메뉴 건너뛰기




Volumn 238, Issue 2, 1996, Pages 453-462

Phosphorylation of proteasomes in mammalian cells Identification of two phosphorylated subunits and the effect of phosphorylation on activity

Author keywords

26S protease; Peptidase activity; Phosphorylation; Proteasome; Regulation

Indexed keywords

MAMMALIA;

EID: 0029892643     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0453z.x     Document Type: Article
Times cited : (116)

References (63)
  • 1
    • 0027516156 scopus 로고
    • Proteasomes-multicatalytic proteinase complexes
    • Rivett, A. J. (1993) Proteasomes-multicatalytic proteinase complexes, Biochem. J. 291, 1-10.
    • (1993) Biochem. J. , vol.291 , pp. 1-10
    • Rivett, A.J.1
  • 3
    • 0028132691 scopus 로고
    • Proteasomes - Protein degradation machines of the cell
    • Peters, J.-M. (1994) Proteasomes - Protein degradation machines of the cell, Trends Biochem. Sci. 19, 377-382.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 377-382
    • Peters, J.-M.1
  • 4
    • 0029353809 scopus 로고
    • The proteasome: A protein-degrading organelle?
    • Rubin, D. M. & Finley, D. (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
  • 5
    • 0026600718 scopus 로고
    • Cloning and sequencing of the gene encoding the large (α-) subunit of the proteasome from Thermoplasma acidophilum
    • Zwickl, P., Lottspeich, F., Dahlmann, B. & Baumeister, W. (1992) Cloning and sequencing of the gene encoding the large (α-) subunit of the proteasome from Thermoplasma acidophilum, Biochemistry 31, 964-972.
    • (1992) Biochemistry , vol.31 , pp. 964-972
    • Zwickl, P.1    Lottspeich, F.2    Dahlmann, B.3    Baumeister, W.4
  • 6
    • 0026649077 scopus 로고
    • Use of serine-protease inhibitors as probes for the different proteolytic activities of the rat liver multicatalytic proteinase complex
    • Djaballah, H., Harness, J. A., Savory, P. J. & Rivett, A. J. (1992) Use of serine-protease inhibitors as probes for the different proteolytic activities of the rat liver multicatalytic proteinase complex, Eur. J. Biochem. 209, 629-634.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 629-634
    • Djaballah, H.1    Harness, J.A.2    Savory, P.J.3    Rivett, A.J.4
  • 7
    • 0027410433 scopus 로고
    • Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acids
    • Orlowski, M., Cardozo, C. & Michaud, C. (1993) Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acids, Biochemistry 32, 1563-1572.
    • (1993) Biochemistry , vol.32 , pp. 1563-1572
    • Orlowski, M.1    Cardozo, C.2    Michaud, C.3
  • 8
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko, A. & Ciechanover, A. (1992) The ubiquitin system for protein degradation, Annu. Rev. Biochem. 61, 761-807.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 9
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome pathway
    • Ciechanover, A. (1994) The ubiquitin-proteasome pathway, Cell 79, 13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 10
    • 0028935165 scopus 로고
    • Ubiquitin and intracellular protein degradation
    • Hochstrasser, M. (1995) Ubiquitin and intracellular protein degradation, Curr. Opin. Cell Biol. 7, 215-223.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 215-223
    • Hochstrasser, M.1
  • 11
    • 0028025326 scopus 로고
    • Identification, purification, and characterization of a high molecular mass, ATP-dependent activator (PA700) of the 20S proteasome
    • Chu-Ping, M., Vu, J. H., Proske, R. J., Slaughter, C. A. & DeMartino, G. N. (1994) Identification, purification, and characterization of a high molecular mass, ATP-dependent activator (PA700) of the 20S proteasome, J. Biol. Chem. 269, 3539-3547.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3539-3547
    • Chu-Ping, M.1    Vu, J.H.2    Proske, R.J.3    Slaughter, C.A.4    DeMartino, G.N.5
  • 12
    • 0027983803 scopus 로고
    • Molecular cloning and expression of a γ-interferon-inducible activator of the multicatalytic protease
    • Realini, C., Dubiel, W., Pratt, G., Ferrell, K. & Rechsteiner, M. (1994) Molecular cloning and expression of a γ-interferon-inducible activator of the multicatalytic protease, J. Biol. Chem. 269, 20727-20732.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20727-20732
    • Realini, C.1    Dubiel, W.2    Pratt, G.3    Ferrell, K.4    Rechsteiner, M.5
  • 13
    • 0029186099 scopus 로고
    • Subunits of the regulatory complex of the 26S protease
    • Dubiel, W., Ferrell, K. & Rechsteiner, M. (1995) Subunits of the regulatory complex of the 26S protease, Mol. Biol. Reports 21, 27-34.
