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Volumn 10, Issue 3, 1999, Pages 741-756

Interaction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; PROTEIN 26S; PROTEIN DOA4; UNCLASSIFIED DRUG;

EID: 0032912818     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.10.3.741     Document Type: Article
Times cited : (107)

References (54)
  • 1
    • 0031030057 scopus 로고    scopus 로고
    • Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum
    • Akopian, T.N., Kisselev, A.F., and Goldberg, A.L. (1997). Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum. J. Biol. Chem. 272, 1791-1798.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1791-1798
    • Akopian, T.N.1    Kisselev, A.F.2    Goldberg, A.L.3
  • 2
    • 0030746105 scopus 로고    scopus 로고
    • In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome
    • Amerik, A.Y., Swaminathan, S., Krantz, B.A., Wilkinson, K.D., and Hochstrasser, M. (1997). In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome. EMBO J. 16, 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
  • 4
    • 0026457302 scopus 로고
    • Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family
    • Baker, R.T., Tobias, J.W., and Varshavsky, A. (1992). Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family. J. Biol. Chem. 267, 23364-23375.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23364-23375
    • Baker, R.T.1    Tobias, J.W.2    Varshavsky, A.3
  • 6
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister, W., Walz, J., Zuhl, F., and Seemuller, E. (1998). The proteasome: paradigm of a self-compartmentalizing protease. Cell 92, 367-380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 7
    • 0028999726 scopus 로고
    • Biogenesis, structure, and function of the yeast 20s proteasome
    • Chen, P., and Hochstrasser, M. (1995). Biogenesis, structure, and function of the yeast 20S proteasome. EMBO J. 14, 2620-2630.
    • (1995) EMBO J. , vol.14 , pp. 2620-2630
    • Chen, P.1    Hochstrasser, M.2
  • 8
    • 0027198563 scopus 로고
    • Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor
    • Chen, P., Johnson, P., Sommer, T., Jentsch, S., and Hochstrasser, M. (1993). Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor. Cell 74, 357-369.
    • (1993) Cell , vol.74 , pp. 357-369
    • Chen, P.1    Johnson, P.2    Sommer, T.3    Jentsch, S.4    Hochstrasser, M.5
  • 9
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., Tanaka, K., and Goldberg, A.L. (1996). Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 10
    • 15444361471 scopus 로고    scopus 로고
    • Involvement of valosin-containing protein, an ATPase copurified with IκBα and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IκBα
    • Dai, R.M., Chen, E., Longo, D.L., Gorbea, C.M., and Li, C.C. (1998). Involvement of valosin-containing protein, an ATPase copurified with IκBα and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IκBα. J. Biol. Chem. 273, 3562-3573.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3562-3573
    • Dai, R.M.1    Chen, E.2    Longo, D.L.3    Gorbea, C.M.4    Li, C.C.5
  • 11
    • 0028883820 scopus 로고
    • The yeast SEN3 gene encodes a regulatory subunit of the 26S proteasome complex required for ubiquitin-dependent protein degradation in vivo
    • DeMarini, D.J., Papa, F.R., Swaminathan, S., Ursic, D., Rasmussen, T.P., Culbertson, M.R., and Hochstrasser, M. (1995). The yeast SEN3 gene encodes a regulatory subunit of the 26S proteasome complex required for ubiquitin-dependent protein degradation in vivo. Mol. Cell. Biol. 15, 6311-6321.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6311-6321
    • DeMarini, D.J.1    Papa, F.R.2    Swaminathan, S.3    Ursic, D.4    Rasmussen, T.P.5    Culbertson, M.R.6    Hochstrasser, M.7
  • 12
    • 0028087582 scopus 로고
    • PA700, an ATP-dependent activator of the 20S 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., Ma, C.-P., Afendis, S.J., Swaffield, J.C., and Slaughter, C.A. (1994). PA700, an ATP-dependent activator of the 20S proteasome, is an ATPase containing multiple members of a nucleotide-binding protein family. J. Biol. Chem. 269, 20878-20884.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20878-20884
    • DeMartino, G.N.1    Moomaw, C.R.2    Zagnitko, O.P.3    Proske, R.J.4    Ma, C.-P.5    Afendis, S.J.6    Swaffield, J.C.7    Slaughter, C.A.8
  • 13
    • 0027480739 scopus 로고
    • Ubiquitin C-terminal hydrolase activity associated with the 26S protease complex
    • Eytan, E., Armon, T., Heller, H., Beck, S., and Hershko, A. (1993). Ubiquitin C-terminal hydrolase activity associated with the 26S protease complex. J. Biol. Chem. 268, 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
  • 14
    • 0028859849 scopus 로고
    • A human deubiquitinating enzyme with both isopeptidase and peptidase activities in vitro
    • Falquet, L., Paquet, N., Frutiger, S., Hughes, G.J., Hoang-Van, K., and Jaton, J.C. (1995). A human deubiquitinating enzyme with both isopeptidase and peptidase activities in vitro. FEBS Lett. 359, 73-77.
