The deubiquitinase USP38 promotes NHEJ repair through regulation of HDAC1 activity and regulates cancer cell response to genotoxic insults

The DNA-damage response in human biology and disease

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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

DNA damage response as a candidate anti-cancer barrier in early human tumorigenesis

Bartkova, J., Hořejší, Z., Koed, K., Krämer, A., Tort, F., Zieger, K., Guldberg, P., Sehested, M., Nesland, J. M., Lukas, C., et al. (2005) · Nature · doi:10.1038/nature03482 · Cited by 2,688 · see citing works

The many roles of histone deacetylases in development and physiology: implications for disease and therapy

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DNA damage, aging, and Cancer

Hoeijmakers, J. H. J. (2009) · New England Journal of Medicine · doi:10.1056/nejmra0804615 · Cited by 2,239 · see citing works

Erasers of Histone Acetylation: The Histone Deacetylase EnzymesPreprint

Seto, E., & Yoshida, M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018713 · Cited by 2,019 · see citing works

HDACs and HDAC Inhibitors in Cancer Development and TherapyPreprint

Li, Y., & Seto, E. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026831 · Cited by 1,309 · see citing works

Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications

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Histone deacetylases and cancer

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Human HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining

Miller, K. M., Tjeertes, J. V., Coates, J., Legube, G., Polo, S. E., Britton, S., & Jackson, S. P. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1899 · Cited by 629 · see citing works

Interplay of p53 and DNA-repair protein XRCC4 in tumorigenesis, genomic stability and development

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Regulation of DNA Damage Responses by Ubiquitin and SUMO

Jackson, S. P., & Durocher, D. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.017 · Cited by 601 · see citing works

DNA repair protein Ku80 suppresses chromosomal aberrations and malignant transformation

Difilippantonio, M. J., Zhu, J., Chen, H. T., Meffre, E., Nussenzweig, M. C., Max, E. E., Ried, T., & Nussenzweig, A. (2000) · Nature · doi:10.1038/35006670 · Cited by 546 · see citing works

DNA Ligase IV Deficiency in Mice Leads to Defective Neurogenesis and Embryonic Lethality via the p53 Pathway

Frank, K. M., Sharpless, N. E., Gao, Y., Sekiguchi, J., Ferguson, D. O., Zhu, C., Manis, J. P., Horner, J. W., DePinho, R. A., & Alt, F. W. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80264-6 · Cited by 492 · see citing works

HDAC and HDAC Inhibitor: From Cancer to Cardiovascular Diseases

Yoon, S., & Eom, G. H. (2016) · Chonnam Medical Journal · doi:10.4068/cmj.2016.52.1.1 · Cited by 469 · see citing works

Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4

Mari, P., Florea, B. I., Persengiev, S. P., Verkaik, N. S., Brüggenwirth, H. T., Modesti, M., Giglia‐Mari, G., Bezstarosti, K., Demmers, J., Luider, T. M., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609061103 · Cited by 423 · see citing works

Autophosphorylation of DNA-PKCS regulates its dynamics at DNA double-strand breaks

Uematsu, N., Weterings, E., Yano, K., Morotomi‐Yano, K., Jakob, B., Taucher-Scholz, G., Mari, P., van Gent, D. C., Chen, B. P. C., & Chen, D. J. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200608077 · Cited by 414 · see citing works

Screen for DNA‐damage‐responsive histone modifications identifies H3K9Ac and H3K56Ac in human cells

Tjeertes, J. V., Miller, K. M., & Jackson, S. P. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.119 · Cited by 347 · see citing works

Quantitative Proteomic Atlas of Ubiquitination and Acetylation in the DNA Damage Response

Elia, A. E. H., Boardman, A. P., Wang, D. C., Huttlin, E. L., Everley, R. A., Dephoure, N., Zhou, C., Koren, I., Gygi, S. P., & Elledge, S. J. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.05.006 · Cited by 324 · see citing works

The physiological roles of histone deacetylase (HDAC) 1 and 2: complex co-stars with multiple leading parts

Kelly, R. D. W., & Cowley, S. M. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130010 · Cited by 297 · see citing works