    • (1995) Mol. Biol. Reports , vol.21 , pp. 27-34
    • Dubiel, W.1    Ferrell, K.2    Rechsteiner, M.3
  • 14
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
    • Palombella, V. J., Rando, O. J., Goldberg, A. L. & Maniatis, T. (1994) The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the 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
  • 15
    • 0027997223 scopus 로고
    • Components of a system that ligates cyclin to ubiquitin and their regulation by the protein kinase cdc2
    • Hershko, A., Ganoth, D., Sudakin, V., Dahan, A., Cohen, L., Luca, F. C., Ruderman, J. V. & Eytan, E. (1994) Components of a system that ligates cyclin to ubiquitin and their regulation by the protein kinase cdc2, J. Biol. Chem. 269, 4940-4946.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4940-4946
    • Hershko, A.1    Ganoth, D.2    Sudakin, V.3    Dahan, A.4    Cohen, L.5    Luca, F.C.6    Ruderman, J.V.7    Eytan, E.8
  • 16
    • 0027493245 scopus 로고
    • Proteasome and cell cycle: Evidence for a regulatory role of the protease on mitotic cyclins in yeast
    • Richter-Ruoff, B. & Wolf, D. H. (1993) Proteasome and cell cycle: Evidence for a regulatory role of the protease on mitotic cyclins in yeast, FEBS Lett. 336, 34-36.
    • (1993) FEBS Lett. , vol.336 , pp. 34-36
    • Richter-Ruoff, B.1    Wolf, D.H.2
  • 18
    • 0028205144 scopus 로고
    • Mutations in Prg1, a yeast proteasome related gene, cause defects in nuclear division and are suppressed by deletion of a mitotic cyclin gene
    • Friedman, H. & Snyder, M. (1994) Mutations in Prg1, a yeast proteasome related gene, cause defects in nuclear division and are suppressed by deletion of a mitotic cyclin gene, Proc. Natl Acad. Sci. USA 91, 2031-2035.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 2031-2035
    • Friedman, H.1    Snyder, M.2
  • 19
    • 0027379925 scopus 로고
    • Defective mitosis due to a mutation in the gene tor a fission yeast 26S protease subunit
    • Gordon, C., McGurk, G., Dillon, P., Rosen, C. & Hastie, N. D. (1993) Defective mitosis due to a mutation in the gene tor 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
  • 20
    • 0027444947 scopus 로고
    • S. cerevisiae 26 S prorease mutants arrest cell division in G2/metaphase
    • Ghislain, M., Udvardy, A. & Mann, C. (1993) S. cerevisiae 26 S prorease 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
  • 21
    • 0029068172 scopus 로고
    • Ubiquitinylation is not an absolute requirement for degradation of c-Jun protein by the 26S proteasome
    • Jariel-Encontre, I., Pariat, M., Martin, F., Carillo, S., Salvat, C. & Piechaczyk, M. (1995) Ubiquitinylation is not an absolute requirement for degradation of c-Jun protein by the 26S proteasome, J. Biol. Chem. 270, 11623-11627.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11623-11627
    • Jariel-Encontre, I.1    Pariat, M.2    Martin, F.3    Carillo, S.4    Salvat, C.5    Piechaczyk, M.6
  • 22
    • 0025771623 scopus 로고
    • A proteasome-related gene between the 2 ABC transporter loci in the class-II region of the human MHC
    • Glynne, R., Powis, S. H., Beck, S., Kelly, A., Kerr, L.-A. & Trowsdale, J. (1991) A proteasome-related gene between the 2 ABC transporter loci in the class-II region of the human MHC, Nature 353, 357-360.
