메뉴 건너뛰기




Volumn 1695, Issue 1-3, 2004, Pages 189-207

Mechanism and function of deubiquitinating enzymes

Author keywords

Deubiquitinating enzyme; Proteasome; Ubiquitin

Indexed keywords

ATAXIN 3; JOSEPHIN; MEMBRANE PROTEIN; OLIGOMER; POLYUBIQUITIN; PROTEASOME; PROTEIN DERIVATIVE; PROTEIN P53; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 9644268864     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2004.10.003     Document Type: Review
Times cited : (811)

References (137)
  • 1
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • M. Hochstrasser Ubiquitin-dependent protein degradation Annu. Rev. Genet. 30 1996 405 439
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 4
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • C.M. Pickart Mechanisms underlying ubiquitination Annu. Rev. Biochem. 70 2001 503 533
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 5
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • A.M. Weissman Themes and variations on ubiquitylation Nat. Rev. Mol. Cell. Biol. 2 2001 169 178
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 6
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • L. Hicke Protein regulation by monoubiquitin Nat. Rev. Mol. Cell. Biol. 2 2001 195 201
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 7
    • 0035856472 scopus 로고    scopus 로고
    • Membrane transport: Ubiquitylation in endosomal sorting
    • S. Dupre, C. Volland, and R. Haguenauer-Tsapis Membrane transport: ubiquitylation in endosomal sorting Curr. Biol. 11 2001 R932 R934
    • (2001) Curr. Biol. , vol.11
    • Dupre, S.1    Volland, C.2    Haguenauer-Tsapis, R.3
  • 8
    • 0023115331 scopus 로고
    • The dynamics of ubiquitin pools within cultured human lung fibroblasts
    • A.L. Haas, and P.M. Bright The dynamics of ubiquitin pools within cultured human lung fibroblasts J. Biol. Chem. 262 1987 345 351
    • (1987) J. Biol. Chem. , vol.262 , pp. 345-351
    • Haas, A.L.1    Bright, P.M.2
  • 9
    • 0032794445 scopus 로고    scopus 로고
    • The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast
    • S. Swaminathan, A.Y. Amerik, and M. Hochstrasser The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast Mol. Biol. Cell 10 1999 2583 2594
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2583-2594
    • Swaminathan, S.1    Amerik, A.Y.2    Hochstrasser, M.3
  • 10
    • 0031038169 scopus 로고    scopus 로고
    • Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
    • Y.A. Lam, W. Xu, G.N. DeMartino, and R.E. Cohen Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome Nature 385 1997 737 740
    • (1997) Nature , vol.385 , pp. 737-740
    • Lam, Y.A.1    Xu, W.2    Demartino, G.N.3    Cohen, R.E.4
  • 12
    • 0024500866 scopus 로고
    • Detection, resolution, and nomenclature of multiple ubiquitin carboxyl-terminal esterases from bovine calf thymus
    • A.N. Mayer, and K.D. Wilkinson Detection, resolution, and nomenclature of multiple ubiquitin carboxyl-terminal esterases from bovine calf thymus Biochemistry 28 1989 166 172
    • (1989) Biochemistry , vol.28 , pp. 166-172
    • Mayer, A.N.1    Wilkinson, K.D.2
  • 13
    • 0033974998 scopus 로고    scopus 로고
    • A novel superfamily of predicted cysteine proteases from eukaryotes, viruses and Chlamydia pneumoniae
    • K.S. Makarova, L. Aravind, and E.V. Koonin A novel superfamily of predicted cysteine proteases from eukaryotes, viruses and Chlamydia pneumoniae Trends Biochem. Sci. 25 2000 50 52
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 50-52
    • Makarova, K.S.1    Aravind, L.2    Koonin, E.V.3
  • 15
    • 0034730713 scopus 로고    scopus 로고
    • Failure to regulate TNF-induced NF-kappaB and cell death responses in A20-deficient mice
    • E.G. Lee, D.L. Boone, S. Chai, S.L. Libby, M. Chien, J.P. Lodolce, and A. Ma Failure to regulate TNF-induced NF-kappaB and cell death responses in A20-deficient mice Science 289 2000 2350 2354
    • (2000) Science , vol.289 , pp. 2350-2354
    • Lee, E.G.1    Boone, D.L.2    Chai, S.3    Libby, S.L.4    Chien, M.5    Lodolce, J.P.6    Ma, A.7
  • 17
    • 1642423503 scopus 로고    scopus 로고
    • Zinc-finger protein A20, a regulator of inflammation and cell survival, has de-ubiquitinating activity
    • P.C. Evans, H. Ovaa, M. Hamon, P.J. Kilshaw, S. Hamm, S. Bauer, H.L. Ploegh, and T.S. Smith Zinc-finger protein A20, a regulator of inflammation and cell survival, has de-ubiquitinating activity Biochem. J. 378 2004 727 734
    • (2004) Biochem. J. , vol.378 , pp. 727-734
    • Evans, P.C.1    Ovaa, H.2    Hamon, M.3    Kilshaw, P.J.4    Hamm, S.5    Bauer, S.6    Ploegh, H.L.7    Smith, T.S.8
