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Volumn 27, Issue C, 1998, Pages 71-104

Cellular Regulation by Ubiquitin-Dependent Processes

(1)  Wilkinson, Keith D a  

a NONE

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0006416590     PISSN: 15692558     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1569-2558(08)60458-0     Document Type: Article
Times cited : (4)

References (175)
  • 1
    • 0028964284 scopus 로고
    • A recognition component of the ubiquitin system is required for peptide transport in Saccharomyces cerevisiae
    • Alagramam K., Naider F., and Becker J.M. A recognition component of the ubiquitin system is required for peptide transport in Saccharomyces cerevisiae. Mol. Microbiol. 15 (1995) 225-234
    • (1995) Mol. Microbiol. , vol.15 , pp. 225-234
    • Alagramam, K.1    Naider, F.2    Becker, J.M.3
  • 2
    • 0019871886 scopus 로고
    • Protein A24 lyase activity in nucleoli of thioacetamide-treated rat liver releases histone 2A and ubiquitin from conjugated protein A24
    • Andersen M.W., Ballal N.R., Goldknopf I.L., and Busch H. Protein A24 lyase activity in nucleoli of thioacetamide-treated rat liver releases histone 2A and ubiquitin from conjugated protein A24. Biochemistry 20 (1981) 1100-1104
    • (1981) Biochemistry , vol.20 , pp. 1100-1104
    • Andersen, M.W.1    Ballal, N.R.2    Goldknopf, I.L.3    Busch, H.4
  • 3
    • 0028073188 scopus 로고
    • Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain
    • Amason T., and Ellison M.J. Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain. Mol. Cell Biol. 14 (1994) 7876-7883
    • (1994) Mol. Cell Biol. , vol.14 , pp. 7876-7883
    • Amason, T.1    Ellison, M.J.2
  • 5
    • 0030028574 scopus 로고    scopus 로고
    • Novel multiubiquitin chain linkages catalyzed by the conjugating enzymes E2EPF and RAD6 are recognized by 26 S proteasome subunit 5
    • Baboshina O.V., and Haas A.L. Novel multiubiquitin chain linkages catalyzed by the conjugating enzymes E2EPF and RAD6 are recognized by 26 S proteasome subunit 5. J. Biol. Chem. 271 (1996) 2823-2831
    • (1996) J. Biol. Chem. , vol.271 , pp. 2823-2831
    • Baboshina, O.V.1    Haas, A.L.2
  • 6
    • 0028314007 scopus 로고
    • Specific complex formation between yeast RAD6 and RAD18 proteins: a potential mechanism for targeting RAD6 ubiquitin-conjugating activity to DNA damage sites
    • Bailly V., Lamb J., Sung P., Prakash S., and Prakash L. Specific complex formation between yeast RAD6 and RAD18 proteins: a potential mechanism for targeting RAD6 ubiquitin-conjugating activity to DNA damage sites. Genes Dev. 8 (1994) 811-820
    • (1994) Genes Dev. , vol.8 , pp. 811-820
    • Bailly, V.1    Lamb, J.2    Sung, P.3    Prakash, S.4    Prakash, L.5
  • 8
    • 0030070803 scopus 로고    scopus 로고
    • Critical role for lysines 21 and 22 in signal-induced, ubiquitin-mediated proteolysis of I kappa B-alpha
    • Baldi L., Brown K., Franzoso G., and Siebenlist U. Critical role for lysines 21 and 22 in signal-induced, ubiquitin-mediated proteolysis of I kappa B-alpha. J. Biol. Chem. 271 (1996) 376-379
    • (1996) J. Biol. Chem. , vol.271 , pp. 376-379
    • Baldi, L.1    Brown, K.2    Franzoso, G.3    Siebenlist, U.4
  • 9
    • 0025261931 scopus 로고
    • A gene pair from the human major histocompatibility complex encodes large proline-rich proteins with multiple repeated motifs and a single ubiquitin-Iike domain
    • Banerji J., Sands J., Strominger J.L., and Spies T. A gene pair from the human major histocompatibility complex encodes large proline-rich proteins with multiple repeated motifs and a single ubiquitin-Iike domain. Proc. Natl. Acad. Sci. USA 87 (1990) 2374-2378
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2374-2378
    • Banerji, J.1    Sands, J.2    Strominger, J.L.3    Spies, T.4
  • 10
    • 0028986667 scopus 로고
    • Gl cyclin turnover and nutrient uptake are controlled by a common pathway in yeast
    • Barral Y., Jentsch S., and Mann C. Gl cyclin turnover and nutrient uptake are controlled by a common pathway in yeast. Genes Dev. 9 (1995) 399-409
    • (1995) Genes Dev. , vol.9 , pp. 399-409
    • Barral, Y.1    Jentsch, S.2    Mann, C.3
  • 11
    • 0025050840 scopus 로고
    • The recognition component of the N-end rule pathway
    • Bartel B., Wunning I., and Varshavsky A. The recognition component of the N-end rule pathway. EMBO J. 9 (1990) 3179-3189
    • (1990) EMBO J. , vol.9 , pp. 3179-3189
    • Bartel, B.1    Wunning, I.2    Varshavsky, A.3
  • 12
    • 0030052841 scopus 로고    scopus 로고
    • Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting
    • Beal R., Deveraux Q., Xia G., Rechsteiner M., and Pickart C. Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting. Proc. Natl. Acad. Sci. USA 93 (1996) 861-866
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 861-866
    • Beal, R.1    Deveraux, Q.2    Xia, G.3    Rechsteiner, M.4    Pickart, C.5
  • 13
    • 0029985369 scopus 로고    scopus 로고
    • Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway
    • Biederer T., Volkwein C., and Sommer T. Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway. EMBO J. 15 (1996) 2069-2076
    • (1996) EMBO J. , vol.15 , pp. 2069-2076
    • Biederer, T.1    Volkwein, C.2    Sommer, T.3
  • 14
    • 0030015075 scopus 로고    scopus 로고
    • Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center
    • Biggins S., Ivanovska I., and Rose M.D. Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center. J. Cell. Biol. 133 (1996) 1331-1346
    • (1996) J. Cell. Biol. , vol.133 , pp. 1331-1346
    • Biggins, S.1    Ivanovska, I.2    Rose, M.D.3
  • 15
    • 0026441880 scopus 로고
    • Reversible histone modifications and the chromosome cell cycle
    • Bradbury E.M. Reversible histone modifications and the chromosome cell cycle. Bioessays 14 (1992) 9-16
    • (1992) Bioessays , vol.14 , pp. 9-16
    • Bradbury, E.M.1
  • 17
    • 0021119145 scopus 로고
    • Ubiquitination of proteins
    • Busch H. Ubiquitination of proteins. Methods Enzymol. 106 (1984) 238-262
    • (1984) Methods Enzymol. , vol.106 , pp. 238-262
    • Busch, H.1
  • 19
    • 0028848152 scopus 로고
    • The carboxyl extensions of two rat ubiquitin fusion proteins are ribosomal proteins S27aand L40
    • Chan Y.L., Suzuki K., and Wool I.G. The carboxyl extensions of two rat ubiquitin fusion proteins are ribosomal proteins S27aand L40. Biochem. Biophys. Res. Commun. 215 (1995) 682-690
    • (1995) Biochem. Biophys. Res. Commun. , vol.215 , pp. 682-690
    • Chan, Y.L.1    Suzuki, K.2    Wool, I.G.3
  • 20
    • 0029099161 scopus 로고
    • The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules
    • Chen H.I., and Sudol M. The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules. Proc. Natl. Acad. Sci. USA 92 (1995) 7819-7823
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7819-7823
    • Chen, H.I.1    Sudol, M.2
  • 21
    • 0027198563 scopus 로고
    • Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor
    • Chen P., Johnson P., Sommer T., Jentsch S., and Hochstrasser M. Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor. Cell 74 (1993) 357-369
    • (1993) Cell , vol.74 , pp. 357-369
    • Chen, P.1    Johnson, P.2    Sommer, T.3    Jentsch, S.4    Hochstrasser, M.5
  • 22
    • 0025644201 scopus 로고
    • A 25-kilodalton ubiquitin carrier protein (E2) catalyzes multi-ubiquitin chain synthesis via lysine 48 of ubiquitin
    • Chen Z., and Pickart C.M. A 25-kilodalton ubiquitin carrier protein (E2) catalyzes multi-ubiquitin chain synthesis via lysine 48 of ubiquitin. J. Biol. Chem. 265 (1990) 21835-21842
    • (1990) J. Biol. Chem. , vol.265 , pp. 21835-21842
    • Chen, Z.1    Pickart, C.M.2
  • 23
    • 0029146930 scopus 로고
    • Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway
    • Chen Z., Hagler J., Palombella V.J., Melandri F., Scherer D., Ballard D., and Maniatis T. Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway. Genes Dev. 9 (1995) 1586-1597
    • (1995) Genes Dev. , vol.9 , pp. 1586-1597
