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Volumn 1843, Issue 1, 2014, Pages 114-128

Regulation of proteolysis by human deubiquitinating enzymes

Author keywords

Deubiquitinating enzyme; Poly ubiquitin; Proteolysis; Regulation; Ubiquitin

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; ATAXIN 3; CYTIDINE DEAMINASE; HISTONE H2A; HISTONE H2B; METALLOPROTEINASE; POLYUBIQUITIN; PROTEIN P53; THIOL PROTEINASE; TRANSCRIPTION FACTOR YY1; UBIQUITIN; UBIQUITIN THIOLESTERASE; UBIQUITINATED PROTEIN;

EID: 84890190983     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2013.06.027     Document Type: Review
Times cited : (154)

References (222)
  • 1
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: structures, functions, mechanisms
    • Pickart C.M., Eddins M.J. Ubiquitin: structures, functions, mechanisms. Biochim. Biophys. Acta 2004, 1695:55-72.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 2
    • 78751498823 scopus 로고    scopus 로고
    • E2s: structurally economical and functionally replete
    • Wenzel D.M., Stoll K.E., Klevit R.E. E2s: structurally economical and functionally replete. Biochem. J. 2011, 433:31-42.
    • (2011) Biochem. J. , vol.433 , pp. 31-42
    • Wenzel, D.M.1    Stoll, K.E.2    Klevit, R.E.3
  • 3
    • 67349256160 scopus 로고    scopus 로고
    • Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways
    • Schulman B.A., Harper J.W. Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways. Nat. Rev. Mol. Cell Biol. 2009, 10:319-331.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 319-331
    • Schulman, B.A.1    Harper, J.W.2
  • 4
    • 79957949190 scopus 로고    scopus 로고
    • UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids
    • Wenzel D.M., Lissounov A., Brzovic P.S., Klevit R.E. UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 2011, 474:105-108.
    • (2011) Nature , vol.474 , pp. 105-108
    • Wenzel, D.M.1    Lissounov, A.2    Brzovic, P.S.3    Klevit, R.E.4
  • 5
    • 33846497347 scopus 로고    scopus 로고
    • Regulation of catalytic activities of HECT ubiquitin ligases
    • Kee Y., Huibregtse J.M. Regulation of catalytic activities of HECT ubiquitin ligases. Biochem. Biophys. Res. Commun. 2007, 354:329-333.
    • (2007) Biochem. Biophys. Res. Commun. , vol.354 , pp. 329-333
    • Kee, Y.1    Huibregtse, J.M.2
  • 7
    • 70350150000 scopus 로고    scopus 로고
    • The emerging complexity of protein ubiquitination
    • Komander D. The emerging complexity of protein ubiquitination. Biochem. Soc. Trans. 2009, 37:937-953.
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 937-953
    • Komander, D.1
  • 8
    • 0017601447 scopus 로고
    • Isopeptide linkage between nonhistone and histone 2A polypeptides of chromosomal conjugate-protein A24
    • Goldknopf I.L., Busch H. Isopeptide linkage between nonhistone and histone 2A polypeptides of chromosomal conjugate-protein A24. Proc. Natl. Acad. Sci. U. S. A. 1977, 74:864-868.
    • (1977) Proc. Natl. Acad. Sci. U. S. A. , vol.74 , pp. 864-868
    • Goldknopf, I.L.1    Busch, H.2
  • 9
    • 84859259227 scopus 로고    scopus 로고
    • Histone ubiquitylation and chromatin dynamics
    • Wright D.E., Wang C.Y., Kao C.F. Histone ubiquitylation and chromatin dynamics. Front. Biosci. 2012, 17:1051-1078.
    • (2012) Front. Biosci. , vol.17 , pp. 1051-1078
    • Wright, D.E.1    Wang, C.Y.2    Kao, C.F.3
  • 10
    • 33750302074 scopus 로고    scopus 로고
    • Endocytosis: the DUB version
    • Clague M.J., Urbe S. Endocytosis: the DUB version. Trends Cell Biol. 2006, 16:551-559.
    • (2006) Trends Cell Biol. , vol.16 , pp. 551-559
    • Clague, M.J.1    Urbe, S.2
  • 11
    • 84858725584 scopus 로고    scopus 로고
    • Regulation of NF-kappaB by deubiquitinases
    • Harhaj E.W., Dixit V.M. Regulation of NF-kappaB by deubiquitinases. Immunol. Rev. 2012, 246:107-124.
    • (2012) Immunol. Rev. , vol.246 , pp. 107-124
    • Harhaj, E.W.1    Dixit, V.M.2
  • 12
    • 63049101044 scopus 로고    scopus 로고
    • Regulatory ubiquitylation in response to DNA double-strand breaks
    • Panier S., Durocher D. Regulatory ubiquitylation in response to DNA double-strand breaks. DNA Repair (Amst) 2009, 8:436-443.
    • (2009) DNA Repair (Amst) , vol.8 , pp. 436-443
    • Panier, S.1    Durocher, D.2
  • 13
    • 27144529182 scopus 로고    scopus 로고
    • Ubiquitylation and cell signaling
    • Haglund K., Dikic I. Ubiquitylation and cell signaling. EMBO J. 2005, 24:3353-3359.
    • (2005) EMBO J. , vol.24 , pp. 3353-3359
    • Haglund, K.1    Dikic, I.2
  • 14
    • 82955193293 scopus 로고    scopus 로고
    • Structure and recognition of polyubiquitin chains of different lengths and linkage
    • Fushman D., Wilkinson K.D. Structure and recognition of polyubiquitin chains of different lengths and linkage. F1000 Biol. Rep. 2011, 3:26.
    • (2011) F1000 Biol. Rep. , vol.3 , pp. 26
    • Fushman, D.1    Wilkinson, K.D.2
  • 15
    • 84255168970 scopus 로고    scopus 로고
    • The emerging role of linear ubiquitination in cell signaling
    • Emmerich C.H., Schmukle A.C., Walczak H. The emerging role of linear ubiquitination in cell signaling. Sci. Signal. 2011, 4:re5.
    • (2011) Sci. Signal. , vol.4
    • Emmerich, C.H.1    Schmukle, A.C.2    Walczak, H.3
  • 16
    • 84862761186 scopus 로고    scopus 로고
    • Diverse ubiquitin signaling in NF-kappaB activation
    • Iwai K. Diverse ubiquitin signaling in NF-kappaB activation. Trends Cell Biol. 2012, 22:355-364.
    • (2012) Trends Cell Biol. , vol.22 , pp. 355-364
    • Iwai, K.1
  • 18
    • 81755162787 scopus 로고    scopus 로고
    • Twists and turns in ubiquitin-like protein conjugation cascades
    • Schulman B.A. Twists and turns in ubiquitin-like protein conjugation cascades. Protein Sci. 2011, 20:1941-1954.
    • (2011) Protein Sci. , vol.20 , pp. 1941-1954
    • Schulman, B.A.1
  • 20
    • 67650620318 scopus 로고    scopus 로고
    • Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes
    • Reyes-Turcu F.E., Ventii K.H., Wilkinson K.D. Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu. Rev. Biochem. 2009, 78:363-397.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 363-397
    • Reyes-Turcu, F.E.1    Ventii, K.H.2    Wilkinson, K.D.3
  • 21
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: structure and function of the deubiquitinases
    • Komander D., Clague M.J., Urbe S. Breaking the chains: structure and function of the deubiquitinases. Nat. Rev. Mol. Cell Biol. 2009, 10:550-563.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 23
    • 72949102636 scopus 로고    scopus 로고
    • Dissection of USP catalytic domains reveals five common insertion points
    • Ye Y., Scheel H., Hofmann K., Komander D. Dissection of USP catalytic domains reveals five common insertion points. Mol. Biosyst. 2009, 5:1797-1808.
    • (2009) Mol. Biosyst. , vol.5 , pp. 1797-1808
    • Ye, Y.1    Scheel, H.2    Hofmann, K.3    Komander, D.4
  • 24
    • 0031011721 scopus 로고    scopus 로고
    • Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution
    • Johnston S.C., Larsen C.N., Cook W.J., Wilkinson K.D., Hill C.P. Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution. EMBO J. 1997, 16:3787-3796.
    • (1997) EMBO J. , vol.16 , pp. 3787-3796
    • Johnston, S.C.1    Larsen, C.N.2    Cook, W.J.3    Wilkinson, K.D.4    Hill, C.P.5
  • 25
    • 0028674466 scopus 로고
    • Catalytic mechanism in papain family of cysteine peptidases
    • Storer A.C., Menard R. Catalytic mechanism in papain family of cysteine peptidases. Methods Enzymol. 1994, 244:486-500.