  • 18
    • 1842509180 scopus 로고    scopus 로고
    • VCIP135 acts as a deubiquitinating enzyme during p97-p47-mediated reassembly of mitotic Golgi fragments
    • Y. Wang, A. Satoh, G. Warren, and H.H. Meyer VCIP135 acts as a deubiquitinating enzyme during p97-p47-mediated reassembly of mitotic Golgi fragments J. Cell Biol. 164 2004 973 978
    • (2004) J. Cell Biol. , vol.164 , pp. 973-978
    • Wang, Y.1    Satoh, A.2    Warren, G.3    Meyer, H.H.4
  • 19
    • 0038449224 scopus 로고    scopus 로고
    • Otubains: A new family of cysteine proteases in the ubiquitin pathway
    • M.Y. Balakirev, S.O. Tcherniuk, M. Jaquinod, and J. Chroboczek Otubains: a new family of cysteine proteases in the ubiquitin pathway EMBO Rep. 4 2003 517 522
    • (2003) EMBO Rep. , vol.4 , pp. 517-522
    • Balakirev, M.Y.1    Tcherniuk, S.O.2    Jaquinod, M.3    Chroboczek, J.4
  • 21
    • 0345099501 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity
    • B. Burnett, F. Li, and R.N. Pittman The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity Hum. Mol. Genet. 12 2003 3195 3205
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 3195-3205
    • Burnett, B.1    Li, F.2    Pittman, R.N.3
  • 22
    • 0242693202 scopus 로고    scopus 로고
    • Elucidation of ataxin-3 and ataxin-7 function by integrative bioinformatics
    • H. Scheel, S. Tomiuk, and K. Hofmann Elucidation of ataxin-3 and ataxin-7 function by integrative bioinformatics Hum. Mol. Genet. 12 2003 2845 2852
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2845-2852
    • Scheel, H.1    Tomiuk, S.2    Hofmann, K.3
  • 24
    • 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
    • V. Maytal-Kivity, N. Reis, K. Hofmann, and M.H. Glickman MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function BMC Biochem. 3 2002 28
    • (2002) BMC Biochem. , vol.3 , pp. 28
    • Maytal-Kivity, V.1    Reis, N.2    Hofmann, K.3    Glickman, M.H.4
  • 25
    • 4143080425 scopus 로고    scopus 로고
    • AMSH is an endosome-associated ubiquitin isopeptidase
    • J. McCullough, M.J. Clague, and S. Urbe AMSH is an endosome-associated ubiquitin isopeptidase J. Cell Biol. 166 2004 487 492
    • (2004) J. Cell Biol. , vol.166 , pp. 487-492
    • McCullough, J.1    Clague, M.J.2    Urbe, S.3
  • 26
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • T. Yao, and R.E. Cohen A cryptic protease couples deubiquitination and degradation by the proteasome Nature 419 2002 403 407
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 27
    • 19344364762 scopus 로고    scopus 로고
    • JAMM: A metalloprotease-like zinc site in the proteasome and signalosome
    • X.I. Ambroggio, D.C. Rees, and R.J. Deshaies JAMM: a metalloprotease-like zinc site in the proteasome and signalosome PLoS Biol. 2 2004 E2
    • (2004) PLoS Biol. , vol.2
    • Ambroggio, X.I.1    Rees, D.C.2    Deshaies, R.J.3
  • 28
    • 0031011721 scopus 로고    scopus 로고
    • Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 Å resolution
    • S.C. Johnston, C.N. Larsen, W.J. Cook, K.D. Wilkinson, and C.P. Hill Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 Å resolution EMBO J. 16 1997 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
  • 29
    • 0033565867 scopus 로고    scopus 로고
    • Structural basis for the specificity of ubiquitin C-terminal hydrolases
    • S.C. Johnston, S.M. Riddle, R.E. Cohen, and C.P. Hill Structural basis for the specificity of ubiquitin C-terminal hydrolases EMBO J. 18 1999 3877 3887
    • (1999) EMBO J. , vol.18 , pp. 3877-3887
    • Johnston, S.C.1    Riddle, S.M.2    Cohen, R.E.3    Hill, C.P.4
  • 30
    • 0037184947 scopus 로고    scopus 로고
    • Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
    • M. Hu, P. Li, M. Li, W. Li, T. Yao, J.W. Wu, W. Gu, R.E. Cohen, and Y. Shi Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde Cell 111 2002 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
  • 31
    • 0141706654 scopus 로고    scopus 로고
    • Structure of the Jab1/MPN domain and its implications for proteasome function
    • H.J. Tran, M.D. Allen, J. Lowe, and M. Bycroft Structure of the Jab1/MPN domain and its implications for proteasome function Biochemistry 42 2003 11460 11465
    • (2003) Biochemistry , vol.42 , pp. 11460-11465
    • Tran, H.J.1    Allen, M.D.2    Lowe, J.3    Bycroft, M.4
  • 33
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell-cycle progression in yeast
    • S.-J. Li, and M. Hochstrasser A new protease required for cell-cycle progression in yeast Nature 398 1999 246 251