    • Chen, Z.1    Hagler, J.2    Palombella, V.J.3    Melandri, F.4    Scherer, D.5    Ballard, D.6    Maniatis, T.7
  • 24
    • 0030004897 scopus 로고    scopus 로고
    • Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity
    • Chen Z.J., Parent L., and Maniatis T. Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity. Cell 84 (1996) 853-862
    • (1996) Cell , vol.84 , pp. 853-862
    • Chen, Z.J.1    Parent, L.2    Maniatis, T.3
  • 25
    • 0021269680 scopus 로고
    • The ubiquitin-mediated proteolytic pathway and mechanisms of energy-dependent intracellular protein degradation
    • Ciechanover A., Finley D., and Varshavsky A. The ubiquitin-mediated proteolytic pathway and mechanisms of energy-dependent intracellular protein degradation. J. Cell Biochem. 24 (1984) 27-53
    • (1984) J. Cell Biochem. , vol.24 , pp. 27-53
    • Ciechanover, A.1    Finley, D.2    Varshavsky, A.3
  • 27
    • 0025944083 scopus 로고
    • The ubiquitin-activating enzyme is required for lysosomal degradation of cellular proteins under stress
    • Ciechanover A., Gropper R., and Schwartz A.L. The ubiquitin-activating enzyme is required for lysosomal degradation of cellular proteins under stress. Biomed. Biochim. Acta 50 (1991) 321-332
    • (1991) Biomed. Biochim. Acta , vol.50 , pp. 321-332
    • Ciechanover, A.1    Gropper, R.2    Schwartz, A.L.3
  • 28
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway [Review]
    • Ciechanover A. The ubiquitin-proteasome proteolytic pathway [Review]. Cell 79 (1994) 13-21
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 29
    • 0028118679 scopus 로고
    • The ubiquitin-mediated proteolytic pathway: mechanisms of recognition of the proteolytic substrate and involvement in the degradation of native cellular proteins [Review]
    • Ciechanover A., and Schwartz A.L. The ubiquitin-mediated proteolytic pathway: mechanisms of recognition of the proteolytic substrate and involvement in the degradation of native cellular proteins [Review]. FASEB J. 8 (1994) 182-191
    • (1994) FASEB J. , vol.8 , pp. 182-191
    • Ciechanover, A.1    Schwartz, A.L.2
  • 30
    • 0026493758 scopus 로고
    • Isoforms of mammalian ubiquitin-activating enzyme
    • Cook J.C., and Chock P.B. Isoforms of mammalian ubiquitin-activating enzyme. J. Biol. Chem. 267 (1992) 24315-24321
    • (1992) J. Biol. Chem. , vol.267 , pp. 24315-24321
    • Cook, J.C.1    Chock, P.B.2
  • 31
    • 0028316184 scopus 로고
    • Structure of tetraubiquitin shows how multiubiquitin chains can be formed
    • Cook W.J., Jeffrey L.C., Kasperek E., and Pickart C.M. Structure of tetraubiquitin shows how multiubiquitin chains can be formed. J. Mol. Biol. 236 (1994) 601-609
    • (1994) J. Mol. Biol. , vol.236 , pp. 601-609
    • Cook, W.J.1    Jeffrey, L.C.2    Kasperek, E.3    Pickart, C.M.4
  • 32
    • 0028110821 scopus 로고
    • The Pichia pastoris PAS4 gene encodes a ubiquitin-conjugating enzyme required for peroxisome assembly
    • Crane D.I., Kalish J.E., and Gould S.J. The Pichia pastoris PAS4 gene encodes a ubiquitin-conjugating enzyme required for peroxisome assembly. J. Biol. Chem. 269 (1994) 21835-21844
    • (1994) J. Biol. Chem. , vol.269 , pp. 21835-21844
    • Crane, D.I.1    Kalish, J.E.2    Gould, S.J.3
  • 33
    • 0028087582 scopus 로고
    • PA700, an ATP-dependent activator of the 20 S proteasome, is an ATPase containing multiple members of a nucleotide-binding protein family
    • DeMartino G.N., Moomaw C.R., Zagnitko O.P., Proske R.J., Chu-Ping M., Afendis S.J., Swaffield J.C., and Slaughter C.A. PA700, an ATP-dependent activator of the 20 S proteasome, is an ATPase containing multiple members of a nucleotide-binding protein family. J. Biol. Chem. 296 (1994) 20878-20884
    • (1994) J. Biol. Chem. , vol.296 , pp. 20878-20884
    • DeMartino, G.N.1    Moomaw, C.R.2    Zagnitko, O.P.3    Proske, R.J.4    Chu-Ping, M.5    Afendis, S.J.6    Swaffield, J.C.7    Slaughter, C.A.8
  • 34
    • 0028985013 scopus 로고
    • Ubiquitination of the Gl cyclin Cln2p by a Cdc34p-dependent pathway
    • Deshaies R.J., Chau V., and Kirschner M. Ubiquitination of the Gl cyclin Cln2p by a Cdc34p-dependent pathway. EMBO J. 14 (1995) 303-312
    • (1995) EMBO J. , vol.14 , pp. 303-312
    • Deshaies, R.J.1    Chau, V.2    Kirschner, M.3
  • 35
    • 0027057882 scopus 로고
    • Selective degradation of cytosolic proteins by lysosomes
    • Dice J.F. Selective degradation of cytosolic proteins by lysosomes. Ann. N.Y. Acad. Sci. 674 (1992) 58-64
    • (1992) Ann. N.Y. Acad. Sci. , vol.674 , pp. 58-64
    • Dice, J.F.1
  • 37
    • 0028293111 scopus 로고
    • The role of the proteasome in cellular protein degradation
    • Driscoll J. The role of the proteasome in cellular protein degradation. Histol. Histopathol. 9 (1994) 197-202
    • (1994) Histol. Histopathol. , vol.9 , pp. 197-202
    • Driscoll, J.1
  • 38
    • 0030041980 scopus 로고    scopus 로고
    • The yeast multidrug transporter Pdr5 of the plasma membrane is ubiquitinated prior to endocytosis and degradation in the vacuole
    • Egner R., and Kuchler K. The yeast multidrug transporter Pdr5 of the plasma membrane is ubiquitinated prior to endocytosis and degradation in the vacuole. FEBS Lett. 378 (1996) 177-181
    • (1996) FEBS Lett. , vol.378 , pp. 177-181
    • Egner, R.1    Kuchler, K.2
  • 39
    • 0024593537 scopus 로고
    • The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis
    • Finley D., Bartel B., and Varshavsky A. The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis. Nature 338 (1989) 394-401
    • (1989) Nature , vol.338 , pp. 394-401
    • Finley, D.1    Bartel, B.2    Varshavsky, A.3
  • 40
    • 15844424064 scopus 로고    scopus 로고
    • Ubiquitination mediated by the Npilp/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease
    • Galan J.M., Moreau V., Andre B., Volland C., and Haguenauer-Tsapis R. Ubiquitination mediated by the Npilp/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease. J. Biol. Chem. 271 (1996) 10946-10952
    • (1996) J. Biol. Chem. , vol.271 , pp. 10946-10952
    • Galan, J.M.1    Moreau, V.2    Andre, B.3    Volland, C.4    Haguenauer-Tsapis, R.5
  • 41
    • 0029557613 scopus 로고
    • The epidermal growth factor receptor is covalently linked to ubiquitin
    • Galcheva-Gargova Z., Theroux S.J., and Davis R.J. The epidermal growth factor receptor is covalently linked to ubiquitin. Oncogene 11 (1995) 2649-2655
    • (1995) Oncogene , vol.11 , pp. 2649-2655
    • Galcheva-Gargova, Z.1    Theroux, S.J.2    Davis, R.J.3
  • 43
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • Glotzer M., Murray A.W., and Kirschner M.W. Cyclin is degraded by the ubiquitin pathway. Nature 349 (1991) 132-138
    • (1991) Nature , vol.349 , pp. 132-138
    • Glotzer, M.1    Murray, A.W.2    Kirschner, M.W.3
  • 44
    • 0029365999 scopus 로고
    • Cell cycle. The only way out of mitosis. [Review]
    • Glotzer M. Cell cycle. The only way out of mitosis. [Review]. Curr. Biol. 5 (1995) 970-972
    • (1995) Curr. Biol. , vol.5 , pp. 970-972
    • Glotzer, M.1
  • 45
    • 0028261956 scopus 로고
    • The Ubc3 (Cdc34) ubiquitin-conjugating enzyme is ubiquiu'nated and phosphorylated in vivo
    • Goebl M.G., Goetsch L., and Byers B. The Ubc3 (Cdc34) ubiquitin-conjugating enzyme is ubiquiu'nated and phosphorylated in vivo. Mol. Cell Biol. 14 (1994) 3022-3029
    • (1994) Mol. Cell Biol. , vol.14 , pp. 3022-3029
    • Goebl, M.G.1    Goetsch, L.2    Byers, B.3
  • 46
    • 0016017019 scopus 로고
    • Intracellular protein degradation in mammalian and bacterial cells
    • Goldberg A.L., and Dice J.F. Intracellular protein degradation in mammalian and bacterial cells. Ann. Rev. Biochem. 43 (1974) 835-869
    • (1974) Ann. Rev. Biochem. , vol.43 , pp. 835-869
    • Goldberg, A.L.1    Dice, J.F.2
  • 47
    • 0029008065 scopus 로고
    • Elevated expression of Unph, a proto-oncogene at 3p21.3, in human lung tumors
    • Gray D.A., Inazawa J., Gupta K., Wong A., Ueda R., and Takahashi T. Elevated expression of Unph, a proto-oncogene at 3p21.3, in human lung tumors. Oncogene 10 (1995) 2179-2183