    • (1995) FEBS Lett. , vol.359 , pp. 73-77
    • Falquet, L.1    Paquet, N.2    Frutiger, S.3    Hughes, G.J.4    Hoang-Van, K.5    Jaton, J.C.6
  • 16
    • 0029043805 scopus 로고
    • A simple p53 functional assay for screening cell lines, blood, and tumors
    • Flaman, J.M., et al. (1995). A simple p53 functional assay for screening cell lines, blood, and tumors. Proc. Natl. Acad. Sci. USA 92, 3963-3967.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3963-3967
    • Flaman, J.M.1
  • 17
    • 0032548779 scopus 로고    scopus 로고
    • Son1p is a component of the 26S proteasome of the yeast Saccharomyces cerevisiae
    • Fujimuro, M., Tanaka, K., Yokosawa, H., and Toh-e, A. (1998). Son1p is a component of the 26S proteasome of the yeast Saccharomyces cerevisiae. FEBS Lett. 423, 149-154.
    • (1998) FEBS Lett. , vol.423 , pp. 149-154
    • Fujimuro, M.1    Tanaka, K.2    Yokosawa, H.3    Toh-e, A.4
  • 18
    • 0030881952 scopus 로고    scopus 로고
    • Ubiquitin Lys63 is involved in ubiquitination of a yeast plasma membrane protein
    • Galan, J., and Haguenauer-Tsapis, R. (1997). Ubiquitin Lys63 is involved in ubiquitination of a yeast plasma membrane protein. EMBO J. 16, 5847-5854.
    • (1997) EMBO J. , vol.16 , pp. 5847-5854
    • Galan, J.1    Haguenauer-Tsapis, R.2
  • 19
    • 0027444947 scopus 로고
    • S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase
    • Ghislain, M., Udvardy, A., and Mann, C. (1993). S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase. Nature 366, 358-362.
    • (1993) Nature , vol.366 , pp. 358-362
    • Ghislain, M.1    Udvardy, A.2    Mann, C.3
  • 20
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-bp restriction sites
    • Gietz, R.D., and Sugino, A. (1988). New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-bp restriction sites. Gene 74, 527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 21
    • 0031815994 scopus 로고    scopus 로고
    • The regulatory particle of the Saccharomyces cerevisiae proteasome
    • Glickman, M.H., Rubin, D.M., Fried, V.A., and Finley, D. (1998). The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol. Cell. Biol. 18, 3149-3162.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3149-3162
    • Glickman, M.H.1    Rubin, D.M.2    Fried, V.A.3    Finley, D.4
  • 22
    • 0029867623 scopus 로고    scopus 로고
    • Proteasomes: Destruction as a program
    • Hilt, W., and Wolf, D.H. (1996). Proteasomes: destruction as a program. Trends Biochem. Sci. 21, 96-102.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 96-102
    • Hilt, W.1    Wolf, D.H.2
  • 23
    • 0028935165 scopus 로고
    • Ubiquitin, proteasomes, and the regulation of intracellular protein degradation
    • Hochstrasser, M. (1995). Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr. Opin. Cell Biol. 7, 215-223.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 215-223
    • Hochstrasser, M.1
  • 24
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser, M. (1996). Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30, 405-439.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 26
    • 0025331090 scopus 로고
    • In vivo degradation of a transcriptional regulator: The yeast α2 repressor
    • Hochstrasser, M., and Varshavsky, A. (1990). In vivo degradation of a transcriptional regulator: the yeast α2 repressor. Cell 62, 697-708.