    • (1999) Nature , vol.398 , pp. 246-251
    • Li, S.-J.1    Hochstrasser, M.2
  • 34
    • 0033638223 scopus 로고    scopus 로고
    • Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast
    • E. Mossessova, and C.D. Lima Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast Mol. Cell 5 2000 865 876
    • (2000) Mol. Cell , vol.5 , pp. 865-876
    • Mossessova, E.1    Lima, C.D.2
  • 35
    • 0037177245 scopus 로고    scopus 로고
    • Catalysis by entropic effects: The action of cytidine deaminase on 5,6-dihydrocytidine
    • M.J. Snider, D. Lazarevic, and R. Wolfenden Catalysis by entropic effects: the action of cytidine deaminase on 5,6-dihydrocytidine Biochemistry 41 2002 3925 3930
    • (2002) Biochemistry , vol.41 , pp. 3925-3930
    • Snider, M.J.1    Lazarevic, D.2    Wolfenden, R.3
  • 37
    • 0033783007 scopus 로고    scopus 로고
    • Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae
    • A.Y. Amerik, S.J. Li, and M. Hochstrasser Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae Biol. Chem. 381 2000 981 992
    • (2000) Biol. Chem. , vol.381 , pp. 981-992
    • Amerik, A.Y.1    Li, S.J.2    Hochstrasser, M.3
  • 38
    • 0034703437 scopus 로고    scopus 로고
    • Detecting and measuring cotranslational protein degradation in vivo
    • G.C. Turner, and A. Varshavsky Detecting and measuring cotranslational protein degradation in vivo Science 289 2000 2117 2120
    • (2000) Science , vol.289 , pp. 2117-2120
    • Turner, G.C.1    Varshavsky, A.2
  • 39
    • 0028146192 scopus 로고
    • Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant
    • D. Finley, S. Sadis, B.P. Monia, P. Boucher, D.J. Ecker, S.T. Crooke, and V. Chau Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant Mol. Cell. Biol. 14 1994 5501 5509
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5501-5509
    • Finley, D.1    Sadis, S.2    Monia, B.P.3    Boucher, P.4    Ecker, D.J.5    Crooke, S.T.6    Chau, V.7
  • 42
    • 0030699383 scopus 로고    scopus 로고
    • Specificity of the ubiquitin isopeptidase in the PA700 regulatory complex of 26S proteasomes
    • Y.A. Lam, G.N. DeMartino, C.M. Pickart, and R.E. Cohen Specificity of the ubiquitin isopeptidase in the PA700 regulatory complex of 26S proteasomes J. Biol. Chem. 272 1997 28438 28446
    • (1997) J. Biol. Chem. , vol.272 , pp. 28438-28446
    • Lam, Y.A.1    Demartino, G.N.2    Pickart, C.M.3    Cohen, R.E.4
  • 43
    • 0027427249 scopus 로고
    • The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene
    • F. Papa, and M. Hochstrasser The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene Nature 366 1993 313 319
    • (1993) Nature , vol.366 , pp. 313-319
    • Papa, F.1    Hochstrasser, M.2
  • 44
    • 0032912818 scopus 로고    scopus 로고
    • Interaction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome
    • F.R. Papa, A.Y. Amerik, and M. Hochstrasser Interaction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome Mol. Biol. Cell 10 1999 741 756
    • (1999) Mol. Biol. Cell , vol.10 , pp. 741-756
    • Papa, F.R.1    Amerik, A.Y.2    Hochstrasser, M.3
  • 45
    • 0035903538 scopus 로고    scopus 로고
    • A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14
    • A. Borodovsky, B.M. Kessler, R. Casagrande, H.S. Overkleeft, K.D. Wilkinson, and H.L. Ploegh A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14 EMBO J. 20 2001 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
  • 47
    • 0027480739 scopus 로고
    • Ubiquitin C-terminal hydrolase activity associated with the 26S protease complex
    • E. Eytan, T. Armon, H. Heller, S. Beck, and A. Hershko Ubiquitin C-terminal hydrolase activity associated with the 26S protease complex J. Biol. Chem. 268 1993 4668 4674
    • (1993) J. Biol. Chem. , vol.268 , pp. 4668-4674
    • Eytan, E.1    Armon, T.2    Heller, H.3    Beck, S.4    Hershko, A.5
  • 48
    • 0032549815 scopus 로고    scopus 로고
    • Cotranslational biogenesis of NF-kappaB p50 by the 26S proteasome
    • L. Lin, G.N. DeMartino, and W.C. Greene Cotranslational biogenesis of NF-kappaB p50 by the 26S proteasome Cell 92 1998 819 828
    • (1998) Cell , vol.92 , pp. 819-828
    • Lin, L.1    Demartino, G.N.2    Greene, W.C.3
  • 49
    • 0034268493 scopus 로고    scopus 로고
    • Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing
    • T. Hoppe, K. Matuschewski, M. Rape, S. Schlenker, H.D. Ulrich, and S. Jentsch Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing Cell 102 2000 577 586
    • (2000) Cell , vol.102 , pp. 577-586
    • Hoppe, T.1    Matuschewski, K.2    Rape, M.3    Schlenker, S.4    Ulrich, H.D.5    Jentsch, S.6
