A BRISC-SHMT Complex Deubiquitinates IFNAR1 and Regulates Interferon Responses

The Inflammasomes

Schroder, K., & Tschopp, J. (2010) · Cell · doi:10.1016/j.cell.2010.01.040 · Cited by 5,475 · 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

Role of Rpn11 Metalloprotease in Deubiquitination and Degradation by the 26 S Proteasome

Verma, R., Aravind, L., Oania, R. S., McDonald, W. H., Yates, J. R., Koonin, E. V., & Deshaies, R. J. (2002) · Science · doi:10.1126/science.1075898 · Cited by 994 · see citing works

Mechanism and function of deubiquitinating enzymes

Amerik, A. Y., & Hochstrasser, M. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.10.003 · Cited by 978 · see citing works

IL-1 pathways in inflammation and human diseases

Gabay, C., Lamacchia, C., & Palmer, G. (2010) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2010.4 · Cited by 897 · see citing works

Type I interferon: friend or foe?

Trinchieri, G. (2010) · The Journal of Experimental Medicine · doi:10.1084/jem.20101664 · Cited by 838 · see citing works

A cryptic protease couples deubiquitination and degradation by the proteasome

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

Deubiquitination of NLRP3 by BRCC3 Critically Regulates Inflammasome Activity

Py, B. F., Kim, M.-S., Vakifahmetoglu-Norberg, H., & Yuan, J. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.11.009 · Cited by 718 · see citing works

RAP80 Targets BRCA1 to Specific Ubiquitin Structures at DNA Damage Sites

Sobhian, B., Shao, G., Lilli, D. R., Culhane, A. C., Moreau, L. A., Xia, B., Livingston, D. M., & Greenberg, R. A. (2007) · Science · doi:10.1126/science.1139516 · Cited by 672 · 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

Regulation of monoubiquitinated PCNA by DUB autocleavage

Huang, T. T., Nijman, S. M. B., Mirchandani, K. D., Galardy, P. J., Cohn, M. A., Haas, W., Gygi, S. P., Ploegh, H. L., Bernards, R., & D’Andrea, A. D. (2006) · Nature Cell Biology · doi:10.1038/ncb1378 · Cited by 585 · see citing works

A weak signal for strong responses: interferon-alpha/beta revisited

Taniguchi, T., & Takaoka, A. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35073080 · Cited by 483 · see citing works

The Secretory Route of the Leaderless Protein Interleukin 1β Involves Exocytosis of Endolysosome-related Vesicles

Andrei, C., Dazzi, C., Lotti, L. V., Torrisi, M. R., Chimini, G., & Rubartelli, A. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.5.1463 · Cited by 475 · see citing works

Constitutive Type I Interferon Modulates Homeostatic Balance through Tonic Signaling

Gough, D. J., Messina, N. L., Clarke, C. J. P., Johnstone, R. W., & Levy, D. E. (2012) · Immunity · doi:10.1016/j.immuni.2012.01.011 · Cited by 472 · see citing works

Central role for type I interferons and Tyk2 in lipopolysaccharide-induced endotoxin shock

Karaghiosoff, M., Steinborn, R., Kovarik, P., Kriegshäuser, G., Baccarini, M., Donabauer, B., Reichart, U., Kolbe, T., Bogdan, C., Leanderson, T., et al. (2003) · Nature Immunology · doi:10.1038/ni910 · Cited by 363 · see citing works

A UAF1-Containing Multisubunit Protein Complex Regulates the Fanconi Anemia Pathway

Cohn, M. A., Kowal, P., Yang, K., Haas, W., Huang, T. T., Gygi, S. P., & D’Andrea, A. D. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.09.031 · Cited by 355 · see citing works

The role of ubiquitylation in receptor endocytosis and endosomal sorting

Haglund, K., & Đikić, I. (2012) · Journal of Cell Science · doi:10.1242/jcs.091280 · Cited by 310 · see citing works

Endocytosis: the DUB version

Clague, M. J., & Urbé, S. (2006) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.09.002 · Cited by 258 · see citing works

Structural and dynamic determinants of type <scp>I</scp> interferon receptor assembly and their functional interpretation

Piehler, J., Thomas, C., Garcia, K. C., & Schreiber, G. (2012) · Immunological Reviews · doi:10.1111/imr.12001 · Cited by 230 · see citing works

K63‐specific deubiquitination by two JAMM/MPN+ complexes: BRISC‐associated Brcc36 and proteasomal Poh1

Cooper, E. M., Cutcliffe, C., Kristiansen, T. Z., Pandey, A., Pickart, C. M., & Cohen, R. E. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.27 · Cited by 223 · see citing works

The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks

Shao, G., Lilli, D. R., Patterson-Fortin, J., Coleman, K. A., Morrissey, D. E., & Greenberg, R. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807485106 · Cited by 218 · see citing works

Regulatory mechanisms involved in the control of ubiquitin homeostasis

Kimura, Y., & Tanaka, K. (2010) · The Journal of Biochemistry · doi:10.1093/jb/mvq044 · Cited by 216 · see citing works

Deficiency of the type I interferon receptor protects mice from experimental lupus

Nacionales, D. C., Kelly‐Scumpia, K. M., Lee, P. Y., Weinstein, J. S., Lyons, R., Sobel, E. S., Satoh, M., & Reeves, W. H. (2007) · Arthritis & Rheumatism · doi:10.1002/art.23023 · Cited by 193 · see citing works

SCFHOS ubiquitin ligase mediates the ligand‐induced down‐regulation of the interferon‐α receptor

Kumar, S., Tang, W., Ravindranath, A. K., Clark, W. A., Croze, E., & Fuchs, S. Y. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg524 · Cited by 187 · see citing works