    • (1994) Methods Enzymol. , vol.244 , pp. 486-500
    • Storer, A.C.1    Menard, R.2
  • 26
    • 9644268864 scopus 로고    scopus 로고
    • Mechanism and function of deubiquitinating enzymes
    • Amerik A.Y., Hochstrasser M. Mechanism and function of deubiquitinating enzymes. Biochim. Biophys. Acta 2004, 1695:189-207.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 189-207
    • Amerik, A.Y.1    Hochstrasser, M.2
  • 27
    • 84875912087 scopus 로고    scopus 로고
    • Reversible inactivation of deubiquitinases by reactive oxygen species in vitro and in cells
    • Lee J.G., Baek K., Soetandyo N., Ye Y. Reversible inactivation of deubiquitinases by reactive oxygen species in vitro and in cells. Nat. Commun. 2013, 4:1568.
    • (2013) Nat. Commun. , vol.4 , pp. 1568
    • Lee, J.G.1    Baek, K.2    Soetandyo, N.3    Ye, Y.4
  • 31
    • 84876105929 scopus 로고    scopus 로고
    • Covalent inhibition of SUMO and ubiquitin-specific cysteine proteases by an in situ thiol-alkyne addition
    • Sommer S., Weikart N.D., Linne U., Mootz H.D. Covalent inhibition of SUMO and ubiquitin-specific cysteine proteases by an in situ thiol-alkyne addition. Bioorg. Med. Chem. 2013, 21:2511-2517.
    • (2013) Bioorg. Med. Chem. , vol.21 , pp. 2511-2517
    • Sommer, S.1    Weikart, N.D.2    Linne, U.3    Mootz, H.D.4
  • 33
    • 0035903538 scopus 로고    scopus 로고
    • A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14
    • Borodovsky A., Kessler B.M., Casagrande R., Overkleeft H.S., Wilkinson K.D., Ploegh H.L. A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14. EMBO J. 2001, 20:5187-5196.
    • (2001) EMBO J. , vol.20 , pp. 5187-5196
    • Borodovsky, A.1    Kessler, B.M.2    Casagrande, R.3    Overkleeft, H.S.4    Wilkinson, K.D.5    Ploegh, H.L.6
  • 34
    • 28844440079 scopus 로고    scopus 로고
    • Derivitization of the C-terminus of ubiquitin and ubiquitin-like proteins using intein chemistry: methods and uses
    • Wilkinson K.D., Gan-Erdene T., Kolli N. Derivitization of the C-terminus of ubiquitin and ubiquitin-like proteins using intein chemistry: methods and uses. Methods Enzymol. 2005, 399:37-51.
    • (2005) Methods Enzymol. , vol.399 , pp. 37-51
    • Wilkinson, K.D.1    Gan-Erdene, T.2    Kolli, N.3
  • 35
    • 0032502276 scopus 로고    scopus 로고
    • Substrate specificity of deubiquitinating enzymes: ubiquitin C-terminal hydrolases
    • Larsen C.N., Krantz B.A., Wilkinson K.D. Substrate specificity of deubiquitinating enzymes: ubiquitin C-terminal hydrolases. Biochemistry 1998, 37:3358-3368.
    • (1998) Biochemistry , vol.37 , pp. 3358-3368
    • Larsen, C.N.1    Krantz, B.A.2    Wilkinson, K.D.3
  • 37
    • 71749110779 scopus 로고    scopus 로고
    • The deubiquitinating enzyme BAP1 regulates cell growth via interaction with HCF-1
    • Machida Y.J., Machida Y., Vashisht A.A., Wohlschlegel J.A., Dutta A. The deubiquitinating enzyme BAP1 regulates cell growth via interaction with HCF-1. J. Biol. Chem. 2009, 284:34179-34188.
    • (2009) J. Biol. Chem. , vol.284 , pp. 34179-34188
    • Machida, Y.J.1    Machida, Y.2    Vashisht, A.A.3    Wohlschlegel, J.A.4    Dutta, A.5
  • 38
    • 0031038169 scopus 로고    scopus 로고
    • Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
    • Lam Y.A., Xu W., DeMartino G.N., Cohen R.E. Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome. Nature 1997, 385:737-740.
    • (1997) Nature , vol.385 , pp. 737-740
    • Lam, Y.A.1    Xu, W.2    DeMartino, G.N.3    Cohen, R.E.4
  • 39
    • 84055178186 scopus 로고    scopus 로고
    • Length of the active-site crossover loop defines the substrate specificity of ubiquitin C-terminal hydrolases for ubiquitin chains
    • Zhou Z.R., Zhang Y.H., Liu S., Song A.X., Hu H.Y. Length of the active-site crossover loop defines the substrate specificity of ubiquitin C-terminal hydrolases for ubiquitin chains. Biochem. J. 2012, 441:143-149.
    • (2012) Biochem. J. , vol.441 , pp. 143-149
    • Zhou, Z.R.1    Zhang, Y.H.2    Liu, S.3    Song, A.X.4    Hu, H.Y.5
  • 40
    • 63649131003 scopus 로고    scopus 로고
    • 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. Substrate filtering by the active site crossover loop in UCHL3 revealed by sortagging and gain-of-function mutations. J. Biol. Chem. 2009, 284:3593-3602.
    • (2009) J. Biol. Chem. , vol.284 , pp. 3593-3602
    • Popp, M.W.1    Artavanis-Tsakonas, K.2    Ploegh, H.L.3
  • 43
    • 33845713194 scopus 로고    scopus 로고
    • HRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37
    • Qiu X.B., Ouyang S.Y., Li C.J., Miao S., Wang L., Goldberg A.L. hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37. EMBO J. 2006, 25:5742-5753.
    • (2006) EMBO J. , vol.25 , pp. 5742-5753
    • Qiu, X.B.1    Ouyang, S.Y.2    Li, C.J.3    Miao, S.4    Wang, L.5    Goldberg, A.L.6
  • 44
    • 33749348820 scopus 로고    scopus 로고
    • A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes
    • Hamazaki J., Iemura S., Natsume T., Yashiroda H., Tanaka K., Murata S. A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes. EMBO J. 2006, 25:4524-4536.
    • (2006) EMBO J. , vol.25 , pp. 4524-4536
    • Hamazaki, J.1    Iemura, S.2    Natsume, T.3    Yashiroda, H.4    Tanaka, K.5    Murata, S.6
  • 47
    • 58249095937 scopus 로고    scopus 로고
    • BRCA1-associated protein 1 interferes with BRCA1/BARD1 RING heterodimer activity
    • Nishikawa H., Wu W., Koike A., Kojima R., Gomi H., Fukuda M., Ohta T. BRCA1-associated protein 1 interferes with BRCA1/BARD1 RING heterodimer activity. Cancer Res. 2009, 69:111-119.
    • (2009) Cancer Res. , vol.69 , pp. 111-119
    • Nishikawa, H.1    Wu, W.2    Koike, A.3    Kojima, R.4    Gomi, H.5    Fukuda, M.6    Ohta, T.7
  • 48
    • 65249186662 scopus 로고    scopus 로고
    • Polyubiquitin binding and disassembly by deubiquitinating enzymes
    • Reyes-Turcu F.E., Wilkinson K.D. Polyubiquitin binding and disassembly by deubiquitinating enzymes. Chem. Rev. 2009, 109:1495-1508.
    • (2009) Chem. Rev. , vol.109 , pp. 1495-1508
    • Reyes-Turcu, F.E.1    Wilkinson, K.D.2
  • 49
    • 0037184947 scopus 로고    scopus 로고
    • Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
    • Hu M., Li P., Li M., Li W., Yao T., Wu J.W., Gu W., Cohen R.E., Shi Y. Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 2002, 111:1041-1054.
    • (2002) Cell , vol.111 , pp. 1041-1054
    • Hu, M.1    Li, P.2    Li, M.3    Li, W.4    Yao, T.5    Wu, J.W.6    Gu, W.7    Cohen, R.E.8    Shi, Y.9
  • 52
    • 0033974998 scopus 로고    scopus 로고
    • A novel superfamily of predicted cysteine proteases from eukaryotes, viruses and Chlamydia pneumoniae
    • Makarova K.S., Aravind L., Koonin E.V. A novel superfamily of predicted cysteine proteases from eukaryotes, viruses and Chlamydia pneumoniae. Trends Biochem. Sci. 2000, 25:50-52.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 50-52
    • Makarova, K.S.1    Aravind, L.2    Koonin, E.V.3
  • 53
    • 0038449224 scopus 로고    scopus 로고
    • Otubains: a new family of cysteine proteases in the ubiquitin pathway
    • Balakirev M.Y., Tcherniuk S.O., Jaquinod M., Chroboczek J. Otubains: a new family of cysteine proteases in the ubiquitin pathway. EMBO Rep. 2003, 4:517-522.
