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Volumn 76, Issue 1, 2000, Pages 103-114

Structural and functional characterization of 20S and 26S proteasomes from bovine brain

Author keywords

20S proteasome; 26S proteasome; Bovine brain

Indexed keywords

ADENOSINE TRIPHOSPHATE; PEPTIDASE; PROTEASOME;

EID: 0034629520     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-328X(99)00337-X     Document Type: Article
Times cited : (23)

References (48)
  • 1
    • 0029891018 scopus 로고    scopus 로고
    • Purification and properties of the 26S proteasome from rat brain: Evidence for its degradation of myelin basic protein in a ubiquitin-dependent manner
    • Akaishi T., Shiomi T., Sawada H., Yokosawa H. Purification and properties of the 26S proteasome from rat brain: evidence for its degradation of myelin basic protein in a ubiquitin-dependent manner. Brain Res. 722:1996;139-144.
    • (1996) Brain Res. , vol.722 , pp. 139-144
    • Akaishi, T.1    Shiomi, T.2    Sawada, H.3    Yokosawa, H.4
  • 2
    • 0024350915 scopus 로고
    • The presence of ATP+ubiquitin-dependent proteinase and multicatalytic proteinase complex in bovine brain
    • Azaryan A., Banay-Schwartz M., Lajtha A. The presence of ATP+ubiquitin-dependent proteinase and multicatalytic proteinase complex in bovine brain. Neurochem. Res. 14:1989;995-1001.
    • (1989) Neurochem. Res. , vol.14 , pp. 995-1001
    • Azaryan, A.1    Banay-Schwartz, M.2    Lajtha, A.3
  • 3
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister W., Walz J., Zühl F., Seemüller E. The proteasome: paradigm of a self-compartmentalizing protease. Cell. 92:1998;367-380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zühl, F.3    Seemüller, E.4
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0026669739 scopus 로고
    • Identification, purification and characterization of a protein activator of the 20S proteasome (Macropain)
    • Chu-Ping M., Slaughter C.A., DeMartino G.N. Identification, purification and characterization of a protein activator of the 20S proteasome (Macropain). J. Biol. Chem. 267:1992;10515-10523.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10515-10523
    • Chu-Ping, M.1    Slaughter, C.A.2    Demartino, G.N.3
  • 6
    • 0028025326 scopus 로고
    • Identification, purification, and characterization of a high molecular weight, ATP-dependent activator (PA700) of the 20S proteasome
    • Chu-Ping M., Vu J.H., Proske R.J., Slaughter C.A., DeMartino G.N. Identification, purification, and characterization of a high molecular weight, ATP-dependent activator (PA700) of the 20S proteasome. J. Biol. Chem. 269:1994;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
  • 7
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome pathway
    • Ciechanover A. The ubiquitin-proteasome pathway. Cell. 79:1994;13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 8
    • 0028500556 scopus 로고
    • The ubiquitin-mediated proteolytic pathway: Mechanisms of action and cellular physiology
    • Ciechanover A. The ubiquitin-mediated proteolytic pathway: mechanisms of action and cellular physiology. Biol. Chem. Hoppe-Seyler. 375:1994;565-581.
    • (1994) Biol. Chem. Hoppe-Seyler , vol.375 , pp. 565-581
    • Ciechanover, A.1
  • 9
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux O., Tanaka K., Goldberg A.L. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65:1996;801-847.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 10
    • 0029039632 scopus 로고
    • Studies of the activation by ATP of the 26S proteasome complex from rat skeletal muscle
    • Dahlmann B., Kuehn L., Reinauer H. Studies of the activation by ATP of the 26S proteasome complex from rat skeletal muscle. Biochem. J. 309:1995;195-202.
    • (1995) Biochem. J. , vol.309 , pp. 195-202
    • Dahlmann, B.1    Kuehn, L.2    Reinauer, H.3
  • 12
    • 0026498493 scopus 로고
    • Purification of an 11S regulator of the multicatalytic protease
    • Dubiel W., Pratt G., Ferrell K., Rechsteiner M. Purification of an 11S regulator of the multicatalytic protease. J. Biol. Chem. 267:1992;22369-22377.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22369-22377