Safety and pharmacodynamics of rontalizumab in patients with systemic lupus erythematosus: Results of a phase I, placebo‐controlled, double‐blind, dose‐escalation study

McBride, J., Jiang, J. Z., Abbas, A. R., Morimoto, A. M., Li, J., Maciuca, R. D., Townsend, M. J., Wallace, D. J., Kennedy, W. P., & Drappa, J. (2012) · Arthritis & Rheumatism · doi:10.1002/art.34632 · Cited by 186 · see citing works

Protein partners of deubiquitinating enzymes

Ventii, K., & Wilkinson, K. D. (2008) · Biochemical Journal · doi:10.1042/bj20080798 · Cited by 185 · see citing works

The ubiquitin system: pathogenesis of human diseases and drug targeting

Ciechanover, A. J., & Schwartz, A. L. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.09.018 · Cited by 169 · see citing works

MERIT40 controls BRCA1–Rap80 complex integrity and recruitment to DNA double-strand breaksPreprint

Shao, G., Patterson-Fortin, J., Messick, T. E., Feng, D., Shanbhag, N. M., Wang, Y., & Greenberg, R. A. (2009) · Genes & Development · doi:10.1101/gad.1739609 · Cited by 154 · see citing works

Polyubiquitin Binding and Disassembly By Deubiquitinating Enzymes

Reyes‐Turcu, F. E., & Wilkinson, K. D. (2009) · Chemical Reviews · doi:10.1021/cr800470j · Cited by 148 · see citing works

Phosphorylation and Specific Ubiquitin Acceptor Sites Are Required for Ubiquitination and Degradation of the IFNAR1 Subunit of Type I Interferon Receptor

Kumar, S., Krolewski, J. J., & Fuchs, S. Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407082200 · Cited by 142 · see citing works

Virus-Induced Unfolded Protein Response Attenuates Antiviral Defenses via Phosphorylation-Dependent Degradation of the Type I Interferon Receptor

Liu, J., HuangFu, W., Kumar, K. G., Qian, J., Casey, J. P., Hamanaka, R. B., Grigoriadou, C., Aldabe, R., Diehl, J. A., & Fuchs, S. Y. (2009) · Cell Host & Microbe · doi:10.1016/j.chom.2008.11.008 · Cited by 135 · see citing works

Site-specific ubiquitination exposes a linear motif to promote interferon-α receptor endocytosis

Kumar, S., Barrière, H., Carbone, C. J., Liu, J., Swaminathan, G., Xu, P., Li, Y., Baker, D. P., Peng, J., Lukács, G. L., et al. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200706034 · Cited by 135 · see citing works

Deficiency of Type I IFN Receptor in Lupus-Prone New Zealand Mixed 2328 Mice Decreases Dendritic Cell Numbers and Activation and Protects from Disease

Agrawal, H., Jacob, N., Carreras, E., Bajaña, S., Putterman, C., Turner, S., Neas, B. R., Mathian, A., Koss, M. N., Stohl, W., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803872 · Cited by 130 · see citing works

The Lys63-specific Deubiquitinating Enzyme BRCC36 Is Regulated by Two Scaffold Proteins Localizing in Different Subcellular Compartments

Feng, L., Wang, J., & Chen, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.135392 · Cited by 122 · see citing works

Dynamic regulation of the proinflammatory cytokine, interleukin-1β: Molecular biology for non-molecular biologists

Watkins, L. R., Hansen, M. K., Nguyen, K. T., Lee, J. E., & Maier, S. F. (1999) · Life Sciences · doi:10.1016/s0024-3205(99)00095-8 · Cited by 114 · see citing works

Differential regulation of JAMM domain deubiquitinating enzyme activity within the RAP80 complex

Patterson-Fortin, J., Shao, G., Bretscher, H., Messick, T. E., & Greenberg, R. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.135319 · Cited by 85 · see citing works

Neutralizing interferon alpha as a therapeutic approach to autoimmune diseases

Stewart, T. A. (2003) · Cytokine & Growth Factor Reviews · doi:10.1016/s1359-6101(02)00088-6 · Cited by 85 · see citing works

Hope and Fear for Interferon: The Receptor-Centric Outlook on the Future of Interferon Therapy

Fuchs, S. Y. (2013) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2012.0117 · Cited by 80 · see citing works

Ligand-Stimulated Downregulation of the Alpha Interferon Receptor: Role of Protein Kinase D2

Zheng, H., Qian, J., Varghese, B., Baker, D. P., & Fuchs, S. Y. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01154-10 · Cited by 75 · see citing works

Specificity of the BRISC Deubiquitinating Enzyme Is Not Due to Selective Binding to Lys63-linked Polyubiquitin

Cooper, E. M., Boeke, J. D., & Cohen, R. E. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.059667 · Cited by 65 · see citing works

Basal Ubiquitin-independent Internalization of Interferon α Receptor Is Prevented by Tyk2-mediated Masking of a Linear Endocytic Motif

Kumar, K. G., Varghese, B., Banerjee, A., Baker, D. P., Constantinescu, S. N., Pellegrini, S., & Fuchs, S. Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800991200 · Cited by 50 · see citing works

Activities of Hepatic Cytosolic and Mitochondrial Forms of Serine Hydroxymethyltransferase and Hepatic Glycine Concentration Are Affected by Vitamin B-6 Intake in Rats

Scheer, J. B., Mackey, A. D., & Gregory, J. F. (2005) · Journal of Nutrition · doi:10.1093/jn/135.2.233 · Cited by 48 · see citing works

Ligand-independent pathway that controls stability of interferon alpha receptor

Liu, J., Plotnikov, A., Banerjee, A., Kumar, K. G., Ragimbeau, J., Marijanovic, Z., Baker, D. P., Pellegrini, S., & Fuchs, S. Y. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.12.137 · Cited by 47 · see citing works

