Activity-based ubiquitin-specific protease (USP) profiling of virus-infected and malignant human cells

The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction

Glickman, M. H., & Ciechanover, A. J. (2002) · Physiological Reviews · doi:10.1152/physrev.00027.2001 · Cited by 4,296

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 1,048

The tumour suppressor CYLD negatively regulates NF-κB signalling by deubiquitination

Kovalenko, A., Chable-Bessia, C., Cantarella, G., Israël, A., Wallach, D., & Courtois, G. (2003) · Nature · doi:10.1038/nature01802 · Cited by 1,018

CYLD is a deubiquitinating enzyme that negatively regulates NF-κB activation by TNFR family members

Trompouki, E., Hatzivassiliou, E., Tsichritzis, T., Farmer, H., Ashworth, A., & Mosialos, G. (2003) · Nature · doi:10.1038/nature01803 · Cited by 964

Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-κB

Brummelkamp, T. R., Nijman, S. M. B., Dirac, A. M. G., & Bernards, R. (2003) · Nature · doi:10.1038/nature01811 · Cited by 947

The Neuron-Specific Protein PGP 9.5 Is a Ubiquitin Carboxyl-Terminal Hydrolase

Wilkinson, K. D., Lee, K., Deshpande, S. S., Duerksen-Hughes, P. J., Boss, J. M., & Pohl, J. (1989) · Science · doi:10.1126/science.2530630 · Cited by 871

The UCH-L1 Gene Encodes Two Opposing Enzymatic Activities that Affect α-Synuclein Degradation and Parkinson's Disease Susceptibility

Liu, Y., Fallon, L., Lashuel, H. A., Liu, Z., & Lansbury, P. T. (2002) · Cell · doi:10.1016/s0092-8674(02)01012-7 · Cited by 786

A cryptic protease couples deubiquitination and degradation by the proteasome

Yao, T., & Cohen, R. E. (2002) · Nature · doi:10.1038/nature01071 · Cited by 727

BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and enhances BRCA1-mediated cell growth suppression

Jensen, D. E., Proctor, M. L., Marquis, S. T., Gardner, H. P., Ha, S. I., Chodosh, L. A., Ishov, A. M., Tommerup, N., Vissing, H., Sekido, Y., et al. (1998) · Oncogene · doi:10.1038/sj.onc.1201861 · Cited by 725

Chemistry-Based Functional Proteomics Reveals Novel Members of the Deubiquitinating Enzyme Family

Borodovsky, A., Ovaa, H., Kolli, N., Gan-Erdene, T., Wilkinson, K. D., Ploegh, H. L., & Kessler, B. M. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00248-x · Cited by 588

The Epstein–Barr virus noncoding RNA EBER2 transactivates the UCHL1 deubiquitinase to accelerate cell growth

Li, Z., Baccianti, F., Delécluse, S., Tsai, M., Shumilov, A., Cheng, X., Ma, S., Hoffmann, I., Poirey, R., & Delecluse, H. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2115508118 · Cited by 29

Chemistry-based functional proteomics for drug target deconvolution

Wang, K., Yang, T., Wu, Q., Zhao, X., Nice, E. C., & Huang, C. (2012) · Expert Review of Proteomics · doi:10.1586/epr.12.19 · Cited by 29

The ubiquitin C‐terminal hydrolase UCH‐L1 regulates B‐cell proliferation and integrin activation

Rolén, U., Freda, E., Xie, J., Pfirrmann, T., Frisan, T., & Masucci, M. G. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00501.x · Cited by 29

Herpes Simplex Virus Type 1 ICP0 Phosphorylation Mutants Impair the E3 Ubiquitin Ligase Activity of ICP0 in a Cell Type-Dependent Manner

Boutell, C., Everett, R. D., Hilliard, J. G., Schaffer, P. A., Orr, A., & Davido, D. J. (2008) · Journal of Virology · doi:10.1128/jvi.01063-08 · Cited by 28

The ubiquitin C-terminal hydrolase UCH-L1 promotes bacterial invasion by altering the dynamics of the actin cytoskeleton

Bassères, E., Coppotelli, G., Pfirrmann, T., Andersen, J. B., Masucci, M. G., & Frisan, T. (2010) · Cellular Microbiology · doi:10.1111/j.1462-5822.2010.01495.x · Cited by 27