    • (2003) EMBO Rep. , vol.4 , pp. 517-522
    • Balakirev, M.Y.1    Tcherniuk, S.O.2    Jaquinod, M.3    Chroboczek, J.4
  • 57
    • 38149051652 scopus 로고    scopus 로고
    • Structure of the A20 OTU domain and mechanistic insights into deubiquitination
    • Komander D., Barford D. Structure of the A20 OTU domain and mechanistic insights into deubiquitination. Biochem. J. 2008, 409:77-85.
    • (2008) Biochem. J. , vol.409 , pp. 77-85
    • Komander, D.1    Barford, D.2
  • 58
    • 77955417276 scopus 로고    scopus 로고
    • Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne
    • Bremm A., Freund S.M., Komander D. Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne. Nat. Struct. Mol. Biol. 2010, 17:939-947.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 939-947
    • Bremm, A.1    Freund, S.M.2    Komander, D.3
  • 64
    • 79953009529 scopus 로고    scopus 로고
    • Crystal structure of a Josephin-ubiquitin complex: evolutionary restraints on ataxin-3 deubiquitinating activity
    • Weeks S.D., Grasty K.C., Hernandez-Cuebas L., Loll P.J. Crystal structure of a Josephin-ubiquitin complex: evolutionary restraints on ataxin-3 deubiquitinating activity. J. Biol. Chem. 2011, 286:4555-4565.
    • (2011) J. Biol. Chem. , vol.286 , pp. 4555-4565
    • Weeks, S.D.1    Grasty, K.C.2    Hernandez-Cuebas, L.3    Loll, P.J.4
  • 65
    • 34547899949 scopus 로고    scopus 로고
    • Josephin domain-containing proteins from a variety of species are active de-ubiquitination enzymes
    • Tzvetkov N., Breuer P. Josephin domain-containing proteins from a variety of species are active de-ubiquitination enzymes. Biol. Chem. 2007, 388:973-978.
    • (2007) Biol. Chem. , vol.388 , pp. 973-978
    • Tzvetkov, N.1    Breuer, P.2
  • 68
    • 24744447434 scopus 로고    scopus 로고
    • Defining the role of ubiquitin-interacting motifs in the polyglutamine disease protein, ataxin-3
    • Berke S.J., Chai Y., Marrs G.L., Wen H., Paulson H.L. Defining the role of ubiquitin-interacting motifs in the polyglutamine disease protein, ataxin-3. J. Biol. Chem. 2005, 280:32026-32034.
    • (2005) J. Biol. Chem. , vol.280 , pp. 32026-32034
    • Berke, S.J.1    Chai, Y.2    Marrs, G.L.3    Wen, H.4    Paulson, H.L.5
  • 69
    • 79960668226 scopus 로고    scopus 로고
    • Polyglutamine diseases: the special case of ataxin-3 and Machado-Joseph disease
    • Matos C.A., de Macedo-Ribeiro S., Carvalho A.L. Polyglutamine diseases: the special case of ataxin-3 and Machado-Joseph disease. Prog. Neurobiol. 2011, 95:26-48.
    • (2011) Prog. Neurobiol. , vol.95 , pp. 26-48
    • Matos, C.A.1    de Macedo-Ribeiro, S.2    Carvalho, A.L.3
  • 70
    • 0242693202 scopus 로고    scopus 로고
    • Elucidation of ataxin-3 and ataxin-7 function by integrative bioinformatics
    • Scheel H., Tomiuk S., Hofmann K. Elucidation of ataxin-3 and ataxin-7 function by integrative bioinformatics. Hum. Mol. Genet. 2003, 12:2845-2852.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2845-2852
    • Scheel, H.1    Tomiuk, S.2    Hofmann, K.3
  • 71
    • 0345099501 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity
    • Burnett B., Li F., Pittman R.N. The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity. Hum. Mol. Genet. 2003, 12:3195-3205.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 3195-3205
    • Burnett, B.1    Li, F.2    Pittman, R.N.3
  • 73
    • 34248350363 scopus 로고    scopus 로고
    • MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function
    • Maytal-Kivity V., Reis N., Hofmann K., Glickman M.H. MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function. BMC Biochem. 2002, 3:28.
    • (2002) BMC Biochem. , vol.3 , pp. 28
    • Maytal-Kivity, V.1    Reis, N.2    Hofmann, K.3    Glickman, M.H.4
  • 74
    • 0141706654 scopus 로고    scopus 로고
    • Structure of the Jab1/MPN domain and its implications for proteasome function
    • Tran H.J., Allen M.D., Lowe J., Bycroft M. Structure of the Jab1/MPN domain and its implications for proteasome function. Biochemistry 2003, 42:11460-11465.
    • (2003) Biochemistry , vol.42 , pp. 11460-11465
    • Tran, H.J.1    Allen, M.D.2    Lowe, J.3    Bycroft, M.4
  • 75
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • Yao T., Cohen R.E. A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 2002, 419:403-407.
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 77
    • 19344364762 scopus 로고    scopus 로고
    • JAMM: a metalloprotease-like zinc site in the proteasome and signalosome
    • Ambroggio X.I., Rees D.C., Deshaies R.J. JAMM: a metalloprotease-like zinc site in the proteasome and signalosome. PLoS Biol. 2004, 2:E2.
    • (2004) PLoS Biol. , vol.2
    • Ambroggio, X.I.1    Rees, D.C.2    Deshaies, R.J.3
  • 78
    • 7744244599 scopus 로고    scopus 로고
    • Recent advances in zinc enzymology
    • Lipscomb W.N., Strater N. Recent advances in zinc enzymology. Chem. Rev. 1996, 96:2375-2434.
    • (1996) Chem. Rev. , vol.96 , pp. 2375-2434
    • Lipscomb, W.N.1    Strater, N.2
  • 80
    • 62649104153 scopus 로고    scopus 로고
    • 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. K63-specific deubiquitination by two JAMM/MPN+complexes: BRISC-associated Brcc36 and proteasomal Poh1. EMBO J. 2009, 28:621-631.
    • (2009) EMBO J. , vol.28 , pp. 621-631
    • Cooper, E.M.1    Cutcliffe, C.2    Kristiansen, T.Z.3    Pandey, A.4    Pickart, C.M.5    Cohen, R.E.6
  • 81
    • 4143080425 scopus 로고    scopus 로고
    • AMSH is an endosome-associated ubiquitin isopeptidase
    • McCullough J., Clague M.J., Urbe S. AMSH is an endosome-associated ubiquitin isopeptidase. J. Cell Biol. 2004, 166:487-492.
    • (2004) J. Cell Biol. , vol.166 , pp. 487-492
    • McCullough, J.1    Clague, M.J.2    Urbe, S.3
  • 84
    • 80054717381 scopus 로고    scopus 로고
    • Structural and thermodynamic comparison of the catalytic domain of AMSH and AMSH-LP: nearly identical fold but different stability
    • Davies C.W., Paul L.N., Kim M.I., Das C. Structural and thermodynamic comparison of the catalytic domain of AMSH and AMSH-LP: nearly identical fold but different stability. J. Mol. Biol. 2011, 413:416-429.
    • (2011) J. Mol. Biol. , vol.413 , pp. 416-429
    • Davies, C.W.1    Paul, L.N.2    Kim, M.I.3    Das, C.4
  • 85
    • 84859827831 scopus 로고    scopus 로고
    • The proteasome: molecular machinery and pathophysiological roles
    • Tanaka K., Mizushima T., Saeki Y. The proteasome: molecular machinery and pathophysiological roles. Biol. Chem. 2012, 393:217-234.
    • (2012) Biol. Chem. , vol.393 , pp. 217-234
    • Tanaka, K.1    Mizushima, T.2    Saeki, Y.3
  • 86
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 2009, 78:477-513.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 87
    • 50949126350 scopus 로고    scopus 로고
    • Protein partners of deubiquitinating enzymes
    • Ventii K.H., Wilkinson K.D. Protein partners of deubiquitinating enzymes. Biochem. J. 2008, 414:161-175.
