메뉴 건너뛰기




Volumn 18, Issue 6, 1998, Pages 3149-3162

The regulatory particle of the Saccharomyces cerevisiae proteasome

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; PROTEASOME; REGULATOR PROTEIN; UBIQUITIN;

EID: 0031815994     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.18.6.3149     Document Type: Article
Times cited : (434)

References (113)
  • 3
    • 0025635889 scopus 로고
    • Assembly of the 26S complex that degrades proteins ligated to ubiquitin is accompanied by the formation of ATPase activity
    • Armon, T., D. Ganoth, and A. Hershko. 1990. Assembly of the 26S complex that degrades proteins ligated to ubiquitin is accompanied by the formation of ATPase activity. J. Biol. Chem. 265:20723-20726.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20723-20726
    • Armon, T.1    Ganoth, D.2    Hershko, A.3
  • 4
    • 0026457302 scopus 로고
    • Ubiquitin-specific proteases of S. cerevisiae. Cloning of UBP2 and UBP3 and functional analysis of the UBP gene family
    • Baker, R. T., J. W. Tobias, and A. Varshavsky. 1992. Ubiquitin-specific proteases of S. 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
  • 5
    • 0041175168 scopus 로고    scopus 로고
    • CADp44: A novel regulatory subunit of the 26S proteasome and the mammalian homolog of ySug2p
    • Bauer, V. W., J. C. Swaffield, S. A. Johnston, and M. T. Andrews. 1996. CADp44: a novel regulatory subunit of the 26S proteasome and the mammalian homolog of ySug2p. Gene 181:63-69.
    • (1996) Gene , vol.181 , pp. 63-69
    • Bauer, V.W.1    Swaffield, J.C.2    Johnston, S.A.3    Andrews, M.T.4
  • 6
    • 0029038912 scopus 로고
    • A protein related to a proteasomal subunit binds to the intracellular domain of the p55 TNF receptor upstream to its death domain
    • Boldin, M. P., I. L. Mett, and D. Wallach. 1995. A protein related to a proteasomal subunit binds to the intracellular domain of the p55 TNF receptor upstream to its death domain. FEBS Lett. 367:39-44.
    • (1995) FEBS Lett. , vol.367 , pp. 39-44
    • Boldin, M.P.1    Mett, I.L.2    Wallach, D.3
  • 7
    • 0028215472 scopus 로고
    • Large-scale analysis of gene expression, protein localization, and gene disruption in S. cerevisiae
    • Burns, N., B. Grimwade, P. B. Ross-MacDonald, E. Y. Choi, K. Finberg, G. S. Roeder, and M. Snyder. 1994. Large-scale analysis of gene expression, protein localization, and gene disruption in S. cerevisiae. Genes Dev. 8: 1087-1105.
    • (1994) Genes Dev. , vol.8 , pp. 1087-1105
    • Burns, N.1    Grimwade, B.2    Ross-MacDonald, P.B.3    Choi, E.Y.4    Finberg, K.5    Roeder, G.S.6    Snyder, M.7
  • 8
    • 0027979074 scopus 로고
    • Mitochondrial morphological and functional defects in yeast caused by yme1 are suppressed by mutation of a 26S protease subunit homologue
    • Campbell, C. L., N. Tanaka, K. H. White, and P. E. Thorsness. 1994. Mitochondrial morphological and functional defects in yeast caused by yme1 are suppressed by mutation of a 26S protease subunit homologue. Mol. Biol. Cell 5:899-905.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 899-905
    • Campbell, C.L.1    Tanaka, N.2    White, K.H.3    Thorsness, P.E.4
  • 9
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover, A. 1994. The ubiquitin-proteasome proteolytic pathway. Cell 79:13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 10
    • 0029761277 scopus 로고    scopus 로고
    • A new group of conserved coactivators that increase the specificity of AP-1 transcription factors
    • Claret, F. X., M. Hibi, S. Dhut, T. Toda, and M. Karin. 1996. A new group of conserved coactivators that increase the specificity of AP-1 transcription factors. Nature 383:453-457.
    • (1996) Nature , vol.383 , pp. 453-457
    • Claret, F.X.1    Hibi, M.2    Dhut, S.3    Toda, T.4    Karin, M.5
  • 11
    • 0029328549 scopus 로고
    • A 200-amino acid ATPase module in search of a basic function
    • Confalonieri, F., and M. Duguet. 1995. A 200-amino acid ATPase module in search of a basic function. Bioessays 17:639-650.