Multifarious proteomic signatures and regional heterogeneity in glioblastomas

Park, C., Jung, J. H., Park, S., Jung, H., & Cho, B.-K. (2009) · Journal of Neuro-Oncology · doi:10.1007/s11060-009-9805-8 · Cited by 25

S‐phase kinase protein 2 is an attractive therapeutic target in a subset of diffuse large B‐cell lymphoma

Shahab Uddin, M. S., Hussain, A. R., Ahmed, M., Belgaumi, A., Al‐Dayel, F., Ajarim, D. S., Bavi, P. P., & Al-Kuraya, K. S. (2008) · The Journal of Pathology · doi:10.1002/path.2433 · Cited by 25

Biological functions of hyaluronan and cytokine-inducible deubiquitinating enzymes

Ramakrishna, S., Suresh, B., & Baek, K. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.11.006 · Cited by 24

Bortezomib-mediated expression of p27Kip1 through S-phase kinase protein 2 degradation in epithelial ovarian cancer

Shahab Uddin, M. S., Ahmed, M., Hussain, A. R., Jehan, Z., Al‐Dayel, F., Munkarah, A. R., Bavi, P. P., & Al-Kuraya, K. S. (2009) · Laboratory Investigation · doi:10.1038/labinvest.2009.75 · Cited by 22

Transcriptional Profiling of Laser Capture Microdissected Rat Arterial Elements: Fenoldopam-induced Vascular Toxicity as a Model System

Dalmas, D. A., Scicchitano, M. S., Chen, Y., Kane, J., Mirabile, R. C., Schwartz, L. W., Thomas, H. C., & Boyce, R. W. (2008) · Toxicologic Pathology · doi:10.1177/0192623307311400 · Cited by 22

KSHV LANA and EBV LMP1 induce the expression of UCH-L1 following viral transformation

Bentz, G. L., Bheda-Malge, A., Wang, L., Shackelford, J., Damania, B., & Pagano, J. S. (2013) · Virology · doi:10.1016/j.virol.2013.10.018 · Cited by 20

Ubiquitin-proteasome genes as targets for modulation of cisplatin sensitivity in fission yeast

Gatti, L., Hoe, K., Hayles, J., Righetti, S. C., Carenini, N., Bo, L. D., Kim, D. U., Park, H. O., & Perego, P. (2011) · BMC Genomics · doi:10.1186/1471-2164-12-44 · Cited by 20

Epithelial Proteomics in Multiple Organs and Tissues: Similarities and Variations between Cells, Organs, and Diseases

Zhao, H., Adler, K. B., Bai, C., Tang, F., & Wang, X. (2006) · Journal of Proteome Research · doi:10.1021/pr050389v · Cited by 20

Inhibition of the deubiquitinating enzyme USP47 as a novel targeted therapy for hematologic malignancies expressing mutant EZH2

Yang, J. C., Weisberg, E., Qi, S., Wei Min, N. I., Mei, H., Wang, Z., Meng, C., Zhang, S., Hou, M., Qi, Z., et al. (2022) · Leukemia · doi:10.1038/s41375-021-01494-w · Cited by 19

The Promise of Proteomics in the Study of Oncogenic Viruses

McBride, A. A. (2017) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o116.065201 · Cited by 19

Discovery of Small Molecule Antagonists of the USP5 Zinc Finger Ubiquitin-Binding Domain

Mann, M. K., Franzoni, I., de Freitas, R. F., Tempel, W., Houliston, S., Smith, L., Vedadi, M., Arrowsmith, C. H., Harding, R., & Schapira, M. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00988 · Cited by 17

PU.1-dependent regulation of UCH L1 expression in B-lymphoma cells

Bheda, A., Yue, W., Gullapalli, A., Shackelford, J., & Pagano, J. S. (2011) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428194.2011.562571 · Cited by 18

Cloning and Characterization of the Human USP22 Gene Promoter

Xiong, J., Che, X., Li, X., Yu, H., Gong, Z., & Li, W. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052716 · Cited by 18

Alterations in gene expression profiles correlated with cisplatin cytotoxicity in the glioma U343 cell line