    • (1991) Nature , vol.353 , pp. 357-360
    • Glynne, R.1    Powis, S.H.2    Beck, S.3    Kelly, A.4    Kerr, L.-A.5    Trowsdale, J.6
  • 23
    • 0025886546 scopus 로고
    • Structural and serological similarity of MHC-linked LMP and proteasome (multicatalytic proteinase) complexes
    • Brown, M. G., Driscoll, J. & Monaco, J. J. (1991) Structural and serological similarity of MHC-linked LMP and proteasome (multicatalytic proteinase) complexes, Nature 353, 355-357.
    • (1991) Nature , vol.353 , pp. 355-357
    • Brown, M.G.1    Driscoll, J.2    Monaco, J.J.3
  • 25
    • 0028109918 scopus 로고
    • Pre5 and Pre6, the last missing genes encoding 20S proteasome subunits from yeast - Indication for a set of 14 different subunits in the eukaryotic proteasome core
    • Heinemeyer, W., Tröndle, N., Albrecht, G. & Wolf, D. H. (1994) Pre5 and Pre6, the last missing genes encoding 20S proteasome subunits from yeast - Indication for a set of 14 different subunits in the eukaryotic proteasome core, Biochemistry 33, 12229-12237.
    • (1994) Biochemistry , vol.33 , pp. 12229-12237
    • Heinemeyer, W.1    Tröndle, N.2    Albrecht, G.3    Wolf, D.H.4
  • 26
    • 0026890061 scopus 로고
    • Enhanced levels of multicatalytic proteinase messenger RNAs in Rous-sarcoma virus transformed cells
    • Balson, D. F., Skilton, H., Sweeney, S., Thomson, S. & Rivett, A. J. (1992) Enhanced levels of multicatalytic proteinase messenger RNAs in Rous-sarcoma virus transformed cells, Biol. Chem. Hoppe-Seyler 373, 623-628.
    • (1992) Biol. Chem. Hoppe-Seyler , vol.373 , pp. 623-628
    • Balson, D.F.1    Skilton, H.2    Sweeney, S.3    Thomson, S.4    Rivett, A.J.5
  • 27
    • 0026783274 scopus 로고
    • Regulation of gene expression of proteasomes (multi-protease complexes) during growth and differentiation of human hematopoietic cells
    • Shimbara, N., Orino, E., Sone, S., Ogura, T., Takashina, M., Shono, M., Tamura, T., Yasuda, H., Tanaka, K. & Ichihara, A. (1992) Regulation of gene expression of proteasomes (multi-protease complexes) during growth and differentiation of human hematopoietic cells, J. Biol. Chem. 267, 18100-18109.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18100-18109
    • Shimbara, N.1    Orino, E.2    Sone, S.3    Ogura, T.4    Takashina, M.5    Shono, M.6    Tamura, T.7    Yasuda, H.8    Tanaka, K.9    Ichihara, A.10
  • 29
    • 0028077607 scopus 로고
    • Differential synthesis and cytolocalization of prosomes in chick embryos during development
    • Pal, J. K., Martins De Sa, C. & Scherrer, K. (1994) Differential synthesis and cytolocalization of prosomes in chick embryos during development, Int. J. Dev. Biol. 38, 525-534.
