Deubiquitylases From Genes to Organism

PGP9.5 as a marker for invasive colorectal cancer.

Yamazaki, T., Hibi, K., Takase, T., Tezel, E., Nakayama, H., Kasai, Y., Ito, K., Akiyama, S., Nagasaka, T., & Nakao, A. (2002) · PubMed · Cited by 139

Interaction of AMSH with ESCRT-III and Deubiquitination of Endosomal Cargo

Agromayor, M., & Martin‐Serrano, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513803200 · Cited by 138

Balanced ubiquitylation and deubiquitylation of Frizzled regulate cellular responsiveness to Wg/Wnt

Mukai, A., Yamamoto‐Hino, M., Awano, W., Watanabe, W., Komada, M., & Goto, S. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.100 · Cited by 138

A Perturbed Ubiquitin Landscape Distinguishes Between Ubiquitin in Trafficking and in Proteolysis

Ziv, I., Matiuhin, Y., Kirkpatrick, D. S., Erpapazoglou, Z., Sébastien Léon, A., Pantazopoulou, M., Kim, W., Gygi, S. P., Haguenauer‐Tsapis, R., Reis, N., et al. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.009753 · Cited by 137

Early Aldosterone-Induced Gene Product Regulates the Epithelial Sodium Channel by Deubiquitylation

Fakitsas, P., Adam, G., Daidie[Combining Acute Accent], D. A. A., van Bemmelen, M. X., Fouladkou, F., Patrignani, A., Wagner, U., Warth, R., Camargo, S. M. R., Staub, O., et al. (2007) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006080902 · Cited by 136

Human ELG1 Regulates the Level of Ubiquitinated Proliferating Cell Nuclear Antigen (PCNA) through Its Interactions with PCNA and USP1

Lee, K., Yang, K., Cohn, M. A., Sikdar, N., D’Andrea, A. D., & Myung, K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.092544 · Cited by 134

Recognition of Polyubiquitin Isoforms by the Multiple Ubiquitin Binding Modules of Isopeptidase T

Reyes‐Turcu, F. E., Shanks, J. R., Komander, D., & Wilkinson, K. D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800947200 · Cited by 134

Ubiquitin as a central cellular regulator

Finley, D. J., Ciechanover, A. J., & Varshavsky, A. J. (2004) · Cell · doi:10.1016/s0092-8674(03)00971-1 · Cited by 133

Retroviruses and insertional mutagenesis in mice: proviral integration at the Mov 34 locus leads to early embryonic death.Preprint

Soriano, P. M., Gridley, T., & Jaenisch, R. (1987) · Genes & Development · doi:10.1101/gad.1.4.366 · Cited by 133

Comparisons of neuronal (PGP 9.5) and non-neuronal ubiquitin C-terminal hydrolases

Wilkinson, K. D., Deshpande, S. S., & Larsen, C. N. (1992) · Biochemical Society Transactions · doi:10.1042/bst0200631 · Cited by 132

Inactivation of the Deubiquitinase CYLD in Hepatocytes Causes Apoptosis, Inflammation, Fibrosis, and Cancer

Nikolaou, K., Tsagaratou, A., Eftychi, C., Kollias, G. A., Mosialos, G., & Talianidis, I. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.04.026 · Cited by 131

Phosphorylation-dependent activity of the deubiquitinase DUBA

Huang, O. W., Ma, X., Yin, J., Flinders, J., Maurer, T., Kayagaki, N., Phung, Q. T., Bosanac, I., Arnott, D. P., Dixit, V. M., et al. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2206 · Cited by 131

USP8 Promotes Smoothened Signaling by Preventing Its Ubiquitination and Changing Its Subcellular Localization

Xia, R., Jia, H., Fan, J., Liu, Y., & Jia, J. (2012) · PLoS Biology · doi:10.1371/journal.pbio.1001238 · Cited by 131

Loss of Usp14 results in reduced levels of ubiquitin in ataxia mice

Anderson, C., Crimmins, S. L., Wilson, J. A., Korbel, G., Ploegh, H. L., & Wilson, S. M. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03409.x · Cited by 128

The therapeutic potential of deubiquitinating enzyme inhibitors

Colland, F. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380137 · Cited by 127