Carminati, P. O., Mello, S. S., Fachin, A. L., Junta, C. M., Sandrin‐Garcia, P., Carlotti, C. G., Donadi, E. A., Passos, G. A. S., & Sakamoto‐Hojo, E. T. (2010) · Genetics and Molecular Biology · doi:10.1590/s1415-47572010005000013 · Cited by 17

Dysregulated expression of SKP2 and its role in hematological malignancies

Kuliński, M., Achkar, I. W., Haris, M., Dermime, S., Mohammad, R. M., & Shahab Uddin, M. S. (2017) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428194.2017.1359740 · Cited by 17

ABPP and Host–Virus Interactions

Desrochers, G. F., & Pezacki, J. P. (2018) · Current topics in microbiology and immunology · doi:10.1007/82_2018_139 · Cited by 17

Proteasomal Serine Hydrolases Are Up-Regulated by and Required for Influenza Virus Infection

Shahiduzzaman, M., Ezatti, P., Xin, G., & Coombs, K. M. (2014) · Journal of Proteome Research · doi:10.1021/pr5001779 · Cited by 16

The Role of Coinfections in the EBV–Host Broken Equilibrium

Sánchez-Ponce, Y., & Fuentes‐Pananá, E. M. (2021) · Viruses · doi:10.3390/v13071399 · Cited by 16

A Novel RNAi Lethality Rescue Screen to Identify Regulators of Adipogenesis

van Beekum, O., Gao, Y., Berger, R., Koppen, A., & Kalkhoven, E. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037680 · Cited by 16

Putting proteomics on target: activity-based profiling of ubiquitin and ubiquitin-like processing enzymes

Kessler, B. M. (2006) · Expert Review of Proteomics · doi:10.1586/14789450.3.2.213 · Cited by 16

The Central Role of the Ubiquitin–Proteasome System in EBV-Mediated Oncogenesis

Pei, Y., & Robertson, E. S. (2022) · Cancers · doi:10.3390/cancers14030611 · Cited by 15

A patent review of ubiquitin-specific protease 7 (USP7) inhibitors (2014-present)

Li, P., Liu, Y., & Liu, H.-M. (2022) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2022.2058873 · Cited by 16

Relapsed/Refractory Multiple Myeloma: Defining Refractory Disease and Identifying Strategies to Overcome Resistance

Siegel, D. S. D. (2012) · Seminars in Hematology · doi:10.1053/j.seminhematol.2012.05.005 · Cited by 15

Biotransformation of Chinese Herbs and Their Ingredients

Bai-ping, M., Feng, B., Hongzhi, H., & Yuwen, C. (2010) · World Science and Technology · doi:10.1016/s1876-3553(11)60012-4 · Cited by 15

Mechanism‐Based Proteomics Tools Based on Ubiquitin and Ubiquitin‐Like Proteins: Crystallography, Activity Profiling, and Protease Identification

Galardy, P. J., Ploegh, H. L., & Ovaa, H. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)99008-3 · Cited by 15

Molecular piracy: manipulation of the ubiquitin system by Kaposi's sarcoma‐associated herpesvirus

Fujimuro, M., Hayward, S. D., & Yokosawa, H. (2007) · Reviews in Medical Virology · doi:10.1002/rmv.549 · Cited by 14

DUBbing Down Translation: The Functional Interaction of Deubiquitinases with the Translational Machinery

Kapadia, B. B., & Gartenhaus, R. B. (2019) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-19-0307 · Cited by 14

Integrative oncoproteomics strategies for anticancer drug discovery

Liu, R., Wang, K., Yuan, K., Wei, Y., & Huang, C. (2010) · Expert Review of Proteomics · doi:10.1586/epr.10.14 · Cited by 13

Viral–Host Interactome Analysis Reveals Chicken STAU2 Interacts With Non-structural Protein 1 and Promotes the Replication of H5N1 Avian Influenza Virus

Wang, Q., Zhang, Q., Zheng, M., Wen, J., Li, Q., & Zhao, G. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.590679 · Cited by 13

Strategies for detection and quantification of cysteine cathepsins-evolution from bench to bedside

Hughes, C. S., Burden, R. E., Gilmore, B., & Scott, C. J. (2015) · Biochimie · doi:10.1016/j.biochi.2015.07.029 · Cited by 13