    • (1994) Int. J. Dev. Biol. , vol.38 , pp. 525-534
    • Pal, J.K.1    Martins De Sa, C.2    Scherrer, K.3
  • 31
    • 0024497473 scopus 로고
    • The Drosophila proteasome undergoes changes in its subunit pattern during development
    • Haass, C. & Kloetzel, P.-M. (1989) The Drosophila proteasome undergoes changes in its subunit pattern during development. Exp. Cell Res. 180, 243-252.
    • (1989) Exp. Cell Res. , vol.180 , pp. 243-252
    • Haass, C.1    Kloetzel, P.-M.2
  • 33
    • 0024447840 scopus 로고
    • The Pros-35 gene encodes the 35kD protein subunit of Drosophila melanogaster proteasome
    • Haass, C., Pesold-Hurt, B., Multhaup, G., Beyreuther, K. & Kloetzel, P.-M. (1989) The Pros-35 gene encodes the 35kD protein subunit of Drosophila melanogaster proteasome, EMBO J. 8, 2373-2379.
    • (1989) EMBO J. , vol.8 , pp. 2373-2379
    • Haass, C.1    Pesold-Hurt, B.2    Multhaup, G.3    Beyreuther, K.4    Kloetzel, P.-M.5
  • 34
    • 0025102687 scopus 로고
    • The Drosophila Pros-28.1 gene is a member of the proteasome gene family
    • Haass, C., Pesold-Hurt, B., Multhaup, G., Beyreuther, K. & Kloetzel, P.-M. (1990) The Drosophila Pros-28.1 gene is a member of the proteasome gene family, Gene 90, 235-241.
    • (1990) Gene , vol.90 , pp. 235-241
    • Haass, C.1    Pesold-Hurt, B.2    Multhaup, G.3    Beyreuther, K.4    Kloetzel, P.-M.5
  • 36
    • 0025012292 scopus 로고
    • Phosphorylation of the multicatalytic proteinase complex from bovine pituitaries by a copurifying cAMP-dependent protein kinase
    • Pereira, M. E. & Wilk, S. (1990) Phosphorylation of the multicatalytic proteinase complex from bovine pituitaries by a copurifying cAMP-dependent protein kinase, Arch. Biochem. Biophys. 283, 68-74.
    • (1990) Arch. Biochem. Biophys. , vol.283 , pp. 68-74
    • Pereira, M.E.1    Wilk, S.2
  • 37
    • 0027267492 scopus 로고
    • Copurification of casein kinase II with 20S proteasomes and phosphorylation of a 30-kDa proteasome subunit
    • Ludemann, R., Lerca, K. M. & Etlinger, J. D. (1993) Copurification of casein kinase II with 20S proteasomes and phosphorylation of a 30-kDa proteasome subunit, J. Biol. Chem. 268, 17413-17417.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17413-17417
    • Ludemann, R.1    Lerca, K.M.2    Etlinger, J.D.3
  • 38
    • 0027234323 scopus 로고
    • Hela cells proteasome interacts with leucine-rich polypeptides and contains a phosphorylated subunit
    • Arrigo, A.-P. & Mehlen, P. (1993) Hela cells proteasome interacts with leucine-rich polypeptides and contains a phosphorylated subunit, Biochem. Biophys. Res. Commun. 194, 1387-1393.
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 1387-1393
    • Arrigo, A.-P.1    Mehlen, P.2
  • 39
    • 0025874217 scopus 로고
    • Properties of subunits of the multicatalytic proteinase complex revealed by the use of subunit specific antibodies
    • Rivett, A. J. & Sweeney, S. T. (1991) Properties of subunits of the multicatalytic proteinase complex revealed by the use of subunit specific antibodies, Biochem. J. 278, 171-177.
    • (1991) Biochem. J. , vol.278 , pp. 171-177
    • Rivett, A.J.1    Sweeney, S.T.2
  • 40
    • 0028673206 scopus 로고
    • Multicatalytic endopeptidase complex: Proteasome
    • Rivett, A. J., Savory, P. J. & Djaballah, M. (1994) Multicatalytic endopeptidase complex: Proteasome, Methods Enzymol. 244, 331-350.