Systematic survey of deubiquitinase localization identifies USP21 as a regulator of centrosome- and microtubule-associated functions

Urbé, S., Liu, H., Hayes, S., Heride, C., Rigden, D. J., & Clague, M. J. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-08-0668 · Cited by 125

The proteasome-associated deubiquitinating enzyme Usp14 is essential for the maintenance of synaptic ubiquitin levels and the development of neuromuscular junctions

Chen, P.-C., Qin, L., Li, X.-M., Walters, B. J., Wilson, J. A., Mei, L., & Wilson, S. M. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.2635-09.2009 · Cited by 124

A Tight Link between Orthologs and Bidirectional Best Hits in Bacterial and Archaeal Genomes

Wolf, Y. I., & Koonin, E. V. (2012) · Genome Biology and Evolution · doi:10.1093/gbe/evs100 · Cited by 124

The Deubiquitinating Enzyme USP10 Regulates the Post-endocytic Sorting of Cystic Fibrosis Transmembrane Conductance Regulator in Airway Epithelial Cells

Bomberger, J. M., Barnaby, R., & Stanton, B. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.001685 · Cited by 122

A Deubiquitinating Enzyme UBPY Regulates the Level of Protein Ubiquitination on Endosomes

Mizuno, E., Kobayashi, K., Yamamoto, A., Kitamura, N., & Komada, M. (2006) · Traffic · doi:10.1111/j.1600-0854.2006.00452.x · Cited by 120

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 119

USP11 augments TGFβ signalling by deubiquitylating ALK5

Al-Salihi, M. A., Herhaus, L., Macartney, T., & Sapkota, G. P. (2012) · Open Biology · doi:10.1098/rsob.120063 · Cited by 118

Control of B Cell Development by the Histone H2A Deubiquitinase MYSM1

Jiang, X., Nguyen, Q., Chou, Y., Wang, T., Nandakumar, V., Yates, P., Jones, L. E., Wang, L., Won, H., Lee, H.-R., et al. (2011) · Immunity · doi:10.1016/j.immuni.2011.11.010 · Cited by 114

Dopaminergic neuronal loss in transgenic mice expressing the Parkinson's disease-associated UCH-L1 I93M mutant

Setsuie, R., Wang, Y.-L., Mochizuki, H., Osaka, H., Hayakawa, H., Ichihara, N., Li, H., Furuta, A., Sano, Y., Sun, Y., et al. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2006.07.015 · Cited by 114

Subunit 6 of the COP9 signalosome promotes tumorigenesis in mice through stabilization of MDM2 and is upregulated in human cancers

Zhao, R., Yeung, S. J., Chen, J., Iwakuma, T., Su, C., Chen, B., Qu, C., Zhang, F., Chen, Y., Lin, Y., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44111 · Cited by 111

Specificity of the Ubiquitin Isopeptidase in the PA700 Regulatory Complex of 26 S Proteasomes

Lam, Y. A., Demartino, G., Pickart, C. M., & Cohen, R. E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.45.28438 · Cited by 110

A20 deficiency in B cells enhances B‐cell proliferation and results in the development of autoantibodies

Hövelmeyer, N., Reißig, S., Xuân, N. T., Adams‐Quack, P., Lukas, D., Nikolaev, A., Schlüter, D., & Waisman, A. (2010) · European Journal of Immunology · doi:10.1002/eji.201041313 · Cited by 109

The COP9 Signalosome Mediates β-Catenin Degradation by Deneddylation and Blocks Adenomatous Polyposis coli Destruction via USP15

Huang, X., Langelotz, C., Hetfeld, B. K. J., Schwenk, W., & Dubiel, W. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.06.066 · Cited by 109

The critical role of histone H2A-deubiquitinase Mysm1 in hematopoiesis and lymphocyte differentiation

Nijnik, A., Clare, S., Hale, C., Raisen, C. L., McIntyre, R. E., Yusa, K., Everitt, A. R., Mottram, L., Podrini, C., Lucas, M., et al. (2011) · Blood · doi:10.1182/blood-2011-05-352666 · Cited by 108