Characterization of Antihuman IFNAR-1 Monoclonal Antibodies: Epitope Localization and Functional Analysis

Goldman, L. A., Zafari, M. R., Cutrone, E. C., Dang, A. M., Brickelmeier, M., Runkel, L., Benjamin, C. D., Ling, L. E., & Langer, J. A. (1999) · Journal of Interferon & Cytokine Research · doi:10.1089/107999099314379 · Cited by 44 · see citing works

Pathogen Recognition Receptor Signaling Accelerates Phosphorylation-Dependent Degradation of IFNAR1

Qian, J., Zheng, H., HuangFu, W., Liu, J., Carbone, C. J., Leu, N. A., Baker, D. P., & Fuchs, S. Y. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002065 · Cited by 44 · see citing works

Ubiquitination-Dependent Regulation of Signaling Receptors in Cancer

HuangFu, W., & Fuchs, S. Y. (2010) · Genes & Cancer · doi:10.1177/1947601910382901 · Cited by 42 · see citing works

Ubiquitination-mediated regulation of interferon responses

Fuchs, S. Y. (2012) · Growth Factors · doi:10.3109/08977194.2012.669382 · Cited by 38 · see citing works

Serine and glycine metabolism in cancer

Amelio, I., Cutruzzolà, F., Antonov, A., Agostini, M., & Melino, G. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.02.004 · Cited by 1,056 · see citing works

Breaking the chains: deubiquitylating enzyme specificity begets function

Clague, M. J., Urbé, S., & Komander, D. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0099-1 · Cited by 839 · see citing works

The role of mitochondria in NLRP3 inflammasome activation

Liu, Q., Zhang, D., Hu, D., Zhou, X., & Zhou, Y. (2018) · Molecular Immunology · doi:10.1016/j.molimm.2018.09.010 · Cited by 475 · see citing works

Deubiquitinases: From mechanisms to their inhibition by small molecules

Lange, S. M., Armstrong, L. A., & Kulathu, Y. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.10.027 · Cited by 344 · see citing works

The ins and outs of serine and glycine metabolism in cancer

Geeraerts, S. L., Heylen, E., Keersmaecker, K. D., & Kampen, K. R. (2021) · Nature Metabolism · doi:10.1038/s42255-020-00329-9 · Cited by 250 · see citing works

Versatile Roles of K63-Linked Ubiquitin Chains in Trafficking

Erpapazoglou, Z., Walker, O., & Haguenauer‐Tsapis, R. (2014) · Cells · doi:10.3390/cells3041027 · Cited by 203 · see citing works

Targeted inhibition of the COP9 signalosome for treatment of cancer

Schlierf, A., Altmann, E., Quancard, J., Jefferson, A. B., Assenberg, R., Renatus, M., Jones, M. D., Hassiepen, U., Schaefer, M., Kiffe, M., et al. (2016) · Nature Communications · doi:10.1038/ncomms13166 · Cited by 192 · see citing works

Deacetylation of serine hydroxymethyl-transferase 2 by SIRT3 promotes colorectal carcinogenesis

Wei, Z., Song, J., Wang, G., Cui, X., Zheng, J., Tang, Y., Chen, X., Li, J., Cui, L., Liu, C., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06812-y · Cited by 188 · see citing works

HDAC11 regulates type I interferon signaling through defatty-acylation of SHMT2

Cao, J., Sun, L., Aramsangtienchai, P., Spiegelman, N. A., Zhang, X., Huang, W., Seto, E., & Lin, H. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1815365116 · Cited by 189 · see citing works

ABRO1 promotes NLRP3 inflammasome activation through regulation of NLRP3 deubiquitination

Ren, G., Zhang, X., Xiao, Y., Zhang, W., Wang, Y., Ma, W., Wang, X., Song, P., Lai, L., Chen, H., et al. (2019) · The EMBO Journal · doi:10.15252/embj.2018100376 · Cited by 154 · see citing works

Integrated Omic analysis of lung cancer reveals metabolism proteome signatures with prognostic impact

Li, L., Wei, Y., To, C., Zhu, C., Tong, J., Pham, N., Taylor, P. P., Ignatchenko, V., Ignatchenko, A., Zhang, W., et al. (2014) · Nature Communications · doi:10.1038/ncomms6469 · Cited by 115 · see citing works

How pyridoxal 5′‐phosphate differentially regulates human cytosolic and mitochondrial serine hydroxymethyltransferase oligomeric state

Giardina, G., Brunotti, P., Fiascarelli, A., Cicalini, A., Costa, M. G. S., Buckle, A. M., di Salvo, M. L., Giorgi, A., Marani, M., Paone, A., et al. (2015) · FEBS Journal · doi:10.1111/febs.13211 · Cited by 104 · see citing works

Metabolic Regulation of Cell Fate and Function

Ghosh-Choudhary, S. K., Liu, J., & Finkel, T. (2020) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.12.005 · Cited by 106 · see citing works

Regulatory mechanisms of one-carbon metabolism enzymes

Petrova, B., Maynard, A. G., Wang, P., & Kanarek, N. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105457 · Cited by 103 · see citing works

Mechanisms of regulation and diversification of deubiquitylating enzyme function

Leźnicki, P., & Kulathu, Y. (2017) · Journal of Cell Science · doi:10.1242/jcs.201855 · Cited by 97 · see citing works

ADP-ribosyltransferase PARP11 modulates the interferon antiviral response by mono-ADP-ribosylating the ubiquitin E3 ligase β-TrCP

Guo, T., Zuo, Y., Qian, L., Liu, J., Yuan, Y., Xu, K., Miao, Y., Feng, Q., Chen, X., Jin, L., et al. (2019) · Nature Microbiology · doi:10.1038/s41564-019-0428-3 · Cited by 97 · see citing works