Ubiquitin-specific protease 5 was involved in the interferon response to RGNNV in sea perch (Lateolabrax japonicus)

Jia, P., Zhang, W., Xiang, Y., Lu, X., Liu, W., Jia, K., & Yi, M. (2020) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2020.04.065 · Cited by 12

Current Approaches on Viral Infection: Proteomics and Functional Validations

Zheng, J., Tan, B. H., Sugrue, R. J., & Tang, K. (2012) · Frontiers in Microbiology · doi:10.3389/fmicb.2012.00393 · Cited by 11

Chlorovirus Skp1-Binding Ankyrin Repeat Protein Interplay and Mimicry of Cellular Ubiquitin Ligase Machinery

Noel, E. A., Kang, M., Adamec, J., Etten, J. L. V., & Oyler, G. A. (2014) · Journal of Virology · doi:10.1128/jvi.02109-14 · Cited by 12

Activity-based protein profiling: an efficient approach to study serine hydrolases and their inhibitors in mammals and microbes

Chen, B., Ge, S.-S., Zhao, Y., Chen, C., & Yang, S. (2016) · RSC Advances · doi:10.1039/c6ra20006k · Cited by 11

Identification of covalent fragment inhibitors for Plasmodium falciparum UCHL3 with anti-malarial efficacy

Imhoff, R. D., Rosenthal, M. R., Ashraf, K., Bhanot, P., Ng, C. L., & Flaherty, D. P. (2023) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2023.129458 · Cited by 10

p38 mitogen-activated protein kinase inhibits USP22 transcription in HeLa cells

Xiong, J., Gong, Z., Zhou, X., Liu, J., He, J., Wu, P., & Li, W. (2015) · Biomedical Reports · doi:10.3892/br.2015.450 · Cited by 10

Differential expression profiling of genes in a complete hydatidiform mole using cDNA microarray analysis

Kim, S. J., Lee, S. Y., Lee, C. M., Kim, I., An, H. J., Kim, J. Y., Baek, K., Kim, E. J., Kim, J. M., Lee, J. B., et al. (2006) · Gynecologic Oncology · doi:10.1016/j.ygyno.2006.05.015 · Cited by 10

Comparative Proteomic Analysis Implicates COMMD Proteins as Epstein–Barr Virus Targets in the BL41 Burkitt’s Lymphoma Cell Line

Gkiafi, Z., & Panayotou, G. (2011) · Journal of Proteome Research · doi:10.1021/pr100793m · Cited by 10

USP22 transcriptional activity is negatively regulated by the histone deacetylase inhibitor trichostatin A

Xiong, J., Xu, X., Zhou, X., LIU, J., Gong, Z., Wu, P., & Li, W. (2014) · Molecular Medicine Reports · doi:10.3892/mmr.2014.2666 · Cited by 10

Role of ubiquitin-specific peptidase 22 in carcinogenesis of human pharyngeal squamous cell carcinoma

Dou, Y., Lin, J.-P., Shu, H., & Jiang, N. (2014) · Molecular Medicine Reports · doi:10.3892/mmr.2014.2589 · Cited by 10

KSHV Viral Protein Kinase Interacts with USP9X to Modulate the Viral Lifecycle

Chappell, D. L., Sandhu, P., Wong, J. P., Bhatt, A. P., Liu, X., Buhrlage, S. J., Temple, B. R. S., Major, M. B., & Damania, B. (2023) · Journal of Virology · doi:10.1128/jvi.01763-22 · Cited by 8

UCHL1-PKM2 axis dysregulation is associated with promoted proliferation and invasiveness of urothelial bladder cancer cells

Zheng, Y., Shi, D., Chen, L., Yang, Y., & Yao, M. (2023) · Aging · doi:10.18632/aging.205097 · Cited by 8

A pathological missense mutation in the deubiquitinase USP5 leads to insensitivity to pain

Antunes, F. T. T., Gandini, M. A., Garcı́a-Caballero, A., Huang, S., Ali, M. Y., Gambeta, E., Souza, I. A., Harding, E. K., Ferron, L., Stray‐Pedersen, A., et al. (2025) · The Journal of Experimental Medicine · doi:10.1084/jem.20241877 · Cited by 8

Monitoring Target Engagement of Deubiquitylating Enzymes Using Activity Probes: Past, Present, and Future