  • 50
    • 0035977095 scopus 로고    scopus 로고
    • Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone
    • M. Rape, T. Hoppe, I. Gorr, M. Kalocay, H. Richly, and S. Jentsch Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone Cell 107 2001 667 677
    • (2001) Cell , vol.107 , pp. 667-677
    • Rape, M.1    Hoppe, T.2    Gorr, I.3    Kalocay, M.4    Richly, H.5    Jentsch, S.6
  • 52
    • 0030746105 scopus 로고    scopus 로고
    • In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome
    • A.Y. Amerik, S. Swaminathan, B.A. Krantz, K.D. Wilkinson, and M. Hochstrasser In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome EMBO J. 16 1997 4826 4838
    • (1997) EMBO J. , vol.16 , pp. 4826-4838
    • Amerik, A.Y.1    Swaminathan, S.2    Krantz, B.A.3    Wilkinson, K.D.4    Hochstrasser, M.5
  • 53
    • 0026530899 scopus 로고
    • A ubiquitin C-terminal isopeptidase that acts on polyubiquitin chains-role in protein degradation
    • T. Hadari, J.V.B. Warms, I.A. Rose, and A. Hershko A ubiquitin C-terminal isopeptidase that acts on polyubiquitin chains-role in protein degradation J. Biol. Chem. 267 1992 719 727
    • (1992) J. Biol. Chem. , vol.267 , pp. 719-727
    • Hadari, T.1    Warms, J.V.B.2    Rose, I.A.3    Hershko, A.4
  • 54
    • 0028823598 scopus 로고
    • Metabolism of the polyubiquitin degradation signal: Structure, mechanism, and role of isopeptidase T
    • K.D. Wilkinson, V.L. Tashayev, L.B. O'Connor, C.N. Larsen, E. Kasperek, and C.M. Pickart Metabolism of the polyubiquitin degradation signal: structure, mechanism, and role of isopeptidase T Biochemistry 34 1995 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
  • 55
    • 0028859849 scopus 로고
    • A human de-ubiquitinating enzyme with both isopeptidase and peptidase activities in vitro
    • L. Falquet, N. Paquet, S. Frutiger, G.J. Hughes, K. Hoang-Van, and J.C. Jaton A human de-ubiquitinating enzyme with both isopeptidase and peptidase activities in vitro FEBS Lett. 359 1995 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
  • 58
    • 0033786796 scopus 로고    scopus 로고
    • The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways
    • A.Y. Amerik, J. Nowak, S. Swaminathan, and M. Hochstrasser The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways Mol. Biol. Cell 11 2000 3365 3680
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3365-3680
    • Amerik, A.Y.1    Nowak, J.2    Swaminathan, S.3    Hochstrasser, M.4
  • 59
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • M. Babst, B. Wendland, E.J. Estepa, and S.D. Emr The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function EMBO J. 17 1998 2982 2993
    • (1998) EMBO J. , vol.17 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estepa, E.J.3    Emr, S.D.4
  • 60
    • 0036696804 scopus 로고    scopus 로고
    • ESCRT III: An endosome-associated heterooligomeric protein complex required for MVB sorting
    • M. Babst, D.J. Katzmann, E.J. Estepa-Sabal, T. Meerloo, and S.D. Emr ESCRT III: an endosome-associated heterooligomeric protein complex required for MVB sorting Dev. Cell 3 2002 271 282
    • (2002) Dev. Cell , vol.3 , pp. 271-282
    • Babst, M.1    Katzmann, D.J.2    Estepa-Sabal, E.J.3    Meerloo, T.4    Emr, S.D.5
  • 61
    • 0034955239 scopus 로고    scopus 로고
    • Deubiquitination step in the endocytic pathway of yeast plasma membrane proteins: Crucial role of Doa4p ubiquitin isopeptidase
    • S. Dupre, and R. Haguenauer-Tsapis Deubiquitination step in the endocytic pathway of yeast plasma membrane proteins: crucial role of Doa4p ubiquitin isopeptidase Mol. Cell. Biol. 21 2001 4482 4494
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4482-4494
    • Dupre, S.1    Haguenauer-Tsapis, R.2
  • 63
    • 0034535340 scopus 로고    scopus 로고
    • A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP
    • M. Kato, K. Miyazawa, and N. Kitamura A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP J. Biol. Chem. 275 2000 37481 37487
    • (2000) J. Biol. Chem. , vol.275 , pp. 37481-37487
    • Kato, M.1    Miyazawa, K.2    Kitamura, N.3
  • 64
    • 0036304360 scopus 로고    scopus 로고
    • The Vps27p Hse1p complex binds ubiquitin and mediates endosomal protein sorting
    • P.S. Bilodeau, J.L. Urbanowski, S.C. Winistorfer, and R.C. Piper The Vps27p Hse1p complex binds ubiquitin and mediates endosomal protein sorting Nat. Cell Biol. 4 2002 534 539
    • (2002) Nat. Cell Biol. , vol.4 , pp. 534-539
    • Bilodeau, P.S.1    Urbanowski, J.L.2    Winistorfer, S.C.3    Piper, R.C.4
  • 65