Metabolic control of BRISC-SHMT2 assembly regulates immune signalling

Walden, M., Tian, L., Ross, R. L., Sykora, U. M., Byrne, D. P., Hesketh, E. L., Masandi, S. K., Cassel, J., George, R., Ault, J. R., et al. (2019) · Nature · doi:10.1038/s41586-019-1232-1 · Cited by 85 · see citing works

Pharmacological targeting of NLRP3 deubiquitination for treatment of NLRP3-associated inflammatory diseases

Ren, G., Li, J., Zhang, X., Wang, Y., Xiao, Y., Zhang, X., Liu, X., Zhang, W., Ma, W., Zhang, J., et al. (2021) · Science Immunology · doi:10.1126/sciimmunol.abe2933 · Cited by 87 · see citing works

Structural basis of BRCC36 function in DNA repair and immune regulation

Rabl, J., Bunker, R. D., Schenk, A. D., Cavadini, S., Gill, M. E., Abdulrahman, W., Andrés-Pons, A., Luijsterburg, M. S., Ibrahim, A. F. M., Branigan, E., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.06.002 · Cited by 84 · see citing works

HDAC11: a multifaceted histone deacetylase with proficient fatty deacylase activity and its roles in physiological processes

Núñez‐Álvarez, Y., & Suelves, M. (2021) · FEBS Journal · doi:10.1111/febs.15895 · Cited by 82 · see citing works

Role of Deubiquitinating Enzymes in DNA Repair

Kee, Y., & Huang, T. T. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00847-15 · Cited by 80 · see citing works

Cytoplasmic SHMT2 drives the progression and metastasis of colorectal cancer by inhibiting β-catenin degradation

Liu, C., Wang, L., Liu, X., Tan, Y., Tao, L., Xiao, Y., Deng, P., Wang, H., Deng, Q., Lin, Y., et al. (2021) · Theranostics · doi:10.7150/thno.48699 · Cited by 76 · see citing works

Type I Interferon Controls Propagation of Long Interspersed Element-1

Yu, Q., Carbone, C. J., Katlinskaya, Y. V., Zheng, H., Zheng, K., Luo, M., Wang, P. J., Greenberg, R. A., & Fuchs, S. Y. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.612374 · Cited by 76 · see citing works

Higher-Order Assembly of BRCC36–KIAA0157 Is Required for DUB Activity and Biological Function

Zeqiraj, E., Tian, L., Piggott, C. A., Pillon, M. C., Duffy, N. M., Ceccarelli, D. F. J., Keszei, A. F. A., Lorenzen, K., Kurinov, I. V., Orlicky, S. M., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.028 · Cited by 66 · see citing works

Abro1 maintains genome stability and limits replication stress by protecting replication fork stabilityPreprint

Xu, S., Wu, X. Y., Wu, L., Castillo, A., Liu, J., Atkinson, E., Paul, A., Su, D., Schlacher, K., Komatsu, Y., et al. (2017) · Genes & Development · doi:10.1101/gad.299172.117 · Cited by 65 · see citing works

Roles of Mitochondrial Serine Hydroxymethyltransferase 2 (SHMT2) in Human Carcinogenesis

Zeng, Y., Zhang, J., Xu, M., Chen, F., Zi, R., Yue, J., Zhang, Y., Chen, N., & Chin, Y. E. (2021) · Journal of Cancer · doi:10.7150/jca.60170 · Cited by 62 · see citing works

The loss of SHMT2 mediates 5-fluorouracil chemoresistance in colorectal cancer by upregulating autophagy

Chen, J., Na, R., Xiao, C. W., Wang, X., Wang, Y., Yan, D., Song, G., Liu, X., Chen, J., Lu, H., et al. (2021) · Oncogene · doi:10.1038/s41388-021-01815-4 · Cited by 61 · see citing works

Hidden features: exploring the non-canonical functions of metabolic enzymes

Huangyang, P., & Simon, M. C. (2018) · Disease Models & Mechanisms · doi:10.1242/dmm.033365 · Cited by 59 · see citing works

ABRO1 suppresses tumourigenesis and regulates the DNA damage response by stabilizing p53

Zhang, J., Cao, M., Dong, J., Li, C., Xu, W., Zhan, Y., Wang, X., Yu, M., Ge, C., Ge, Z., et al. (2014) · Nature Communications · doi:10.1038/ncomms6059 · Cited by 58 · see citing works

A review of small-molecule inhibitors of one-carbon enzymes: SHMT2 and MTHFD2 in the spotlight

Cuthbertson, C. R., Arabzada, Z., Bankhead, A., Kyani, A., & Neamati, N. (2021) · ACS Pharmacology &amp; Translational Science · doi:10.1021/acsptsci.0c00223 · Cited by 57 · see citing works

The deubiquitinating enzyme complex BRISC is required for proper mitotic spindle assembly in mammalian cells

Yan, K., Li, L., Wang, X., Hong, R.-S., Zhang, Y., Yang, H., Lin, M. T., Zhang, S., He, Q., Zheng, D., et al. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201503039 · Cited by 53 · see citing works

SHMT2 and the BRCC36/BRISC deubiquitinase regulate HIV-1 Tat K63-ubiquitylation and destruction by autophagy

Xu, M., Moresco, J. J., Chang, M. W., Mukim, A., Smith, D. M., Diedrich, J. K., Yates, J. R., & Jones, K. A. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007071 · Cited by 49 · see citing works

H2A-DUBbing the mammalian epigenome: Expanding frontiers for histone H2A deubiquitinating enzymes in cell biology and physiology