SIRT1 collaborates with ATM and HDAC1 to maintain genomic stability in neurons

Dobbin, M. M., Madabhushi, R., Pan, L., Chen, Y., Kim, D., Gao, J., Ahanonu, B., Pao, P.-C., Qiu, Y., Zhao, Y., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3460 · Cited by 250 · see citing works

The ubiquitous role of ubiquitin in the DNA damage response

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

PARP-1 mechanism for coupling DNA damage detection to poly(ADP-ribose) synthesis

Langelier, M.-F., & Pascal, J. M. (2013) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2013.01.003 · Cited by 215 · see citing works

Alternative end-joining catalyzes robust IgH locus deletions and translocations in the combined absence of ligase 4 and Ku70

Boboilă, C., Janković, M., Yan, C. T., Wang, J. H., Wesemann, D. R., Zhang, T., Fazeli, A., Feldman, L., Nussenzweig, A., Nussenzweig, M. C., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0915067107 · Cited by 206 · see citing works

Regulatory ubiquitylation in response to DNA double-strand breaks

Panier, S., & Durocher, D. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.01.013 · Cited by 193 · see citing works

Lymphocyte-Specific Compensation for XLF/Cernunnos End-Joining Functions in V(D)J Recombination

Li, G., Alt, F. W., Cheng, H.-L., Brush, J. W., Goff, P. H., Murphy, M., Franco, S., Zhang, Y., & Zha, S. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.017 · Cited by 191 · see citing works

USP1 Is Required for Replication Fork Protection in BRCA1-Deficient Tumors

Lim, K. S., Li, H., Roberts, E. A., Gaudiano, E. F., Clairmont, C. S., Sambel, L. A., Ponnienselvan, K., Liu, J., Yang, C., Kozono, D., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.10.045 · Cited by 174 · see citing works

Targeting Histone Deacetylases for Cancer Therapy: From Molecular Mechanisms to Clinical Implications

Li, Z., & Zhu, W. (2014) · International Journal of Biological Sciences · doi:10.7150/ijbs.9067 · Cited by 160 · see citing works

Chromosomal Loop Domains Direct the Recombination of Antigen Receptor Genes

Hu, J., Zhang, Y., Zhao, L., Frock, R. L., Du, Z., Meyers, R. M., Meng, F., Schatz, D. G., & Alt, F. W. (2015) · Cell · doi:10.1016/j.cell.2015.10.016 · Cited by 157 · see citing works

SUMO-mediated regulation of DNA damage repair and responses

Sarangi, P., & Zhao, X. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.02.006 · Cited by 155 · see citing works

Regulation of histone modification and chromatin structure by the p53–PADI4 pathway

Tanikawa, C., Espinosa‐Cantellano, M., Suzuki, A., Masuda, K., Yamamoto, K., Tsuchiya, E., Ueda, K., Daigo, Y., Nakamura, Y., & Matsuda, K. (2012) · Nature Communications · doi:10.1038/ncomms1676 · Cited by 153 · see citing works

RNF111-Dependent Neddylation Activates DNA Damage-Induced Ubiquitination

Ma, T., Chen, Y., Zhang, F., Yang, C., Wang, S., & Yu, X. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.006 · Cited by 148 · see citing works

USP38 Inhibits Type I Interferon Signaling by Editing TBK1 Ubiquitination through NLRP4 Signalosome

Lin, M., Zhao, Z., Yang, Z., Meng, Q., Tan, P., Xie, W., Qin, Y., Wang, R., & Cui, J. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.029 · Cited by 145 · see citing works

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 · see citing works

The multifaceted influence of histone deacetylases on DNA damage signalling and DNA repair

Roos, W. P., & Krumm, A. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw922 · Cited by 140 · see citing works

Ubiquitin-specific protease 7 sustains DNA damage response and promotes cervical carcinogenesis

Su, D., Ma, S., Shan, L., Wang, Y., Wang, Y., Cao, C., Liu, B., Yang, C., Wang, L., Tian, S., et al. (2018) · Journal of Clinical Investigation · doi:10.1172/jci120518 · Cited by 114 · see citing works

MDM2 E3 ligase-mediated ubiquitination and degradation of HDAC1 in vascular calcification