    • (1995) Oncogene , vol.10 , pp. 2179-2183
    • Gray, D.A.1    Inazawa, J.2    Gupta, K.3    Wong, A.4    Ueda, R.5    Takahashi, T.6
  • 50
    • 0025060326 scopus 로고
    • Identification of a viral gene encoding a ubiquitin-like protein
    • Guarino L.A. Identification of a viral gene encoding a ubiquitin-like protein. Proc. Natl. Acad. Sci. USA 87 (1990) 409-413
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 409-413
    • Guarino, L.A.1
  • 51
    • 0028916482 scopus 로고
    • Yeast DNA repair protein RAD23 promotes complex formation between transcription factor TFIIH and DNA damage recognition factor RAD14
    • Guzder S.N., Bailly V., Sung P., Prakash L., and Prakash S. Yeast DNA repair protein RAD23 promotes complex formation between transcription factor TFIIH and DNA damage recognition factor RAD14. J. Biol. Chem. 270 (1995) 8385-8388
    • (1995) J. Biol. Chem. , vol.270 , pp. 8385-8388
    • Guzder, S.N.1    Bailly, V.2    Sung, P.3    Prakash, L.4    Prakash, S.5
  • 52
    • 0023160888 scopus 로고
    • Interferon induces a 15-kilodalton protein exhibiting marked homology to ubiquitin
    • Haas A.L., Ahrens P., Bright P.M., and Ankel H. 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
  • 53
    • 0029986285 scopus 로고    scopus 로고
    • Functional characterization of the ubiquitin variant encoded by the baculovirus Autographa californica
    • Haas A.L., Katzung D.J., Reback P.M., and Guarino L.A. Functional characterization of the ubiquitin variant encoded by the baculovirus Autographa californica. Biochemistry 35 (1996) 5385-5394
    • (1996) Biochemistry , vol.35 , pp. 5385-5394
    • Haas, A.L.1    Katzung, D.J.2    Reback, P.M.3    Guarino, L.A.4
  • 54
    • 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., and Hershko A. 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.2    Rose, I.A.3    Hershko, A.4
  • 55
    • 0026769411 scopus 로고
    • Multiple forms of ubiquitin-activating enzyme El from wheat. Identification of an essential cysteine by in vitro mutagenesis
    • Hatfield P.M., and Vierstra R.D. Multiple forms of ubiquitin-activating enzyme El from wheat. Identification of an essential cysteine by in vitro mutagenesis. J. Biol. Chem. 267 (1992) 14799-14803
    • (1992) J. Biol. Chem. , vol.267 , pp. 14799-14803
    • Hatfield, P.M.1    Vierstra, R.D.2
  • 56
    • 0027304239 scopus 로고
    • Regulatory subunits of cAMP-dependent protein kinases are degraded after conjugation to ubiquitin: a molecular mechanism underlying long-term synaptic plasticity
    • Hegde A.N., Goldberg A.L., and Schwartz J.H. Regulatory subunits of cAMP-dependent protein kinases are degraded after conjugation to ubiquitin: a molecular mechanism underlying long-term synaptic plasticity. Proc. Natl. Acad. Sci. USA 90 (1993) 7436-7440
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7436-7440
    • Hegde, A.N.1    Goldberg, A.L.2    Schwartz, J.H.3
  • 57
    • 0028971506 scopus 로고
    • NP11, an essential yeast gene involved in induced degradation of Gapl and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase
    • Hein C., Springael J.Y., Volland C., Haguenauer-Tsapis R., and Andre B. NP11, an essential yeast gene involved in induced degradation of Gapl and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase. Mol. Microbiol. 18 (1995) 77-87
    • (1995) Mol. Microbiol. , vol.18 , pp. 77-87
    • Hein, C.1    Springael, J.Y.2    Volland, C.3    Haguenauer-Tsapis, R.4    Andre, B.5
  • 58
    • 0029866606 scopus 로고    scopus 로고
    • Ubiquitinylation of transcription factors c-Jun and c-Fos using reconstituted ubiquitiny lating enzymes
    • Hermida-Matsumoto M.L., Chock P.B., Curran T., and Yang D.C. Ubiquitinylation of transcription factors c-Jun and c-Fos using reconstituted ubiquitiny lating enzymes. J. Biol. Chem. 271 (1996) 4930-4936
    • (1996) J. Biol. Chem. , vol.271 , pp. 4930-4936
    • Hermida-Matsumoto, M.L.1    Chock, P.B.2    Curran, T.3    Yang, D.C.4
  • 59
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko A., and Ciechanover A. The ubiquitin system for protein degradation. Ann. Rev. Biochem. 61 (1992) 761-807
    • (1992) Ann. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 60
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • Hicke L., and Riezman H. Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 84 (1996) 277-287
    • (1996) Cell , vol.84 , pp. 277-287
    • Hicke, L.1    Riezman, H.2
  • 61
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitiri-proteasome pathway
    • Hiller M.M., Finger A., Schweiger M., and Wolf D.H. ER degradation of a misfolded luminal protein by the cytosolic ubiquitiri-proteasome pathway. Science 273 (1996) 1725-1728
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 62
  • 63
    • 0028935165 scopus 로고
    • Ubiquitin, proteasomes, and the regulation of intracellular protein degradation
    • Hochstrasser M. Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr. Opin. Cell Biol. 7 (1995) 215-223
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 215-223
    • Hochstrasser, M.1
  • 64
    • 85047669941 scopus 로고    scopus 로고
    • The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway
    • Hofmann K., and Bucher P. The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway. Trends Biochem. Sci. 21 (1996) 172-173
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 172-173
    • Hofmann, K.1    Bucher, P.2
  • 65
    • 0028969392 scopus 로고
    • Sister chromatid separation in vivo and in vitro [Review]
    • Holloway S.L. Sister chromatid separation in vivo and in vitro [Review]. Curr. Opin. Genet. Dev. 5 (1995) 243-248
    • (1995) Curr. Opin. Genet. Dev. , vol.5 , pp. 243-248
    • Holloway, S.L.1
  • 66
    • 0029000098 scopus 로고
    • Analysis of a 42.5 kb DNA sequence of chromosome X reveals three tRNA genes and 14 new open reading frames including a gene most probably belonging to the family of ubiquitin-protein ligases
    • Huang M.E., Chuat J.C., and Galibert F. Analysis of a 42.5 kb DNA sequence of chromosome X reveals three tRNA genes and 14 new open reading frames including a gene most probably belonging to the family of ubiquitin-protein ligases. Yeast 11 (1995) 775-781
    • (1995) Yeast , vol.11 , pp. 775-781
    • Huang, M.E.1    Chuat, J.C.2    Galibert, F.3
  • 67
    • 0025932933 scopus 로고
    • A cellular protein mediates association of p53 with the E6 oncoprotein of human papillomavirus types 16 or 18
    • Huibregtse J.M., Scheffner M., and Howley P.M. A cellular protein mediates association of p53 with the E6 oncoprotein of human papillomavirus types 16 or 18. EMBO J. 10 (1991) 4129-4135
    • (1991) EMBO J. , vol.10 , pp. 4129-4135
    • Huibregtse, J.M.1    Scheffner, M.2    Howley, P.M.3
  • 68
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen T.J., Loo M.A., Pind S., Williams D.B., Goldberg A.L., and Riordan J.R. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83 (1995) 129-135
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Pind, S.3    Williams, D.B.4    Goldberg, A.L.5    Riordan, J.R.6
  • 69
    • 0023236126 scopus 로고
    • The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme
    • Jentsch S., McGrath J.P., and Varshavsky A. The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme. Nature 329 (1987) 131-134
    • (1987) Nature , vol.329 , pp. 131-134
    • Jentsch, S.1    McGrath, J.P.2    Varshavsky, A.3
  • 70
    • 0027053491 scopus 로고
    • The ubiquitin-conjugation system
    • Jentsch S. The ubiquitin-conjugation system. Annu. Rev. Genet. 26 (1992) 179-207
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 179-207
    • Jentsch, S.1
  • 71
    • 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., and Hill C.P. Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A 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
  • 72
    • 0029004815 scopus 로고
    • A 20S complex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation of ubiquitin to cyclinB