    • (1990) Cell , vol.62 , pp. 697-708
    • Hochstrasser, M.1    Varshavsky, A.2
  • 27
    • 0026539795 scopus 로고
    • Multiple forms of the 20 S multicatalytic and the 26 S ubiquitin/ATP-dependent proteases from rabbit reticulocyte lysate
    • Hoffman, L., Pratt, G., and Rechsteiner, M. (1992). Multiple forms of the 20 S multicatalytic and the 26 S ubiquitin/ATP-dependent proteases from rabbit reticulocyte lysate. J. Biol. Chem. 267, 22362-22368.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22362-22368
    • Hoffman, L.1    Pratt, G.2    Rechsteiner, M.3
  • 28
    • 0026551489 scopus 로고
    • Demonstration that a human 26S proteolytic complex consists of a proteasome and multiple associated protein components and hydrolyzes ATP and ubiquitin-ligated proteins by closely linked mechanisms
    • Kanayama, H.O., Tamura, T., Ugai, S., Kagawa, S., Tanahashi, N., Yoshimura, T., Tanaka, K., and Ichihara, A. (1992). Demonstration that a human 26S proteolytic complex consists of a proteasome and multiple associated protein components and hydrolyzes ATP and ubiquitin-ligated proteins by closely linked mechanisms. Eur. J. Biochem. 206, 567-578.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 567-578
    • Kanayama, H.O.1    Tamura, T.2    Ugai, S.3    Kagawa, S.4    Tanahashi, N.5    Yoshimura, T.6    Tanaka, K.7    Ichihara, A.8
  • 29
    • 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. (1997). Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome. Nature 385, 737-740.
    • (1997) Nature , vol.385 , pp. 737-740
    • Lam, Y.A.1    Xu, W.2    DeMartino, G.N.3    Cohen, R.E.4
  • 30
    • 0024404907 scopus 로고
    • Purification of a ubiquitin protein peptidase from yeast with efficient in vitro assays
    • Liu, C.C., Miller, H.I., Kohr, W.J., and Silber, J.I. (1989). Purification of a ubiquitin protein peptidase from yeast with efficient in vitro assays. J. Biol. Chem. 264, 20331-20338.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20331-20338
    • Liu, C.C.1    Miller, H.I.2    Kohr, W.J.3    Silber, J.I.4
  • 31
    • 0031950846 scopus 로고    scopus 로고
    • Role for the ubiquitin-proteasome system in the vacuolar degradation of Ste6p, the a-factor transporter in Saccharomyces cerevisiae
    • Loayza, D., and Michaelis, S. (1998). Role for the ubiquitin-proteasome system in the vacuolar degradation of Ste6p, the a-factor transporter in Saccharomyces cerevisiae. Mol. Cell. Biol. 18, 779-789.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 779-789
    • Loayza, D.1    Michaelis, S.2
  • 32
    • 0028025326 scopus 로고
    • Identification, purification, and characterization of a high molecular weight, ATP-dependent activator (PA700) of the 20 S proteasome
    • Ma, C.P., Vu, J.H., Proske, R.J., Slaughter, C.A., and DeMartino, G.N. (1994). Identification, purification, and characterization of a high molecular weight, ATP-dependent activator (PA700) of the 20 S proteasome. J. Biol. Chem. 269, 3539-3547.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3539-3547
    • Ma, C.P.1    Vu, J.H.2    Proske, R.J.3    Slaughter, C.A.4    DeMartino, G.N.5
  • 33
    • 0023615620 scopus 로고
    • Plasmid construction by homologous recombination in yeast
    • Ma, H., Kunes, S., Schatz, P., and Botstein, D. (1987). Plasmid construction by homologous recombination in yeast. Gene 58, 201-216.
    • (1987) Gene , vol.58 , pp. 201-216
    • Ma, H.1    Kunes, S.2    Schatz, P.3    Botstein, D.4
  • 34
    • 0026501752 scopus 로고
    • A rapid method for localized mutagenesis of yeast genes
    • Muhlrad, D., Hunter, R., Parker, R. (1992). A rapid method for localized mutagenesis of yeast genes. Yeast 8, 79-82.
    • (1992) Yeast , vol.8 , pp. 79-82
    • Muhlrad, D.1    Hunter, R.2    Parker, R.3
  • 36
    • 0025123346 scopus 로고
    • The multicatalytic proteinase complex, a major extralysomal proteolytic system
    • Orlowski, M. (1990). The multicatalytic proteinase complex, a major extralysomal proteolytic system. Biochemistry 29, 10289-10297.