Belle, J. I., & Nijnik, A. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.03.004 · Cited by 44 · see citing works

Overexpression of SHMT2 predicts a poor prognosis and promotes tumor cell growth in bladder cancer

Zhang, P., & Yang, Q. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.682856 · Cited by 41 · see citing works

BRISC is required for optimal activation of NF-κB in Kupffer cells induced by LPS and contributes to acute liver injury

Zhang, W., Liu, K., Ren, G., Wang, Y., Wang, T., Liu, X., Li, D., Xiao, Y., Chen, X., Li, Y., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06268-z · Cited by 40 · see citing works

Pseudo-DUBs as allosteric activators and molecular scaffolds of protein complexes

Walden, M., Masandi, S. K., Pawłowski, K., & Zeqiraj, E. (2018) · Biochemical Society Transactions · doi:10.1042/bst20160268 · Cited by 39 · see citing works

Structural and Functional Basis of JAMM Deubiquitinating Enzymes in Disease

Pan, X., Wu, S., Wei, W., Chen, Z.-X., Wu, Y., & Gong, K.-Z. (2022) · Biomolecules · doi:10.3390/biom12070910 · Cited by 35 · see citing works

Mechanisms orchestrating the enzymatic activity and cellular functions of deubiquitinases

Estavoyer, B., Messmer, C., Echbicheb, M., Rudd, C. E., Milot, É., & Affar, E. B. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102198 · Cited by 37 · see citing works

Lysine Fatty Acylation: Regulatory Enzymes, Research Tools, and Biological Function

Komaniecki, G., & Lin, H. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.717503 · Cited by 37 · see citing works

Deubiquitinases and cancer: A snapshot

Singh, N., & Singh, A. B. (2016) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2016.04.018 · Cited by 36 · see citing works

Haploinsufficiency of A20 impairs protein–protein interactome and leads into caspase-8-dependent enhancement of NLRP3 inflammasome activation

Rajamäki, K., Keskitalo, S., Seppänen, M. R. J., Kuismin, O., Vähäsalo, P., Trotta, L., Väänänen, A., Glumoff, V., Keskitalo, P. L., Kaarteenaho, R. L., et al. (2018) · RMD Open · doi:10.1136/rmdopen-2018-000740 · Cited by 34 · see citing works

The BRISC deubiquitinating enzyme complex limits hematopoietic stem cell expansion by regulating JAK2 K63-ubiquitination

Donaghy, R., Han, X., Rozenova, K., Lv, K., Jiang, Q., Doepner, M., Greenberg, R. A., & Tong, W. (2019) · Blood · doi:10.1182/blood-2018-10-877563 · Cited by 33 · see citing works

Metformin Is a Pyridoxal-5′-phosphate (PLP)-Competitive Inhibitor of SHMT2

Tramonti, A., Cuyàs, E., Encinar, J. A., Pietzke, M., Paone, A., Verdura, S., Arbusà, A., Martı́n-Castillo, B., Giardina, G., Joven, J., et al. (2021) · Cancers · doi:10.3390/cancers13164009 · Cited by 31 · see citing works

Deubiquitination complex platform: A plausible mechanism for regulating the substrate specificity of deubiquitinating enzymes

Fang, Y.-Z., Li, J., He, Q., Cao, J., & Yang, B. (2023) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2023.02.019 · Cited by 32 · see citing works

BRCA1-A and BRISC: multifunctional molecular machines for ubiquitin signaling

Rabl, J. (2020) · Biomolecules · doi:10.3390/biom10111503 · Cited by 31 · see citing works

Fine-tuning the ubiquitin code at DNA double-strand breaks: deubiquitinating enzymes at work

Citterio, E. (2015) · Frontiers in Genetics · doi:10.3389/fgene.2015.00282 · Cited by 29 · see citing works

Serine hydroxymethyltransferase 2: a novel target for human cancer therapy

Xie, M., & Pei, D. (2021) · Investigational New Drugs · doi:10.1007/s10637-021-01144-z · Cited by 30 · see citing works

Functional characterization of BRCC3 mutations in acute myeloid leukemia with t(8;21)(q22;q22.1)

Meyer, T., Jahn, N., Lindner, S., Röhner, L., Dolnik, A., Weber, D., Scheffold, A., Köpff, S., Paschka, P., Gaidzik, V. I., et al. (2019) · Leukemia · doi:10.1038/s41375-019-0578-6 · Cited by 27 · see citing works

Ubiquitination network in the type I IFN‐induced antiviral signaling pathway

Zhao, Q., Zhang, R., Qiao, C., Miao, Y., Yuan, Y., & Zheng, H. (2023) · European Journal of Immunology · doi:10.1002/eji.202350384 · Cited by 27 · see citing works

MERIT40 cooperates with BRCA2 to resolve DNA interstrand cross-linksPreprint

Jiang, Q., Paramasivam, M., Aressy, B., Wu, J., Bellani, M. A., Tong, W., Seidman, M. M., & Greenberg, R. A. (2015) · Genes & Development · doi:10.1101/gad.264192.115 · Cited by 26 · see citing works

Three-Dimensional Architecture of the Human BRCA1-A Histone Deubiquitinase Core Complex

Kyrieleis, O. J. P., McIntosh, P. B., Webb, S. R., Calder, L. J., Lloyd, J., Patel, N. A., Martin, S. R., Robinson, C. V., Rosenthal, P. B., & Smerdon, S. J. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.11.063 · Cited by 25 · see citing works

Cancer proteome and metabolite changes linked to SHMT2

Tong, J., Krieger, J. R., Taylor, P., Bagshaw, R., Kang, J., Jeedigunta, S., Wybenga-Groot, L. E., Zhang, W., Badr, H., Mirhadi, S., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0237981 · Cited by 24 · see citing works