Harrigan, J. A., & Jacq, X. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3756-1_26 · Cited by 7

Pirarubicin reduces USP22 expression by inhibiting CREB‑1 phosphorylation in HeLa cells

Zhou, X., Gan, L., Liu, J., Xie, X., Wang, T., & Xiong, J. (2019) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2019.7447 · Cited by 7

RUNX1 regulates MCM2/CDC20 to promote COAD progression modified by deubiquitination of USP31

Tian, W., Zhao, J., Zhang, X., Li, P., Li, X., Yuan, H., & Li, S. (2024) · Scientific Reports · doi:10.1038/s41598-024-64726-w · Cited by 6

Dynamics of Ubiquitination in Differentiation and Dedifferentiation of Pancreatic β-cells: Putative Target for Diabetes

Kumar, A., Francis, M., Bhaskar, S., Vishnuvajhala, S., & Prasanna, J. (2022) · Current Protein and Peptide Science · doi:10.2174/1389203723666220422092023 · Cited by 6

Is there an alternative to the proteasome in cytosolic protein degradation?

Antón, L. C., & Villasevil, E. M. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360839 · Cited by 6

Walking the tightrope: UCH-L1 as an mTOR inhibitor and B-cell oncogene

Bedekovics, T., Hussain, S., & Galardy, P. J. (2019) · Oncotarget · doi:10.18632/oncotarget.27154 · Cited by 6

Identification of Interconnected Markers for T-Cell Acute Lymphoblastic Leukemia

Guven‐Maiorov, E., Keskin, Ö., Ng, Ö. H., Özbek, U., & Gürsoy, A. (2013) · BioMed Research International · doi:10.1155/2013/210253 · Cited by 5

RANBP2 and USP9x regulate nuclear import of adenovirus minor coat protein IIIa

Ismail, A. M., Saha, A., Lee, J. S., Painter, D. F., Chen, Y., Singh, G., Condezo, G. N., Chodosh, J., Martín, C. S., & Rajaiya, J. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010588 · Cited by 5

Characterization of the deubiquitination activity and substrate specificity of the chicken ubiquitin-specific protease 1/USP associated factor 1 complex

Zheng, H., Wang, M., Zhao, C., Wu, S., Yu, P., Lü, Y., Wang, T., & Ai, Y. (2017) · PLoS ONE · doi:10.1371/journal.pone.0186535 · Cited by 5

Method for Measuring the Activity of Deubiquitinating Enzymes in Cell Lines and Tissue Samples

Griffin, P. Y., Sexton, A., MacNeill, L., Iizuka, Y., Lee, M. K., & Bazzaro, M. (2015) · Journal of Visualized Experiments · doi:10.3791/52784 · Cited by 5

Targeting the Ubiquitin Proteasome System in Cancer

Kumari, N., Lee, K. K., & Jha, S. (2018) · InTech eBooks · doi:10.5772/intechopen.76705 · Cited by 5

Sample Preparation of Body Fluids for Proteomics Analysis

Govorukhina, N. I., & Bischoff, R. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-432-2_2 · Cited by 4

Activity-Based Imaging and Biochemical Profiling Tools for Analysis of the Cancer Degradome

Dive, V., Paulick, M. G., McIntyre, J. O., Matrisian, L. M., & Bogyo, M. S. (2008) · Springer eBooks · doi:10.1007/978-0-387-69057-5_7 · Cited by 4

Molecular diagnosis of parathyroid carcinoma: a reality in the near future

Falchetti, A., Cavalli, L., Cavalli, T., Giusti, F., Marcucci, G., Marini, F., & Brandi, M. L. (2011) · Expert Opinion on Medical Diagnostics · doi:10.1517/17530059.2012.634796 · Cited by 4

Biotransformation of Chinese Herbs and Their Ingredients

Rongcai, Y., Lei, S., Shikai, Y., Zhao, J., & Zhang, W. (2010) · World Science and Technology · doi:10.1016/s1876-3553(11)60019-7 · Cited by 3

Omics-Level Approaches to Studying Gammaherpesvirus Infection

Hisam, F., Konakalla, A. R., Berisha, E., Castro, M. D. C. C., Mukherjee, S., Wang, C., Sheirbon, B. R., Delgado, T., & Sanchez, E. L. (2026) · Pathogens · doi:10.3390/pathogens15070713 · Cited by 2