Kwon, D., Eom, G. H., Ko, J. H., Shin, S., Joung, H., Choe, N., Nam, Y. S., Min, H.-K., Kook, T., Yoon, S., et al. (2016) · Nature Communications · doi:10.1038/ncomms10492 · Cited by 107 · see citing works

PAXX and XLF DNA repair factors are functionally redundant in joining DNA breaks in a G1-arrested progenitor B-cell line

Kumar, V., Alt, F. W., & Frock, R. L. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1611882113 · Cited by 106 · see citing works

The deubiquitylating enzyme USP15 regulates homologous recombination repair and cancer cell response to PARP inhibitors

Peng, Y., Liao, Q., Tan, W., Peng, C., Hu, Z., Chen, Y., Li, Z., Li, J., Zhen, B., Zhu, W., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09232-8 · Cited by 104 · see citing works

Selective cancer targeting with prodrugs activated by histone deacetylases and a tumour-associated protease

Ueki, N., Lee, S., Sampson, N. S., & Hayman, M. J. (2013) · Nature Communications · doi:10.1038/ncomms3735 · Cited by 100 · see citing works

USP51 deubiquitylates H2AK13,15ub and regulates DNA damage responsePreprint

Wang, Z., Zhang, H., Liu, J., Cheruiyot, A., Lee, J., Ördög, T., Lou, Z., You, Z., & Zhang, Z. (2016) · Genes & Development · doi:10.1101/gad.271841.115 · Cited by 95 · see citing works

Suppression of Nonhomologous End Joining Repair by Overexpression of HMGA2

Li, A. Y. J., Boo, L. M., Wang, S., Lin, H. H., Wang, C. C. C., Yen, Y., Chen, B. P. C., Chen, D. J., & Ann, D. K. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-4833 · Cited by 90 · see citing works

Modulation of LSD1 phosphorylation by CK2/WIP1 regulates RNF168-dependent 53BP1 recruitment in response to DNA damage

Peng, B., Wang, J., Hu, Y., Zhao, H., Hou, W., Zhao, H., Wang, H., Liao, J., & Xu, X. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv528 · Cited by 78 · see citing works

USP4 Auto-Deubiquitylation Promotes Homologous Recombination

Wijnhoven, P. W. G., Konietzny, R., Blackford, A. N., Travers, J., Kessler, B. M., Nishi, R., & Jackson, S. P. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.09.019 · Cited by 78 · see citing works

Regulation of the DNA damage response by ubiquitin conjugation

Brinkmann, K., Schell, M. J., Hoppe, T., & Kashkar, H. (2015) · Frontiers in Genetics · doi:10.3389/fgene.2015.00098 · Cited by 70 · see citing works

The ubiquitin specific protease USP34 promotes ubiquitin signaling at DNA double-strand breaks

Sy, S. M.-H., Jiang, J., O, W. S., Deng, Y., & Huen, M. S. Y. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt622 · Cited by 68 · see citing works

Ubiquitin-specific protease 21 stabilizes BRCA2 to control DNA repair and tumor growth

Liu, J., Kruswick, A., Dang, H. T., Tran, A. D., Kwon, S. M., Wang, X. W., & Oberdoerffer, P. (2017) · Nature Communications · doi:10.1038/s41467-017-00206-2 · Cited by 59 · see citing works

Chromatin modifications during repair of environmental exposure‐induced DNA damage: A potential mechanism for stable epigenetic alterations

O’Hagan, H. M. (2013) · Environmental and Molecular Mutagenesis · doi:10.1002/em.21830 · Cited by 58 · see citing works

Histone modification and chromatin remodeling during NER

Waters, R., van Eijk, P., & Reed, S. H. (2015) · DNA repair · doi:10.1016/j.dnarep.2015.09.013 · Cited by 57 · see citing works

Regulation of histone modifying enzymes by the ubiquitin–proteasome system

Zou, C., & Mallampalli, R. K. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.12.016 · Cited by 53 · see citing works

USP38 critically promotes asthmatic pathogenesis by stabilizing JunB protein

Chen, S., Yun, F., Yao, Y., Cao, M., Zhang, Y., Wang, J., Song, X., & Qian, Y. (2018) · The Journal of Experimental Medicine · doi:10.1084/jem.20172026 · Cited by 49 · see citing works