Deubiquitination of EGFR by Cezanne-1 contributes to cancer progression

Pareja, F. G., Ferraro, D. A., Rubin, C., Cohen‐Dvashi, H., Zhang, F., Aulmann, S., Ben‐Chetrit, N., Pines, G., Navon, R., Crosetto, N., et al. (2011) · Oncogene · doi:10.1038/onc.2011.587 · Cited by 105

Differential redox regulation within the PTP superfamily

Ross, S. H., Lindsay, Y. E., Safrany, S. T., Lorenzo, Ó., Villa, F., Toth, R. L., Clague, M. J., Downes, C. P., & Leslie, N. R. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.01.026 · Cited by 103

The various roles of ubiquitin in Wnt pathway regulation

Tauriello, D. V. F., & Maurice, M. M. (2010) · Cell Cycle · doi:10.4161/cc.9.18.13204 · Cited by 102

Zinc-finger UBPs: regulators of deubiquitylation

Bonnet, J., Romier, C., Tora, L., & Devys, D. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.05.005 · Cited by 101

Ubiquitinated Proteins Activate the Proteasomal ATPases by Binding to Usp14 or Uch37 Homologs

Peth, A., Kukushkin, N. V., Bosse, M. M., & Goldberg, A. L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.441907 · Cited by 101

Applied Bioinformatics

Hendrix, D. A. (2019) · doi:10.5399/osu/1140 · Cited by 100

Usp46 is a quantitative trait gene regulating mouse immobile behavior in the tail suspension and forced swimming tests

Tomida, S., Mamiya, T., Sakamaki, H., Miura, M., Aosaki, T., Masuda, M., Niwa, M., Kameyama, T., Kobayashi, J., Iwaki, Y., et al. (2009) · Nature Genetics · doi:10.1038/ng.344 · Cited by 99

14-3-3-dependent inhibition of the deubiquitinating activity of UBPY and its cancellation in the M phase

Mizuno, E., Kitamura, N., & Komada, M. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.07.028 · Cited by 98

Biochemical characterization of USP7 reveals post-translational modification sites and structural requirements for substrate processing and subcellular localization.

Fernández‐Montalván, A., Bouwmeester, T., Joberty, G., Mader, R., Mahnke, M., Pierrat, B., Schlaeppi, J., Worpenberg, S., & Gerhartz, B. (2007) · The FEBS Journal · doi:10.1111/j.1742-4658.2007.05952.x · Cited by 96

Ubiquitin Homeostasis Is Critical for Synaptic Development and Function

Chen, P., Bhattacharyya, B. J., Hanna, J. W., Minkel, H. R., Wilson, J. A., Finley, D. J., Miller, R. J., & Wilson, S. M. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.2922-11.2011 · Cited by 94

Decoding ubiquitin sorting signals for clathrin-dependent endocytosis by CLASPs

Traub, L. M., & Lukács, G. L. (2007) · Journal of Cell Science · doi:10.1242/jcs.03385 · Cited by 94

Molecular Mechanisms of Ubiquitin-Dependent Membrane Traffic

Hurley, J. H., & Stenmark, H. (2011) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-042910-155404 · Cited by 93

Three Gene-Targeted Mouse Models of RNA Splicing Factor RP Show Late-Onset RPE and Retinal Degeneration

Graziotto, J. J., Farkas, M. H., Bujakowska, K. M., Deramaudt, B. M. J. ‐., Zhang, Q., Nandrot, E. F., Inglehearn, C. F., Bhattacharya, S. S., & Pierce, E. A. (2010) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.10-5194 · Cited by 92

Activity and Cellular Functions of the Deubiquitinating Enzyme and Polyglutamine Disease Protein Ataxin-3 Are Regulated by Ubiquitination at Lysine 117

Todi, S. V., Scaglione, K. M., Blount, J. R., Basrur, V., Conlon, K. P., Pastore, A., Elenitoba‐Johnson, K. S. J., & Paulson, H. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.181610 · Cited by 90

A Global Census of Fission Yeast Deubiquitinating Enzyme Localization and Interaction Networks Reveals Distinct Compartmentalization Profiles and Overlapping Functions in Endocytosis and Polarity

Kouranti, I., McLean, J. R., Feoktistova, A., Liang, P., Johnson, A. E., Roberts-Galbraith, R. H., & Gould, K. L. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000471 · Cited by 90