    • (1995) Bioessays , vol.17 , pp. 639-650
    • Confalonieri, F.1    Duguet, M.2
  • 12
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., K. Tanaka, and A. L. Goldberg. 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
  • 14
    • 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., F. R. Papa, S. Swaminathan, D. Ursic, T. P. Rasmussen, M. R. Culbertson, and M. Hochstrasser. 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
  • 15
    • 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., C. R. Moomaw, O. P. Zagnitko, R. J. Proske, C. P. Ma, S. J. Afendis, J. C. Swaffield, and C. A. Slaughter. 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
  • 16
    • 1842345479 scopus 로고
    • Glycosylation affects cleavage of an H6N2 influenza virus hemagglutinin and regulates virulence
    • Deshpande, K. L., V. A. Fried, M. E. Ando, and R. G. Webster. 1987. Glycosylation affects cleavage of an H6N2 influenza virus hemagglutinin and regulates virulence. Proc. Natl. Acad. Sci. USA 84:36-40.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 36-40
    • Deshpande, K.L.1    Fried, V.A.2    Ando, M.E.3    Webster, R.G.4
  • 17
    • 0028848212 scopus 로고
    • Molecular cloning and expression of a 26S proteasome subunit enriched in dileucine repeats
    • Deveraux, Q., C. Jensen, and M. Rechsteiner. 1995. Molecular cloning and expression of a 26S proteasome subunit enriched in dileucine repeats. J. Biol. Chem. 270:23726-23729.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23726-23729
    • Deveraux, Q.1    Jensen, C.2    Rechsteiner, M.3
  • 19
    • 0028967102 scopus 로고
    • Molecular cloning and expression of subunit 12: A non-MCP and non-ATPase subunit of the 26S protease
    • Dubiel, W., K. Ferrell, R. Dumdey, S. Standera, S. Prehn, and M. Rechsteiner. 1995. Molecular cloning and expression of subunit 12: a non-MCP and non-ATPase subunit of the 26S protease. FEBS Lett. 363:97-100.
    • (1995) FEBS Lett. , vol.363 , pp. 97-100
    • Dubiel, W.1    Ferrell, K.2    Dumdey, R.3    Standera, S.4    Prehn, S.5    Rechsteiner, M.6
  • 20
    • 0026486168 scopus 로고
    • Subunit 4 of the 26S protease is a member of a novel eukaryotic ATPase family
    • Dubiel, W., K. Ferrell, G. Pratt, and M. Rechsteiner. 1992. Subunit 4 of the 26S protease is a member of a novel eukaryotic ATPase family. J. Biol. Chem. 267:22669-22702.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22669-22702
    • Dubiel, W.1    Ferrell, K.2    Pratt, G.3    Rechsteiner, M.4
  • 21
    • 0027204580 scopus 로고
    • Peptide sequencing identifies MSS1, a modulator of HIV Tat-mediated transactivation, as subunit 7 of the 26S protease
    • Dubiel, W., K. Ferrell, and M. Rechsteiner. 1993. Peptide sequencing identifies MSS1, a modulator of HIV Tat-mediated transactivation, as subunit 7 of the 26S protease. FEBS Lett. 323:276-278.
    • (1993) FEBS Lett. , vol.323 , pp. 276-278
    • Dubiel, W.1    Ferrell, K.2    Rechsteiner, M.3
  • 22
    • 0029186099 scopus 로고
    • Subunits of the regulatory complex of the 26S proteasome
    • Dubiel, W., K. Ferrell, and M. Rechsteiner. 1995. Subunits of the regulatory complex of the 26S proteasome. Mol. Biol. Rep. 21:27-34.
    • (1995) Mol. Biol. Rep. , vol.21 , pp. 27-34
    • Dubiel, W.1    Ferrell, K.2    Rechsteiner, M.3
  • 23
    • 0028802445 scopus 로고
    • cDNA cloning of a human 100 kDa deubiquitinating enzyme: The deubiquitinase belongs to the ubiquitin C-terminal hydrolase family 2 (UCH2)
    • Falquet, L., N. Paquet, S. Frutiger, G. J. Hughes, K. Hoang-Van, and J. C. Jaton. 1995. cDNA cloning of a human 100 kDa deubiquitinating enzyme: the deubiquitinase belongs to the ubiquitin C-terminal hydrolase family 2 (UCH2). FEBS Lett. 376:233-237.
    • (1995) FEBS Lett. , vol.376 , pp. 233-237
    • Falquet, L.1    Paquet, N.2    Frutiger, S.3    Hughes, G.J.4    Hoang-Van, K.5    Jaton, J.C.6
  • 24
    • 0023666139 scopus 로고
    • The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses
    • Finley, D., E. Özkaynak, and A. Varshavsky. 1987. The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses. Cell 48:1035-1046.
    • (1987) Cell , vol.48 , pp. 1035-1046
    • Finley, D.1    Özkaynak, E.2    Varshavsky, A.3
  • 25
    • 0019820048 scopus 로고
    • Membrane biogenesis: Evidence that a soluble chimeric polypeptide can serve as a precursor of a mutant lac permease in E. coli
    • Fried, V. A. 1981. Membrane biogenesis: evidence that a soluble chimeric polypeptide can serve as a precursor of a mutant lac permease in E. coli. J. Biol. Chem. 256:244-252.
    • (1981) J. Biol. Chem. , vol.256 , pp. 244-252
    • Fried, V.A.1
  • 26
    • 0031890210 scopus 로고    scopus 로고
    • Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26S proteasome subunit Mcbl
    • Fu, H., S. Sadis, D. M. Rubin, M. H. Glickman, S. van Nocker, D. Finley, and R. D. Vierstra. 1998. Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26S proteasome subunit Mcbl. J. Biol. Chem. 273:1970-1989.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1970-1989
    • Fu, H.1    Sadis, S.2    Rubin, D.M.3    Glickman, M.H.4    Van Nocker, S.5    Finley, D.6    Vierstra, R.D.7
  • 27
    • 0032548779 scopus 로고    scopus 로고
    • Son1p is a component of the 26S proteasome of the yeast Saccharomyces cerevisiae
    • Fujimuro, M., K. Tanaka, H. Yokosawa, and A. Toh-e. 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
  • 28
    • 0029950614 scopus 로고    scopus 로고
    • cDNA cloning of p42, a shared subunit of two proteasome regulatory proteins, reveals a novel member of the AAA protein family
    • Fujiwara, T., T. K. Watanabe, K. Tanaka, C. A. Slaughter, and G. N. DeMartino. 1996. cDNA cloning of p42, a shared subunit of two proteasome regulatory proteins, reveals a novel member of the AAA protein family. FEBS Lett. 387:184-188.