    • (1994) Methods Enzymol. , vol.244 , pp. 331-350
    • Rivett, A.J.1    Savory, P.J.2    Djaballah, M.3
  • 42
    • 0026498673 scopus 로고
    • Monoclonal antibodies to the human multicatalytic proteinase (proteasome)
    • Kaltoft, M.-B., Koch, C., Uerkvitz, W. & Hendil, K. B. (1992) Monoclonal antibodies to the human multicatalytic proteinase (proteasome), Hybridoma 11, 507-517.
    • (1992) Hybridoma , vol.11 , pp. 507-517
    • Kaltoft, M.-B.1    Koch, C.2    Uerkvitz, W.3    Hendil, K.B.4
  • 43
    • 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
  • 44
    • 0016711037 scopus 로고
    • High resolution, two-dimensional electrophoresis of proteins
    • O'Farrell, P. H. (1975) High resolution, two-dimensional electrophoresis of proteins, J. Biol. Chem. 250, 4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 45
    • 0021418471 scopus 로고
    • Evaluation of isoelectric-focusing running conditions during 2-dimensional isoelectric-focusing sodium dodecyl sulfate-polyacrylamide gel-electrophoresis - Variation of gel patterns with changing conditions and optimized isoelectric-focusing conditions
    • Duncan, R. & Hershey, J. W. B. (1984) Evaluation of isoelectric-focusing running conditions during 2-dimensional isoelectric-focusing sodium dodecyl sulfate-polyacrylamide gel-electrophoresis - variation of gel patterns with changing conditions and optimized isoelectric-focusing conditions, Anal. Biochem. 138, 144-155.
    • (1984) Anal. Biochem. , vol.138 , pp. 144-155
    • Duncan, R.1    Hershey, J.W.B.2
  • 46
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from acrylamide gels to nitrocellulose sheets: Procedure and applications
    • Towbin, H., Staehelin, T. & Gordon, J. (1979) Electrophoretic transfer of proteins from acrylamide gels to nitrocellulose sheets: procedure and applications, Proc. Natl Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 48
    • 0000109995 scopus 로고
    • Transforming gene product of Rous sarcoma virus phosphorylates tyrosine
    • Hunter, T. & Sefton, B. M. (1980) Transforming gene product of Rous sarcoma virus phosphorylates tyrosine, Proc. Natl Acad. Sci. USA 77, 1311-1315.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 1311-1315
    • Hunter, T.1    Sefton, B.M.2
  • 51
    • 0021112875 scopus 로고
    • Phosphorylation by cyclic GMP-dependent protein kinase of a synthetic peptide corresponding to the autophosphorylation site in the enzyme
    • Glass, D. B. & Smith, S. B. (1983) Phosphorylation by cyclic GMP-dependent protein kinase of a synthetic peptide corresponding to the autophosphorylation site in the enzyme, J. Biol. Chem. 258, 14797-14803.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14797-14803
    • Glass, D.B.1    Smith, S.B.2
  • 53
    • 1542560174 scopus 로고
    • Modulation of the multicatalytic proteinase complex by lipids, interconversion and proteolytic processing
    • Arizti, P., Arribas, J. & Castaño, J. G. (1994) Modulation of the multicatalytic proteinase complex by lipids, interconversion and proteolytic processing, Enzyme and Protein 47, 187-188.
    • (1994) Enzyme and Protein , vol.47 , pp. 187-188
    • Arizti, P.1    Arribas, J.2    Castaño, J.G.3
  • 54
    • 0027722138 scopus 로고
    • Casein kinase II in signal transduction and cell cycle regulation
    • Litchfield, D. W. & Lüscher, B. (1993) Casein kinase II in signal transduction and cell cycle regulation, Mol. Cell. Biochem. 127/ 128, 187-199.