The Translation Initiation Factor 3f (eIF3f) Exhibits a Deubiquitinase Activity Regulating Notch Activation

Moretti, J., Chastagner, P., Gastaldello, S., Heuss, S. F., Dirac, A. M. G., Bernards, R., Masucci, M. G., Israël, A., & Brou, C. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000545 · Cited by 89

Regulators of the Proteasome Pathway, Uch37 and Rpn13, Play Distinct Roles in Mouse Development

Al-Shami, A., Jhaver, K. G., Vogel, P., Wilkins, C., Humphries, J., Davis, J. J., Xu, N., Potter, D., Gerhardt, B., Mullinax, R. A., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013654 · Cited by 87

Proteotoxic stress increases nuclear localization of ataxin-3

Reina, C. P., Zhong, X., & Pittman, R. N. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp482 · Cited by 86

Gene Expression Profiling in Ataxin-3 Expressing Cell Lines Reveals Distinct Effects of Normal and Mutant Ataxin-3

Evert, B. O., Vogt, I. R., Vieira-Saecker, A. M. M., Ozimek, L., de Vos, R. A. I., Brunt, E. R. P., Klockgether, T., & Wüllner, U. (2003) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/62.10.1006 · Cited by 83

The Machado-Joseph disease deubiquitylase ATX-3 couples longevity and proteostasis

Kuhlbrodt, K., Janiesch, P. C., Kevei, É., Segref, A., Barikbin, R., & Hoppe, T. (2011) · Nature Cell Biology · doi:10.1038/ncb2200 · Cited by 82

Transgenic Rescue ofataxiaMice with Neuronal-Specific Expression of Ubiquitin-Specific Protease 14

Crimmins, S. L., Jin, Y. N., Wheeler, C. G., et al. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.3600-06.2006 · Cited by 80

Roles of HAUSP-mediated p53 regulation in central nervous system development

Kon, N., Zhong, J., Kobayashi, Y., Li, M., Szabolcs, M., Ludwig, T., Canoll, P. D., & Gu, W. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2011.12 · Cited by 79

Ubiquitin C-Terminal Hydrolase-L1 Potentiates Cancer Chemosensitivity by Stabilizing NOXA

Brinkmann, K., Zigrino, P., Witt, A., Schell, M. J., Ackermann, L., Broxtermann, P. N., Schüll, S., Andree, M., Coutelle, O., Yazdanpanah, B., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.02.014 · Cited by 78

Mice Lacking the USP2 Deubiquitinating Enzyme Have Severe Male Subfertility Associated with Defects in Fertilization and Sperm Motility

Bedard, N., Yang, Y., Gregory, M., Cyr, D. G., Suzuki, J., Xiong, Y., Chian, R., Hermo, L., O’Flaherty, C., Smith, C. E., et al. (2011) · Biology of Reproduction · doi:10.1095/biolreprod.110.088542 · Cited by 75

The ubiquitin-specific protease USP2a prevents endocytosis-mediated EGFR degradation

Liu, Z., Zanata, S. M., Kim, J., Peterson, M. A., Vizio, D. D., Chirieac, L. R., Pyne, S., Agostini, M., Freeman, M. R., & Loda, M. F. (2012) · Oncogene · doi:10.1038/onc.2012.188 · Cited by 74

Targeted inactivation of the COP9 signalosome impairs multiple stagesof T cell development

Panattoni, M., Sanvito, F., Basso, V., Doglioni, C., Casorati, G., Montini, E., Bender, J. R., Mondino, A., & Pardi, R. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20070725 · Cited by 74

Genome-wide loss-of-function analysis of deubiquitylating enzymes for zebrafish development

Tse, W. K. F., Eisenhaber, B., Ho, S. H., Ng, Q., Eisenhaber, F., & Jiang, Y. (2009) · BMC Genomics · doi:10.1186/1471-2164-10-637 · Cited by 73

Molecular Basis of Lys-63-linked Polyubiquitination Inhibition by the Interaction between Human Deubiquitinating Enzyme OTUB1 and Ubiquitin-conjugating Enzyme UBC13

Sato, Y., Yamagata, A., Goto‐Ito, S., Kubota, K., Miyamoto, R., Nakada, S., & Fukai, S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.364752 · Cited by 72