    • (1996) FEBS Lett. , vol.387 , pp. 184-188
    • Fujiwara, T.1    Watanabe, T.K.2    Tanaka, K.3    Slaughter, C.A.4    DeMartino, G.N.5
  • 29
    • 1842405431 scopus 로고    scopus 로고
    • Yeast cycloheximide-resistant crl mutants are proteasome mutants defective in protein degradation
    • Gerlinger, U. M., M. Hoffmann, D. H. Wolf, and W. Hilt. 1997. Yeast cycloheximide-resistant crl mutants are proteasome mutants defective in protein degradation. Mol. Biol. Cell 8:2487-2499.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2487-2499
    • Gerlinger, U.M.1    Hoffmann, M.2    Wolf, D.H.3    Hilt, W.4
  • 30
    • 0027444947 scopus 로고
    • S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase
    • Ghislain, M., A. Udvardy, and C. Mann. 1993. S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase. Nature 366:358-361.
    • (1993) Nature , vol.366 , pp. 358-361
    • Ghislain, M.1    Udvardy, A.2    Mann, C.3
  • 31
    • 0028954118 scopus 로고
    • Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure
    • Gietz, R. D., R. H. Schiestl, A. R. Willems, and R. A. Woods. 1995. Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast 11:355-360.
    • (1995) Yeast , vol.11 , pp. 355-360
    • Gietz, R.D.1    Schiestl, R.H.2    Willems, A.R.3    Woods, R.A.4
  • 32
    • 0024266139 scopus 로고
    • New yeast-E. coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz, R. D., and A. Sugino. 1988. New yeast-E. coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74:527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 33
    • 0024462161 scopus 로고
    • Viral proteins containing the NTP binding pattern
    • Gorbalenya, A. E., and E. V. Koonin. 1989. Viral proteins containing the NTP binding pattern. Nucleic Acids Res. 17:8413-8437.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 8413-8437
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 34
    • 0024344173 scopus 로고
    • Two related superfamilies of putative helicases involved in replication, repair, and expression of DNA and RNA genomes
    • Gorbalenya, A. E., E. V. Koonin, A. P. Donchenko, and V. M. Blinov. 1989. Two related superfamilies of putative helicases involved in replication, repair, and expression of DNA and RNA genomes. Nucleic Acids Res. 17: 4713-4729.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4713-4729
    • Gorbalenya, A.E.1    Koonin, E.V.2    Donchenko, A.P.3    Blinov, V.M.4
  • 35
    • 0027379925 scopus 로고
    • Defective mitosis due to a mutation in the gene for a fission yeast 26S protease subunit
    • Gordon, C., G. McGurk, P. Dillon, C. Rosen, and N. D. Hastie. 1993. Defective mitosis due to a mutation in the gene for a fission yeast 26S protease subunit. Nature 366:355-357.
    • (1993) Nature , vol.366 , pp. 355-357
    • Gordon, C.1    McGurk, G.2    Dillon, P.3    Rosen, C.4    Hastie, N.D.5
  • 36
    • 0030936847 scopus 로고    scopus 로고
    • Protein quality control: Triage by chaperones and proteases
    • Gottesmann, S., S. Wickner, and M. R. Maurizi. 1997. Protein quality control: triage by chaperones and proteases. Genes Dev. 11:815-823.
    • (1997) Genes Dev. , vol.11 , pp. 815-823
    • Gottesmann, S.1    Wickner, S.2    Maurizi, M.R.3
  • 37
    • 0025947328 scopus 로고
    • The murine Mov-34 gene: Full length cDNA and genomic organization
    • Gridley, T., R. Jaenisch, and M. G. Maguire. 1991. The murine Mov-34 gene: full length cDNA and genomic organization. Genomics 11:501-507.
    • (1991) Genomics , vol.11 , pp. 501-507
    • Gridley, T.1    Jaenisch, R.2    Maguire, M.G.3
  • 39
    • 0029811218 scopus 로고    scopus 로고
    • Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
    • Hampton, R. Y., R. G. Gardner, and J. Rine. 1996. Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol. Biol. Cell 7:2029-2044.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 2029-2044
    • Hampton, R.Y.1    Gardner, R.G.2    Rine, J.3
  • 40
    • 0029165247 scopus 로고
    • Cloning and sequencing a non-ATPase subunit of the regulatory complex of the Drosophila 26S protease
    • Haracska, L., and A. Udvardy. 1995. Cloning and sequencing a non-ATPase subunit of the regulatory complex of the Drosophila 26S protease. Eur. J. Biochem. 231:720-725.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 720-725
    • Haracska, L.1    Udvardy, A.2
  • 41
    • 0030749261 scopus 로고    scopus 로고
    • Mapping the ubiquitin-binding domains in the p54 regulatory complex subunit of the Drosophila 26S protease
    • Haracska, L., and A. Udvardy. 1997. Mapping the ubiquitin-binding domains in the p54 regulatory complex subunit of the Drosophila 26S protease. FEBS Lett. 412:331-336.