USP19 deubiquitinates HDAC1/2 to regulate DNA damage repair and control chromosomal stability

Wu, M., Tu, H.-Q., Chang, Y., Tan, B., Wang, G., Zhou, J., Wang, L., Mu, R., & Zhang, W. (2016) · Oncotarget · doi:10.18632/oncotarget.11116 · Cited by 36 · see citing works

Subdivision of molecularly-classified groups by new gene signatures in breast cancer patients

Armakolas, A., Stathopoulos, G. P., Nezos, A., Theos, A., Stathaki, M., & Koutsilieris, M. (2012) · Oncology Reports · doi:10.3892/or.2012.2018 · Cited by 24 · see citing works

The Commercial Antibodies Widely Used to Measure H3 K56 Acetylation Are Non-Specific in Human and Drosophila Cells

Pal, S., Graves, H. K., Ohsawa, R., Huang, T. H., Wang, P., Harmacek, L. D., & Tyler, J. K. (2016) · PLoS ONE · doi:10.1371/journal.pone.0155409 · Cited by 16 · see citing works

ABIN1 inhibits HDAC1 ubiquitination and protects it from both proteasome‐ and lysozyme‐dependent degradation

Ma, Y., Yuan, S., Tian, X., Lin, S., Wei, S., Hu, T., Chen, S., Li, X., Chen, S., Wu, D., et al. (2017) · Journal of Cellular Biochemistry · doi:10.1002/jcb.26428 · Cited by 10 · see citing works

Drug resistance mechanisms and treatment strategies mediated by Ubiquitin-Specific Proteases (USPs) in cancers: new directions and therapeutic options

Gao, H., Xi, Z., Dai, J., Xue, J., Guan, X., Zhao, L., Chen, Z., & Xing, F. (2024) · Molecular Cancer · doi:10.1186/s12943-024-02005-y · Cited by 79 · see citing works

Role of K63-linked ubiquitination in cancer

Cao, L., Liu, X., Zheng, B., Xing, C., & Liu, J. (2022) · Cell Death Discovery · doi:10.1038/s41420-022-01204-0 · Cited by 73 · see citing works

Multi-ancestry genome-wide association study of kidney cancer identifies 63 susceptibility regions

Purdue, M. P., Dutta, D., Machiela, M. J., Gorman, B. R., Winter, T., Okuhara, D. Y., Cleland, S., Ferreiro-Iglesias, A., Scheet, P. A., Liu, A., et al. (2024) · Nature Genetics · doi:10.1038/s41588-024-01725-7 · Cited by 60 · see citing works

Deubiquitinating enzymes: Promising targets for drug resistance

Ge, F., Li, Y., Yuan, T., Wu, Y., He, Q., Yang, B., & Zhu, H. (2022) · Drug Discovery Today · doi:10.1016/j.drudis.2022.06.009 · Cited by 56 · see citing works

HDACs and the epigenetic plasticity of cancer cells: target the complexity

Brancolini, C., Gagliano, T., & Minisini, M. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108190 · Cited by 55 · see citing works

Mitochondrial dysfunction induces radioresistance in colorectal cancer by activating [Ca2+]m-PDP1-PDH-histone acetylation retrograde signaling

Shi, Y., Wang, Y., Jiang, H., Sun, X., Xu, H., Xue, W., Yan, W., Xiao, G., Song, Z., & Zhou, F. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03984-2 · Cited by 55 · see citing works

Histone post-translational modification and the DNA damage response

Song, H., Shen, R., Liu, X., Yang, X., Xie, K., Guo, Z., & Wang, D. (2022) · Genes & Diseases · doi:10.1016/j.gendis.2022.04.002 · Cited by 54 · see citing works

DNA Double-Strand Breaks as Pathogenic Lesions in Neurological Disorders

Provasek, V. E., Mitra, J., Malojirao, V. H., & Hegde, M. L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094653 · Cited by 51 · see citing works

Deubiquitinase OTUD6A promotes breast cancer progression by increasing TopBP1 stability and rendering tumor cells resistant to DNA-damaging therapy

Zhao, Y., Huang, X., Zhu, D., Wei, M., Luo, J., Yu, S., Tian, Y., & Zheng, X. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01036-6 · Cited by 50 · see citing works