Global functional profiling of human ubiquitome identifies E3 ubiquitin ligase DCST1 as a novel negative regulator of Type-I interferon signaling

Nair, S., Bist, P., Dikshit, N., & Krishnan, M. N. (2016) · Scientific Reports · doi:10.1038/srep36179 · Cited by 24 · see citing works

Deubiquitinases in cell death and inflammation

Newton, K., & Gitlin, A. D. (2022) · Biochemical Journal · doi:10.1042/bcj20210735 · Cited by 25 · see citing works

ABRO1 stabilizes the deubiquitinase BRCC3 through inhibiting its degradation mediated by the E3 ubiquitin ligase WWP2

Zhang, W., Tao, S., Wang, T., Zhang, J., Liu, X., Li, Y., Chen, H., Zhan, Y., Yu, M., Ge, C., et al. (2020) · FEBS Letters · doi:10.1002/1873-3468.13970 · Cited by 22 · see citing works

TRIM10 binds to IFN‐α/β receptor 1 to negatively regulate type I IFN signal transduction

Guo, M., Cao, W., Chen, S., Tian, R., Wang, L., Liu, Q., Zhang, L., Wang, Z., Zhao, M., Lu, Q., et al. (2021) · European Journal of Immunology · doi:10.1002/eji.202049073 · Cited by 18 · see citing works

HSV-1-encoded ICP0 degrades the host deubiquitinase BRCC36 to antagonize interferon antiviral response

Zhang, L., Huang, F., Liu, J., Xu, Y., Miao, Y., Yuan, Y., Chen, X., Zhang, H.-G., Wang, J., Zheng, H., et al. (2021) · Molecular Immunology · doi:10.1016/j.molimm.2021.03.027 · Cited by 17 · see citing works

Molecular Pathogenic Mechanisms of Hypomyelinating Leukodystrophies (HLDs)

Torii, T., & Yamauchi, J. (2023) · Neurology International · doi:10.3390/neurolint15030072 · Cited by 16 · see citing works

One-carbon metabolism in cancer: moonlighting functions of metabolic enzymes and anti-tumor therapy

Cao, X., Guo, Y., Guo, Z., Liu, Y., Dou, Y., & Xue, L. (2025) · Cancer and Metastasis Reviews · doi:10.1007/s10555-025-10308-9 · Cited by 16 · see citing works

Phosphorylated SHMT2 Regulates Oncogenesis Through m6A Modification in Lung Adenocarcinoma

Han, T., Wang, Y., Cheng, M., Hu, Q., Wan, X., Huang, M.-L., Liu, Y., Xun, W., Xu, J., Wang, L., et al. (2024) · Advanced Science · doi:10.1002/advs.202307834 · Cited by 14 · see citing works

Regulatory interplay between deubiquitinating enzymes and cytokines

Woo, B., & Baek, K. (2019) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2019.06.001 · Cited by 15 · see citing works

Maternal malnutrition and anaemia in India: dysregulations leading to the ‘thin-fat’ phenotype in newborns

Pandit, P., Galande, S., & Iris, F. (2021) · Journal of Nutritional Science · doi:10.1017/jns.2021.83 · Cited by 14 · see citing works

An Integrated View of Deubiquitinating Enzymes Involved in Type I Interferon Signaling, Host Defense and Antiviral Activities

Qian, G., Zhu, L., Li, G. L., Liu, Y., Zhang, Z., Pan, J., & Lv, H. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.742542 · Cited by 13 · see citing works

Estrogen-responsive genes for environmental studies

Kiyama, R., Zhu, Y., Kawaguchi, K., Iitake, N., Wada‐Kiyama, Y., & Dong, S. (2014) · Environmental Technology & Innovation · doi:10.1016/j.eti.2014.09.001 · Cited by 13 · see citing works

Spike S1 domain interactome in non-pulmonary systems: A role beyond the receptor recognition

Iacobucci, I., Monaco, V., Canè, L., Bibbò, F., Cioffi, V., Cozzolino, F., Guarino, A., Zollo, M., & Monti, M. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.975570 · Cited by 12 · see citing works

Molecular glues that inhibit deubiquitylase activity and inflammatory signaling

Chandler, F., Reddy, P. A. N., Bhutda, S., Ross, R. L., Datta, A., Walden, M., Walker, K., Donato, S. D., Cassel, J. A., Prakesch, M. A., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01517-5 · Cited by 10 · see citing works

Inactivity of YGL082W in vitro due to impairment of conformational change in the catalytic center loop

Lu, L., Guo, Y., Wang, T., Liang, L., Zhao, S., Wang, F., & Liu, L. (2019) · Science China Chemistry · doi:10.1007/s11426-019-9623-0 · Cited by 10 · see citing works

MERIT40 deficiency expands hematopoietic stem cell pools by regulating thrombopoietin receptor signaling

Rozenova, K., Jiang, J., Donaghy, R., Aressy, B., Greenberg, R. A., & Tong, W. (2015) · Blood · doi:10.1182/blood-2014-07-588145 · Cited by 9 · see citing works

Protein Post‐Translational Modification‐Mediated Control of Type I Interferon Cascade Signaling

Chen, X., Cheng, Q., Gong, F., & Zheng, H. (2025) · Medicine Bulletin · doi:10.1002/mdb2.70000 · Cited by 9 · see citing works

BRCA1-A and LIG4 complexes mediate ecDNA biogenesis and cancer drug resistance

Chung, O. W., Yao, S., Wang, L., Yang, F., Schier, L., Aldana, M., Cerda-Smith, C. G., Hutchinson, H. M., Wood, K. C., Su, W., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2530443123 · Cited by 9 · see citing works