    • King R.W., Peters J.M., Tugcndreich S., Rolfe M., Hieter P., and Kirschner M.W. A 20S complex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation of ubiquitin to cyclinB. Cell 81 (1995) 279-288
    • (1995) Cell , vol.81 , pp. 279-288
    • King, R.W.1    Peters, J.M.2    Tugcndreich, S.3    Rolfe, M.4    Hieter, P.5    Kirschner, M.W.6
  • 73
    • 0029937513 scopus 로고    scopus 로고
    • The 'destruction box' of cyclin A allows B-type cyclins to be ubiquinated, but not efficiently destroyed
    • Klotzbucher A., Stewart E., Harrison D., and Hunt T. The 'destruction box' of cyclin A allows B-type cyclins to be ubiquinated, but not efficiently destroyed. EMBO J. 15 (1996) 3053-3064
    • (1996) EMBO J. , vol.15 , pp. 3053-3064
    • Klotzbucher, A.1    Stewart, E.2    Harrison, D.3    Hunt, T.4
  • 74
    • 0028277963 scopus 로고
    • The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants
    • Rolling R., and Hollenberg C.P. The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants. EMBO J. 13 (1994) 3261-3271
    • (1994) EMBO J. , vol.13 , pp. 3261-3271
    • Rolling, R.1    Hollenberg, C.P.2
  • 75
    • 0028607143 scopus 로고
    • Regulated degradation of the transcription factor Gcn4
    • Kornitzer D., Raboy B., Kulka R.G., and Fink G.R. Regulated degradation of the transcription factor Gcn4. EMBO J. 13 (1994) 6021-6030
    • (1994) EMBO J. , vol.13 , pp. 6021-6030
    • Kornitzer, D.1    Raboy, B.2    Kulka, R.G.3    Fink, G.R.4
  • 76
    • 0029982968 scopus 로고    scopus 로고
    • Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes
    • Kovalenko O., Plug A.W., Haaf T., Gonda D.K., Ashley T., Ward D.C., Radding C.M., and Golub E.I. Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes. Proc. Natl. Acad. Sci. USA 93 (1996) 2958-2963
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2958-2963
    • Kovalenko, O.1    Plug, A.W.2    Haaf, T.3    Gonda, D.K.4    Ashley, T.5    Ward, D.C.6    Radding, C.M.7    Golub, E.I.8
  • 77
    • 0027165193 scopus 로고
    • Cloning of a cDNA which encodes a novel ubiquitin-like protein
    • Kumar S., Yoshida Y., and Noda M. Cloning of a cDNA which encodes a novel ubiquitin-like protein. Biochem. Biophys. Res. Commun. 195 (1993) 393-399
    • (1993) Biochem. Biophys. Res. Commun. , vol.195 , pp. 393-399
    • Kumar, S.1    Yoshida, Y.2    Noda, M.3
  • 78
    • 0029112238 scopus 로고
    • Viability of wild type p53-containing and p53-deficient tumor cells following anticancer treatment: the use of human papillomavirus E6 to target p53
    • Labrecque S., and Matlashewski G.J. Viability of wild type p53-containing and p53-deficient tumor cells following anticancer treatment: the use of human papillomavirus E6 to target p53. Oncogene 11 (1995) 387-392
    • (1995) Oncogene , vol.11 , pp. 387-392
    • Labrecque, S.1    Matlashewski, G.J.2
  • 79
    • 0028817813 scopus 로고
    • The gap junction protein connexin43 is degraded via the ubiquitin proteasome pathway
    • Laing J.G., and Beyer E.C. The gap junction protein connexin43 is degraded via the ubiquitin proteasome pathway. J. Biol. Chem. 270 (1995) 26399-26403
    • (1995) J. Biol. Chem. , vol.270 , pp. 26399-26403
    • Laing, J.G.1    Beyer, E.C.2
  • 80
    • 0031038169 scopus 로고    scopus 로고
    • Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
    • Lam Y.A., Xu W., DeMartino G.N., and Cohen R.E. 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
  • 81
    • 0032502276 scopus 로고    scopus 로고
    • Substrate Specificity of Deubiquitinating Enzymes: Ubiquitin C-terminal Hydrolases
    • In press
    • Larsen, C.N., Krantz, B.A., & Wilkinson, K.D. (1998). Substrate Specificity of Deubiquitinating Enzymes: Ubiquitin C-terminal Hydrolases. Biochemistry (In press).
    • (1998) Biochemistry
    • Larsen, C.N.1    Krantz, B.A.2    Wilkinson, K.D.3
  • 82
    • 0028199891 scopus 로고
    • Inhibition of p53 DNA binding by human papillomavirus E6 proteins
    • Lechner M.S., and Laimins L.A. Inhibition of p53 DNA binding by human papillomavirus E6 proteins. J. Virol. 68 (1994) 4262-4273
    • (1994) J. Virol. , vol.68 , pp. 4262-4273
    • Lechner, M.S.1    Laimins, L.A.2
  • 83
    • 0030894069 scopus 로고    scopus 로고
    • Bryostatin 1 and phorbol ester downmodulate protein kinase C-α and -ε via the ubiquitin/proteasome pathway in human fibroblasts
    • Lee H.W., Smith L., Pettit G.R., and Smith J.B. Bryostatin 1 and phorbol ester downmodulate protein kinase C-α and -ε via the ubiquitin/proteasome pathway in human fibroblasts. Mol. Pharm. 51 (1997) 439-447
    • (1997) Mol. Pharm. , vol.51 , pp. 439-447
    • Lee, H.W.1    Smith, L.2    Pettit, G.R.3    Smith, J.B.4
  • 84
    • 0029812896 scopus 로고    scopus 로고
    • Ubiquitination of protein kinase C-a and degradation by the proteasome
    • Lee H.W., Smith L., Petit G.R., Vinitsky A., and Smith J.B. Ubiquitination of protein kinase C-a and degradation by the proteasome. J. Biol. Chem. 271 (1996) 20973-20976
    • (1996) J. Biol. Chem. , vol.271 , pp. 20973-20976
    • Lee, H.W.1    Smith, L.2    Petit, G.R.3    Vinitsky, A.4    Smith, J.B.5
  • 85
    • 0029917002 scopus 로고    scopus 로고
    • Processing and delivery of peptides presented by MHC class I molecules
    • Lehner P.J., and Cresswell P. Processing and delivery of peptides presented by MHC class I molecules. Curr. Opin. Immunol. 8 (1996) 59-67
    • (1996) Curr. Opin. Immunol. , vol.8 , pp. 59-67
    • Lehner, P.J.1    Cresswell, P.2
  • 86
    • 0027310692 scopus 로고
    • Two related localized mRNAs from Xenopus laevis encode ubiquitin-like fusion proteins
    • Linnen J.M., Bailey C.P., and Weeks D.L. Two related localized mRNAs from Xenopus laevis encode ubiquitin-like fusion proteins. Gene 128 (1993) 181-188
    • (1993) Gene , vol.128 , pp. 181-188
    • Linnen, J.M.1    Bailey, C.P.2    Weeks, D.L.3
  • 87
    • 0028109693 scopus 로고
    • Conjugates of ubiquitin cross-reactive protein distribute in a cytoskeletal pattern
    • Loeb K.R., and Haas A.L. Conjugates of ubiquitin cross-reactive protein distribute in a cytoskeletal pattern. Mol. Cell Biol. 14 (1994) 8408-8419
    • (1994) Mol. Cell Biol. , vol.14 , pp. 8408-8419
    • Loeb, K.R.1    Haas, A.L.2
  • 88
    • 0025203978 scopus 로고
    • Purification and partial amino acid sequence analysis of two distinct tumor necrosis factor receptors from HL60 cells
    • Loetscher H., Schlaeger E.J., Lahm H.W., Pan Y.C., Lesslauer W., and Brockhaus M. Purification and partial amino acid sequence analysis of two distinct tumor necrosis factor receptors from HL60 cells. J. Biol. Chem. 265 (1990) 20131-20138
    • (1990) J. Biol. Chem. , vol.265 , pp. 20131-20138
    • Loetscher, H.1    Schlaeger, E.J.2    Lahm, H.W.3    Pan, Y.C.4    Lesslauer, W.5    Brockhaus, M.6
  • 89
    • 0029000789 scopus 로고
    • Related organelles of the endosome-lysosome system contain a different repertoire of ubiquitinated proteins in Sf9 insect cells
    • Low P., Doherty F.J., Fellinger E., Sass M., Mayer R.J., and Laszlo L. Related organelles of the endosome-lysosome system contain a different repertoire of ubiquitinated proteins in Sf9 insect cells. FEBS Lett. 368 (1995) 125-131
    • (1995) FEBS Lett. , vol.368 , pp. 125-131
    • Low, P.1    Doherty, F.J.2    Fellinger, E.3    Sass, M.4    Mayer, R.J.5    Laszlo, L.6
  • 90
    • 0028783565 scopus 로고
    • Immunohistochemical localization of ubiquitin cross-reactive protein in human tissues
    • Lowe J., McDermott H., Loeb K., Landon M., Haas A.L., and Mayer R.J. Immunohistochemical localization of ubiquitin cross-reactive protein in human tissues. J. Pathol. 177 (1995) 163-169
    • (1995) J. Pathol. , vol.177 , pp. 163-169
    • Lowe, J.1    McDermott, H.2    Loeb, K.3    Landon, M.4    Haas, A.L.5    Mayer, R.J.6
  • 91
    • 0028169361 scopus 로고
    • Degradation of G alpha by the N-end rule pathway
    • Madura K., and Varshavsky A. Degradation of G alpha by the N-end rule pathway. Science 265 (1994) 1454-1458
    • (1994) Science , vol.265 , pp. 1454-1458