    • (2008) Biochem. J. , vol.414 , pp. 161-175
    • Ventii, K.H.1    Wilkinson, K.D.2
  • 90
    • 56449094567 scopus 로고    scopus 로고
    • The COP9 signalosome: more than a protease
    • Wei N., Serino G., Deng X.W. The COP9 signalosome: more than a protease. Trends Biochem. Sci. 2008, 33:592-600.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 592-600
    • Wei, N.1    Serino, G.2    Deng, X.W.3
  • 91
    • 80052873994 scopus 로고    scopus 로고
    • Roles of COP9 signalosome in cancer
    • Lee M.H., Zhao R., Phan L., Yeung S.C. Roles of COP9 signalosome in cancer. Cell Cycle 2011, 10:3057-3066.
    • (2011) Cell Cycle , vol.10 , pp. 3057-3066
    • Lee, M.H.1    Zhao, R.2    Phan, L.3    Yeung, S.C.4
  • 93
    • 79955938866 scopus 로고    scopus 로고
    • The multifaceted roles of USP7: new therapeutic opportunities
    • Nicholson B., Suresh Kumar K.G. The multifaceted roles of USP7: new therapeutic opportunities. Cell Biochem. Biophys. 2011, 60:61-68.
    • (2011) Cell Biochem. Biophys. , vol.60 , pp. 61-68
    • Nicholson, B.1    Suresh Kumar, K.G.2
  • 94
    • 0036674617 scopus 로고    scopus 로고
    • Live or let die: the cell's response to p53
    • Vousden K.H., Lu X. Live or let die: the cell's response to p53. Nat. Rev. Cancer 2002, 2:594-604.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 594-604
    • Vousden, K.H.1    Lu, X.2
  • 95
    • 0037317840 scopus 로고    scopus 로고
    • Inhibiting the p53-MDM2 interaction: an important target for cancer therapy
    • Chene P. Inhibiting the p53-MDM2 interaction: an important target for cancer therapy. Nat. Rev. Cancer 2003, 3:102-109.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 102-109
    • Chene, P.1
  • 96
    • 1842421376 scopus 로고    scopus 로고
    • A dynamic role of HAUSP in the p53-Mdm2 pathway
    • Li M., Brooks C.L., Kon N., Gu W. A dynamic role of HAUSP in the p53-Mdm2 pathway. Mol. Cell 2004, 13:879-886.
    • (2004) Mol. Cell , vol.13 , pp. 879-886
    • Li, M.1    Brooks, C.L.2    Kon, N.3    Gu, W.4
  • 97
    • 0037061508 scopus 로고    scopus 로고
    • 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. Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature 2002, 416:648-653.
    • (2002) Nature , vol.416 , pp. 648-653
    • Li, M.1    Chen, D.2    Shiloh, A.3    Luo, J.4    Nikolaev, A.Y.5    Qin, J.6    Gu, W.7
  • 99
    • 77951168849 scopus 로고    scopus 로고
    • Regulation of virus-triggered signaling by OTUB1- and OTUB2-mediated deubiquitination of TRAF3 and TRAF6
    • Li S., Zheng H., Mao A.P., Zhong B., Li Y., Liu Y., Gao Y., Ran Y., Tien P., Shu H.B. Regulation of virus-triggered signaling by OTUB1- and OTUB2-mediated deubiquitination of TRAF3 and TRAF6. J. Biol. Chem. 2010, 285:4291-4297.
    • (2010) J. Biol. Chem. , vol.285 , pp. 4291-4297
    • Li, S.1    Zheng, H.2    Mao, A.P.3    Zhong, B.4    Li, Y.5    Liu, Y.6    Gao, Y.7    Ran, Y.8    Tien, P.9    Shu, H.B.10
  • 100
    • 67650215581 scopus 로고    scopus 로고
    • OTU Domain-containing ubiquitin aldehyde-binding protein 1 (OTUB1) deubiquitinates estrogen receptor (ER) alpha and affects ERalpha transcriptional activity
    • Stanisic V., Malovannaya A., Qin J., Lonard D.M., O'Malley B.W. OTU Domain-containing ubiquitin aldehyde-binding protein 1 (OTUB1) deubiquitinates estrogen receptor (ER) alpha and affects ERalpha transcriptional activity. J. Biol. Chem. 2009, 284:16135-16145.
    • (2009) J. Biol. Chem. , vol.284 , pp. 16135-16145
    • Stanisic, V.1    Malovannaya, A.2    Qin, J.3    Lonard, D.M.4    O'Malley, B.W.5
  • 101
    • 77952715402 scopus 로고    scopus 로고
    • Post-translational modification of the deubiquitinating enzyme otubain 1 modulates active RhoA levels and susceptibility to Yersinia invasion
    • Edelmann M.J., Kramer H.B., Altun M., Kessler B.M. Post-translational modification of the deubiquitinating enzyme otubain 1 modulates active RhoA levels and susceptibility to Yersinia invasion. FEBS J. 2010, 277:2515-2530.
    • (2010) FEBS J. , vol.277 , pp. 2515-2530
    • Edelmann, M.J.1    Kramer, H.B.2    Altun, M.3    Kessler, B.M.4
  • 102
    • 84855287943 scopus 로고    scopus 로고
    • Ataxin-3 deubiquitination is coupled to Parkin ubiquitination via E2 ubiquitin-conjugating enzyme
    • Durcan T.M., Kontogiannea M., Bedard N., Wing S.S., Fon E.A. Ataxin-3 deubiquitination is coupled to Parkin ubiquitination via E2 ubiquitin-conjugating enzyme. J. Biol. Chem. 2012, 287:531-541.
    • (2012) J. Biol. Chem. , vol.287 , pp. 531-541
    • Durcan, T.M.1    Kontogiannea, M.2    Bedard, N.3    Wing, S.S.4    Fon, E.A.5
  • 103
    • 84856415004 scopus 로고    scopus 로고
    • Positive regulation of p53 stability and activity by the deubiquitinating enzyme Otubain 1
    • Sun X.X., Challagundla K.B., Dai M.S. Positive regulation of p53 stability and activity by the deubiquitinating enzyme Otubain 1. EMBO J. 2012, 31:576-592.
    • (2012) EMBO J. , vol.31 , pp. 576-592
    • Sun, X.X.1    Challagundla, K.B.2    Dai, M.S.3
  • 105
    • 84862806447 scopus 로고    scopus 로고
    • The mechanism of OTUB1-mediated inhibition of ubiquitination
    • Wiener R., Zhang X., Wang T., Wolberger C. The mechanism of OTUB1-mediated inhibition of ubiquitination. Nature 2012, 483:618-622.
    • (2012) Nature , vol.483 , pp. 618-622
    • Wiener, R.1    Zhang, X.2    Wang, T.3    Wolberger, C.4
  • 106
    • 0022033183 scopus 로고
    • The human ubiquitin multigene family: some genes contain multiple directly repeated ubiquitin coding sequences
    • Wiborg O., Pedersen M.S., Wind A., Berglund L.E., Marcker K.A., Vuust J. The human ubiquitin multigene family: some genes contain multiple directly repeated ubiquitin coding sequences. EMBO J. 1985, 4:755-759.
    • (1985) EMBO J. , vol.4 , pp. 755-759
    • Wiborg, O.1    Pedersen, M.S.2    Wind, A.3    Berglund, L.E.4    Marcker, K.A.5    Vuust, J.6
  • 107
    • 0020630852 scopus 로고
    • Isolation of PGP 9.5, a new human neurone-specific protein detected by high-resolution two-dimensional electrophoresis
    • Doran J.F., Jackson P., Kynoch P.A., Thompson R.J. Isolation of PGP 9.5, a new human neurone-specific protein detected by high-resolution two-dimensional electrophoresis. J. Neurochem. 1983, 40:1542-1547.
    • (1983) J. Neurochem. , vol.40 , pp. 1542-1547
    • Doran, J.F.1    Jackson, P.2    Kynoch, P.A.3    Thompson, R.J.4
  • 111
    • 0025326719 scopus 로고
    • Ubiquitin carboxyl-terminal hydrolase (PGP 9.5) is selectively present in ubiquitinated inclusion bodies characteristic of human neurodegenerative diseases
    • Lowe J., McDermott H., Landon M., Mayer R.J., Wilkinson K.D. Ubiquitin carboxyl-terminal hydrolase (PGP 9.5) is selectively present in ubiquitinated inclusion bodies characteristic of human neurodegenerative diseases. J. Pathol. 1990, 161:153-160.
