USP7 regulates the stability and function of HLTF through deubiquitination.

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

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

Defining the Human Deubiquitinating Enzyme Interaction Landscape

Sowa, M. E., Bennett, E. J., Gygi, S. P., & Harper, J. W. (2009) · Cell · doi:10.1016/j.cell.2009.04.042 · Cited by 1,512 · see citing works

Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization

Li, M., Chen, D., Shiloh, A., Luo, J., Nikolaev, A. Y., Qin, J., & Gu, W. J. (2002) · Nature · doi:10.1038/nature737 · Cited by 1,027 · see citing works

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 · 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

A dynamic role of HAUSP in the p53-Mdm2 pathway

Li, M., Brooks, C. L., Kon, N., & Gu, W. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00157-1 · Cited by 679 · see citing works

The Deubiquitinating Enzyme USP1 Regulates the Fanconi Anemia Pathway

Nijman, S. M. B., Huang, T. T., Dirac, A. M. G., Brummelkamp, T. R., Kerkhoven, R. M., D’Andrea, A. D., & Bernards, R. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.01.008 · Cited by 586 · see citing works

A novel ubiquitin‐specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein

Everett, R. D., Meredith, M., Orr, A., Cross, A., Kathoria, M., & Parkinson, J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.7.1519 · Cited by 491 · see citing works

A Role for the Deubiquitinating Enzyme USP28 in Control of the DNA-Damage Response

Zhang, D., Zaugg, K., Mak, T. W., & Elledge, S. J. (2006) · Cell · doi:10.1016/j.cell.2006.06.039 · Cited by 325 · 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

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 · see citing works

Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2.

Meulmeester, E., Maurice, M. M., Boutell, C., Teunisse, A. F. A. S., Ovaa, H., Abraham, T. E., Dirks, R. W., & Jochemsen, A. G. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.024 · Cited by 260 · see citing works

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

Unk, I., Hajdú, I., Fátyol, K., Hurwitz, J., Yoon, J.-H., Prakash, L., Prakash, S., & Haracska, L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800563105 · Cited by 250 · see citing works

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 · see citing works

HLTF gene silencing in human colon cancer

Moinova, H., Chen, W.-D. D., Shen, L., Smiraglia, D. J., Olechnowicz, J., Ravi, L., Kasturi, L., Myeroff, L. L., Plass, C., Parsons, R. E., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.062459899 · Cited by 173 · see citing works

The Functional Role of Calcineurin in Hypertrophy, Regeneration, and Disorders of Skeletal Muscle

Sakuma, K., & Yamaguchi, A. (2010) · BioMed Research International · doi:10.1155/2010/721219 · Cited by 128 · see citing works

USP7 counteracts SCFβTrCP- but not APCCdh1-mediated proteolysis of Claspin

Faustrup, H., Bekker-Jensen, S., Bartek, J., Lukas, J., & Mailand, N. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200807137 · Cited by 113 · see citing works

Deubiquitination of Chfr, a checkpoint protein, by USP7/HAUSP regulates its stability and activity

Oh, Y. M., Yoo, S. J., & Seol, J. H. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.03.193 · Cited by 52 · see citing works

Promoter methylation of helicase-like transcription factor is associated with the early stages of gastric cancer with family history

Kim, J. J., Chung, S. W., Kim, J. H., Kim, J. W., Oh, J. S., Kim, S., Song, S. Y., Park, J., & Kim, D.-H. (2006) · Annals of Oncology · doi:10.1093/annonc/mdl018 · Cited by 32 · see citing works

The activity-dependent stimuli increase SUMO modification in SHSY5Y cells

Han, L., Liu, B., You, S., Xue, Q., Zhang, F., Cheng, J., & Yu, B. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.10.065 · Cited by 19 · see citing works

CHFR functions as a ubiquitin ligase for HLTF to regulate its stability and functions

Kim, J. M., Cho, E. N., Kwon, Y. E., Bae, S. J., Kim, M., & Seol, J. H. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.04.052 · Cited by 19 · see citing works