    • (1990) Biochemistry , vol.29 , pp. 10289-10297
    • Orlowski, M.1
  • 37
    • 0027427249 scopus 로고
    • The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene
    • Papa, F., and Hochstrasser, M. (1993), The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene. Nature 366, 313-319.
    • (1993) Nature , vol.366 , pp. 313-319
    • Papa, F.1    Hochstrasser, M.2
  • 38
    • 0026265918 scopus 로고
    • Ultrastructure of the approximately 26S complex containing the approximately 20S cylinder particle (multicatalytic proteinase/proteasome)
    • Peters, J.M., Harris, J.R., and Kleinschmidt, J.A. (1991). Ultrastructure of the approximately 26S complex containing the approximately 20S cylinder particle (multicatalytic proteinase/proteasome). Eur. J. Cell. Biol. 56, 422-432.
    • (1991) Eur. J. Cell. Biol. , vol.56 , pp. 422-432
    • Peters, J.M.1    Harris, J.R.2    Kleinschmidt, J.A.3
  • 39
    • 0030772933 scopus 로고    scopus 로고
    • Targeting of substrates to the 26S proteasome
    • Pickart, C.M. (1997). Targeting of substrates to the 26S proteasome. FASEB J. 11, 1055-1066.
    • (1997) FASEB J. , vol.11 , pp. 1055-1066
    • Pickart, C.M.1
  • 40
    • 0032168508 scopus 로고    scopus 로고
    • Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome
    • Rubin, D.M., Glickman, M.H., Larsen, C.N., Dhruvakumar, S., and Finley, D. (1998). Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome. EMBO J. 17, 4909-4919.
    • (1998) EMBO J. , vol.17 , pp. 4909-4919
    • Rubin, D.M.1    Glickman, M.H.2    Larsen, C.N.3    Dhruvakumar, S.4    Finley, D.5
  • 42
    • 0029926295 scopus 로고    scopus 로고
    • Coordinating DNA replication to produce one copy of the genome requires genes that act in ubiquitin metabolism
    • Singer, J.D., Manning, B.M., and Formosa, T. (1996). Coordinating DNA replication to produce one copy of the genome requires genes that act in ubiquitin metabolism. Mol. Cell. Biol. 16, 1356-1366.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1356-1366
    • Singer, J.D.1    Manning, B.M.2    Formosa, T.3
  • 43
    • 0028890360 scopus 로고
    • A highly conserved ATPase protein as a mediator between acidic activation domains and the TATA-binding protein
    • Swaffield, J.C., Melcher, K., and Johnston, S.A. (1995). A highly conserved ATPase protein as a mediator between acidic activation domains and the TATA-binding protein. Nature 374, 88-91.
    • (1995) Nature , vol.374 , pp. 88-91
    • Swaffield, J.C.1    Melcher, K.2    Johnston, S.A.3
  • 44
    • 0026509543 scopus 로고
    • The Cln3-Cdc28 kinase complex of S. cerevisiae is regulated by proteolysis and phosphorylation
    • Tyers, M., Tokiwa, G., Nash, R., and Futcher, B. (1992). The Cln3-Cdc28 kinase complex of S. cerevisiae is regulated by proteolysis and phosphorylation. EMBO J. 11, 1773-1784.
    • (1992) EMBO J. , vol.11 , pp. 1773-1784
    • Tyers, M.1    Tokiwa, G.2    Nash, R.3    Futcher, B.4
  • 45
    • 0027502883 scopus 로고
    • Purification and characterization of a multiprotein component of the Drosophila 26 S (1500 kDa) proteolytic complex
    • Udvardy, A. (1993). Purification and characterization of a multiprotein component of the Drosophila 26 S (1500 kDa) proteolytic complex. J. Biol. Chem. 268, 9055-9062.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9055-9062
    • Udvardy, A.1
  • 46
    • 0027319343 scopus 로고
    • Purification and characterization of the 26S proteasome complex catalyzing ATP-dependent breakdown of ubiquitin-ligated proteins from rat liver
    • Ugai, S., Tamura, T., Tanahashi, N., Takai, S., Komi, N., Chung, C.H., Tanaka, K., and Ichihara, A. (1993). Purification and characterization of the 26S proteasome complex catalyzing ATP-dependent breakdown of ubiquitin-ligated proteins from rat liver. J. Biochem. 113, 754-768.