USP38 Inhibits Zika Virus Infection by Removing Envelope Protein Ubiquitination

Wang, Y., Li, Q., Hu, D., Gao, D., Wang, W., Wu, K., & Wu, J. (2021) · Viruses · doi:10.3390/v13102029 · Cited by 36 · see citing works

Role of deubiquitinating enzymes in DNA double-strand break repair

Li, Y., & Yuan, J. (2021) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b2000309 · Cited by 24 · see citing works

Ubiquitin specific protease 38 aggravates pathological cardiac remodeling by stabilizing phospho-TBK1

Xiao, Z., Dai, C., Yu, T., Zhu, J., Pan, Y., Shuai, W., Kong, B., & Huang, H. (2024) · International Journal of Biological Sciences · doi:10.7150/ijbs.85562 · Cited by 22 · see citing works

METTL7B-induced histone lactylation prevents heart failure by ameliorating cardiac remodelling

Chen, Z., Zhong, M., Lin, Y., Zhang, W., Zhu, Y., Chen, L., Huang, Z., Luo, K., Lu, Z., Huang, Z., et al. (2025) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2025.03.006 · Cited by 22 · see citing works

The deubiquitinase USP38 promotes cell proliferation through stabilizing c-Myc

Xu, Z., Hu, H. Q., Fang, D., Wang, J., & Zhao, K. (2021) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2021.106023 · Cited by 21 · see citing works

Histone lysine modifying enzymes and their critical roles in DNA double-strand break repair

Zhang, J., Lu, X., MoghaddamKohi, S., Shi, L., Xu, X., & Zhu, W. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103206 · Cited by 18 · see citing works

USP38 inhibits colorectal cancer cell proliferation and migration via downregulating HMX3 ubiquitylation

Wang, J., Gu, Y., Yan, X., Zhang, J., Wang, J., & Ding, Y. J. (2022) · Cell Cycle · doi:10.1080/15384101.2022.2042776 · Cited by 16 · see citing works

The Emerging Role of Deubiquitinases in Radiosensitivity

Cao, X., Yan, Z., Chen, Z., Ge, Y., Hu, X., Peng, F., Huang, W., Zhang, P., Sun, R., Chen, J., et al. (2023) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2023.12.003 · Cited by 15 · see citing works

Ubiquitin specific peptidase 38 epigenetically regulates KLF transcription factor 5 to augment malignant progression of lung adenocarcinoma

Zhang, T., Su, F., Wang, B., Liu, L., Lu, Y., Su, H., Ling, R., Yue, P., Dai, H., Yang, T., et al. (2024) · Oncogene · doi:10.1038/s41388-024-02985-7 · Cited by 16 · see citing works

Lactylation of Hdac1 regulated by Ldh prevents the pluripotent-to-2C state conversion

Dong, Q., Yang, X., Wang, L., Zhang, Q., Zhao, N., Nai, S., Du, X., & Chen, L. (2024) · Stem Cell Research & Therapy · doi:10.1186/s13287-024-04027-1 · Cited by 12 · see citing works

USP38 functions as an oncoprotein by downregulating the p53 pathway through deubiquitination and stabilization of MDM2

Zhao, S., Liu, X., Luo, R., Jian, Z., Xu, C., Hou, Y., Liu, X., & Zhang, P. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01462-2 · Cited by 10 · see citing works

Platinum-Resistant Ovarian Cancer Is Vulnerable to the cJUN-XRCC4 Pathway Inhibition

Xu, M., Huang, X., Zheng, C., Long, J., Dai, Q., Chen, Y., Lu, J., Pan, C., Yao, S., & Li, J. (2022) · Cancers · doi:10.3390/cancers14246068 · Cited by 9 · see citing works

Recent advances in HDAC-targeted imaging probes for cancer detection

Tang, C. C., Wang, X., Jin, Y., & Wang, F. (2022) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2022.188788 · Cited by 9 · see citing works

Discovery of deoxyandrographolide and its novel effect on vascular senescence by targeting HDAC1