    • 0029561529 scopus 로고
    • Control of cell fate by a deubiquitinating enzyme encoded by the fat facets gene
    • Y. Huang, R.T. Baker, and J.A. Fischer-Vize Control of cell fate by a deubiquitinating enzyme encoded by the fat facets gene Science 270 1995 1828 1831
    • (1995) Science , vol.270 , pp. 1828-1831
    • Huang, Y.1    Baker, R.T.2    Fischer-Vize, J.A.3
  • 66
    • 0027087073 scopus 로고
    • The fat facets gene is required for Drosophila eye and embryo development
    • J.A. Fischer-Vize, G.M. Rubin, and R. Lehmann The fat facets gene is required for Drosophila eye and embryo development Development 116 1992 985 1000
    • (1992) Development , vol.116 , pp. 985-1000
    • Fischer-Vize, J.A.1    Rubin, G.M.2    Lehmann, R.3
  • 67
    • 0030822549 scopus 로고    scopus 로고
    • Mutagenesis screens for interacting genes reveal three roles for fat facets during Drosophila eye development
    • J.A. Fischer, S.K. Leavell, and Q. Li Mutagenesis screens for interacting genes reveal three roles for fat facets during Drosophila eye development Dev. Genet. 21 1997 167 174
    • (1997) Dev. Genet. , vol.21 , pp. 167-174
    • Fischer, J.A.1    Leavell, S.K.2    Li, Q.3
  • 68
    • 0034052305 scopus 로고    scopus 로고
    • The function of the Drosophila fat facets deubiquitinating enzyme in limiting photoreceptor cell number is intimately associated with endocytosis
    • A.L. Cadavid, A. Ginzel, and J.A. Fischer The function of the Drosophila fat facets deubiquitinating enzyme in limiting photoreceptor cell number is intimately associated with endocytosis Development 127 2000 1727 1736
    • (2000) Development , vol.127 , pp. 1727-1736
    • Cadavid, A.L.1    Ginzel, A.2    Fischer, J.A.3
  • 69
    • 0036468145 scopus 로고    scopus 로고
    • A specific protein substrate for a deubiquitinating enzyme: Liquid facets is the substrate of fat facets
    • X. Chen, B. Zhang, and J.A. Fischer A specific protein substrate for a deubiquitinating enzyme: liquid facets is the substrate of fat facets Genes Dev. 16 2002 289 294
    • (2002) Genes Dev. , vol.16 , pp. 289-294
    • Chen, X.1    Zhang, B.2    Fischer, J.A.3
  • 70
    • 0030941458 scopus 로고    scopus 로고
    • P53, the cellular gatekeeper for growth and division
    • A.J. Levine p53, the cellular gatekeeper for growth and division Cell 88 1997 323 331
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 72
  • 73
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degrdation of p53
    • Y. Haupt, R. Maya, A. Kazaz, and M. Oren Mdm2 promotes the rapid degrdation of p53 Nature 387 1997 296 299
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 74
    • 0037061508 scopus 로고    scopus 로고
    • Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
    • M. Li, D. Chen, A. Shiloh, J. Luo, A.Y. Nikolaev, J. Qin, and W. Gu Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization Nature 416 2002 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
  • 75
    • 0030895008 scopus 로고    scopus 로고
    • A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein
    • R.D. Everett, M. Meredith, A. Orr, A. Cross, M. Kathoria, and J. Parkinson A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein EMBO J. 16 1997 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
  • 77
    • 0028210480 scopus 로고
    • Position-effect variegation and the new biology of heterochromatin
    • G.H. Karpen Position-effect variegation and the new biology of heterochromatin Curr. Opin. Genet. Dev. 4 1994 281 291
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 281-291
    • Karpen, G.H.1
  • 78
    • 0023340731 scopus 로고
    • Four genes responsible for a position effect on expression from HML and HMR in Saccharomyces cerevisiae
    • J. Rine, and I. Herskowitz Four genes responsible for a position effect on expression from HML and HMR in Saccharomyces cerevisiae Genetics 116 1987 9 22
    • (1987) Genetics , vol.116 , pp. 9-22
    • Rine, J.1    Herskowitz, I.2
  • 79
    • 0024280881 scopus 로고
    • Extremely conserved histone H4 N terminus is dispensable for growth but essential for repressing the silent mating loci in yeast
    • P.S. Kayne, U.J. Kim, M. Han, J.R. Mullen, F. Yoshizaki, and M. Grunstein Extremely conserved histone H4 N terminus is dispensable for growth but essential for repressing the silent mating loci in yeast Cell 55 1988 27 39
    • (1988) Cell , vol.55 , pp. 27-39
    • Kayne, P.S.1    Kim, U.J.2    Han, M.3    Mullen, J.R.4    Yoshizaki, F.5    Grunstein, M.6
  • 80
    • 0025002966 scopus 로고