Identification and evaluation of UL36 protein from Dermacentor silvarum salivary gland and its interaction with Anaplasma ovis VirB10

Mukhtar, M. U., Iqbal, N., Yang, J., Niu, Q., Zhao, S., Li, Z., Zhao, Y., Rashid, I., Chen, Z., Guan, G., et al. (2020) · Parasites & Vectors · doi:10.1186/s13071-020-3975-9 · Cited by 2

The Deubiquitylase USP5 Knockdown Reduces Semliki Forest Virus Replication in HeLa Cells

Nubgan, A. (2022) · Maǧallaẗ ǧāmiʿaẗ al-Sulṭān Qābūs li-l-ʿulūm/Sultan Qaboos University journal for science · doi:10.53539/squjs.vol26iss2pp76-85 · Cited by 2

Activity Based Profiling of Deubiquitylating Enzymes and Inhibitors in Animal Tissues

McLellan, L., Forder, C., Cranston, A. N., Harrigan, J. A., & Jacq, X. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3756-1_27 · Cited by 2

Chemical Synthesis of Activity-Based Diubiquitin Probes

Li, G., Yuan, L., & Zhuang, Z. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6539-7_16 · Cited by 2

Targeting Proteasomal Degradation of Soluble, Misfolded Proteins

Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801944-3.00003-5 · Cited by 2

Cracking the Ubiquitin Code: the Ubiquitin Toolbox

Mulder, M. P. C., Witting, K. F., & Ovaa, H. (2019) · Caister Academic Press eBooks · doi:10.21775/9781912530120.02 · Cited by 2

Dissecting Intracellular Proteolysis Using Small Molecule Inhibitors and Molecular Probes

Ovaa, H., Overkleeft, H. S., Kessler, B. M., & Ploegh, H. L. (2005) · Wiley eBooks · doi:10.1002/9783527620210.ch3 · Cited by 2

DIG-DUBs: mechanisms and functions of ISG15 deconjugation by human and viral cross-reactive ubiquitin proteases

Bonacci, T., & Emanuele, M. J. (2025) · Biochemical Society Transactions · doi:10.1042/bst20240859 · Cited by 3

Proteome Analysis of the Ubiquitin Pathway

Peng, J. (2008) · Wiley eBooks · doi:10.1002/9780470369630.ch30 · Cited by 1

Ubiquitination and deubiquitination involved in cell cycle progression

van Leuken, R. J. (2008) · Utrecht University Repository (Utrecht University)

Epstein-Barr virus encoded deconjugases and AmotL2 in control of cell topology

Hildebrand, S. (2014) · Figshare

MECHANISTIC STUDY OF USP15-DEPENDENT DEUBIQUITINATION AND CHARACTERIZATION OF NATURAL COMPOUNDS THAT MODULATE THE NRF2-KEAP1 ANTIOXIDANT RESPONSE

Villeneuve, N. (2011) · UA Campus Repository (The University of Arizona)

Inhibition of Deubiquitinase Activity and Ubiquitination of Jak2 Blocks Cytokine Signaling and Induces Tumor Cell Apoptosis

Kapuria, V. (2010) · Digital Commons-TMC (Texas Medical Center)

Chemical and biochemical studies of ubiquitin conjugation machinery

Pandya, R. K. (2010) · DSpace@MIT (Massachusetts Institute of Technology)

Development of Biomolecular Tools for Studying Host-Virus Interactions of the Hepatitis C Virus

Ardekan, N. N. (2015) · uO Research (University of Ottawa) · doi:10.20381/ruor-4753

UCH-L1 in DLBCL: marker or target?