Lin, Z., He, H., Xian, Y., Cai, J., Ge, Q., Guo, M., Zheng, Q., Liu, X., Mo, C., Zhang, X., et al. (2023) · MedComm · doi:10.1002/mco2.338 · Cited by 8 · see citing works

Role of liquid–liquid phase separation in cancer: Mechanisms and therapeutic implications

Li, X., & Yu, Z. (2024) · Cancer Innovation · doi:10.1002/cai2.144 · Cited by 8 · see citing works

Emerging Roles of Non-proteolytic Ubiquitination in Tumorigenesis

Yin, X., Liu, Q., Liu, F., Tian, X., Yan, T., Han, J., & Jiang, S. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.944460 · Cited by 8 · see citing works

Post-Translational Modifications by Lipid Metabolites during the DNA Damage Response and Their Role in Cancer

Zhu, G.-R., Zheng, X., Wang, Z., & Xu, X. (2022) · Biomolecules · doi:10.3390/biom12111655 · Cited by 8 · see citing works

Ubiquitin-specific protease 38 exacerbates diabetic cardiomyopathy via post-translational modification of ACAD11

Xiao, Z., Pan, Y., Meng, H., Qu, Z., Guo, L., Kong, B., Shuai, W., & Huang, H. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103704 · Cited by 7 · see citing works

USP38 exacerbates pressure overload-induced left ventricular electrical remodeling

Pan, Y., Xiao, Z., Yang, H., Kong, B., Meng, H., Shuai, W., & Huang, H. (2024) · Molecular Medicine · doi:10.1186/s10020-024-00846-3 · Cited by 7 · see citing works

USP5 ‐dependent HDAC1 promotes cisplatin resistance and the malignant progression of non–small cell lung cancer by regulating RILP acetylation levels

Lu, R., Jin, Y., & Zheng, M. (2024) · Thoracic Cancer · doi:10.1111/1759-7714.15478 · Cited by 6 · see citing works

Mechanisms of cisplatin sensitivity and resistance in testicular germ cell tumors and potential therapeutic agents (Review)

Zhan, Z., Luo, X., Shi, J., Chen, L., Ye, M., & Jin, X. (2025) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2025.12832 · Cited by 6 · see citing works

Decoding the ubiquitin network: molecular mechanisms and therapeutic vulnerabilities for precision radio-sensitization in cancer

Zhao, F.-Y., Shi, L., Yu, L.-J., Wang, S., Sun, C.-Y., Zhang, N., & Wang, H. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02433-4 · Cited by 6 · see citing works

Fusion of Tumor Cells with Lipid-Associated Macrophages Drives Metastatic Progression of Breast Cancer

Cheng, Y., Huang, G., Liu, X., Wu, C., Lian, J., Cao, J., Duan, L., Zhao, B., Yang, Y., Chen, S., et al. (2025) · Cancer Research · doi:10.1158/0008-5472.can-25-0261 · Cited by 6 · see citing works

AKT and DUBs: a bidirectional relationship

Serratore, V., Lucibello, M., Malanga, D., Viglietto, G., & Marco, C. D. (2025) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-025-00753-3 · Cited by 5 · see citing works

ADAR promotes USP38 auto-deubiquitylation and stabilization in an RNA editing–independent manner in esophageal squamous cell carcinoma

Hu, Q., Chen, Y., Zhou, Q., Deng, S., Hou, W., Yi, Y., Li, C., & Tang, J. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107789 · Cited by 5 · see citing works

Integrated analysis of histone modification features in clear cell renal cancer for risk stratification and therapeutic prediction

Ma, W., Ge, Q., Guan, Y., Zhang, L., Huang, L., Chen, L., Xu, W., Meng, J., Yang, G., & Liang, C. Y. (2024) · Translational Oncology · doi:10.1016/j.tranon.2024.102042 · Cited by 5 · see citing works

USP38 promotes oxidative stress and inflammation and aggravates doxorubicin-induced cardiotoxicity by deubiquitinating and stabilizing PTEN

Xu, C., Pan, Y., Guo, L., Meng, H., Shuai, W., & Huang, H. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.115750 · Cited by 4 · see citing works

Useful genes for predicting the efficacy of transarterial chemoembolization in hepatocellular carcinoma