Functional genomics and biochemical characterization of the C. elegans orthologue of the Machado‐Joseph disease protein ataxin‐3

Rodrigues, A. J., Coppola, G., Santos, C. S., Costa, M. D. C., Ailion, M., Sequeiros, J., Geschwind, D. H., & Maciel, P. (2007) · The FASEB Journal · doi:10.1096/fj.06-7002com · Cited by 70

Vasopressin-inducible ubiquitin-specific protease 10 increases ENaC cell surface expression by deubiquitylating and stabilizing sorting nexin 3

Boulkroun, S., Ruffieux-Daidié, D., Vitagliano, J., Poirot, O., Charles, R., Lagnaz, D., Firsov, D., Kellenberger, S., & Staub, O. (2008) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00001.2008 · Cited by 69

USP32 is an active, membrane-bound ubiquitin protease overexpressed in breast cancers

Akhavantabasi, S., Akman, H. B., Sapmaz, A., et al. (2010) · Mammalian Genome · doi:10.1007/s00335-010-9268-4 · Cited by 66

Ubiquitin in NF-κB Signaling

Chiu, Y., Zhao, M., & Chen, Z. J. (2009) · Chemical Reviews · doi:10.1021/cr800554j · Cited by 66

Substrate Filtering by the Active Site Crossover Loop in UCHL3 Revealed by Sortagging and Gain-of-function Mutations

Popp, M. W., Artavanis‐Tsakonas, K., & Ploegh, H. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807172200 · Cited by 66

Structure and recognition of polyubiquitin chains of different lengths and linkage

Fushman, D., & Wilkinson, K. D. (2011) · F1000 Biology Reports · doi:10.3410/b3-26 · Cited by 66

Understanding the Role of the Josephin Domain in the PolyUb Binding and Cleavage Properties of Ataxin-3

Nicastro, G., Todi, S. V., Karaca, E., Bonvin, A. M. J. J., Paulson, H. L., & Pastore, A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012430 · Cited by 65

Essential role of maternal UCHL1 and UCHL3 in fertilization and preimplantation embryo development

Mtango, N. R., Sutovsky, M., Šušor, A., Zhong, Z., Latham, K. E., & Šutovský, P. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22876 · Cited by 65

Systematic Analysis of the Physiological Importance of Deubiquitinating Enzymes

Tsou, W., Sheedlo, M. J., Morrow, M. E., Blount, J. R., McGregor, K. M., Das, C., & Todi, S. V. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043112 · Cited by 64

The Deubiquitinating Enzyme USP-46 Negatively Regulates the Degradation of Glutamate Receptors to Control Their Abundance in the Ventral Nerve Cord ofCaenorhabditis elegans

Kowalski, J. R., Dahlberg, C. L., & Juo, P. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.4765-10.2011 · Cited by 64

Splice Isoforms of the Polyglutamine Disease Protein Ataxin-3 Exhibit Similar Enzymatic yet Different Aggregation Properties

Harris, G. M., Dodelzon, K., Gong, L., Gonzalez‐Alegre, P., & Paulson, H. L. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013695 · Cited by 63

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 62

Solution Structure of the Ubp-M BUZ Domain, a Highly Specific Protein Module that Recognizes the C-terminal Tail of Free Ubiquitin

Pai, M., Tzeng, S., Kovacs, J. J., Keaton, M., Li, S. S. ‐., Yao, T., & Zhou, P. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.04.015 · Cited by 62

Hydrogen Peroxide Prolongs Nuclear Localization of NF-κB in Activated Cells by Suppressing Negative Regulatory Mechanisms

Enesa, K., Ito, K., Luong, L. A., Thorbjornsen, I., Phua, C., To, Y., Dean, J. L. E., Haskard, D. O., Boyle, J., Adcock, I. M., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801312200 · Cited by 61

The Role of Deubiquitinating Enzymes in Synaptic Function and Nervous System Diseases

Kowalski, J. R., & Juo, P. (2012) · Neural Plasticity · doi:10.1155/2012/892749 · Cited by 60

Length of the active-site crossover loop defines the substrate specificity of ubiquitin C-terminal hydrolases for ubiquitin chains