    • (1997) FEBS Lett. , vol.412 , pp. 331-336
    • Haracska, L.1    Udvardy, A.2
  • 42
    • 0030887633 scopus 로고    scopus 로고
    • Ubiquitin C-terminal hydrolase is an immediate early gene essential for long term facilitation in Aplysia
    • Hegde, A. N., K. Inokuchi, W. Pei, A. Casadio, M. Ghirardi, E. R. Kandel, and J. H. Schwartz. 1997. Ubiquitin C-terminal hydrolase is an immediate early gene essential for long term facilitation in Aplysia. Cell 89:115-126.
    • (1997) Cell , vol.89 , pp. 115-126
    • Hegde, A.N.1    Inokuchi, K.2    Pei, W.3    Casadio, A.4    Ghirardi, M.5    Kandel, E.R.6    Schwartz, J.H.7
  • 43
    • 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
  • 44
    • 0026539795 scopus 로고
    • Multiple forms of the 20S multicatalytic and the 26S ubiquitin/ATP-dependent proteases from rabbit reticulocyte lysate
    • Hoffman, L., G. Pratt, and M. Rechsteiner. 1992. Multiple forms of the 20S multicatalytic and the 26S 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
  • 45
    • 0028365076 scopus 로고
    • Activation of the multicatalytic protease
    • Hoffman, L., and M. Rechsteiner. 1994. Activation of the multicatalytic protease. J. Biol. Chem. 269:16890-16895.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16890-16895
    • Hoffman, L.1    Rechsteiner, M.2
  • 46
    • 0031049548 scopus 로고    scopus 로고
    • Molecular cloning of subunit 9 of the 26S proteasome
    • Hoffman, L., and M. Rechsteiner. 1997. Molecular cloning of subunit 9 of the 26S proteasome. FEBS Lett. 404:179-184.
    • (1997) FEBS Lett. , vol.404 , pp. 179-184
    • Hoffman, L.1    Rechsteiner, M.2
  • 47
    • 16944366641 scopus 로고    scopus 로고
    • Nucleotidase activities of the 26S proteasome and its regulatory complex
    • Hoffman, L., and M. Rechsteiner. 1996. Nucleotidase activities of the 26S proteasome and its regulatory complex. J. Biol. Chem. 271:32538-32545.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32538-32545
    • Hoffman, L.1    Rechsteiner, M.2
  • 48
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson, E. S., P. C. Ma, I. M. Ota, and A. Varshavsky. 1995. A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 270:17442-17456.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 52
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 53
    • 2642659424 scopus 로고    scopus 로고
    • Personal communication
    • Lam, A., and R. Cohen. Personal communication.
    • Lam, A.1    Cohen, R.2
  • 54
    • 0030699383 scopus 로고    scopus 로고
    • Specificity of the ubiquitin isopeptidase in the PA700 regulatory complex of the 26S proteasome
    • Lam, Y. A., G. N. DeMartino, C. M. Pickart, and R. E. Cohen. 1997. Specificity of the ubiquitin isopeptidase in the PA700 regulatory complex of the 26S proteasome. J. Biol. Chem. 272:28438-28446.
    • (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
  • 55
    • 0031038169 scopus 로고    scopus 로고
    • Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
    • Lam, Y. A., W. Xu, G. N. DeMartino, and R. E. Cohen. 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
  • 56
    • 2642627725 scopus 로고    scopus 로고
    • Personal communication
    • Larsen, C., and S. Sadis. Personal communication.
    • Larsen, C.1    Sadis, S.2
  • 57
    • 0030726159 scopus 로고    scopus 로고
    • Protein translocation channels in the proteasome and other proteases
    • Larsen, C. N., and D. Finley. 1997. Protein translocation channels in the proteasome and other proteases. Cell 91:431-434.
    • (1997) Cell , vol.91 , pp. 431-434
    • Larsen, C.N.1    Finley, D.2
  • 58
    • 0028876893 scopus 로고
    • Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor
    • Lee, J. W., H. S. Choi, J. Gyuris, R. Brent, and D. D. Moore. 1995. Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. Mol. Endocrinol. 9:243-254.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 243-254
    • Lee, J.W.1    Choi, H.S.2    Gyuris, J.3    Brent, R.4    Moore, D.D.5
  • 60
    • 2642624674 scopus 로고    scopus 로고
    • Personal communication
    • Levin, D. Personal communication.
    • Levin, D.1
  • 62
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archeon T. acidophilum at 3.4 Å resolution
    • Löwe, J., D. Stock, B. Jap, P. Zwickl, W. Baumeister, and R. Huber. 1995. Crystal structure of the 20S proteasome from the archeon T. acidophilum at 3.4 Å resolution. Science 268:533-539.