    • Madura, K.1    Varshavsky, A.2
  • 92
    • 0025718671 scopus 로고
    • Evidence for a paniculate location of ubiquitin conjugates and ubiquitin-conjugating enzymes in rabbit brain
    • Magnani M., Serafini G., Antonelli A., Malatesta M., and Gazzanelli G. Evidence for a paniculate location of ubiquitin conjugates and ubiquitin-conjugating enzymes in rabbit brain. J. Biol. Chem. 266 (1991) 21018-21024
    • (1991) J. Biol. Chem. , vol.266 , pp. 21018-21024
    • Magnani, M.1    Serafini, G.2    Antonelli, A.3    Malatesta, M.4    Gazzanelli, G.5
  • 93
    • 0028289659 scopus 로고
    • The soluble but not mitochondrially bound hexokinase is a substrate for the ATP- and ubiquitin-dependcnt proteolytic system
    • Magnani M., Crinelli R., Antonelli A., Casabianca A., and Serafini G. The soluble but not mitochondrially bound hexokinase is a substrate for the ATP- and ubiquitin-dependcnt proteolytic system. Biochim. Biophys. Acta 1206 (1994) 180-190
    • (1994) Biochim. Biophys. Acta , vol.1206 , pp. 180-190
    • Magnani, M.1    Crinelli, R.2    Antonelli, A.3    Casabianca, A.4    Serafini, G.5
  • 94
    • 0028269240 scopus 로고
    • Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23
    • Masutani C., Sugasawa K., Yanagisawa J., Sonoyama T., Ui M., Enomoto T., Takio K., Tanaka K., van der Spek P.J., and Bootsma D. Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23. EMBO J. 13 (1994) 1831-1843
    • (1994) EMBO J. , vol.13 , pp. 1831-1843
    • Masutani, C.1    Sugasawa, K.2    Yanagisawa, J.3    Sonoyama, T.4    Ui, M.5    Enomoto, T.6    Takio, K.7    Tanaka, K.8    van der Spek, P.J.9    Bootsma, D.10
  • 96
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-Iike modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis M.J., Coutavas E., and Blobel G. A novel ubiquitin-Iike 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
  • 97
    • 0024500866 scopus 로고
    • Detection, resolution, and nomenclature of multiple ubiquitin carboxyl-terminal esterases from bovine calf thymus
    • Mayer A.N., and Wilkinson K.D. 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
  • 98
    • 0029837381 scopus 로고    scopus 로고
    • Degradation of 3-hydroxy-3-methylglutaryl-CoA reductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis
    • McGee T.P., Cheng H.H., Kumagai H., Omura S., and Simoni R.D. Degradation of 3-hydroxy-3-methylglutaryl-CoA reductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis. J. Biol. Chem. 271 (1996) 25630-25638
    • (1996) J. Biol. Chem. , vol.271 , pp. 25630-25638
    • McGee, T.P.1    Cheng, H.H.2    Kumagai, H.3    Omura, S.4    Simoni, R.D.5
  • 99
    • 0028885860 scopus 로고
    • Coupling of the proto-oncogene product c-Cbl to the epidermal growth factor receptor
    • Meisner H., and Czech M.P. Coupling of the proto-oncogene product c-Cbl to the epidermal growth factor receptor. J. Biol. Chem. 270 (1995) 25332-25335
    • (1995) J. Biol. Chem. , vol.270 , pp. 25332-25335
    • Meisner, H.1    Czech, M.P.2
  • 100
    • 0022839236 scopus 로고
    • Antibodies directed against ubiquitin inhibit high affinity [3H]choline uptake in rat cerebral cortical synaptosomes
    • Meyer E.M., West C.M., and Chau V. Antibodies directed against ubiquitin inhibit high affinity [3H]choline uptake in rat cerebral cortical synaptosomes. J. Biol. Chem. 261 (1986) 14365-14368
    • (1986) J. Biol. Chem. , vol.261 , pp. 14365-14368
    • Meyer, E.M.1    West, C.M.2    Chau, V.3
  • 101
    • 0023617641 scopus 로고
    • Ubiquitin-directed antibodies inhibit neuronal transporters in rat brain synaptosomes
    • Meyer E.M., West C.M., Stevens B.R., Chau V., Nguyen M.T., and Judkins J.H. Ubiquitin-directed antibodies inhibit neuronal transporters in rat brain synaptosomes. J. Neurochem. 49 (1987) 1815-1819
    • (1987) J. Neurochem. , vol.49 , pp. 1815-1819
    • Meyer, E.M.1    West, C.M.2    Stevens, B.R.3    Chau, V.4    Nguyen, M.T.5    Judkins, J.H.6
  • 102
    • 0027263157 scopus 로고
    • A role for the ubiquitin-dependent proteolytic pathway in MHC class I-restricted antigen presentation
    • Michalek M.T., Grant E.P., Gramm C., Goldberg A.L., and Rock K.L. A role for the ubiquitin-dependent proteolytic pathway in MHC class I-restricted antigen presentation. Nature 363 (1993) 552-554
    • (1993) Nature , vol.363 , pp. 552-554
    • Michalek, M.T.1    Grant, E.P.2    Gramm, C.3    Goldberg, A.L.4    Rock, K.L.5
  • 103
    • 0027219757 scopus 로고
    • Ubi cDNA encodes a ubiquitin-like-S30 fusion protein and is expressed as an antisense sequence in the Finkel-Biskis-Reilly murine sarcoma virus
    • Michiels L., Van der Rauwelaert E., Van Hasselt F., Kas K., and Merregaert J. Ubi cDNA encodes a ubiquitin-like-S30 fusion protein and is expressed as an antisense sequence in the Finkel-Biskis-Reilly murine sarcoma virus. Oncogene 8 (1993) 2537-2546
    • (1993) Oncogene , vol.8 , pp. 2537-2546
    • Michiels, L.1    Van der Rauwelaert, E.2    Van Hasselt, F.3    Kas, K.4    Merregaert, J.5
  • 104
    • 0024308204 scopus 로고
    • Cloning and Expression of a Yeast Ubiquitin-protein Cleaving Activity in Escherichia coli
    • Miller H.I., Henzel W.J., Ridgeway J.B., Kuang W., Chisholm V., and Liu C. Cloning and Expression of a Yeast Ubiquitin-protein Cleaving Activity in Escherichia coli. Biotechnology 7 (1989) 698-704
    • (1989) Biotechnology , vol.7 , pp. 698-704
    • Miller, H.I.1    Henzel, W.J.2    Ridgeway, J.B.3    Kuang, W.4    Chisholm, V.5    Liu, C.6
  • 105
    • 0028158499 scopus 로고
    • Ligand-dependent polyubiquitination of c-kit gene product: a possible mechanism of receptor down modulation in M07e cells
    • Miyazawa K., Toyama K., Gotoh A., Hendrie P.C., Mantel C., and Broxmeyer H.E. Ligand-dependent polyubiquitination of c-kit gene product: a possible mechanism of receptor down modulation in M07e cells. Blood 83 (1994) 137-145
    • (1994) Blood , vol.83 , pp. 137-145
    • Miyazawa, K.1    Toyama, K.2    Gotoh, A.3    Hendrie, P.C.4    Mantel, C.5    Broxmeyer, H.E.6
  • 106
    • 0029036680 scopus 로고
    • p53 in complex with DNA is resistant to ubiquitin-dependent proteolysis in the presence of HPV-16 E6
    • Molinari M., and Milner J. p53 in complex with DNA is resistant to ubiquitin-dependent proteolysis in the presence of HPV-16 E6. Oncogene 10 (1995) 1849-1854
    • (1995) Oncogene , vol.10 , pp. 1849-1854
    • Molinari, M.1    Milner, J.2
  • 108
    • 0028932603 scopus 로고
    • Cell cycle regulation in response to DNA damage in mammalian cells: a historical perspective [Review]
    • Murnane J.P. Cell cycle regulation in response to DNA damage in mammalian cells: a historical perspective [Review]. Cancer Metastasis Rev. 14 (1995) 17-29
    • (1995) Cancer Metastasis Rev. , vol.14 , pp. 17-29
    • Murnane, J.P.1
  • 109
    • 0029051233 scopus 로고
    • Cyclin ubiquitination: the destructive end of mitosis [Review]
    • Murray A. Cyclin ubiquitination: the destructive end of mitosis [Review]. Cell 81 (1995) 149-152
    • (1995) Cell , vol.81 , pp. 149-152
    • Murray, A.1
  • 110
    • 0028967413 scopus 로고
    • Molecular cloning and characterization of a cDNA encoding monoclonal nonspecific suppressor factor
    • Nakamura M., Xavier R.M., Tsunematsu T., and Tanigawa Y. Molecular cloning and characterization of a cDNA encoding monoclonal nonspecific suppressor factor. Proc. Natl. Acad. Sci. USA 92 (1995) 3463-3567
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3463-3567
    • Nakamura, M.1    Xavier, R.M.2    Tsunematsu, T.3    Tanigawa, Y.4
  • 111
    • 0030583866 scopus 로고    scopus 로고
    • Ubiquitin-like moiety of the monoclonal nonspecific suppressor factor beta is responsible for its activity
    • Nakamura M., Xavier R.M., and Tanigawa Y. Ubiquitin-like moiety of the monoclonal nonspecific suppressor factor beta is responsible for its activity. J. Immunol. 156 (1996) 532-538
    • (1996) J. Immunol. , vol.156 , pp. 532-538
    • Nakamura, M.1    Xavier, R.M.2    Tanigawa, Y.3
  • 112