    • Genetic evidence for an interaction between SIR3 and histone H4 in the repression of the silent mating loci in Saccharomyces cerevisiae
    • L.M. Johnson, P.S. Kayne, E.S. Kahn, and M. Grunstein Genetic evidence for an interaction between SIR3 and histone H4 in the repression of the silent mating loci in Saccharomyces cerevisiae Proc. Natl. Acad. Sci. U. S. A. 87 1990 6286 6290
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 6286-6290
    • Johnson, L.M.1    Kayne, P.S.2    Kahn, E.S.3    Grunstein, M.4
  • 81
    • 0030598895 scopus 로고    scopus 로고
    • A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S. cerevisiae
    • D. Moazed, and D. Johnson A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S. cerevisiae Cell 86 1996 667 677
    • (1996) Cell , vol.86 , pp. 667-677
    • Moazed, D.1    Johnson, D.2
  • 82
    • 0029791553 scopus 로고    scopus 로고
    • The dose of a putative ubiquitin-specific protease affects position-effect variegation in Drosophila melanogaster
    • S. Henchoz, F. De Rubertis, D. Pauli, and P. Spierer The dose of a putative ubiquitin-specific protease affects position-effect variegation in Drosophila melanogaster Mol. Cell. Biol. 10 1996 5717 5725
    • (1996) Mol. Cell. Biol. , vol.10 , pp. 5717-5725
    • Henchoz, S.1    De Rubertis, F.2    Pauli, D.3    Spierer, P.4
  • 83
    • 0032849084 scopus 로고    scopus 로고
    • DOT4 links silencing and cell growth in Saccharomyces cerevisiae
    • A. Kahana, and D.E. Gottschling DOT4 links silencing and cell growth in Saccharomyces cerevisiae Mol. Cell. Biol. 19 1999 6608 6620
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6608-6620
    • Kahana, A.1    Gottschling, D.E.2
  • 84
    • 0034695456 scopus 로고    scopus 로고
    • Rad6-dependent ubiquitination of histone H2B in yeast
    • K. Robzyk, J. Recht, and M.A. Osley Rad6-dependent ubiquitination of histone H2B in yeast Science 287 2000 501 504
    • (2000) Science , vol.287 , pp. 501-504
    • Robzyk, K.1    Recht, J.2    Osley, M.A.3
  • 85
    • 0037077178 scopus 로고    scopus 로고
    • Dot1p modulates silencing in yeast by methylation of the nucleosome core
    • F. van Leeuwen, P.R. Gafken, and D.E. Gottschling Dot1p modulates silencing in yeast by methylation of the nucleosome core Cell 109 2002 745 756
    • (2002) Cell , vol.109 , pp. 745-756
    • Van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 90
    • 0037184348 scopus 로고    scopus 로고
    • NF-kB signaling. Many roads lead to Madrid
    • V. Dixit, and T.W. Mak NF-kB signaling. Many roads lead to Madrid Cell 111 2002 615 619
    • (2002) Cell , vol.111 , pp. 615-619
    • Dixit, V.1    Mak, T.W.2
  • 91
    • 0033712615 scopus 로고    scopus 로고
    • Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKg) upon receptor stimulation
    • S.Q. Zhang, A. Kovalenko, G. Cantarella, and D. Wallach Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKg) upon receptor stimulation Immunity 12 2000 301 311
    • (2000) Immunity , vol.12 , pp. 301-311
    • Zhang, S.Q.1    Kovalenko, A.2    Cantarella, G.3    Wallach, D.4
  • 92
    • 0029949257 scopus 로고    scopus 로고
    • TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex
    • H. Hsu, J. Huang, H.B. Shu, V. Baichwal, and D.V. Goeddel TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex Immunity 4 1996 387 396
    • (1996) Immunity , vol.4 , pp. 387-396
    • Hsu, H.1    Huang, J.2    Shu, H.B.3    Baichwal, V.4    Goeddel, D.V.5
  • 93
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IkB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • L. Deng, C. Wang, E. Spencer, L. Yang, A. Braun, J. You, C. Slaughter, C. Pickart, and Z.J. Chen Activation of the IkB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain Cell 103 2000 351 361
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.4    Braun, A.5    You, J.6    Slaughter, C.7    Pickart, C.8    Chen, Z.J.9
  • 94
    • 0038742813 scopus 로고    scopus 로고
    • Recruitment of TNF receptor 1 to lipid rafts is essential for TNFa-mediated NF-kB activation
    • D.F. Legler, O. Micheau, M.A. Doucey, J. Tschopp, and C. Bron Recruitment of TNF receptor 1 to lipid rafts is essential for TNFa-mediated NF-kB activation Immunity 18 2003 655 664
    • (2003) Immunity , vol.18 , pp. 655-664
    • Legler, D.F.1    Micheau, O.2    Doucey, M.A.3    Tschopp, J.4    Bron, C.5
  • 99
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NF-kB activation by TNFR family members
    • E. Trompouki, E. Hatzivassiliou, T. Tsichritzis, H. Farmer, A. Ashworth, and G. Mosialos CYLD is a deubiquitinating enzyme that negatively regulates NF-kB activation by TNFR family members Nature 424 2003 793 796