Guo, Y., Hu, H., Xu, S., Xia, W., & Li, H.-L. (2022) · Journal of Cancer Research and Therapeutics · doi:10.4103/jcrt.jcrt_1479_22 · Cited by 4 · see citing works

HDAC1: An Essential and Conserved Member of the Diverse Zn2+-Dependent HDAC Family Driven by Divergent Selection Pressure

Yang, J., Shi, L.-R., Wang, K.-C., Huang, L., Deng, Y.-S., Chen, M., Wan, F., & Zhou, Z. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242317072 · Cited by 4 · see citing works

Impact of life adversity and gene expression on psychiatric symptoms in children and adolescents: findings from the Brazilian high risk cohort study

Ota, V., de Oliveira, A. M., Bugiga, A., Conceição, H. B., Galante, P. A. F., Asprino, P. F., Schäfer, J., Hoffmann, M. S., Bressan, R. A., Brietzke, E. M., et al. (2025) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2025.1505421 · Cited by 4 · see citing works

Interplay Between the Cytoskeleton and DNA Damage Response in Cancer Progression

Halim, C. E., Deng, S., Crasta, K., & Yap, C. T. (2025) · Cancers · doi:10.3390/cancers17081378 · Cited by 5 · see citing works

USP38: an important regulatory factor in tumor malignant progression

Li, J., Zhong, J., Ye, J., Xiang, Y., Yi, Q., Zhu, G., Deng, S., & Wang, X. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1612723 · Cited by 3 · see citing works

Advancing the Exploration of the Ubiquitin‐like Protein FUBI with Synthetic Chemical Tools

D’Amico, F., Ormeño, C. M. P. T., Poeran, S., Akkermans, J. J. L. L., Tjokrodirijo, R. T. N., Sampadi, B. K., van Veelen, P. A., Sapmaz, A., & Mulder, M. P. C. (2025) · ChemBioChem · doi:10.1002/cbic.202500321 · Cited by 3 · see citing works

USP38 protein alleviates neuroinflammation of cerebral ischemia–reperfusion injury via KDM5B expression

Wang, H., & Xue, X. (2021) · Molecular & Cellular Toxicology · doi:10.1007/s13273-021-00154-5 · Cited by 2 · see citing works

Deubiquitinating enzyme JOSD2 affects susceptibility of non-small cell lung carcinoma cells to anti-cancer drugs through DNA damage repair

Ge, F., Liu, X., Zhang, H., Yuan, T., Zhu, H. M., Yang, B., & He, Q. (2023) · Journal of Zhejiang University (Medical Sciences) · doi:10.3724/zdxbyxb-2023-0256 · Cited by 2 · see citing works

Regulatory mechanism and prognostic value of sex hormone pathways connected with metabolism and immune signaling in clear cell renal cell carcinoma

Geng, X., Shan, J., Dai, Y., Liu, Z., Min, S., Zhao, S., Zhang, Z., Shi, K., Zhang, D., Ji, T., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-97163-4 · Cited by 1 · see citing works

Deubiquitinases in DNA damage repair: Implication and mechanism in cancer

Li, L., Gu, X., & Zhang, T. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.152914 · Cited by 1 · see citing works

Inhibiting ubiquitin-specific protease 38 safeguards against diabetic nephropathy by limiting tubular epithelial cell ferroptotic death through the suppression of IREB2-mediated iron overload

Gao, S., Dong, C., Li, H., Li, J., & Abula, A. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.116307 · Cited by 1 · see citing works

Linking Gene Fusions to Bone Marrow Failure and Malignant Transformation in Dyskeratosis Congenita

Güllülü, Ö., Mayer, B. E., & Toplek, F. B. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031606 · Cited by 1 · see citing works

Exploring the Mechanism of Echinatin against Cervical Cancer Based on Network Pharmacology

Chen, H., & Wang, J. (2024) · Journal of Clinical Pharmacy and Therapeutics · doi:10.1155/2024/7008847 · Cited by 1 · see citing works

Unveiling the conversion mechanism of glioblastoma from the mesenchymal to the proneural subtype driven by HDAC1/p-SMAD3-TP53I11 axisPreprint

Zhao, K., Hai, Z., Shang, R., Liang, H., Wang, C., Zhu, M., & Chen, W. (2024) · Research Square · doi:10.21203/rs.3.rs-4733991/v1