    • 0030042942 scopus 로고    scopus 로고
    • Conjugation of the 15-kDa interferon-induced ubiquitin homolog is distinct from that of ubiquitin
    • Narasimhan J., Potter J.L., and Haas A.L. Conjugation of the 15-kDa interferon-induced ubiquitin homolog is distinct from that of ubiquitin. J. Biol. Chem. 271 (1996) 324-330
    • (1996) J. Biol. Chem. , vol.271 , pp. 324-330
    • Narasimhan, J.1    Potter, J.L.2    Haas, A.L.3
  • 113
    • 0030006130 scopus 로고    scopus 로고
    • Publ acts as an E6-AP-like protein ubiquitin ligase in the degradation of the cdc 25
    • Nefsky B., and Beach D. Publ acts as an E6-AP-like protein ubiquitin ligase in the degradation of the cdc 25. EMBOJ. 15 (1996) 1301-1312
    • (1996) EMBOJ. , vol.15 , pp. 1301-1312
    • Nefsky, B.1    Beach, D.2
  • 114
    • 0029100143 scopus 로고
    • Ubiquitination of the rat uterine estrogen receptor: dependence on estradiol
    • Nirmala P.B., and Thampan R.V. Ubiquitination of the rat uterine estrogen receptor: dependence on estradiol. Biochem. Biophys. Res. Commun. 213 (1995) 24-31
    • (1995) Biochem. Biophys. Res. Commun. , vol.213 , pp. 24-31
    • Nirmala, P.B.1    Thampan, R.V.2
  • 115
    • 0027305778 scopus 로고
    • The carboxyl extension- of a ubiquitin-like protein is rat ribosomal protein S30
    • Olvera J., and Wool I.G. The carboxyl extension- of a ubiquitin-like protein is rat ribosomal protein S30. J. Biol. Chem. 268 (1993) 17967-17974
    • (1993) J. Biol. Chem. , vol.268 , pp. 17967-17974
    • Olvera, J.1    Wool, I.G.2
  • 116
    • 0023336183 scopus 로고
    • The yeast ubiquitin genes: a family of natural gene fusions
    • Ozkaynak E., Finley D., Solomon M.J., and Varshavsky A. The yeast ubiquitin genes: a family of natural gene fusions. EMBO J. 6 (1987) 1429-1439
    • (1987) EMBO J. , vol.6 , pp. 1429-1439
    • Ozkaynak, E.1    Finley, D.2    Solomon, M.J.3    Varshavsky, A.4
  • 117
    • 0029024015 scopus 로고
    • Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27 [see comments]
    • Pagano M., Tarn S.W., Theodoras A.M., Beer-Romero P., Del Sal G., Chau V., Yew P.R., Draetta G.F., and Rolfe M. Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27 [see comments]. Science 269 (1995) 682-685
    • (1995) Science , vol.269 , pp. 682-685
    • Pagano, M.1    Tarn, S.W.2    Theodoras, A.M.3    Beer-Romero, P.4    Del Sal, G.5    Chau, V.6    Yew, P.R.7    Draetta, G.F.8    Rolfe, M.9
  • 118
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B
    • Palombella V.J., Rando O.J., Goldberg A.L., and Maniatis T. The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell 78 (1994) 773-785
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 119
    • 0029671073 scopus 로고    scopus 로고
    • p120cbl is a major substrate of tyrosine phosphorylation upon B cell antigen receptor stimulation and interacts in vivo with Fyn and Syk tyrosine kinases, Grb2 and She adaptors, and the p85 subunit of phosphatidylinositol 3-kinase
    • Panchamoorthy G., Fukazawa T., Miyake S., Soltoff S., Reedquist K., Druker B., Shoelson S., Cantley L., and Band H. p120cbl is a major substrate of tyrosine phosphorylation upon B cell antigen receptor stimulation and interacts in vivo with Fyn and Syk tyrosine kinases, Grb2 and She adaptors, and the p85 subunit of phosphatidylinositol 3-kinase. J. Biol. Chem. 271 (1996) 3187-3194
    • (1996) J. Biol. Chem. , vol.271 , pp. 3187-3194
    • Panchamoorthy, G.1    Fukazawa, T.2    Miyake, S.3    Soltoff, S.4    Reedquist, K.5    Druker, B.6    Shoelson, S.7    Cantley, L.8    Band, H.9
  • 120
    • 0027458572 scopus 로고
    • Cell surface control of the multiubiquitination and deubiquitination of high-affinity immunoglobulin E receptors
    • Paolini R., and Kinet J.P. Cell surface control of the multiubiquitination and deubiquitination of high-affinity immunoglobulin E receptors. EMBO J. 12 (1993) 779-786
    • (1993) EMBO J. , vol.12 , pp. 779-786
    • Paolini, R.1    Kinet, J.P.2
  • 121
    • 0027427249 scopus 로고
    • The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene
    • Papa F.R., and Hochstrasser M. 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.R.1    Hochstrasser, M.2
  • 122
    • 0027176974 scopus 로고
    • Demonstration of a ubiquitin binding site on murine haemopoietic progenitor cells: implication of ubiquitin in homing and adhesion
    • Parakh K.A., and Kannan K. Demonstration of a ubiquitin binding site on murine haemopoietic progenitor cells: implication of ubiquitin in homing and adhesion. Br. J. Haematol. 84 (1993) 212-218
    • (1993) Br. J. Haematol. , vol.84 , pp. 212-218
    • Parakh, K.A.1    Kannan, K.2
  • 123
    • 0029788023 scopus 로고    scopus 로고
    • Degradation of a mutant secretory protein, alphal-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity
    • Qu D., Teckman J.H., Omura S., and Perlmutter D.H. Degradation of a mutant secretory protein, alphal-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity. J. Biol. Chem. 271 (1996) 22791-22795
    • (1996) J. Biol. Chem. , vol.271 , pp. 22791-22795
    • Qu, D.1    Teckman, J.H.2    Omura, S.3    Perlmutter, D.H.4
  • 124
    • 0029923685 scopus 로고    scopus 로고
    • The viral ubiquitin gene of Autographa californica nuclear polyhedrosis virus is not essential for viral replication
    • Reilly L.M., and Guarino L.A. The viral ubiquitin gene of Autographa californica nuclear polyhedrosis virus is not essential for viral replication. Virology 218 (1996) 243-247
    • (1996) Virology , vol.218 , pp. 243-247
    • Reilly, L.M.1    Guarino, L.A.2
  • 125
    • 0026651895 scopus 로고
    • Electron microscopic localization of the multicatalytic proteinase complex in rat liver and in cultured cells
    • Rivett A.J., Palmer A., and Knecht E. Electron microscopic localization of the multicatalytic proteinase complex in rat liver and in cultured cells. J. Histochem. Cytochem. 40 (1992) 1165-1172
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 1165-1172
    • Rivett, A.J.1    Palmer, A.2    Knecht, E.3
  • 126
    • 0027516156 scopus 로고
    • Proteasomes: Multicatalytic proteinase complexes
    • Rivett A.J. Proteasomes: Multicatalytic proteinase complexes. Biochem. J. 291 (1993) 1-10
    • (1993) Biochem. J. , vol.291 , pp. 1-10
    • Rivett, A.J.1
  • 127
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block degradation of most cell proteins and the generation of peptides presented on MHC Class I molecules
    • Rock K.L., Gramm C., Rothstein L., Clark K., Stein R., Dick L., Hwang D., and Goldberg A.L. Inhibitors of the proteasome block degradation of most cell proteins and the generation of peptides presented on MHC Class I molecules. Cell 78 (1994) 761-771
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 128
    • 0029353809 scopus 로고
    • Proteolysis. The proteasome: a protein-degrading organelle? [Review]
    • Rubin D.M., and Finley D. Proteolysis. The proteasome: a protein-degrading organelle? [Review]. Curr. Biol. 5 (1995) 854-858
    • (1995) Curr. Biol. , vol.5 , pp. 854-858
    • Rubin, D.M.1    Finley, D.2
  • 129
    • 0025639158 scopus 로고
    • The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53
    • Scheffner M., Wemess B.A., Huibregtse J.M., and Levine A.J. The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53. Cell 63 (1990) 1129-1136
    • (1990) Cell , vol.63 , pp. 1129-1136
    • Scheffner, M.1    Wemess, B.A.2    Huibregtse, J.M.3    Levine, A.J.4
  • 130
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner M., Huibregtse J.M., Vierstra R.D., and Howley P.M. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75 (1993) 495-505
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 131
    • 0028607435 scopus 로고
    • Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53
    • Scheffner M., Huibregtse J.M., and Howley P.M. Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53. Proc. Natl. Acad. Sci. USA 91 (1994) 8797-8801
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8797-8801
    • Scheffner, M.1    Huibregtse, J.M.2    Howley, P.M.3