    • (1990) J. Pathol. , vol.161 , pp. 153-160
    • Lowe, J.1    McDermott, H.2    Landon, M.3    Mayer, R.J.4    Wilkinson, K.D.5
  • 112
    • 1842581669 scopus 로고    scopus 로고
    • Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases
    • Choi J., Levey A.I., Weintraub S.T., Rees H.D., Gearing M., Chin L.S., Li L. Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases. J. Biol. Chem. 2004, 279:13256-13264.
    • (2004) J. Biol. Chem. , vol.279 , pp. 13256-13264
    • Choi, J.1    Levey, A.I.2    Weintraub, S.T.3    Rees, H.D.4    Gearing, M.5    Chin, L.S.6    Li, L.7
  • 114
    • 64149087218 scopus 로고    scopus 로고
    • Suppression of the deubiquitinating enzyme USP5 causes the accumulation of unanchored polyubiquitin and the activation of p53
    • Dayal S., Sparks A., Jacob J., Allende-Vega N., Lane D.P., Saville M.K. Suppression of the deubiquitinating enzyme USP5 causes the accumulation of unanchored polyubiquitin and the activation of p53. J. Biol. Chem. 2009, 284:5030-5041.
    • (2009) J. Biol. Chem. , vol.284 , pp. 5030-5041
    • Dayal, S.1    Sparks, A.2    Jacob, J.3    Allende-Vega, N.4    Lane, D.P.5    Saville, M.K.6
  • 115
    • 0028823598 scopus 로고
    • Metabolism of the polyubiquitin degradation signal: structure, mechanism, and role of isopeptidase T
    • Wilkinson K.D., Tashayev V.L., O'Connor L.B., Larsen C.N., Kasperek E., Pickart C.M. Metabolism of the polyubiquitin degradation signal: structure, mechanism, and role of isopeptidase T. Biochemistry 1995, 34:14535-14546.
    • (1995) Biochemistry , vol.34 , pp. 14535-14546
    • Wilkinson, K.D.1    Tashayev, V.L.2    O'Connor, L.B.3    Larsen, C.N.4    Kasperek, E.5    Pickart, C.M.6
  • 116
    • 0028859849 scopus 로고
    • A human de-ubiquitinating enzyme with both isopeptidase and peptidase activities in vitro
    • Falquet L., Paquet N., Frutiger S., Hughes G.J., Hoang-Van K., Jaton J.C. A human de-ubiquitinating enzyme with both isopeptidase and peptidase activities in vitro. FEBS Lett. 1995, 359:73-77.
    • (1995) FEBS Lett. , vol.359 , pp. 73-77
    • Falquet, L.1    Paquet, N.2    Frutiger, S.3    Hughes, G.J.4    Hoang-Van, K.5    Jaton, J.C.6
  • 117
    • 0026530899 scopus 로고
    • A ubiquitin C-terminal isopeptidase that acts on polyubiquitin chains. Role in protein degradation
    • Hadari T., Warms J.V., Rose I.A., Hershko A. A ubiquitin C-terminal isopeptidase that acts on polyubiquitin chains. Role in protein degradation. J. Biol. Chem. 1992, 267:719-727.
    • (1992) J. Biol. Chem. , vol.267 , pp. 719-727
    • Hadari, T.1    Warms, J.V.2    Rose, I.A.3    Hershko, A.4
  • 118
    • 26944465404 scopus 로고    scopus 로고
    • Diverse polyubiquitin interaction properties of ubiquitin-associated domains
    • Raasi S., Varadan R., Fushman D., Pickart C.M. Diverse polyubiquitin interaction properties of ubiquitin-associated domains. Nat. Struct. Mol. Biol. 2005, 12:708-714.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 708-714
    • Raasi, S.1    Varadan, R.2    Fushman, D.3    Pickart, C.M.4
  • 119
    • 33646066025 scopus 로고    scopus 로고
    • The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin
    • Reyes-Turcu F.E., Horton J.R., Mullally J.E., Heroux A., Cheng X., Wilkinson K.D. The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin. Cell 2006, 124:1197-1208.
    • (2006) Cell , vol.124 , pp. 1197-1208
    • Reyes-Turcu, F.E.1    Horton, J.R.2    Mullally, J.E.3    Heroux, A.4    Cheng, X.5    Wilkinson, K.D.6
  • 120
    • 50349102579 scopus 로고    scopus 로고
    • 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. Recognition of polyubiquitin isoforms by the multiple ubiquitin binding modules of isopeptidase T. J. Biol. Chem. 2008, 283:19581-19592.
    • (2008) J. Biol. Chem. , vol.283 , pp. 19581-19592
    • Reyes-Turcu, F.E.1    Shanks, J.R.2    Komander, D.3    Wilkinson, K.D.4
  • 121
    • 1942538492 scopus 로고    scopus 로고
    • ATM and DNA-PK function redundantly to phosphorylate H2AX after exposure to ionizing radiation
    • Stiff T., O'Driscoll M., Rief N., Iwabuchi K., Lobrich M., Jeggo P.A. ATM and DNA-PK function redundantly to phosphorylate H2AX after exposure to ionizing radiation. Cancer Res. 2004, 64:2390-2396.
    • (2004) Cancer Res. , vol.64 , pp. 2390-2396
    • Stiff, T.1    O'Driscoll, M.2    Rief, N.3    Iwabuchi, K.4    Lobrich, M.5    Jeggo, P.A.6
  • 122
    • 66849138419 scopus 로고    scopus 로고
    • Solving the RIDDLE of 53BP1 recruitment to sites of damage
    • Stewart G.S. Solving the RIDDLE of 53BP1 recruitment to sites of damage. Cell Cycle 2009, 8:1532-1538.
    • (2009) Cell Cycle , vol.8 , pp. 1532-1538
    • Stewart, G.S.1
  • 123
    • 63049138322 scopus 로고    scopus 로고
    • NBA1, a new player in the Brca1 A complex, is required for DNA damage resistance and checkpoint control
    • Wang B., Hurov K., Hofmann K., Elledge S.J. NBA1, a new player in the Brca1 A complex, is required for DNA damage resistance and checkpoint control. Genes Dev. 2009, 23:729-739.
    • (2009) Genes Dev. , vol.23 , pp. 729-739
    • Wang, B.1    Hurov, K.2    Hofmann, K.3    Elledge, S.J.4
  • 124
    • 63049083118 scopus 로고    scopus 로고
    • MERIT40 facilitates BRCA1 localization and DNA damage repair
    • Feng L., Huang J., Chen J. MERIT40 facilitates BRCA1 localization and DNA damage repair. Genes Dev. 2009, 23:719-728.
    • (2009) Genes Dev. , vol.23 , pp. 719-728
    • Feng, L.1    Huang, J.2    Chen, J.3
  • 126
    • 62549140202 scopus 로고    scopus 로고
    • 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. The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:3166-3171.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 3166-3171
    • Shao, G.1    Lilli, D.R.2    Patterson-Fortin, J.3    Coleman, K.A.4    Morrissey, D.E.5    Greenberg, R.A.6
  • 127
    • 84872782298 scopus 로고    scopus 로고
    • Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity
    • Py B.F., Kim M.S., Vakifahmetoglu-Norberg H., Yuan J. Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity. Mol. Cell 2013, 49:331-338.
    • (2013) Mol. Cell , vol.49 , pp. 331-338
    • Py, B.F.1    Kim, M.S.2    Vakifahmetoglu-Norberg, H.3    Yuan, J.4
  • 128
    • 84867898782 scopus 로고    scopus 로고
    • A20: linking a complex regulator of ubiquitylation to immunity and human disease
    • Ma A., Malynn B.A. A20: linking a complex regulator of ubiquitylation to immunity and human disease. Nat. Rev. Immunol. 2012, 12:774-785.
    • (2012) Nat. Rev. Immunol. , vol.12 , pp. 774-785
    • Ma, A.1    Malynn, B.A.2
  • 129
    • 39449083378 scopus 로고    scopus 로고
    • The E3 ligase Itch negatively regulates inflammatory signaling pathways by controlling the function of the ubiquitin-editing enzyme A20
    • Shembade N., Harhaj N.S., Parvatiyar K., Copeland N.G., Jenkins N.A., Matesic L.E., Harhaj E.W. The E3 ligase Itch negatively regulates inflammatory signaling pathways by controlling the function of the ubiquitin-editing enzyme A20. Nat. Immunol. 2008, 9:254-262.