Lys-63-specific deubiquitinase BRCC36 enhances the sensitivity of multiple myeloma cells to lenalidomide by inhibiting lysosomal degradation of cereblon

Wang, B., Li, M., Cao, D., Sun, Q., Yu, W.-J., Ma, J., Ren, H., Xu, G., & Zhou, L. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05390-1 · Cited by 8 · see citing works

SHMT proteins: An emerging set of serine hydroxymethyltransferase in cancer

Fu, R., Sun, F., Wang, W., Wang, R., Zhang, H., He, X., Liu, A., & Yang, L. (2025) · Cellular Signalling · doi:10.1016/j.cellsig.2025.111977 · Cited by 7 · see citing works

BRCC36 functions noncatalytically to promote antiviral response by maintaining STAT1 protein stability

Cheng, Q., Feng, Q., Xu, Y., Zuo, Y., Liu, J., Yuan, Y., Miao, Y., Liu, Y., Lei, L., Guo, T., et al. (2020) · European Journal of Immunology · doi:10.1002/eji.202048537 · Cited by 7 · see citing works

Deubiquitinase Vulnerabilities Identified through Activity-Based Protein Profiling in Non-Small Cell Lung Cancer

Mahajan, S., Majumder, A., Stewart, P. A., Chen, Y. A., Adhikari, E., Fang, B., Yan, Y., Lawrence, H. R., Kinose, F., Koomen, J. M., et al. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.2c00018 · Cited by 6 · see citing works

The PKR-Like Endoplasmic Reticulum Kinase Promotes the Dissemination of Myc-Induced Leukemic Cells

Gui, J., Katlinski, K. V., Koumenis, C., Diehl, J. A., & Fuchs, S. Y. (2019) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-19-0002 · Cited by 6 · see citing works

A bacterial RING ubiquitin ligase triggering stepwise degradation of BRISC via TOLLIP-mediated selective autophagy manipulates host inflammatory response

Pan, X., Sun, Y., Liu, J., Chen, R., Zhang, Z., Li, C., Yao, H., & Ma, J. (2025) · Autophagy · doi:10.1080/15548627.2025.2468140 · Cited by 5 · see citing works

Different HCV Exposure Drives Specific miRNA Profile in PBMCs of HIV Patients

Valle‐Millares, D., Brochado‐Kith, O., Martín‐Carbonero, L., Domínguez, L., Ryan, P., Santos, I. D. L., de la Fuente, S., Castro, J. M., Lagarde, M., Cuevas, G., et al. (2021) · Biomedicines · doi:10.3390/biomedicines9111627 · Cited by 4 · see citing works

RXXPEG motif of MERIT40 is required to maintain spindle structure and function through its interaction with Tankyrase1

Zheng, D., Xie, W., Li, L., Jiang, W., Zou, Y., Chiang, C., Shao, G., & Yan, K. (2018) · Cell Biology International · doi:10.1002/cbin.11086 · Cited by 4 · see citing works

Identification of BRCC3 and BRCA1 as Regulators of TAZ Stability and Activity

Sberna, S., Lopez-Hernandez, A., Biancotto, C., Motta, L., Andronache, A., Verhoef, L. G. G. C., Cagánová, M., & Campaner, S. (2023) · Cells · doi:10.3390/cells12202431 · Cited by 3 · see citing works

A new subtype of type I IFN receptor, CRFB5b, plays an active role in host antiviral and antibacterial functions in Japanese eel (Anguilla japonica)

Wang, T., Lin, P., Wang, Y., Lai, X., Chen, P., Li, F., & Feng, J. (2023) · Aquaculture International · doi:10.1007/s10499-023-01375-2 · Cited by 2 · see citing works

Genetics of Moyamoya Beyond RNF213: Monogenic Moyamoya Syndromes

Guey, S., Kraemer, M., Grangeon, L., Riant, F., Kossorotoff, M., Hervé, D., & Tournier‐Lasserve, E. (2017) · Current topics in environmental health and preventive medicine · doi:10.1007/978-981-10-2711-6_9 · Cited by 2 · see citing works

Loss of SHMT2 mediates 5-FU chemoresistance by inducing autophagy in colorectal cancerPreprint

Chen, J., Fan, G., Xiao, C. W., Wang, X., Wang, Y., Song, G., Liu, X., Chen, J., Lu, H., Guo, W.-P., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/680892 · Cited by 2 · see citing works

Complexes Formed by the K63-Specific Deubiquitinating Enzyme BRCC36: New Promising Therapeutic Targets in Human Disease

Zhang, X., Pang, X., Chen, Y., Liu, G., Huang, J., & Zeng, Y. (2025) · Biomolecules · doi:10.3390/biom15121724 · Cited by 1 · see citing works

The Role of One‐Carbon Metabolism in Cancer and Its Therapeutic Significance

Jiang, Y., Zhou, G., Zhang, Q., & Zhou, S. (2026) · MedComm – Oncology · doi:10.1002/mog2.70062 · Cited by 1 · see citing works

Mechanism of K63-linked polyubiquitin recognition and cleavage by the BRCA1-A complex

Foglizzo, M., Datta, A., Degtjarik, O., Perera, H., Liburd, J., Sykora, U. M., Ganji, S. R., Wildsmith, G. C., Chandler, F., Campbell, L. J., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-75795-y · Cited by 1 · see citing works

Structural and functional defects of mitochondrial serine hydroxymethyltransferase genetic variants responsible for a novel neurodevelopmental syndrome

Boumis, G., Breccia, S., Pistoia, G., Spizzichino, S., Zamparelli, C., Troilo, F., Matteo, A. D., Travaglini‐Allocatelli, C., Contestabile, R., Tramonti, A., et al. (2026) · Frontiers in Chemical Biology · doi:10.3389/fchbi.2026.1941005 · Cited by 1 · see citing works