  • 133
    • 0026535391 scopus 로고
    • Stress-induced alterations in autophagic pathway: relationship to ubiquitin system
    • Schwartz A.L., Brandt R.A., Geuze H., and Ciechanover A. Stress-induced alterations in autophagic pathway: relationship to ubiquitin system. Am. J. Physiol. 262 (1992) C1031-C1038
    • (1992) Am. J. Physiol. , vol.262
    • Schwartz, A.L.1    Brandt, R.A.2    Geuze, H.3    Ciechanover, A.4
  • 134
    • 0029008487 scopus 로고
    • Herbimycin A induces the 20 S proteasome- and ubiquitin-dependent degradation of receptor tyrosine kinases
    • Sepp-Lorenzino L., Ma Z., Lebwohl D.E., Vinitsky A., and Rosen N. Herbimycin A induces the 20 S proteasome- and ubiquitin-dependent degradation of receptor tyrosine kinases. J. Biol. Chem. 270 (1995) 16580-16587
    • (1995) J. Biol. Chem. , vol.270 , pp. 16580-16587
    • Sepp-Lorenzino, L.1    Ma, Z.2    Lebwohl, D.E.3    Vinitsky, A.4    Rosen, N.5
  • 135
    • 0026505189 scopus 로고
    • Immunocytochemical localization of ubiquitin at human neuromuscular junctions
    • Serdaroglu P., Askanas V., and Engel W.K. Immunocytochemical localization of ubiquitin at human neuromuscular junctions. Neuropathol. Appl. Neurobiol. 18 (1992) 232-236
    • (1992) Neuropathol. Appl. Neurobiol. , vol.18 , pp. 232-236
    • Serdaroglu, P.1    Askanas, V.2    Engel, W.K.3
  • 136
    • 0030249870 scopus 로고    scopus 로고
    • UBL1, ahuman ubiquitinlike protein associating with human RAD51/RAD52 proteins
    • Shen Z., Pardington-Purtymun P.E., Comeaux J.C., Moyzis R.K., and Chen D.J. UBL1, ahuman ubiquitinlike protein associating with human RAD51/RAD52 proteins. Genomics 36 (1996) 271-279
    • (1996) Genomics , vol.36 , pp. 271-279
    • Shen, Z.1    Pardington-Purtymun, P.E.2    Comeaux, J.C.3    Moyzis, R.K.4    Chen, D.J.5
  • 137
    • 0022644026 scopus 로고
    • Cell surface molecule associated with lymphocyte homing is a ubiquitinated branched-chain glycoprotein
    • Siegelman M., Bond M.W., Gallatin W.M., St. John T., Smith H.T., Fried V.A., and Weissman I.L. Cell surface molecule associated with lymphocyte homing is a ubiquitinated branched-chain glycoprotein. Science 231 (1986) 823-829
    • (1986) Science , vol.231 , pp. 823-829
    • Siegelman, M.1    Bond, M.W.2    Gallatin, W.M.3    St. John, T.4    Smith, H.T.5    Fried, V.A.6    Weissman, I.L.7
  • 138
    • 33749122931 scopus 로고    scopus 로고
    • Production of nonphosphorylated, ubiquinated protein kinase C (PKC) from autophosphorylated enzyme in human fibroblasts
    • Smith J.B., Lee H.-W., and Smith L. Production of nonphosphorylated, ubiquinated protein kinase C (PKC) from autophosphorylated enzyme in human fibroblasts. FASEB J. 10 (1996) A1397
    • (1996) FASEB J. , vol.10
    • Smith, J.B.1    Lee, H.-W.2    Smith, L.3
  • 139
    • 0029671427 scopus 로고    scopus 로고
    • p120cbl is a cytosolic adapter protein that associates with phosphoinositide 3-kinase in response to epidermal growth factor in PC12 and other cells
    • Soltoff S.P., and Cantley L.C. p120cbl is a cytosolic adapter protein that associates with phosphoinositide 3-kinase in response to epidermal growth factor in PC12 and other cells. J. Biol. Chem. 271 (1996) 563-567
    • (1996) J. Biol. Chem. , vol.271 , pp. 563-567
    • Soltoff, S.P.1    Cantley, L.C.2
  • 140
    • 0027327659 scopus 로고
    • A protein translocation defect linked to ubiquitin conjugation at the endoplasmic rcticulum
    • Sommer T., and Jentsch S. A protein translocation defect linked to ubiquitin conjugation at the endoplasmic rcticulum. Nature 365 (1993) 176-179
    • (1993) Nature , vol.365 , pp. 176-179
    • Sommer, T.1    Jentsch, S.2
  • 141
    • 0028347283 scopus 로고
    • New era of calpain research. Discovery of tissue-specific calpains. [Review]
    • Sorimachi H., Saido T.C., and Suzuki K. New era of calpain research. Discovery of tissue-specific calpains. [Review]. FEBS Lett. 343 (1994) 1-5
    • (1994) FEBS Lett. , vol.343 , pp. 1-5
    • Sorimachi, H.1    Saido, T.C.2    Suzuki, K.3
  • 142
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
    • Spence J., Sadis S., Haas A.L., and Finley D. A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol. Cell Biol. 15 (1995) 1265-1273
    • (1995) Mol. Cell Biol. , vol.15 , pp. 1265-1273
    • Spence, J.1    Sadis, S.2    Haas, A.L.3    Finley, D.4
  • 143
    • 0024278671 scopus 로고
    • Rabbit liver growth hormone receptor and serum binding protein. Purification, characterization, and sequence
    • Spencer S.A., Hammonds R.G., Henzel W.J., Rodriguez H., Waters M.J., and Wood W.I. Rabbit liver growth hormone receptor and serum binding protein. Purification, characterization, and sequence. J. Biol. Chem. 263 (1988) 7862-7867
    • (1988) J. Biol. Chem. , vol.263 , pp. 7862-7867
    • Spencer, S.A.1    Hammonds, R.G.2    Henzel, W.J.3    Rodriguez, H.4    Waters, M.J.5    Wood, W.I.6
  • 144
    • 0029670679 scopus 로고    scopus 로고
    • Ubiquitination-dependent proteolysis of 06-methylguanine-DNA methyltransferase in human and munne tumor cells following inactivation with O6-benzylguanine or 1,3-bis(2-chloroethyl)-1-nitrosourea
    • Srivenugopal K.S., Yuan X.H., Friedman H.S., and Ali-Osman F. Ubiquitination-dependent proteolysis of 06-methylguanine-DNA methyltransferase in human and munne tumor cells following inactivation with O6-benzylguanine or 1,3-bis(2-chloroethyl)-1-nitrosourea. Biochemistry 35 (1996) 1328-1334
    • (1996) Biochemistry , vol.35 , pp. 1328-1334
    • Srivenugopal, K.S.1    Yuan, X.H.2    Friedman, H.S.3    Ali-Osman, F.4
  • 145
    • 0028834782 scopus 로고
    • Degradation of the proto-oncogene product c-Fos by the ubiquitin proteolytic system in vivo and in vitro: identification and characterization of the conjugating enzymes
    • Stancovski I., Gonen H., Orian A., Schwartz A.L., and Ciechanover A. Degradation of the proto-oncogene product c-Fos by the ubiquitin proteolytic system in vivo and in vitro: identification and characterization of the conjugating enzymes. Mol. Cell Biol. 15 (1995) 7106-7116
    • (1995) Mol. Cell Biol. , vol.15 , pp. 7106-7116
    • Stancovski, I.1    Gonen, H.2    Orian, A.3    Schwartz, A.L.4    Ciechanover, A.5
  • 146
    • 0029874436 scopus 로고    scopus 로고
    • WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome
    • Staub O., Dho S., Correa J., Ishikawa T., McGlade J., and Rotin D. WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome. EMBOJ. 15 (1996) 2371-2381
    • (1996) EMBOJ. , vol.15 , pp. 2371-2381
    • Staub, O.1    Dho, S.2    Correa, J.3    Ishikawa, T.4    McGlade, J.5    Rotin, D.6
  • 147
    • 0028801196 scopus 로고
    • Kinetic studies of isopeptidase T: modulation of peptidase activity by ubiquitin
    • Stein R.L., Chen Z., and Melandri F. Kinetic studies of isopeptidase T: modulation of peptidase activity by ubiquitin. Biochemistry 34 (1995) 12616-12623
    • (1995) Biochemistry , vol.34 , pp. 12616-12623
    • Stein, R.L.1    Chen, Z.2    Melandri, F.3
  • 148
    • 0029025606 scopus 로고
    • The cyclosome, a large complex containing cyclin-selective ubiquitin ligase activity, targets cyclins for destruction at the end of mitosis
    • Sudakin V., Ganoth D., Dahan A., Heller H., Hershko J., Luca F.C., Ruderman J.V., and Hershko A. The cyclosome, a large complex containing cyclin-selective ubiquitin ligase activity, targets cyclins for destruction at the end of mitosis. Mol. Cell Biol. 6 (1995) 185-197
    • (1995) Mol. Cell Biol. , vol.6 , pp. 185-197
    • Sudakin, V.1    Ganoth, D.2    Dahan, A.3    Heller, H.4    Hershko, J.5    Luca, F.C.6    Ruderman, J.V.7    Hershko, A.8
  • 149
    • 0028997651 scopus 로고
    • Characterization of the mammalian YAP (Yes-associated protein) gene and its role in defining a novel protein module, the WW domain
    • Sudol M., Bork P., Einbond A., Kastury K., Druck T., Negrini M., Huebner K., and Lehman D. Characterization of the mammalian YAP (Yes-associated protein) gene and its role in defining a novel protein module, the WW domain. J. Biol. Chem. 270 (1995) 14733-14741