    • (2008) Nat. Immunol. , vol.9 , pp. 254-262
    • Shembade, N.1    Harhaj, N.S.2    Parvatiyar, K.3    Copeland, N.G.4    Jenkins, N.A.5    Matesic, L.E.6    Harhaj, E.W.7
  • 130
    • 77649225756 scopus 로고    scopus 로고
    • Inhibition of NF-kappaB signaling by A20 through disruption of ubiquitin enzyme complexes
    • Shembade N., Ma A., Harhaj E.W. Inhibition of NF-kappaB signaling by A20 through disruption of ubiquitin enzyme complexes. Science 2010, 327:1135-1139.
    • (2010) Science , vol.327 , pp. 1135-1139
    • Shembade, N.1    Ma, A.2    Harhaj, E.W.3
  • 132
    • 33947506493 scopus 로고    scopus 로고
    • Site-specific Lys-63-linked tumor necrosis factor receptor-associated factor 6 auto-ubiquitination is a critical determinant of I kappa B kinase activation
    • Lamothe B., Besse A., Campos A.D., Webster W.K., Wu H., Darnay B.G. Site-specific Lys-63-linked tumor necrosis factor receptor-associated factor 6 auto-ubiquitination is a critical determinant of I kappa B kinase activation. J. Biol. Chem. 2007, 282:4102-4112.
    • (2007) J. Biol. Chem. , vol.282 , pp. 4102-4112
    • Lamothe, B.1    Besse, A.2    Campos, A.D.3    Webster, W.K.4    Wu, H.5    Darnay, B.G.6
  • 134
    • 79959847254 scopus 로고    scopus 로고
    • The role of deubiquitinating enzymes in chromatin regulation
    • Atanassov B.S., Koutelou E., Dent S.Y. The role of deubiquitinating enzymes in chromatin regulation. FEBS Lett. 2011, 585:2016-2023.
    • (2011) FEBS Lett. , vol.585 , pp. 2016-2023
    • Atanassov, B.S.1    Koutelou, E.2    Dent, S.Y.3
  • 135
    • 84863793933 scopus 로고    scopus 로고
    • A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase
    • Gatti M., Pinato S., Maspero E., Soffientini P., Polo S., Penengo L. A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase. Cell Cycle 2012, 11:2538-2544.
    • (2012) Cell Cycle , vol.11 , pp. 2538-2544
    • Gatti, M.1    Pinato, S.2    Maspero, E.3    Soffientini, P.4    Polo, S.5    Penengo, L.6
  • 138
    • 84863363343 scopus 로고    scopus 로고
    • Systematic survey of deubiquitinase localization identifies USP21 as a regulator of centrosome- and microtubule-associated functions
    • Urbe S., Liu H., Hayes S.D., Heride C., Rigden D.J., Clague M.J. Systematic survey of deubiquitinase localization identifies USP21 as a regulator of centrosome- and microtubule-associated functions. Mol. Biol. Cell 2012, 23:1095-1103.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 1095-1103
    • Urbe, S.1    Liu, H.2    Hayes, S.D.3    Heride, C.4    Rigden, D.J.5    Clague, M.J.6
  • 140
    • 34547730282 scopus 로고    scopus 로고
    • A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation
    • Zhu P., Zhou W., Wang J., Puc J., Ohgi K.A., Erdjument-Bromage H., Tempst P., Glass C.K., Rosenfeld M.G. A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation. Mol. Cell 2007, 27:609-621.
    • (2007) Mol. Cell , vol.27 , pp. 609-621
    • Zhu, P.1    Zhou, W.2    Wang, J.3    Puc, J.4    Ohgi, K.A.5    Erdjument-Bromage, H.6    Tempst, P.7    Glass, C.K.8    Rosenfeld, M.G.9
  • 141
    • 45849133054 scopus 로고    scopus 로고
    • USP22, an hSAGA subunit and potential cancer stem cell marker, reverses the polycomb-catalyzed ubiquitylation of histone H2A
    • Zhang X.Y., Pfeiffer H.K., Thorne A.W., McMahon S.B. USP22, an hSAGA subunit and potential cancer stem cell marker, reverses the polycomb-catalyzed ubiquitylation of histone H2A. Cell Cycle 2008, 7:1522-1524.
    • (2008) Cell Cycle , vol.7 , pp. 1522-1524
    • Zhang, X.Y.1    Pfeiffer, H.K.2    Thorne, A.W.3    McMahon, S.B.4
  • 143
    • 38149078715 scopus 로고    scopus 로고
    • The putative cancer stem cell marker USP22 is a subunit of the human SAGA complex required for activated transcription and cell-cycle progression
    • Zhang X.Y., Varthi M., Sykes S.M., Phillips C., Warzecha C., Zhu W., Wyce A., Thorne A.W., Berger S.L., McMahon S.B. The putative cancer stem cell marker USP22 is a subunit of the human SAGA complex required for activated transcription and cell-cycle progression. Mol. Cell 2008, 29:102-111.
    • (2008) Mol. Cell , vol.29 , pp. 102-111
    • Zhang, X.Y.1    Varthi, M.2    Sykes, S.M.3    Phillips, C.4    Warzecha, C.5    Zhu, W.6    Wyce, A.7    Thorne, A.W.8    Berger, S.L.9    McMahon, S.B.10
  • 146
    • 29144487990 scopus 로고    scopus 로고
    • Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing
    • Cao R., Tsukada Y., Zhang Y. Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing. Mol. Cell 2005, 20:845-854.
    • (2005) Mol. Cell , vol.20 , pp. 845-854
    • Cao, R.1    Tsukada, Y.2    Zhang, Y.3
  • 148
    • 11144237618 scopus 로고    scopus 로고
    • Ring1b-mediated H2A ubiquitination associates with inactive X chromosomes and is involved in initiation of X inactivation
    • Fang J., Chen T., Chadwick B., Li E., Zhang Y. Ring1b-mediated H2A ubiquitination associates with inactive X chromosomes and is involved in initiation of X inactivation. J. Biol. Chem. 2004, 279:52812-52815.
    • (2004) J. Biol. Chem. , vol.279 , pp. 52812-52815
    • Fang, J.1    Chen, T.2    Chadwick, B.3    Li, E.4    Zhang, Y.5
  • 150
    • 70349469565 scopus 로고    scopus 로고
    • Mechanisms of polycomb gene silencing: knowns and unknowns
    • Simon J.A., Kingston R.E. Mechanisms of polycomb gene silencing: knowns and unknowns. Nat. Rev. Mol. Cell Biol. 2009, 10:697-708.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 697-708
    • Simon, J.A.1    Kingston, R.E.2
  • 151
    • 33845799903 scopus 로고    scopus 로고
    • Polycomb silencing mechanisms and the management of genomic programmes
    • Schwartz Y.B., Pirrotta V. Polycomb silencing mechanisms and the management of genomic programmes. Nat. Rev. Genet. 2007, 8:9-22.
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 9-22
    • Schwartz, Y.B.1    Pirrotta, V.2
  • 153
    • 77955419051 scopus 로고    scopus 로고
    • Ubiquitin-specific proteases 7 and 11 modulate Polycomb regulation of the INK4a tumour suppressor
    • Maertens G.N., El Messaoudi-Aubert S., Elderkin S., Hiom K., Peters G. Ubiquitin-specific proteases 7 and 11 modulate Polycomb regulation of the INK4a tumour suppressor. EMBO J. 2010, 29:2553-2565.
    • (2010) EMBO J. , vol.29 , pp. 2553-2565
    • Maertens, G.N.1    El Messaoudi-Aubert, S.2    Elderkin, S.3    Hiom, K.4    Peters, G.5
  • 156
    • 34250823511 scopus 로고    scopus 로고
    • E2F activation of S phase promoters via association with HCF-1 and the MLL family of histone H3K4 methyltransferases
    • Tyagi S., Chabes A.L., Wysocka J., Herr W. E2F activation of S phase promoters via association with HCF-1 and the MLL family of histone H3K4 methyltransferases. Mol. Cell 2007, 27:107-119.
    • (2007) Mol. Cell , vol.27 , pp. 107-119
    • Tyagi, S.1    Chabes, A.L.2    Wysocka, J.3    Herr, W.4
  • 160
    • 84861233188 scopus 로고    scopus 로고
    • A distinct subset of atypical Spitz tumors is characterized by BRAF mutation and loss of BAP1 expression
    • Wiesner T., Murali R., Fried I., Cerroni L., Busam K., Kutzner H., Bastian B.C. A distinct subset of atypical Spitz tumors is characterized by BRAF mutation and loss of BAP1 expression. Am. J. Surg. Pathol. 2012, 36:818-830.