The Crossroads of Ubiquitination and DNA Repair: A Structural Perspective

Lingaraju, G. M., Böhm, K., Rabl, J., Cavadini, S., Fischer, E. S., Kassube, S. A., & Thomä, N. H. (2016) · Springer eBooks · doi:10.1007/978-4-431-55873-6_9 · Cited by 1 · see citing works

BRISC inactivation alleviates alcohol-induced liver injury in mice

Wang, T., Zhang, W., Liu, X., Liu, K., Ren, G., Xiang, S., Zhan, Y., Chen, H., Gao, H., Zhao, K., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-89796-2 · Cited by 1 · see citing works

PPTC7 acts as an essential co-factor of the SCF FBXL4 ubiquitin ligase complex to restrict BNIP3/BNIP3L-dependent mitophagyPreprint

Xu, X., Chen, Y., Li, Y., Zhao, S., & Wang, C. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.20.599818 · Cited by 1 · see citing works

Transcriptional regulation of human abraxas brother protein 1 expression by yin yang 1

Song, P., Hong, J., Wang, Y., Yao, X., Zhan, Y., Yin, R., Yu, M., Li, C., Yang, X., & Ge, C. (2020) · Biochemistry and Cell Biology · doi:10.1139/bcb-2019-0279

Interaction Analysis of SHMT1/2 Gene Variants with HCC in Chinese PatientsPreprint

Sun, Y., Gao, J., Shi, C., Liu, X., Zhang, F., Shi, X., Wang, Y., He, Y., Guo, W.-Z., & Zhang, S. (2022) · Research Square · doi:10.21203/rs.3.rs-2197291/v1

Aspirin improves both reactivity and durability of type-I interferon signaling to achieve functional cure of chronic hepatitis BPreprint

Miao, Y., Yuan, Y., Chen, Y., Liu, J., Fan, H., Zhang, T., Zhang, R., Zhao, Q., Cui, Q., Tian, W., et al. (2024) · medRxiv · doi:10.1101/2024.06.14.24308555

Molecular glues that inhibit deubiquitylase activity and inflammatory signallingPreprint

Chandler, F., Reddy, P. A. N., Bhutda, S., Ross, R. L., Datta, A., Walden, M., Walker, K., Donato, S. D., Cassel, J. A., Prakesch, M. A., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.07.611787

Small-molecule glues selectively restrict deubiquitylase activity and inflammatory signaling

(2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01518-4

Brcc36 isopeptidase

Rawlings, N. D. (2025) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-443-28849-4.00290-3

Proximity labeling reveals non-catalytic interactions between DPP9 and ubiquitin signaling complexes

Wirtgen, V. E., Saied, L., Zolg, S., Alonso, M. C., Mayer, B. A., Donzelli, L., Maurer, U., Timmers, H. T. M., Knobeloch, K., Kleifeld, O., et al. (2026) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-025-06021-z

DPP9 inhibition boosts antitumor immunity by disrupting BRISC-mediated PD-L1 expression in clear cell renal cell carcinoma

Zhang, W., Wang, Y., Feng, T., Cai, T., Wang, W., Zhu, S., Chen, Y., Zhang, H., Ye, D., Wang, C., et al. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01704-x

Etude fonctionnelle du suppresseur de tumeur WWOX et de ses partenaires protéiques dans le contexte de la carcinogenèse mammaire

Taouis, K. (2021) · theses.fr (ABES) · doi:10.70675/61149bf8zda59z4272za995zb95cad47c765

Serine Hydroxymethyltransferase (SHMT) in biology and disease: molecular mechanisms and therapeutic targeting

Li, J.-Y., Zhang, X., & Sheng, R. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-08044-x · Cited by 1 · see citing works

Endothelial SHMT2 Drives Pulmonary Vascular Remodeling Through Noncanonical Pathway in Pulmonary Hypertension

Wang, Q., Tian, J., Liu, D., Zheng, T., Liu, X. M., Zhao, Y., Li, X., Zhong, H., Pan, J., Yuan, C., et al. (2026) · Circulation · doi:10.1161/circulationaha.125.066183

Ubiquitination and Deubiquitination in Cellular Responses

Patterson-Fortin, J. (2011) · Scholarly Commons (University of Pennsylvania)

First‐in‐class Deubiquitylase Inhibitors Reveal New Enzyme Conformations

Chandler, F., Walden, M., Reddy, P. A. N., Cassel, J. A., Bell, L., Campbell, L. J., Foglizzo, M., Sicheri, F., Salvino, J. M., Greenberg, R. A., et al. (2022) · The FASEB Journal · doi:10.1096/fasebj.2022.36.s1.r4428

Molecular glues that inhibit deubiquitylase activity and inflammatory signaling

Chandler, F., Reddy, P. A. N., Bhutda, S., Ross, R. L., Datta, A., Walden, M., Walker, K., Donato, S. D., Cassel, J. A., Prakesch, M. A., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01517-5 · Cited by 10 · see citing works

Molecular glues that inhibit deubiquitylase activity and inflammatory signallingPreprint

Chandler, F., Reddy, P. A. N., Bhutda, S., Ross, R. L., Datta, A., Walden, M., Walker, K., Donato, S. D., Cassel, J. A., Prakesch, M. A., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.07.611787

Deubiquitylase (DUB) BRCC36 Isopeptidase Complex (BRISC) Inhibitors Prevent IFNAR1 Deubiquitination to Restore Natural Type I IFN Response in Autoimmunity

Ross, R., Reddy, P. A. N., Salvino, J., Zeqiraj, E., & Galdo, F. D. (2024) · White Rose Research Online (University of Leeds, The University of Sheffield, University of York)