    • (1993) Mol. Cell. Biochem. , vol.127-128 , pp. 187-199
    • Litchfield, D.W.1    Lüscher, B.2
  • 55
    • 0028802362 scopus 로고
    • The regulation of protein transport to the nucleus by phosphorylation
    • Jans, D. A. (1995) The regulation of protein transport to the nucleus by phosphorylation, Biochem. J. 311, 705-716.
    • (1995) Biochem. J. , vol.311 , pp. 705-716
    • Jans, D.A.1
  • 56
    • 0026026630 scopus 로고
    • The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T-antigen
    • Rihs, H.-P., Jans, D. A., Fan, H. & Peters, R. (1991) The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T-antigen, EMBO J. 10, 633-639.
    • (1991) EMBO J. , vol.10 , pp. 633-639
    • Rihs, H.-P.1    Jans, D.A.2    Fan, H.3    Peters, R.4
  • 57
    • 0029143239 scopus 로고
    • Nuclear multicatalytic proteinase a subunit RRC3: Differential size, tyrosine phosphorylation, and susceptibility to antisense oligonucleotide treatment
    • Benedict, C. M., Ren, L. & Clawson, G. A. (1995) Nuclear multicatalytic proteinase a subunit RRC3: Differential size, tyrosine phosphorylation, and susceptibility to antisense oligonucleotide treatment, Biochemistry 34, 9587-9598.
    • (1995) Biochemistry , vol.34 , pp. 9587-9598
    • Benedict, C.M.1    Ren, L.2    Clawson, G.A.3
  • 59
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution
    • Löwe, J., Stock, D., Jap, B., Zwickl, P. Baumeister, W. & Huber, R. (1995) Crystal structure of the 20S proteasome from the archaeon 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
  • 60
    • 0027327041 scopus 로고
    • The multicatalytic proteinase complex (proteasome): Structure and conformational changes associated with changes in proteolytic activity
    • Djaballah, H., Rowe, A. J., Harding, S. E. & Rivett, A. J. (1993) The multicatalytic proteinase complex (proteasome): structure and conformational changes associated with changes in proteolytic activity, Biochem. J. 292, 857-862.
    • (1993) Biochem. J. , vol.292 , pp. 857-862
    • Djaballah, H.1    Rowe, A.J.2    Harding, S.E.3    Rivett, A.J.4
  • 61
    • 0026498493 scopus 로고
    • Purification of an 11 S regulator of the multicalalytic protease
    • Dubiel, W. D., Pratt, G., Ferrell, K. & Rechsteiner, M. (1992) Purification of an 11 S regulator of the multicalalytic protease, J. Biol. Chem. 267, 22369-22377.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22369-22377
    • Dubiel, W.D.1    Pratt, G.2    Ferrell, K.3    Rechsteiner, M.4
  • 62
    • 0026486168 scopus 로고
    • Subunit 4 of the 26 S protease is a member of a novel eukaryotic ATPase family
    • Dubiel, W., Ferrell, K., Pratt, G. & Rechsteiner, M. (1992) Subunit 4 of the 26 S protease is a member of a novel eukaryotic ATPase family, J. Biol. Chem. 267, 22699-22702.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22699-22702
    • Dubiel, W.1    Ferrell, K.2    Pratt, G.3    Rechsteiner, M.4
  • 63
    • 0029132743 scopus 로고
    • Phosphorylation of proteasome substrate by a protein kinase associated with the 26 S proteasome is linked to the ATP-dependent proteolysis of the 26 S proteasome
    • Satoh, K., Nishikawa, T., Yokosawa, H. & Sawada, H. (1995) Phosphorylation of proteasome substrate by a protein kinase associated with the 26 S proteasome is linked to the ATP-dependent proteolysis of the 26 S proteasome, Biochem. Biophys. Res. Commun. 213, 7-14.
    • (1995) Biochem. Biophys. Res. Commun. , vol.213 , pp. 7-14
    • Satoh, K.1    Nishikawa, T.2    Yokosawa, H.3    Sawada, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.