USP38 deletion improved diastolic dysfunction and arrhythmogenesis in heart failure mice with preserved ejection fraction

Meng, H., Qu, Z., Guo, L., Kong, B., Yang, H., Huang, H., & Shuai, W. (2025) · Heart Rhythm · doi:10.1016/j.hrthm.2025.04.024

Genomic Evidence for Elevational Segregation and Adaptive Introgression in Prunellidae Radiation

Wu, X., Zang, W., Ericson, P. G. P., & Qu, Y. (2025) · Molecular Ecology · doi:10.1111/mec.70213

Additional file 1 of USP38 exacerbates pressure overload-induced left ventricular electrical remodeling

Pan, Y., Xiao, Z., Yang, H., Kong, B., Meng, H., Shuai, W., & Huang, H. (2024) · Figshare · doi:10.6084/m9.figshare.26122747

Deubiquitinase USP38 Stabilizes PLK1 Expression to Boost DNA Damage Repair in Ovarian Cancer

Ma, Y., Li, Y., & Li, K. (2026) · The Kaohsiung Journal of Medical Sciences · doi:10.1002/kjm2.70197 · Cited by 1 · see citing works

Modulation des voies de réparation des cassures double-brin de l’ADN par ZEB1, un facteur de transcription impliqué dans l’EMT, dans le cancer du sein

Prodhomme, M. K. (2020) · theses.fr (ABES) · doi:10.70675/b91f7284z097fz467czb4d1ze6e33914f9d7

Unveiling the conversion mechanism of glioblastoma from the mesenchymal to the proneural subtype driven by HDAC1/p-SMAD3-TP53I11 axis

Wang, C., Shang, R., Liang, H., Zhu, M., Chen, W., & Zhao, K. (2026) · Translational Oncology · doi:10.1016/j.tranon.2026.102912

Orchestrating cancer stem cell plasticity: deubiquitinases as key regulators of EMT and metabolic rewiring

Qin, T., Wang, Y., Li, M., Liu, Q., Yue, L., Liang, S., & Sun, D. (2026) · Frontiers in Medicine · doi:10.3389/fmed.2026.1957953

Tight regulation of ubiquitin-mediated DNA damage response by USP3 preserves the functional integrity of hematopoietic stem cells

Lancini, C., van den Berk, P. C. M., Vissers, J. H. A., Gargiulo, G., Song, J., Hulsman, D., Serresi, M., Tanger, E., Blom, M., Vens, C., et al. (2014) · The Journal of Experimental Medicine · doi:10.1084/jem.20131436 · Cited by 78 · see citing works

USP38 regulates the stemness and chemoresistance of human colorectal cancer via regulation of HDAC3

Zhan, W., Liao, X., Liu, J., Tian, T., Yu, L., & Li, R. (2020) · Oncogenesis · doi:10.1038/s41389-020-0234-z · Cited by 51 · see citing works

The E3 ubiquitin ligase DTX3L and the deubiquitinase USP28 fine-tune DNA repair through mutual regulation of their protein levels

Mennerich, D., Ashok, Y., Vela‐Rodríguez, C., Hentilä, H. I., Rall-Scharpf, M., Wiesmüller, L., Prunskaite‐Hyyryläinen, R., Lehtiö, L., & Kietzmann, T. (2025) · iScience · doi:10.1016/j.isci.2025.112990 · Cited by 10 · see citing works

Deubiquitinase USP38 Stabilizes PLK1 Expression to Boost DNA Damage Repair in Ovarian Cancer

Ma, Y., Li, Y., & Li, K. (2026) · The Kaohsiung Journal of Medical Sciences · doi:10.1002/kjm2.70197 · Cited by 1 · see citing works

USP25 Elevates SHLD2‐Mediated DNA Double‐Strand Break Repair and Regulates Chemoresponse in Cancer

Li, Y., Li, L., Wang, X., Zhao, F., Yang, Y., Zhou, Y., Zhang, J., Wang, L., Jiang, Z., Zhang, Y., et al. (2024) · Advanced Science · doi:10.1002/advs.202403485 · Cited by 11 · see citing works