    • (1995) Science , vol.268 , pp. 533-539
    • Löwe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 63
    • 0030926522 scopus 로고    scopus 로고
    • A repetitive sequence in subunits of the 26S proteasome and 20S cyclosome (APC)
    • Lupas, A., and W. Baumeister. 1997. A repetitive sequence in subunits of the 26S proteasome and 20S cyclosome (APC). Trends Biochem. Sci. 22: 195-196.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 195-196
    • Lupas, A.1    Baumeister, W.2
  • 65
    • 0026356891 scopus 로고
    • Predicted coiled-coils from protein sequences
    • Lupas, A., M. van Dyke, and J. Stock. 1991. Predicted coiled-coils from protein sequences. Science 252:1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 66
    • 0026669739 scopus 로고
    • Identification, purification, and characterization of a protein activator (PA28) of the 20S proteasome
    • Ma, C. P., C. A. Slaughter, and G. N. DeMartino. 1992. Identification, purification, and characterization of a protein activator (PA28) of the 20S proteasome. J. Biol. Chem. 267:10515-10523.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10515-10523
    • Ma, C.P.1    Slaughter, C.A.2    DeMartino, G.N.3
  • 67
    • 0028025326 scopus 로고
    • Identification, purification, and characterization of a high molecular weight ATP-dependent activator (PA700) of the 26S proteasome
    • Ma, C. P., J. H. Vu, R. J. Proske, C. A. Slaughter, and G. N. DeMartino. 1994. Identification, purification, and characterization of a high molecular weight ATP-dependent activator (PA700) of the 26S 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
  • 68
    • 0024024371 scopus 로고
    • Cycloheximide-resistant temperature-sensitive lethal mutations of S. cerevisiae
    • McCusker, J. H., and J. E. Haber. 1988. Cycloheximide-resistant temperature-sensitive lethal mutations of S. cerevisiae. Genetics 119:303-315.
    • (1988) Genetics , vol.119 , pp. 303-315
    • McCusker, J.H.1    Haber, J.E.2
  • 69
    • 0030997922 scopus 로고    scopus 로고
    • A proteasome cap subunit required for spindle pole body duplication in yeast
    • McDonald, H. B., and B. Byers. 1997. A proteasome cap subunit required for spindle pole body duplication in yeast. J. Cell Biol. 137:539-553.
    • (1997) J. Cell Biol. , vol.137 , pp. 539-553
    • McDonald, H.B.1    Byers, B.2
  • 70
    • 0027408305 scopus 로고
    • Sequence similarities between cell regulation factors, heat shock proteins and RNA helicases
    • Mian, I. S. 1993. Sequence similarities between cell regulation factors, heat shock proteins and RNA helicases. Trends Biochem. Sci. 18:125-127.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 125-127
    • Mian, I.S.1
  • 71
    • 0025339890 scopus 로고
    • A cDNA for a protein that interacts with the human immunodeficiency virus Tat trans-activator
    • Nelbrock, P., P. J. Dillon, A. Perkins, and C. R. Rosen. 1990. A cDNA for a protein that interacts with the human immunodeficiency virus Tat trans-activator. Science 248:1650-1654.
    • (1990) Science , vol.248 , pp. 1650-1654
    • Nelbrock, P.1    Dillon, P.J.2    Perkins, A.3    Rosen, C.R.4
  • 72
    • 0027230956 scopus 로고
    • Extragenic suppressors of mutations in the cytoplasmic C terminus of SEC63 define five genes in Saccharomyces cerevisiae
    • Nelson, M. K., T. Kurihara, and P. A. Silver. 1993. Extragenic suppressors of mutations in the cytoplasmic C terminus of SEC63 define five genes in Saccharomyces cerevisiae. Genetics 134:159-173.
    • (1993) Genetics , vol.134 , pp. 159-173
    • Nelson, M.K.1    Kurihara, T.2    Silver, P.A.3
  • 73
    • 0027465924 scopus 로고
    • The type 1 human immunodeficiency virus Tat binding protein is a transcription activator belonging to an additional family of evolutionarily conserved genes
    • Ohana, B., P. A. Moore, S. M. Ruben, C. D. Southgate, M. R. Green, and C. A. Rosen. 1993. The type 1 human immunodeficiency virus Tat binding protein is a transcription activator belonging to an additional family of evolutionarily conserved genes. Proc. Natl. Acad. Sci. USA 90:138-142.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 138-142
    • Ohana, B.1    Moore, P.A.2    Ruben, S.M.3    Southgate, C.D.4    Green, M.R.5    Rosen, C.A.6
  • 74
    • 0027980321 scopus 로고
    • The ubiquitin proteasome pathway is required for processing the NF-κB1 precursor protein and activation of NF-κB
    • Palombella, V. J., O. J. Rando, A. L. Goldberg, and T. Maniatis. 1994. The ubiquitin proteasome pathway is required for processing the NF-κB1 precursor protein and activation of NF-κB. Cell 78:773-785.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 75
    • 0028234770 scopus 로고
    • Distinct 19S and 20S subcomplexes of the proteasome and their distribution in the nucleus and the cytoplasm
    • Peters, J. M., W. W. Franke, and J. A. Kleinschmidt. 1994. Distinct 19S and 20S subcomplexes of the proteasome and their distribution in the nucleus and the cytoplasm. J. Biol. Chem. 269:7709-7718.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7709-7718
    • Peters, J.M.1    Franke, W.W.2    Kleinschmidt, J.A.3
  • 76
  • 77
    • 0030703686 scopus 로고    scopus 로고
    • Dynamics of proteasome distribution in living cells
    • Reits, E. A. J., A. M. Benham, J. Neefjes, and J. Trowsdale. 1997. Dynamics of proteasome distribution in living cells. EMBO J. 16:6087-6094.