ATM-mediated stabilization of ZEB1 promotes DNA damage response and radioresistance through CHK1

Zhang, P., Wei, Y., Wang, L., Debeb, B. G., Yuan, Y., Zhang, J., Yuan, J., Wang, M., Chen, D., Sun, Y., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3013 · Cited by 454 · see citing works

USP7: Structure, substrate specificity, and inhibition

Pozhidaeva, A., & Bezsonova, I. (2019) · DNA Repair · doi:10.1016/j.dnarep.2019.02.005 · Cited by 178 · see citing works

USP7: Novel Drug Target in Cancer Therapy

Wang, Z., Kang, W.-T., You, Y., Pang, J., Ren, H., Suo, Z., Liu, H., & Zheng, Y. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00427 · Cited by 124 · see citing works

USP7 Is a Master Regulator of Genome Stability

Valles, G. J., Bezsonova, I., Woodgate, R., & Ashton, N. W. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00717 · Cited by 114 · see citing works

USP7 - a crucial regulator of cancer hallmarks

Saha, G., Roy, S., Basu, M., & Ghosh, M. K. (2023) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2023.188903 · Cited by 106 · see citing works

Functions of Ubiquitin and SUMO in DNA Replication and Replication Stress

García‐Rodríguez, N., Wong, R. P. C., & Ulrich, H. D. (2016) · Frontiers in Genetics · doi:10.3389/fgene.2016.00087 · Cited by 82 · see citing works

Long noncoding RNA LINC02582 acts downstream of miR-200c to promote radioresistance through CHK1 in breast cancer cells

Wang, B., Zheng, J., Li, R., Tian, Y., Lin, J., Liang, Y., Sun, Q., Xu, A., Zheng, R., Liu, M., et al. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1996-0 · Cited by 80 · see citing works

USP7 is essential for maintaining Rad18 stability and DNA damage tolerance.

Zlatanou, A., Sabbioneda, S., Miller, E. S., Greenwalt, A., Aggathanggelou, A., Maurice, M. M., Lehmann, A. R., Stankovic, T., Reverdy, C., Colland, F., et al. (2016) · Oncogene · doi:10.1038/onc.2015.149 · Cited by 77 · see citing works

USP7 is a suppressor of PCNA ubiquitination and oxidative-stress-induced mutagenesis in human cells.

Kashiwaba, S.-I., Kanao, R., Masuda, Y., Kusumoto-Matsuo, R., Hanaoka, F., & Masutani, C. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.11.014 · Cited by 71 · see citing works

STAT3 repressed USP7 expression is crucial for colon cancer development

Zhi, Y., ShouJun, H., Shan, Y., Haijun, L., Yume, X., Kai, Y., Li, X.-W., & Xue-li, Z. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.06.025 · Cited by 48 · see citing works

Ubiquitin-specific Protease 7 Is a Regulator of Ubiquitin-conjugating Enzyme UbE2E1

Sarkari, F., Wheaton, K., Delfa, A. L., Mohamed, M., Shaikh, F., Khatun, R., Arrowsmith, C. H., Frappier, L., Saridakis, V., & Sheng, Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.469262 · Cited by 47 · see citing works

The helicase-like transcription factor (HLTF) in cancer: loss of function or oncomorphic conversion of a tumor suppressor?

Dhont, L., Mascaux, C., & Belayew, A. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2060-6 · Cited by 44 · see citing works

Structural Characterization of Interaction between Human Ubiquitin-specific Protease 7 and Immediate-Early Protein ICP0 of Herpes Simplex Virus-1

Pozhidaeva, A., Mohni, K. N., Dhe‐Paganon, S., Arrowsmith, C. H., Weller, S. K., Korzhnev, D. M., & Bezsonova, I. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.664805 · Cited by 40 · see citing works

FBXL5-mediated degradation of single-stranded DNA-binding protein hSSB1 controls DNA damage response

