics · doi:10.1371/journal.pgen.1011181 · Cited by 3

Clearance of roadblocks in replication fork restart

Longerich, S., & Sung, P. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110698108 · Cited by 3

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

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

Implications of ubiquitination and the maintenance of replication fork stability in cancer therapy

Xia, D., Zhu, X., Wang, Y., Gong, P., Su, H.-S., & Xu, X. (2023) · Bioscience Reports · doi:10.1042/bsr20222591 · Cited by 3

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

USP7 regulates the stability and function of HLTF through deubiquitination.

Qing, P., Han, L., Bin, L., Yan, L., & Ping, W. X. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23317 · Cited by 35

Biochemical characterisation of the SWI/SNF family member HLTF

MacKay, C., Toth, R. L., & Rouse, J. W. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.08.151 · Cited by 39

HLTF (helicase-like transcription factor)

Dhont, L., & Belayew, A. (2018) · Atlas of Genetics and Cytogenetics in Oncology and Haematology · doi:10.4267/2042/68527

Role of Double-Stranded DNA Translocase Activity of Human HLTF in Replication of Damaged DNA

Blastyák, A., Hajdú, I., Unk, I., & Haracska, L. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00863-09 · Cited by 197