    • (1997) EMBO J. , vol.16 , pp. 6087-6094
    • Reits, E.A.J.1    Benham, A.M.2    Neefjes, J.3    Trowsdale, J.4
  • 78
    • 0031001763 scopus 로고    scopus 로고
    • Specific interactions between ATPase subunits of the 26S proteasome
    • Richmond, C., C. Gorbea, and M. Rechsteiner. 1997. Specific interactions between ATPase subunits of the 26S proteasome. J. Biol. Chem. 272: 13403-13411.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13403-13411
    • Richmond, C.1    Gorbea, C.2    Rechsteiner, M.3
  • 79
    • 0029053890 scopus 로고
    • A Saccharomyces cerevisiae gene essential for viability has been conserved in evolution
    • Rinaldi, T., M. Bolotin-Fukuhara, and L. Frontali. 1995. A Saccharomyces cerevisiae gene essential for viability has been conserved in evolution. Gene 160:135-136.
    • (1995) Gene , vol.160 , pp. 135-136
    • Rinaldi, T.1    Bolotin-Fukuhara, M.2    Frontali, L.3
  • 81
    • 0026694947 scopus 로고
    • In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional electrophoresis
    • Rosenfeld, J., J. Capdevielle, J. C. Guillemont, and P. Ferrara. 1992. In-gel digestion of proteins for internal sequence analysis after one-or two-dimensional electrophoresis. Anal. Biochem. 203:173-179.
    • (1992) Anal. Biochem. , vol.203 , pp. 173-179
    • Rosenfeld, J.1    Capdevielle, J.2    Guillemont, J.C.3    Ferrara, P.4
  • 82
    • 0030061512 scopus 로고    scopus 로고
    • Identification of the gal4 suppressor Sug1 as a subunit of the yeast 26S proteasome
    • Rubin, D. M., O. Coux, I. Wefes, C. Hengartner, R. A. Young, A. L. Goldberg, and D. Finley. 1996. Identification of the gal4 suppressor Sug1 as a subunit of the yeast 26S proteasome. Nature 379:655-657.
    • (1996) Nature , vol.379 , pp. 655-657
    • Rubin, D.M.1    Coux, O.2    Wefes, I.3    Hengartner, C.4    Young, R.A.5    Goldberg, A.L.6    Finley, D.7
  • 83
    • 0029353809 scopus 로고
    • The proteasome: A protein degrading organelle?
    • Rubin, D. M., and D. Finley. 1995. The proteasome: a protein degrading organelle? Curr. Biol. 5:854-858.
    • (1995) Curr. Biol. , vol.5 , pp. 854-858
    • Rubin, D.M.1    Finley, D.2
  • 84
    • 0030464067 scopus 로고    scopus 로고
    • Isolation and characterization of SUG2: A novel ATPase family component of the yeast 26S proteasome
    • Russell, S. J., U. G. Sathyanarayana, and S. A. Johnston. 1996. Isolation and characterization of SUG2: a novel ATPase family component of the yeast 26S proteasome. J. Biol. Chem. 271:32810-32817.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32810-32817
    • Russell, S.J.1    Sathyanarayana, U.G.2    Johnston, S.A.3
  • 86
    • 0030742610 scopus 로고    scopus 로고
    • Difference between PA700-like proteasome activator complex and the regulatory complex dissociated from the 26S proteasome implies the involvement of modulating factors in the 26S proteasome assembly
    • Sawada, H., T. Akaishi, M. Katsu, and H. Yokosawa. 1997. Difference between PA700-like proteasome activator complex and the regulatory complex dissociated from the 26S proteasome implies the involvement of modulating factors in the 26S proteasome assembly. FEBS Lett. 412:521-525.
    • (1997) FEBS Lett. , vol.412 , pp. 521-525
    • Sawada, H.1    Akaishi, T.2    Katsu, M.3    Yokosawa, H.4
  • 87
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner, M., J. Huibregste, R. D. Vierstra, and P. M. Howley. 1993. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75:495-500.
    • (1993) Cell , vol.75 , pp. 495-500
    • Scheffner, M.1    Huibregste, J.2    Vierstra, R.D.3    Howley, P.M.4
  • 88
    • 0028071874 scopus 로고
    • Identification of a set of yeast genes coding for a novel family of putative ATPases with high similarity to constituents of the 26S protease complex
    • Schnall, R., G. Mannhaupt, R. Stuka, R. Tauer, S. Ehnle, C. Schwarzlose, I. Vetter, and H. Feldmann. 1994. Identification of a set of yeast genes coding for a novel family of putative ATPases with high similarity to constituents of the 26S protease complex. Yeast 10:1141-1155.
    • (1994) Yeast , vol.10 , pp. 1141-1155
    • Schnall, R.1    Mannhaupt, G.2    Stuka, R.3    Tauer, R.4    Ehnle, S.5    Schwarzlose, C.6    Vetter, I.7    Feldmann, H.8
  • 89
    • 0028841139 scopus 로고
    • Use of polymerase chain reaction epitope tagging for protein tagging in S. cerevisiae
    • Schneider, B. L., W. Seufert, B. Steiner, Q. H. Yang, and A. B. Futcher. 1995. Use of polymerase chain reaction epitope tagging for protein tagging in S. cerevisiae. Yeast 11:1265-1274.