    • (1993) J. Biochem. , vol.113 , pp. 754-768
    • Ugai, S.1    Tamura, T.2    Tanahashi, N.3    Takai, S.4    Komi, N.5    Chung, C.H.6    Tanaka, K.7    Ichihara, A.8
  • 47
    • 0030867774 scopus 로고    scopus 로고
    • The ubiquitin system
    • Varshavsky, A. (1997). The ubiquitin system. Trends Biochem. Sci. 22, 383-387.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 383-387
    • Varshavsky, A.1
  • 48
    • 0029095673 scopus 로고
    • Roles of ubiquitinylation in proteolysis and cellular regulation
    • Wilkinson, K.D. (1995). Roles of ubiquitinylation in proteolysis and cellular regulation. Annu. Rev. Nutr. 15, 161-189.
    • (1995) Annu. Rev. Nutr. , vol.15 , pp. 161-189
    • Wilkinson, K.D.1
  • 49
    • 0002657323 scopus 로고    scopus 로고
    • Deubiquitinating enzymes
    • ed. J.M. Peters, J.R. Harris, and D. Finley, New York: Plenum Press
    • Wilkinson, K.D., and Hochstrasser, M. (1998). Deubiquitinating enzymes. In: Ubiquitin and the Biology of the Cell, ed. J.M. Peters, J.R. Harris, and D. Finley, New York: Plenum Press, 99-125.
    • (1998) Ubiquitin and the Biology of the Cell , pp. 99-125
    • Wilkinson, K.D.1    Hochstrasser, M.2
  • 50
    • 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, C.M. (1995). Metabolism of the polyubiquitin degradation signal: structure, mechanism, and role of isopeptidase T. Biochemistry 34, 14535-14546.
    • (1995) Biochemistry , vol.34 , pp. 14535-14546
    • Wilkinson, K.D.1    Tashayev, V.L.2    O'Connor, L.B.3    Larsen, C.N.4    Kasperek, E.5    Pickart, C.M.6
  • 51
    • 0022755757 scopus 로고
    • The PEP4 gene encodes an aspartyl protease implicated in the posttranslational regulation of Saccharomyces cerevisiae vacuolar hydrolases
    • Woolford, C.A., Daniels, L.B., Park, F.J., Jones, E.W., Van Arsdell, J.N., and Innis, M.A. (1986). The PEP4 gene encodes an aspartyl protease implicated in the posttranslational regulation of Saccharomyces cerevisiae vacuolar hydrolases. Mol. Cell. Biol. 6, 2500-2510.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 2500-2510
    • Woolford, C.A.1    Daniels, L.B.2    Park, F.J.3    Jones, E.W.4    Van Arsdell, J.N.5    Innis, M.A.6
  • 52
    • 0027988524 scopus 로고
    • UBP5 encodes a putative yeast ubiquitin-specific protease that is related to the human Tre-2 oncogene product
    • Xiao, W., Fontanie, T., and Tang, M. (1994). UBP5 encodes a putative yeast ubiquitin-specific protease that is related to the human Tre-2 oncogene product. Yeast 10, 1497-1502.
    • (1994) Yeast , vol.10 , pp. 1497-1502
    • Xiao, W.1    Fontanie, T.2    Tang, M.3
  • 53
    • 8944250216 scopus 로고    scopus 로고
    • cDNA cloning of p112, the largest regulatory subunit of the human 26S proteasome, and functional analysis of its yeast homologue, Sen3p
    • Yokota, K., et al. (1996). cDNA cloning of p112, the largest regulatory subunit of the human 26S proteasome, and functional analysis of its yeast homologue, Sen3p. Mol. Biol. Cell 7, 853-870.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 853-870
    • Yokota, K.1
  • 54
    • 0027812238 scopus 로고
    • Molecular characterization of the "26S" proteasome complex from rat liver
    • Yoshimura, T., et al. (1993). Molecular characterization of the "26S" proteasome complex from rat liver. J. Struct. Biol. 111, 200-211.
    • (1993) J. Struct. Biol. , vol.111 , pp. 200-211
    • Yoshimura, T.1


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