Chen, Z., Liu, B., Tang, N., Xu, Y., Ye, X., Li, Z., Niu, X., Shen, S.-P., Lu, S., & Xu, L. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku876 · Cited by 37 · see citing works

Targeting ubiquitin specific protease 7 in cancer: A deubiquitinase with great prospects

Khusbu, F. Y., Chen, F., & Chen, H. (2018) · Cell Biochemistry and Function · doi:10.1002/cbf.3336 · Cited by 36 · see citing works

Current and future directions of USP7 interactome in cancer study

Park, H., & Baek, K. (2023) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2023.188992 · Cited by 35 · see citing works

Environmental contaminants and microRNA regulation: Transcription factors as regulators of toxicant-altered microRNA expression

Sollome, J. J., Martin, E. M., Sethupathy, P., & Fry, R. C. (2016) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2016.06.009 · Cited by 32 · see citing works

Targeting Deubiquitinating Enzymes in Glioblastoma Multiforme: Expectations and Challenges

Jin, W., Mao, X., & Qiu, G. (2016) · Medicinal Research Reviews · doi:10.1002/med.21421 · Cited by 32 · see citing works

MicroRNA-205 regulates ubiquitin specific peptidase 7 protein expression in hepatocellular carcinoma cells

Zhu, L. W., Liu, R., Zhang, W., Qian, S., & Wang, J. (2015) · Molecular Medicine Reports · doi:10.3892/mmr.2015.3998 · Cited by 30 · see citing works

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 28 · see citing works

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 · see citing works

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 23 · see citing works

Ubiquitin-Specific Peptidase 7: A Novel Deubiquitinase That Regulates Protein Homeostasis and Cancers

Zhou, L., Ouyang, T., Li, M., Hong, T., Alriashy, M. H. S., Meng, W., & Zhang, N. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.784672 · Cited by 23 · see citing works

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 · see citing works

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 22 · see citing works

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 18 · see citing works

The BAH domain of BAF180 is required for PCNA ubiquitination

Niimi, A., Hopkins, S. R., Downs, J. A., & Masutani, C. (2015) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2015.06.006 · Cited by 18 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

CD137L promotes immune surveillance in melanoma via HLTF regulation

Liang, L., Zhu, L., Li, X., Zhou, W., Zhang, Y., Hung, M., Zhang, G., Chen, Y., Kuang, X., Su, J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-63338-w · Cited by 2 · see citing works

Structural Insight into the Mechanisms of Activation and Substrate Specificity of Human Deubiquitinating Enzyme USP7

Pozhidaeva, A. (2016) · OpenCommons at University of Connecticut (University of Connecticut)

Identification and Characterisation of Human Cytomegalovirus-Mediated Degradation of Helicase-Like Transcription Factor

Lin, K. (2021) · Apollo (University of Cambridge) · doi:10.17863/cam.65163

The Role of Ubiquitylation and SUMOylation in DNA Replication

Abbas, T. (2019) · Caister Academic Press eBooks · doi:10.21775/9781912530120.14

Ubiquitin’s code: UPS orchestrating DNA repair and genomic stability under genotoxic stress

Roy, S., Saha, G., Basu, M., & Ghosh, M. K. (2026) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-026-05498-x

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

Unk, I., Hajdú, I., Fátyol, K., Hurwitz, J., Yoon, J.-H., Prakash, L., Prakash, S., & Haracska, L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800563105 · Cited by 250 · 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

Helicase-Like Transcription Factor HLTF and E3 Ubiquitin Ligase SHPRH Confer DNA Damage Tolerance through Direct Interactions with Proliferating Cell Nuclear Antigen (PCNA)

Seelinger, M., & Otterlei, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21030693 · Cited by 23 · see citing works

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 31 · see citing works

USP7 modulates UV-induced PCNA monoubiquitination by regulating DNA polymerase eta stability.

Qian, J., Pentz, K., Zhu, Q., Wang, Q., He, J., Srivastava, A. K., & Wani, A. A. (2015) · Oncogene · doi:10.1038/onc.2014.394 · Cited by 61 · see citing works