    • (1995) Yeast , vol.11 , pp. 1265-1274
    • Schneider, B.L.1    Seufert, W.2    Steiner, B.3    Yang, Q.H.4    Futcher, A.B.5
  • 90
    • 0030297778 scopus 로고    scopus 로고
    • Characteristics of 26S proteases from fission yeast mutants which arrest in mitosis
    • Seeger, M., C. Gordon, K. Ferrell, and W. Dubiel. 1996. Characteristics of 26S proteases from fission yeast mutants which arrest in mitosis. J. Mol. Biol. 263:423-431.
    • (1996) J. Mol. Biol. , vol.263 , pp. 423-431
    • Seeger, M.1    Gordon, C.2    Ferrell, K.3    Dubiel, W.4
  • 91
    • 0026689020 scopus 로고
    • New human gene encoding a positive modulator of HIV Tat-mediated transactivation
    • Shibuya, H., K. Irie, J. Ninomiya-Tsuji, M. Goebl, T. Taniguchi, and K. Matsumoto. 1992. New human gene encoding a positive modulator of HIV Tat-mediated transactivation. Nature 357:700-702.
    • (1992) Nature , vol.357 , pp. 700-702
    • Shibuya, H.1    Irie, K.2    Ninomiya-Tsuji, J.3    Goebl, M.4    Taniguchi, T.5    Matsumoto, K.6
  • 92
    • 0028898060 scopus 로고
    • A novel essential fission yeast gene padl( + ) positively regulates papl( + )-dependent transcription and is implicated in the maintenance of chromosome structure
    • Shimanuki, M., Y. Saka, M. Yanagida, and T. Toda. 1995. A novel essential fission yeast gene padl( + ) positively regulates papl( + )-dependent transcription and is implicated in the maintenance of chromosome structure. J. Cell Sci. 108:569-579.
    • (1995) J. Cell Sci. , vol.108 , pp. 569-579
    • Shimanuki, M.1    Saka, Y.2    Yanagida, M.3    Toda, T.4
  • 93
    • 0028954475 scopus 로고
    • Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor
    • Song, H. Y., J. D. Dunbar, Y. X. Zhang, D. Guo, and D. B. Donner. 1995. Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor. J. Biol. Chem. 270:3574-3581.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3574-3581
    • Song, H.Y.1    Dunbar, J.D.2    Zhang, Y.X.3    Guo, D.4    Donner, D.B.5
  • 94
    • 0030728770 scopus 로고    scopus 로고
    • Resistance to diverse drugs and UV light conferred by overexpression of a novel 26S proteasome subunit
    • Spataro, V., T. Toda, R. Craig, M. Seeger, W. Dubiel, A. L. Harris, and C. Norbury. 1997. Resistance to diverse drugs and UV light conferred by overexpression of a novel 26S proteasome subunit. J. Biol. Chem. 272: 30470-30475.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30470-30475
    • Spataro, V.1    Toda, T.2    Craig, R.3    Seeger, M.4    Dubiel, W.5    Harris, A.L.6    Norbury, C.7
  • 95
    • 0030831134 scopus 로고    scopus 로고
    • Identification of a phylogenetically conserved Sug1 CAD member that is differentially expressed in the mouse nervous system
    • Sun, D., J. C. Swaffield, S. A. Johnston, C. E. Milligan, R. T. Zoeller, and L. M. Schwartz. 1997. Identification of a phylogenetically conserved Sug1 CAD member that is differentially expressed in the mouse nervous system. J. Neurobiol. 33:877-890.
    • (1997) J. Neurobiol. , vol.33 , pp. 877-890
    • Sun, D.1    Swaffield, J.C.2    Johnston, S.A.3    Milligan, C.E.4    Zoeller, R.T.5    Schwartz, L.M.6
  • 97
    • 0026681291 scopus 로고
    • Alterations in a yeast protein resembling HIV Tat-binding protein relieve requirement for an acidic activation domain in GAL4
    • Swaffield, J. C., J. F. Bromberg, and S. A. Johnston. 1992. Alterations in a yeast protein resembling HIV Tat-binding protein relieve requirement for an acidic activation domain in GAL4. Nature 357:700-702.
    • (1992) Nature , vol.357 , pp. 700-702
    • Swaffield, J.C.1    Bromberg, J.F.2    Johnston, S.A.3
  • 98
    • 0011188052 scopus 로고    scopus 로고
    • Specific developmental changes in the regulatory subunits of the 26S proteasome in intersegmental muscles preceding eclosion in Manduca sexta
    • Takayanagi, K., S. Dawson, S. E. Reynolds, and R. J. Mayer. 1996, Specific developmental changes in the regulatory subunits of the 26S proteasome in intersegmental muscles preceding eclosion in Manduca sexta. Biochem. Biophys. Res. Commun. 228:517-523.
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 517-523
    • Takayanagi, K.1    Dawson, S.2    Reynolds, S.E.3    Mayer, R.J.4
  • 100
    • 2642602124 scopus 로고    scopus 로고
    • Personal communication
    • Toh-e, A., and K. Tanaka. Personal communication.