    • (2012) Am. J. Surg. Pathol. , vol.36 , pp. 818-830
    • Wiesner, T.1    Murali, R.2    Fried, I.3    Cerroni, L.4    Busam, K.5    Kutzner, H.6    Bastian, B.C.7
  • 164
    • 80053434128 scopus 로고    scopus 로고
    • Germline BAP1 mutations and tumor susceptibility
    • Goldstein A.M. Germline BAP1 mutations and tumor susceptibility. Nat. Genet. 2011, 43:925-926.
    • (2011) Nat. Genet. , vol.43 , pp. 925-926
    • Goldstein, A.M.1
  • 166
    • 0033020726 scopus 로고    scopus 로고
    • A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic chromosomes and blocks cell division
    • Cai S.Y., Babbitt R.W., Marchesi V.T. A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic chromosomes and blocks cell division. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:2828-2833.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 2828-2833
    • Cai, S.Y.1    Babbitt, R.W.2    Marchesi, V.T.3
  • 167
    • 33745713133 scopus 로고    scopus 로고
    • Regulation of chromatin structure by histone H3S10 phosphorylation
    • Johansen K.M., Johansen J. Regulation of chromatin structure by histone H3S10 phosphorylation. Chromosome Res. 2006, 14:393-404.
    • (2006) Chromosome Res. , vol.14 , pp. 393-404
    • Johansen, K.M.1    Johansen, J.2
  • 168
    • 34249707437 scopus 로고    scopus 로고
    • Solution structure of the Ubp-M BUZ domain, a highly specific protein module that recognizes the C-terminal tail of free ubiquitin
    • Pai M.T., Tzeng S.R., Kovacs J.J., Keaton M.A., Li S.S., Yao T.P., Zhou P. Solution structure of the Ubp-M BUZ domain, a highly specific protein module that recognizes the C-terminal tail of free ubiquitin. J. Mol. Biol. 2007, 370:290-302.
    • (2007) J. Mol. Biol. , vol.370 , pp. 290-302
    • Pai, M.T.1    Tzeng, S.R.2    Kovacs, J.J.3    Keaton, M.A.4    Li, S.S.5    Yao, T.P.6    Zhou, P.7
  • 169
    • 78650323748 scopus 로고    scopus 로고
    • HDAC6 and Ubp-M BUZ domains recognize specific C-terminal sequences of proteins
    • Hard R.L., Liu J., Shen J., Zhou P., Pei D. HDAC6 and Ubp-M BUZ domains recognize specific C-terminal sequences of proteins. Biochemistry 2010, 49:10737-10746.
    • (2010) Biochemistry , vol.49 , pp. 10737-10746
    • Hard, R.L.1    Liu, J.2    Shen, J.3    Zhou, P.4    Pei, D.5
  • 170
    • 73449097872 scopus 로고    scopus 로고
    • EBNA1-mediated recruitment of a histone H2B deubiquitylating complex to the Epstein-Barr virus latent origin of DNA replication
    • Sarkari F., Sanchez-Alcaraz T., Wang S., Holowaty M.N., Sheng Y., Frappier L. EBNA1-mediated recruitment of a histone H2B deubiquitylating complex to the Epstein-Barr virus latent origin of DNA replication. PLoS Pathog. 2009, 5:e1000624.
    • (2009) PLoS Pathog. , vol.5
    • Sarkari, F.1    Sanchez-Alcaraz, T.2    Wang, S.3    Holowaty, M.N.4    Sheng, Y.5    Frappier, L.6
  • 172
    • 79955940965 scopus 로고    scopus 로고
    • Regulation of endocytic sorting by ESCRT-DUB-mediated deubiquitination
    • Wright M.H., Berlin I., Nash P.D. Regulation of endocytic sorting by ESCRT-DUB-mediated deubiquitination. Cell Biochem. Biophys. 2011, 60:39-46.
    • (2011) Cell Biochem. Biophys. , vol.60 , pp. 39-46
    • Wright, M.H.1    Berlin, I.2    Nash, P.D.3
  • 175
    • 34948911522 scopus 로고    scopus 로고
    • Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis
    • Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K., Sundquist W.I. Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis. EMBO J. 2007, 26:4215-4227.
    • (2007) EMBO J. , vol.26 , pp. 4215-4227
    • Morita, E.1    Sandrin, V.2    Chung, H.Y.3    Morham, S.G.4    Gygi, S.P.5    Rodesch, C.K.6    Sundquist, W.I.7
  • 176
    • 79955484976 scopus 로고    scopus 로고
    • The spatial and temporal organization of ubiquitin networks
    • Grabbe C., Husnjak K., Dikic I. The spatial and temporal organization of ubiquitin networks. Nat. Rev. Mol. Cell Biol. 2011, 12:295-307.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 295-307
    • Grabbe, C.1    Husnjak, K.2    Dikic, I.3
  • 177
    • 27644438783 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor down-regulation by UBPY-mediated deubiquitination at endosomes
    • Mizuno E., Iura T., Mukai A., Yoshimori T., Kitamura N., Komada M. Regulation of epidermal growth factor receptor down-regulation by UBPY-mediated deubiquitination at endosomes. Mol. Biol. Cell 2005, 16:5163-5174.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5163-5174
    • Mizuno, E.1    Iura, T.2    Mukai, A.3    Yoshimori, T.4    Kitamura, N.5    Komada, M.6
  • 179
    • 33646788800 scopus 로고    scopus 로고
    • The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation
    • Row P.E., Prior I.A., McCullough J., Clague M.J., Urbe S. The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation. J. Biol. Chem. 2006, 281:12618-12624.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12618-12624
    • Row, P.E.1    Prior, I.A.2    McCullough, J.3    Clague, M.J.4    Urbe, S.5
  • 180
    • 33745754789 scopus 로고    scopus 로고
    • A deubiquitinating enzyme UBPY regulates the level of protein ubiquitination on endosomes
    • Mizuno E., Kobayashi K., Yamamoto A., Kitamura N., Komada M. A deubiquitinating enzyme UBPY regulates the level of protein ubiquitination on endosomes. Traffic 2006, 7:1017-1031.
    • (2006) Traffic , vol.7 , pp. 1017-1031
    • Mizuno, E.1    Kobayashi, K.2    Yamamoto, A.3    Kitamura, N.4    Komada, M.5
  • 181
    • 4344646977 scopus 로고    scopus 로고
    • Stabilization of the E3 ubiquitin ligase Nrdp1 by the deubiquitinating enzyme USP8
    • Wu X., Yen L., Irwin L., Sweeney C., Carraway K.L. Stabilization of the E3 ubiquitin ligase Nrdp1 by the deubiquitinating enzyme USP8. Mol. Cell. Biol. 2004, 24:7748-7757.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7748-7757
    • Wu, X.1    Yen, L.2    Irwin, L.3    Sweeney, C.4    Carraway, K.L.5
  • 182
    • 77950487987 scopus 로고    scopus 로고
    • Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems
    • Korolchuk V.I., Menzies F.M., Rubinsztein D.C. Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems. FEBS Lett. 2010, 584:1393-1398.
    • (2010) FEBS Lett. , vol.584 , pp. 1393-1398
    • Korolchuk, V.I.1    Menzies, F.M.2    Rubinsztein, D.C.3
  • 183
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin V., McEwan D.G., Novak I., Dikic I. A role for ubiquitin in selective autophagy. Mol. Cell 2009, 34:259-269.
    • (2009) Mol. Cell , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 184
    • 39049148153 scopus 로고    scopus 로고
    • Aggresome formation and neurodegenerative diseases: therapeutic implications
    • Olzmann J.A., Li L., Chin L.S. Aggresome formation and neurodegenerative diseases: therapeutic implications. Curr. Med. Chem. 2008, 15:47-60.
    • (2008) Curr. Med. Chem. , vol.15 , pp. 47-60
    • Olzmann, J.A.1    Li, L.2    Chin, L.S.3
  • 185
  • 186
    • 84865207113 scopus 로고    scopus 로고
    • Ataxin-3 regulates aggresome formation of copper-zinc superoxide dismutase (SOD1) by editing K63-linked polyubiquitin chains
    • Wang H., Ying Z., Wang G. Ataxin-3 regulates aggresome formation of copper-zinc superoxide dismutase (SOD1) by editing K63-linked polyubiquitin chains. J. Biol. Chem. 2012, 287:28576-28585.