Pagano, J. S., & Shackelford, J. (2016) · Blood · doi:10.1182/blood-2016-01-689984

A Protocol for Protein Profiling Using Chemoselective Cleavable Linker Probes in Semi-permeabilized Cells

Claessen, J. H. L., & Witte, M. D. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6439-0_13

Novel activity-based probes for functional analysis of deubiquitinating enzymes

Iphöfer, A. (2012) · Digitale Bibliothek Braunschweig (Verbundzentrale Göttingen (VZG)) · doi:10.24355/dbbs.084-201205021132-0

Dissecting Intracellular Proteolysis Using Small Molecule Inhibitors and Molecular Probes

Ovaa, H., Overkleeft, H. S., Kessler, B. M., & Ploegh, H. L. (2007) · Wiley eBooks · doi:10.1002/9783527619320.ch3a

Montelukast Performs Synergistic Effect with Carfilzomib in Multiple Myeloma by Inhibiting the Deubiquitinase UCHL1

Wang, Y., Wei, W., Peng, R., Chen, H., Zhou, N., Wu, L., Shi, H., Chen, X., Wang, D., Wei, J., et al. (2022) · Austin Journal of Cancer and Clinical Research · doi:10.26420/austinjcancerclinres.2022.1101

Data from Bortezomib (Velcade) Induces p27Kip1 Expression through S-Phase Kinase Protein 2 Degradation in Colorectal Cancer

Shahab Uddin, M. S., Ahmed, M., Bavi, P. P., El-Sayed, R., Al-Sanea, N. A., Abduljabbar, A. S., Ashari, L. H. S., Alhomoud, S. J., Al‐Dayel, F., Hussain, A. R., et al. (2023) · doi:10.1158/0008-5472.c.6497727

Data from Bortezomib (Velcade) Induces p27Kip1 Expression through S-Phase Kinase Protein 2 Degradation in Colorectal Cancer

Shahab Uddin, M. S., Ahmed, M., Bavi, P. P., El-Sayed, R., Al-Sanea, N. A., Abduljabbar, A. S., Ashari, L. H. S., Alhomoud, S. J., Al‐Dayel, F., Hussain, A. R., et al. (2023) · doi:10.1158/0008-5472.c.6497727.v1

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Bornkamm, G. W., Kelly, G. L., & Ross, A. M. (2025) · Current topics in microbiology and immunology · doi:10.1007/82_2025_301 · Cited by 2

BindingDB Entry 50018466: Recent advances in the development of ubiquitin-specific-processing protease 7 (USP7) inhibitors.

BindingDB (2024) · UC San Diego · doi:10.7270/q2bv7mvn

BindingDB Entry 50020291: Identification of covalent fragment inhibitors for Plasmodium falciparum UCHL3 with anti-malarial efficacy.

BindingDB (2024) · UC San Diego · doi:10.7270/q2xw4q79

BindingDB Entry 50007936: Advances in Discovering Deubiquitinating Enzyme (DUB) Inhibitors.

BindingDB (2021) · UC San Diego · doi:10.7270/q2gf0xtc

BindingDB Entry 50032222: Mechanisms, biology and inhibitors of deubiquitinating enzymes.

BindingDB (2011) · UC San Diego · doi:10.7270/q2kw5g7p

BindingDB Entry 50009668: Discovery of Small Molecule Antagonists of the USP5 Zinc Finger Ubiquitin-Binding Domain.

BindingDB (2021) · UC San Diego · doi:10.7270/q23r0xbs

Proteinase Optical Imaging Tools for Cancer Detection and Response to Therapy

McIntyre, J. O., & Matrisian, L. M. (2009) · Springer eBooks · doi:10.1007/978-0-387-93874-5_7

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Rolén, U. (2005) · Figshare

Activity profiling of deubiquitinating enzymes in cervical carcinoma biopsies and cell lines

Rolén, U., Kobzeva, V., Gasparjan, N., Ovaa, H., Winberg, G., Kisseljov, F. L., & Masucci, M. G. (2006) · Molecular Carcinogenesis · doi:10.1002/mc.20177 · Cited by 112

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Rolén, U. (2007) · Figshare

The role of ubiquitination during B cell proliferation induced by the Epstein-Barr virus

Großkopf, H. (2018) · Digitale Bibliothek Braunschweig (Verbundzentrale Göttingen (VZG)) · doi:10.24355/dbbs.084-201802140950

Molecular regulation by ubiquitin-specific proteases (USPs) in HCC: cell cycle, oncogenic signaling, and beyond

Al-Khateeb, F. N., YOUSIF, A. Y., Al‐Shawi, S. G., Alkhathami, A. G., Roopashree, R., Kashyap, A., Nathiya, D., Ray, S., Alnajar, M. J., & Kareem, M. (2025) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-025-04395-2 · Cited by 4