Zhou, Z., Zhang, Y., Liu, S., Song, A., & Hu, H. (2011) · Biochemical Journal · doi:10.1042/bj20110699 · Cited by 57

Structural Basis for ESCRT-III CHMP3 Recruitment of AMSH

Solomons, J., Sabin, C., Poudevigne, E., Usami, Y., Hulsik, D. L., Machebœuf, P., Hartlieb, B., Göttlinger, H. G., & Weissenhorn, W. (2011) · Structure · doi:10.1016/j.str.2011.05.011 · Cited by 56

Structural and Thermodynamic Comparison of the Catalytic Domain of AMSH and AMSH-LP: Nearly Identical Fold but Different Stability

Davies, C., Paul, L. N., Kim, M.-I., & Das, C. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.08.029 · Cited by 52

Direct and Indirect Control of Mitogen-activated Protein Kinase Pathway-associated Components, BRAP/IMP E3 Ubiquitin Ligase and CRAF/RAF1 Kinase, by the Deubiquitylating Enzyme USP15

Hayes, S., Liu, H., MacDonald, E., Sanderson, C. M., Coulson, J. M., Clague, M. J., & Urbé, S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.386938 · Cited by 50

Loss of Neurons in the Hippocampus and Cerebral Cortex of AMSH-Deficient Mice

Ishii, N., Owada, Y., Yamada, M., Miura, S., Murata, K., Asao, H., Kondo, H., & Sugamura, K. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.24.8626-8637.2001 · Cited by 50

Serine Phosphorylation Is Critical for the Activation of Ubiquitin-Specific Protease 1 and Its Interaction with WD40-Repeat Protein UAF1

Villamil, M. A., Liang, Q., Chen, J., Choi, Y. S., Hou, S., Lee, K. H., & Zhuang, Z. (2012) · Biochemistry · doi:10.1021/bi300845s · Cited by 49

Selectivity of the ubiquitin‐binding modules

Rahighi, S., & Đikić, I. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.04.053 · Cited by 45

The Ataxia (axJ) Mutation Causes Abnormal GABAA Receptor Turnover in Mice

Lappe-Siefke, C., Loebrich, S., Hevers, W., Waidmann, O. B., Schweizer, M., Fehr, S., Fritschy, J., Đikić, I., Eilers, J., Wilson, S. M., et al. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000631 · Cited by 44

Dissection of the Carboxyl-Terminal Domain of the Proteasomal Subunit Rpn11 in Maintenance of Mitochondrial Structure and Function

Rinaldi, T., Hofmann, L., Gambadoro, A., Cossard, R., Livnat‐Levanon, N., Glickman, M. H., Frontali, L., & Delahodde, A. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-07-0717 · Cited by 43

N-Ethyl-N-Nitrosourea–Induced Mutation in Ubiquitin-Specific Peptidase 18 Causes Hyperactivation of IFN-αβ Signaling and Suppresses STAT4-Induced IFN-γ Production, Resulting in Increased Susceptibility to Salmonella Typhimurium

Richer, É., Prendergast, C., Zhang, D., Qureshi, S. T., Vidal, S. M., & Malo, D. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000890 · Cited by 41

A global survey of CRM1-dependent nuclear export sequences in the human deubiquitinase family

García‐Santisteban, I., Bañuelos, S., & Rodríguez, J. A. (2011) · Biochemical Journal · doi:10.1042/bj20111300 · Cited by 41

Ubiquitin removal in the TGF-β pathway

Aggarwal, K., & Massagué, J. (2012) · Nature Cell Biology · doi:10.1038/ncb2534 · Cited by 41

Ubiquitin Carboxyl-Terminal Hydrolase L3 Promotes Insulin Signaling and Adipogenesis

Suzuki, M., Setsuie, R., & Wada, K. (2009) · Endocrinology · doi:10.1210/en.2009-0332 · Cited by 38

Ubiquitin-Specific Peptidase 46 (Usp46) Regulates Mouse Immobile Behavior in the Tail Suspension Test through the GABAergic System

Imai, S., Mamiya, T., Tsukada, A., Sakai, Y., Mouri, A., Nabeshima, T., & Ebihara, S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039084 · Cited by 37

Basal and stress-induced Hsp70 are modulated by ataxin-3

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