    • (2012) J. Biol. Chem. , vol.287 , pp. 28576-28585
    • Wang, H.1    Ying, Z.2    Wang, G.3
  • 187
    • 15444372240 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin 3 regulates aggresome formation
    • Burnett B.G., Pittman R.N. The polyglutamine neurodegenerative protein ataxin 3 regulates aggresome formation. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:4330-4335.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 4330-4335
    • Burnett, B.G.1    Pittman, R.N.2
  • 188
    • 79955470830 scopus 로고    scopus 로고
    • Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes
    • (R110 003871)
    • Lee M.J., Lee B.H., Hanna J., King R.W., Finley D. Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes. Mol. Cell. Proteomics 2011, 10. (R110 003871).
    • (2011) Mol. Cell. Proteomics , vol.10
    • Lee, M.J.1    Lee, B.H.2    Hanna, J.3    King, R.W.4    Finley, D.5
  • 189
    • 41649091606 scopus 로고    scopus 로고
    • Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome
    • Koulich E., Li X., DeMartino G.N. Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome. Mol. Biol. Cell 2008, 19:1072-1082.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1072-1082
    • Koulich, E.1    Li, X.2    DeMartino, G.N.3
  • 190
    • 0347993105 scopus 로고    scopus 로고
    • Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool
    • Chernova T.A., Allen K.D., Wesoloski L.M., Shanks J.R., Chernoff Y.O., Wilkinson K.D. Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool. J. Biol. Chem. 2003, 278:52102-52115.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52102-52115
    • Chernova, T.A.1    Allen, K.D.2    Wesoloski, L.M.3    Shanks, J.R.4    Chernoff, Y.O.5    Wilkinson, K.D.6
  • 192
    • 0031709394 scopus 로고    scopus 로고
    • A mutation in a novel yeast proteasomal gene, RPN11/MPR1, produces a cell cycle arrest, overreplication of nuclear and mitochondrial DNA, and an altered mitochondrial morphology
    • Rinaldi T., Ricci C., Porro D., Bolotin-Fukuhara M., Frontali L. A mutation in a novel yeast proteasomal gene, RPN11/MPR1, produces a cell cycle arrest, overreplication of nuclear and mitochondrial DNA, and an altered mitochondrial morphology. Mol. Biol. Cell 1998, 9:2917-2931.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2917-2931
    • Rinaldi, T.1    Ricci, C.2    Porro, D.3    Bolotin-Fukuhara, M.4    Frontali, L.5
  • 193
    • 0030863993 scopus 로고    scopus 로고
    • Inhibition of the 26S proteasome by polyubiquitin chains synthesized to have defined lengths
    • Piotrowski J., Beal R., Hoffman L., Wilkinson K.D., Cohen R.E., Pickart C.M. Inhibition of the 26S proteasome by polyubiquitin chains synthesized to have defined lengths. J. Biol. Chem. 1997, 272:23712-23721.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23712-23721
    • Piotrowski, J.1    Beal, R.2    Hoffman, L.3    Wilkinson, K.D.4    Cohen, R.E.5    Pickart, C.M.6
  • 199
    • 59849116083 scopus 로고    scopus 로고
    • USP7 counteracts SCFbetaTrCP- but not APCCdh1-mediated proteolysis of Claspin
    • Faustrup H., Bekker-Jensen S., Bartek J., Lukas J., Mailand N. USP7 counteracts SCFbetaTrCP- but not APCCdh1-mediated proteolysis of Claspin. J. Cell Biol. 2009, 184:13-19.
    • (2009) J. Cell Biol. , vol.184 , pp. 13-19
    • Faustrup, H.1    Bekker-Jensen, S.2    Bartek, J.3    Lukas, J.4    Mailand, N.5
  • 201
    • 0031023690 scopus 로고    scopus 로고
    • A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein
    • Everett R.D., Meredith M., Orr A., Cross A., Kathoria M., Parkinson J. A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein. EMBO J. 1997, 16:566-577.
    • (1997) EMBO J. , vol.16 , pp. 566-577
    • Everett, R.D.1    Meredith, M.2    Orr, A.3    Cross, A.4    Kathoria, M.5    Parkinson, J.6
  • 202
    • 0041529593 scopus 로고    scopus 로고
    • Protein profiling with Epstein-Barr nuclear antigen-1 reveals an interaction with the herpesvirus-associated ubiquitin-specific protease HAUSP/USP7
    • Holowaty M.N., Zeghouf M., Wu H., Tellam J., Athanasopoulos V., Greenblatt J., Frappier L. Protein profiling with Epstein-Barr nuclear antigen-1 reveals an interaction with the herpesvirus-associated ubiquitin-specific protease HAUSP/USP7. J. Biol. Chem. 2003, 278:29987-29994.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29987-29994
    • Holowaty, M.N.1    Zeghouf, M.2    Wu, H.3    Tellam, J.4    Athanasopoulos, V.5    Greenblatt, J.6    Frappier, L.7
  • 204
    • 39749202339 scopus 로고    scopus 로고
    • Final stages of cytokinesis and midbody ring formation are controlled by BRUCE
    • Pohl C., Jentsch S. Final stages of cytokinesis and midbody ring formation are controlled by BRUCE. Cell 2008, 132:832-845.
    • (2008) Cell , vol.132 , pp. 832-845
    • Pohl, C.1    Jentsch, S.2
  • 205
    • 70350514475 scopus 로고    scopus 로고
    • Endosomal deubiquitinating enzymes control ubiquitination and down-regulation of protease-activated receptor 2
    • Hasdemir B., Murphy J.E., Cottrell G.S., Bunnett N.W. Endosomal deubiquitinating enzymes control ubiquitination and down-regulation of protease-activated receptor 2. J. Biol. Chem. 2009, 284:28453-28466.
    • (2009) J. Biol. Chem. , vol.284 , pp. 28453-28466
    • Hasdemir, B.1    Murphy, J.E.2    Cottrell, G.S.3    Bunnett, N.W.4
  • 206
    • 33846021632 scopus 로고    scopus 로고
    • Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8)
    • Avvakumov G.V., Walker J.R., Xue S., Finerty P.J., Mackenzie F., Newman E.M., Dhe-Paganon S. Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8). J. Biol. Chem. 2006, 281:38061-38070.
    • (2006) J. Biol. Chem. , vol.281 , pp. 38061-38070
    • Avvakumov, G.V.1    Walker, J.R.2    Xue, S.3    Finerty, P.J.4    Mackenzie, F.5    Newman, E.M.6    Dhe-Paganon, S.7
  • 208
    • 74049114641 scopus 로고    scopus 로고
    • Ubiquitin-specific peptidase 21 inhibits tumor necrosis factor alpha-induced nuclear factor kappaB activation via binding to and deubiquitinating receptor-interacting protein 1
    • Xu G., Tan X., Wang H., Sun W., Shi Y., Burlingame S., Gu X., Cao G., Zhang T., Qin J., Yang J. Ubiquitin-specific peptidase 21 inhibits tumor necrosis factor alpha-induced nuclear factor kappaB activation via binding to and deubiquitinating receptor-interacting protein 1. J. Biol. Chem. 2010, 285:969-978.
    • (2010) J. Biol. Chem. , vol.285 , pp. 969-978
    • Xu, G.1    Tan, X.2    Wang, H.3    Sun, W.4    Shi, Y.5    Burlingame, S.6    Gu, X.7    Cao, G.8    Zhang, T.9    Qin, J.10    Yang, J.11
  • 209
  • 211
    • 77952708547 scopus 로고    scopus 로고
    • Ubiquitin vinyl methyl ester binding orients the misaligned active site of the ubiquitin hydrolase UCHL1 into productive conformation
    • Boudreaux D.A., Maiti T.K., Davies C.W., Das C. Ubiquitin vinyl methyl ester binding orients the misaligned active site of the ubiquitin hydrolase UCHL1 into productive conformation. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:9117-9122.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 9117-9122
    • Boudreaux, D.A.1    Maiti, T.K.2    Davies, C.W.3    Das, C.4
  • 218
    • 33748988214 scopus 로고    scopus 로고
    • Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3
    • Wang Q., Li L., Ye Y. Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3. J. Cell Biol. 2006, 174:963-971.
    • (2006) J. Cell Biol. , vol.174 , pp. 963-971
    • Wang, Q.1    Li, L.2    Ye, Y.3
  • 221
    • 77951533710 scopus 로고    scopus 로고
    • AMSH interacts with ESCRT-0 to regulate the stability and trafficking of CXCR4
    • Sierra M.I., Wright M.H., Nash P.D. AMSH interacts with ESCRT-0 to regulate the stability and trafficking of CXCR4. J. Biol. Chem. 2010, 285:13990-14004.
    • (2010) J. Biol. Chem. , vol.285 , pp. 13990-14004
    • Sierra, M.I.1    Wright, M.H.2    Nash, P.D.3


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