    • (2003) Nature , vol.424 , pp. 793-796
    • Trompouki, E.1    Hatzivassiliou, E.2    Tsichritzis, T.3    Farmer, H.4    Ashworth, A.5    Mosialos, G.6
  • 100
    • 0036775723 scopus 로고    scopus 로고
    • Genetics of Parkinson's disease and biochemical studies of implicated gene products
    • P.T. Lansbury Jr., and A. Brice Genetics of Parkinson's disease and biochemical studies of implicated gene products Curr. Opin. Cell Biol. 14 2002 653 660
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 653-660
    • Lansbury Jr., P.T.1    Brice, A.2
  • 101
    • 0035959931 scopus 로고    scopus 로고
    • Parkin and the molecular pathways of Parkinson's disease
    • B.I. Giasson, and V.M. Lee Parkin and the molecular pathways of Parkinson's disease Neuron 31 2001 885 888
    • (2001) Neuron , vol.31 , pp. 885-888
    • Giasson, B.I.1    Lee, V.M.2
  • 102
    • 0032502276 scopus 로고    scopus 로고
    • Substrate specificity of deubiquitinating enzymes: Ubiquitin C-terminal hydrolases
    • C.N. Larsen, B.A. Krantz, and K.D. Wilkinson Substrate specificity of deubiquitinating enzymes: ubiquitin C-terminal hydrolases Biochemistry 10 1998 3358 3368
    • (1998) Biochemistry , vol.10 , pp. 3358-3368
    • Larsen, C.N.1    Krantz, B.A.2    Wilkinson, K.D.3
  • 104
    • 0037131567 scopus 로고    scopus 로고
    • The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility
    • Y. Liu, L. Fallon, H.A. Lashuel, Z. Liu, and P.T. Lansbury Jr. The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility Cell 111 2002 209 218
    • (2002) Cell , vol.111 , pp. 209-218
    • Liu, Y.1    Fallon, L.2    Lashuel, H.A.3    Liu, Z.4    Lansbury Jr., P.T.5
  • 105
    • 0034725918 scopus 로고    scopus 로고
    • All in the ubiquitin family
    • M. Hochstrasser All in the ubiquitin family Science 289 2000 563 564
    • (2000) Science , vol.289 , pp. 563-564
    • Hochstrasser, M.1
  • 106
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • R. Mahajan, C. Delphin, T. Guan, L. Gerace, and F. Melchior A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2 Cell 88 1997 97 107
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 107
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • M.J. Matunis, E. Coutavas, and G. Blobel A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex J. Cell Biol. 135 1996 1457 1470
    • (1996) J. Cell Biol. , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 108
    • 0032498541 scopus 로고    scopus 로고
    • SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex
    • M.J. Matunis, J. Wu, and G. Blobel SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex J. Cell Biol. 140 1998 499 509
    • (1998) J. Cell Biol. , vol.140 , pp. 499-509
    • Matunis, M.J.1    Wu, J.2    Blobel, G.3
  • 110
    • 0029736651 scopus 로고    scopus 로고
    • PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia
    • M.N. Boddy, K. Howe, L.D. Etkin, E. Solomon, and P.S. Freemont PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia Oncogene 13 1996 971 982
    • (1996) Oncogene , vol.13 , pp. 971-982
    • Boddy, M.N.1    Howe, K.2    Etkin, L.D.3    Solomon, E.4    Freemont, P.S.5
  • 111
    • 0031426631 scopus 로고    scopus 로고
    • Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1
    • T. Sternsdorf, K. Jensen, and H. Will Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1 J. Cell Biol. 139 1997 1621 1634
    • (1997) J. Cell Biol. , vol.139 , pp. 1621-1634
    • Sternsdorf, T.1    Jensen, K.2    Will, H.3
  • 112
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IkBa inhibits NF-kB activation
    • J.M.P. Desterro, M.S. Rodriguez, and R.T. Hay SUMO-1 modification of IkBa inhibits NF-kB activation Mol. Cell 2 1998 233 239
    • (1998) Mol. Cell , vol.2 , pp. 233-239
    • Desterro, J.M.P.1    Rodriguez, M.S.2    Hay, R.T.3
  • 113
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • E.S. Johnson Protein modification by SUMO Annu. Rev. Biochem. 73 2004 355 382
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 114
    • 0036237383 scopus 로고    scopus 로고
    • Versatile protein tag, SUMO: Its enzymology and biological function
    • K.I. Kim, S.H. Baek, and C.H. Chung Versatile protein tag, SUMO: its enzymology and biological function J. Cell. Physiol. 191 2002 257 268
    • (2002) J. Cell. Physiol. , vol.191 , pp. 257-268
    • Kim, K.I.1    Baek, S.H.2    Chung, C.H.3
  • 115
    • 0034018312 scopus 로고    scopus 로고
    • The yeast ULP2 (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein
    • S.J. Li, and M. Hochstrasser The yeast ULP2 (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein Mol. Cell. Biol. 20 2000 2367 2377
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2367-2377
    • Li, S.J.1    Hochstrasser, M.2
  • 116
    • 0029914251 scopus 로고    scopus 로고
    • Crystal structure of the human adenovirus proteinase with its 11 amino acid cofactor
    • J. Ding, W.J. McGrath, R.M. Sweet, and W.F. Mangel Crystal structure of the human adenovirus proteinase with its 11 amino acid cofactor EMBO J. 15 1996 1778 1783
    • (1996) EMBO J. , vol.15 , pp. 1778-1783
    • Ding, J.1    McGrath, W.J.2    Sweet, R.M.3    Mangel, W.F.4
  • 118
    • 0036615561 scopus 로고    scopus 로고
    • Rub1p processing by Yuh1p is required for wild-type levels of Rub1p conjugation to Cdc53p
    • B. Linghu, J. Callis, and M.G. Goebl Rub1p processing by Yuh1p is required for wild-type levels of Rub1p conjugation to Cdc53p Euk. Cell 1 2002 491 494
    • (2002) Euk. Cell , vol.1 , pp. 491-494
    • Linghu, B.1    Callis, J.2    Goebl, M.G.3
  • 120
    • 0034640373 scopus 로고    scopus 로고
    • Identification of a novel isopeptidase with dual specificity for ubiquitin- and NEDD8-conjugated proteins
    • L. Gong, T. Kamitani, S. Millas, and E.T. Yeh Identification of a novel isopeptidase with dual specificity for ubiquitin- and NEDD8-conjugated proteins J. Biol. Chem. 275 2000 14212 14216
    • (2000) J. Biol. Chem. , vol.275 , pp. 14212-14216
    • Gong, L.1    Kamitani, T.2    Millas, S.3    Yeh, E.T.4
  • 123
    • 3142570737 scopus 로고    scopus 로고
    • Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity
    • D.P. Xirodimas, M.K. Saville, J.C. Bourdon, R.T. Hay, and D.P. Lane Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity Cell 118 2004 83 97
    • (2004) Cell , vol.118 , pp. 83-97
    • Xirodimas, D.P.1    Saville, M.K.2    Bourdon, J.C.3    Hay, R.T.4    Lane, D.P.5
  • 124
    • 0033279836 scopus 로고    scopus 로고
    • SCF and Cullin/Ring H2-based ubiquitin ligases
    • R.J. Deshaies SCF and Cullin/Ring H2-based ubiquitin ligases Annu. Rev. Cell Dev. Biol. 15 1999 435 467
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 128
    • 0032483546 scopus 로고    scopus 로고
    • A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3
    • M.H. Glickman, D.M. Rubin, O. Coux, I. Wefes, G. Pfeifer, Z. Cjeka, W. Baumeister, V.A. Fried, and D. Finley A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3 Cell 94 1998 615 623
    • (1998) Cell , vol.94 , pp. 615-623
    • Glickman, M.H.1    Rubin, D.M.2    Coux, O.3    Wefes, I.4    Pfeifer, G.5    Cjeka, Z.6    Baumeister, W.7    Fried, V.A.8    Finley, D.9
  • 131
    • 0023160888 scopus 로고
    • Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin
    • A.L. Haas, P. Ahrens, P.M. Bright, and H. Ankel Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin J. Biol. Chem. 262 1987 11315 11323
    • (1987) J. Biol. Chem. , vol.262 , pp. 11315-11323
    • Haas, A.L.1    Ahrens, P.2    Bright, P.M.3    Ankel, H.4
  • 132
    • 0026722530 scopus 로고
    • The interferon-inducible 15-kDa ubiquitin homolog conjugates to intracellular proteins
    • K.R. Loeb, and A.L. Haas The interferon-inducible 15-kDa ubiquitin homolog conjugates to intracellular proteins J. Biol. Chem. 267 1992 7806 7813
    • (1992) J. Biol. Chem. , vol.267 , pp. 7806-7813
    • Loeb, K.R.1    Haas, A.L.2
  • 135
    • 0033609852 scopus 로고    scopus 로고
    • Precursor processing of pro-ISG15/UCRP, an interferon-beta-induced ubiquitin-like protein
    • J.L. Potter, J. Narasimhan, L. Mende-Mueller, and A.L. Haas Precursor processing of pro-ISG15/UCRP, an interferon-beta-induced ubiquitin-like protein J. Biol. Chem. 274 1999 25061 25068
    • (1999) J. Biol. Chem. , vol.274 , pp. 25061-25068
    • Potter, J.L.1    Narasimhan, J.2    Mende-Mueller, L.3    Haas, A.L.4
  • 136
    • 0035286734 scopus 로고    scopus 로고
    • Molecular dissection of autophagy: Two ubiquitin-like systems
    • Y. Ohsumi Molecular dissection of autophagy: two ubiquitin-like systems Nat. Rev. Mol. Cell. Biol. 2 2001 211 216
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 211-216
    • Ohsumi, Y.1
  • 137
    • 0033616143 scopus 로고    scopus 로고
    • Deubiquitinating enzymes: Their diversity and emerging roles
    • C.H. Chung, and S.H. Baek Deubiquitinating enzymes: their diversity and emerging roles Biochem. Biophys. Res. Commun. 266 1999 633 640
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 633-640
    • Chung, C.H.1    Baek, S.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.