    • Toh-e, A.1    Tanaka, K.2
  • 101
    • 0029029476 scopus 로고
    • cDNA cloning of p40, a regulatory subunit of the human 26S proteasome, and a homolog of the Mov-34 gene product
    • Tsurumi, C., G. N. DeMartino, C. A. Slaughter, N. Shimbara, and K. Tanaka. 1995. cDNA cloning of p40, a regulatory subunit of the human 26S proteasome, and a homolog of the Mov-34 gene product. Biochem. Biophys. Res. Commun. 210:600-608.
    • (1995) Biochem. Biophys. Res. Commun. , vol.210 , pp. 600-608
    • Tsurumi, C.1    DeMartino, G.N.2    Slaughter, C.A.3    Shimbara, N.4    Tanaka, K.5
  • 103
    • 0027502883 scopus 로고
    • Purification and characterisation of a multiprotein component of the Drosophila 26S proteolytic complex
    • Udvardy, A. 1993. Purification and characterisation of a multiprotein component of the Drosophila 26S proteolytic complex. J. Biol. Chem. 268: 9055-9062.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9055-9062
    • Udvardy, A.1
  • 104
    • 0027319343 scopus 로고
    • Purification and characterisation of the 26S proteasome complex catalysing ATP dependent breakdown of ubiquitin ligated proteins from rat liver
    • Ugai, S. I., T. Tamura, N. Tanahashi, S. Takai, N. Komi, C. H. Chung, K. Tanaka, and A. Ichihara. 1993. Purification and characterisation of the 26S proteasome complex catalysing 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.I.1    Tamura, T.2    Tanahashi, N.3    Takai, S.4    Komi, N.5    Chung, C.H.6    Tanaka, K.7    Ichihara, A.8
  • 105
    • 0030033982 scopus 로고    scopus 로고
    • Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome
    • van Nocker, S., Q. Deveraux, M. Rechsteiner, and R. D. Vierstra. 1996. Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome. Proc. Natl. Acad. Sci. USA 93:856-860.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 856-860
    • Van Nocker, S.1    Deveraux, Q.2    Rechsteiner, M.3    Vierstra, R.D.4
  • 106
    • 0029806477 scopus 로고    scopus 로고
    • The multiubiquitin chain binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover
    • van Nocker, S., S. Sadis, D. M. Rubin, M. H. Glickman, H. Fu, O. Coux, I. Wefes, D. Finley, and R. D. Vierstra. 1996. The multiubiquitin chain binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover. Mol. Cell. Biol. 11:6020-6028.
    • (1996) Mol. Cell. Biol. , vol.11 , pp. 6020-6028
    • Van Nocker, S.1    Sadis, S.2    Rubin, D.M.3    Glickman, M.H.4    Fu, H.5    Coux, O.6    Wefes, I.7    Finley, D.8    Vierstra, R.D.9
  • 107
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., M. Sarasate, M. J. Runswick, and N. J. Gay. 1982. Distantly related sequences in the α-and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1:945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Sarasate, M.2    Runswick, M.J.3    Gay, N.J.4
  • 108
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin proteasome pathway
    • Ward, C. L., S. Omura, and R. R. Kopito. 1995. Degradation of CFTR by the ubiquitin proteasome pathway. Cell 83:121-127.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 109
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in a dilute solution in the presence of detergents and lipids
    • Wessel, D., and U. I. Flugge. 1984. A method for the quantitative recovery of protein in a dilute solution in the presence of detergents and lipids. Anal. Biochem. 138:141-143.
    • (1984) Anal. Biochem. , vol.138 , pp. 141-143
    • Wessel, D.1    Flugge, U.I.2
  • 110
    • 0030808452 scopus 로고    scopus 로고
    • Mts4, a non-ATPase subunit of the 26S proteasc in fission yeast, is essential for mitosis and interacts directly with the ATPase subunit Mts2
    • Wilkinson, C. R. M., M. Wallace, M. Seeger, W. Dubiel, and C. Gordon. 1997. Mts4, a non-ATPase subunit of the 26S proteasc in fission yeast, is essential for mitosis and interacts directly with the ATPase subunit Mts2. J. Biol. Chem. 272:25768-25777.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25768-25777
    • Wilkinson, C.R.M.1    Wallace, M.2    Seeger, M.3    Dubiel, W.4    Gordon, C.5
  • 111
    • 0028823598 scopus 로고
    • Metabolism of the polyubiquitin degradation signal: Structure, mechanism, and role of isopeptidase T
    • Wilkinson, K. D., V. L. Tashayev, L. B. O'Connor, C. N. Larsen, E. Kasperel, and C. M. Pickart. 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    Kasperel, E.5    Pickart, C.M.6
  • 113
    • 0032489524 scopus 로고    scopus 로고
    • Characterization of two polyubiquitin binding sites in the 26 S protease subunit 5a
    • Young, P., Q. Deveraux, R. E. Beal, C. M. Pickart, and M. Rechsteiner. 1998. Characterization of two polyubiquitin binding sites in the 26 S protease subunit 5a. J. Biol. Chem. 273:5461-5467.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5461-5467
    • Young, P.1    Deveraux, Q.2    Beal, R.E.3    Pickart, C.M.4    Rechsteiner, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.