    • (1995) J. Biol. Chem. , vol.270 , pp. 14733-14741
    • Sudol, M.1    Bork, P.2    Einbond, A.3    Kastury, K.4    Druck, T.5    Negrini, M.6    Huebner, K.7    Lehman, D.8
  • 150
    • 0024117989 scopus 로고
    • The RAD6 protein of Saccharomyces cerevisiae polyubiquitinates histones, and its acidic domain mediates this activity
    • Sung P., Prakash S., and Prakash L. The RAD6 protein of Saccharomyces cerevisiae polyubiquitinates histones, and its acidic domain mediates this activity. Genes Dev. 2 (1988) 1476-1485
    • (1988) Genes Dev. , vol.2 , pp. 1476-1485
    • Sung, P.1    Prakash, S.2    Prakash, L.3
  • 151
    • 0027089685 scopus 로고
    • Modulation of cellular signals by calpain [Review]
    • Suzuki K., Saido T.C., and Hirai S. Modulation of cellular signals by calpain [Review]. Ann. N.Y. Acad. Sci. 674 (1992) 218-227
    • (1992) Ann. N.Y. Acad. Sci. , vol.674 , pp. 218-227
    • Suzuki, K.1    Saido, T.C.2    Hirai, S.3
  • 153
    • 0028000102 scopus 로고
    • Role of proteasomes modified by interferon-gamma in antigen processing [Review]
    • Tanaka K. Role of proteasomes modified by interferon-gamma in antigen processing [Review]. J. Leukoc. Biol. 56 (1994) 571-575
    • (1994) J. Leukoc. Biol. , vol.56 , pp. 571-575
    • Tanaka, K.1
  • 154
    • 0027360808 scopus 로고
    • Processing of poly-ubiquitin in the polyprotein of an RNA virus
    • Tautz N., Meyers G., and Thiel H.J. Processing of poly-ubiquitin in the polyprotein of an RNA virus. Virology. 197 (1993) 74-85
    • (1993) Virology. , vol.197 , pp. 74-85
    • Tautz, N.1    Meyers, G.2    Thiel, H.J.3
  • 155
    • 0025991456 scopus 로고
    • Cloning and functional analysis of the ubiquitin-specific protease gene UBP1 of Saccharomyces cerevisiae
    • Tobias J.W., and Varshavsky A. Cloning and functional analysis of the ubiquitin-specific protease gene UBP1 of Saccharomyces cerevisiae. J. Biol. Chem. 266 (1991) 12021-12028
    • (1991) J. Biol. Chem. , vol.266 , pp. 12021-12028
    • Tobias, J.W.1    Varshavsky, A.2
  • 156
    • 0004783940 scopus 로고
    • A housekeeping: gene on the X chromosome encodes a protein similar to ubiquitin
    • Toniolo D., Persico M., and Alcalay M. A housekeeping: gene on the X chromosome encodes a protein similar to ubiquitin. Proc. Natl. Acad. Sci. USA 85 (1988) 851-855
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 851-855
    • Toniolo, D.1    Persico, M.2    Alcalay, M.3
  • 158
    • 0028948230 scopus 로고
    • The levels of ubiquitinated histone H2A are highly upregulated in transformed human cells: partial colocalization of uH2A clusters and PCNA/cyclin foci in a fraction of cells in S-phase
    • Vassilev A.P., Rasmussen H.H., Christensen E.I., Nielsen S., and Celis J.E. The levels of ubiquitinated histone H2A are highly upregulated in transformed human cells: partial colocalization of uH2A clusters and PCNA/cyclin foci in a fraction of cells in S-phase. J. Cell Sci. 108 (1995) 1205-1215
    • (1995) J. Cell Sci. , vol.108 , pp. 1205-1215
    • Vassilev, A.P.1    Rasmussen, H.H.2    Christensen, E.I.3    Nielsen, S.4    Celis, J.E.5
  • 160
    • 0030058105 scopus 로고    scopus 로고
    • c-Cbl is transiently tyrosine-phosphorylated, ubiquitinated, and membrane-targeted following CSF-1 stimulation of macrophages
    • Wang Y., Yeung Y.G., Langdon W.Y., and Stanley E.R. c-Cbl is transiently tyrosine-phosphorylated, ubiquitinated, and membrane-targeted following CSF-1 stimulation of macrophages. J. Biol. Chem. 271 (1996) 17-20
    • (1996) J. Biol. Chem. , vol.271 , pp. 17-20
    • Wang, Y.1    Yeung, Y.G.2    Langdon, W.Y.3    Stanley, E.R.4
  • 161
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward C.L., Omura S., and Kopito R.R. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83 (1995) 121-127
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 162
    • 0027367944 scopus 로고
    • The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function
    • Watkins J.F., Sung P., Prakash L., and Prakash S. The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function. Mol. Cell Biol. 13 (1993) 7757-7765
    • (1993) Mol. Cell Biol. , vol.13 , pp. 7757-7765
    • Watkins, J.F.1    Sung, P.2    Prakash, L.3    Prakash, S.4
  • 163
    • 0027403115 scopus 로고
    • The extremely conserved amino terminus of RAD6 ubiquitin-conjugating enzyme is essential for amino-end rule-dependent protein degradation
    • Watkins J.F., Sung P., Prakash S., and Prakash L. The extremely conserved amino terminus of RAD6 ubiquitin-conjugating enzyme is essential for amino-end rule-dependent protein degradation. Genes Dev. 7 (1993) 250-261
    • (1993) Genes Dev. , vol.7 , pp. 250-261
    • Watkins, J.F.1    Sung, P.2    Prakash, S.3    Prakash, L.4
  • 164
    • 0026782393 scopus 로고
    • The Pas2 protein essential forperoxisome biogenesis is related to ubiquitin-conjugating enzymes
    • Wiebel F.F., and Kunau W.H. The Pas2 protein essential forperoxisome biogenesis is related to ubiquitin-conjugating enzymes. Nature 359 (1992) 73-76
    • (1992) Nature , vol.359 , pp. 73-76
    • Wiebel, F.F.1    Kunau, W.H.2
  • 165
    • 0003315338 scopus 로고
    • Purification and structural Properties of ubiquitin
    • Rechsteiner M. (Ed), Plenum Press, New York
    • Wilkinson K.D. Purification and structural Properties of ubiquitin. In: Rechsteiner M. (Ed). Ubiquitin (1988), Plenum Press, New York 5-38
    • (1988) Ubiquitin , pp. 5-38
    • Wilkinson, K.D.1
  • 167
    • 0026757444 scopus 로고
    • Comparisons of neuronal (PGP 9.5) and non-neuronal ubiquitin C-terminal hydrolases
    • Wilkinson K.D., Deshpande S., and Larsen C.N. Comparisons of neuronal (PGP 9.5) and non-neuronal ubiquitin C-terminal hydrolases. Biochem. Soc. Trans. 20 (1992) 631-637
    • (1992) Biochem. Soc. Trans. , vol.20 , pp. 631-637
    • Wilkinson, K.D.1    Deshpande, S.2    Larsen, C.N.3
  • 168
    • 0029095673 scopus 로고
    • Roles of ubiquitinylation in proteolysis and cellular regulation [Review]
    • Wilkinson K.D. Roles of ubiquitinylation in proteolysis and cellular regulation [Review]. Annu. Rev. Nutr. 15 (1995) 161-189
    • (1995) Annu. Rev. Nutr. , vol.15 , pp. 161-189
    • Wilkinson, K.D.1
  • 169
    • 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., and Pickart CM. 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, CM.6
  • 170
    • 0343299453 scopus 로고    scopus 로고
    • The deubiquitinating enzymes
    • Finley D.J., and Peters J.-M. (Eds), Plenum, New York In press
    • Wilkinson K.D., and Hochstrasser M. The deubiquitinating enzymes. In: Finley D.J., and Peters J.-M. (Eds). Ubiquitin (1997), Plenum, New York In press
    • (1997) Ubiquitin
    • Wilkinson, K.D.1    Hochstrasser, M.2
  • 173
    • 0029920469 scopus 로고    scopus 로고
    • Antigen processing and presentation by the class I major histocompatibility complex
    • York I.A., and Rock K.L. Antigen processing and presentation by the class I major histocompatibility complex. Annu. Rev. Immunol. 14 (1996) 369-396
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 369-396
    • York, I.A.1    Rock, K.L.2
  • 174
    • 0024416864 scopus 로고
    • Ubiquitin is involved in the in vitro insertion of monoamine oxidase B into mitochondrial outer membranes
    • Zhaung Z.P., and McCauley R. Ubiquitin is involved in the in vitro insertion of monoamine oxidase B into mitochondrial outer membranes. J. Biol. Chem. 264 (1989) 14594-14596
    • (1989) J. Biol. Chem. , vol.264 , pp. 14594-14596
    • Zhaung, Z.P.1    McCauley, R.2
  • 175
    • 0026580106 scopus 로고
    • The insertion of monoamine oxidase A into the outer membrane of rat liver mitochondria
    • Zhuang Z.P., Marks B., and McCauley R.B. The insertion of monoamine oxidase A into the outer membrane of rat liver mitochondria. J. Biol. Chem. 267 (1992) 591-596
    • (1992) J. Biol. Chem. , vol.267 , pp. 591-596
    • Zhuang, Z.P.1    Marks, B.2    McCauley, R.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.