    • Dubiel, W.1    Pratt, G.2    Ferrell, K.3    Rechsteiner, M.4
  • 13
    • 0029186099 scopus 로고
    • Subunits of the regulatory complex of the 26S protease
    • Dubiel W., Ferrell K., Rechsteiner M. Subunits of the regulatory complex of the 26S protease. Mol. Biol. Rep. 21:1995;27-34.
    • (1995) Mol. Biol. Rep. , vol.21 , pp. 27-34
    • Dubiel, W.1    Ferrell, K.2    Rechsteiner, M.3
  • 14
    • 85058247630 scopus 로고    scopus 로고
    • Unified nomenclature for subunits of the Saccharomyces cerevisiae proteasome regulatory particle
    • Finley D.et al. Unified nomenclature for subunits of the Saccharomyces cerevisiae proteasome regulatory particle. TIBS. 23:1998;244-245.
    • (1998) TIBS , vol.23 , pp. 244-245
    • Finley, D.1
  • 15
    • 0024976878 scopus 로고
    • Ubiquitous variations in nerves
    • Gallo J.-M., Anderton B.H. Ubiquitous variations in nerves. Nature. 337:1989;687-688.
    • (1989) Nature , vol.337 , pp. 687-688
    • Gallo, J.-M.1    Anderton, B.H.2
  • 18
    • 0030248766 scopus 로고
    • Peptide antigen production by the proteasome: Complexity provides efficiency
    • Groettrup M., Soza A., Kuckelkorn U., Kloetzel P.-M. Peptide antigen production by the proteasome: complexity provides efficiency. Immunol. Today. 17:1986;429-435.
    • (1986) Immunol. Today , vol.17 , pp. 429-435
    • Groettrup, M.1    Soza, A.2    Kuckelkorn, U.3    Kloetzel, P.-M.4
  • 21
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko A., Ciechanover A. The ubiquitin system for protein degradation. Annu. Rev. Biochem. 61:1992;761-807.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 22
    • 0026539795 scopus 로고
    • Multiple forms of the 20S multicatalytic and the 26S ubiquitin/ATP-dependent proteases from rabbit reticulocytes lysate
    • Hoffman L., Pratt G., Rechsteiner M. Multiple forms of the 20S multicatalytic and the 26S ubiquitin/ATP-dependent proteases from rabbit reticulocytes lysate. J. Biol. Chem. 267:1992;22362-22368.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22362-22368
    • Hoffman, L.1    Pratt, G.2    Rechsteiner, M.3
  • 23
    • 0022967107 scopus 로고
    • Ubiquitin lysozyme conjugates: Purification and susceptibility to proteolysis
    • Hough R., Rechsteiner M. Ubiquitin lysozyme conjugates: purification and susceptibility to proteolysis. J. Biol. Chem. 261:1986;2391-2399.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2391-2399
    • Hough, R.1    Rechsteiner, M.2
  • 24
    • 0023655017 scopus 로고
    • Purification of two high molecular weight proteases from rabbit reticulocytes lysate
    • Hough R., Pratt G., Rechsteiner M. Purification of two high molecular weight proteases from rabbit reticulocytes lysate. J. Biol. Chem. 262:1987;8303-8313.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8303-8313
    • Hough, R.1    Pratt, G.2    Rechsteiner, M.3
  • 25
    • 0026539331 scopus 로고
    • Alzheimer's disease: A cell biological perspective
    • Kosik K.S. Alzheimer's disease: a cell biological perspective. Science. 256:1992;780-783.
    • (1992) Science , vol.256 , pp. 780-783
    • Kosik, K.S.1
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0025326719 scopus 로고
    • Ubiquitin carboxyl-terminal hydrolase (PGP 9.5) is selectively present in ubiquitinylated inclusion bodies characteristic of human neurodegenerative diseases
    • Lowe J., McDermott H., Landon M., Mayer R.J., Wilkinson K.D. Ubiquitin carboxyl-terminal hydrolase (PGP 9.5) is selectively present in ubiquitinylated inclusion bodies characteristic of human neurodegenerative diseases. J. Pathol. 161:1990;153-160.
    • (1990) J. Pathol. , vol.161 , pp. 153-160
    • Lowe, J.1    McDermott, H.2    Landon, M.3    Mayer, R.J.4    Wilkinson, K.D.5
  • 30
    • 0024600924 scopus 로고
    • The high molecular weight multicatalytic proteinase, macropain, exists in a latent form in human erythrocytes
    • McGuire M.J., McCullough M.L., Croall D.E., DeMartino G.N. The high molecular weight multicatalytic proteinase, macropain, exists in a latent form in human erythrocytes. Biochim. Biophys. Acta. 995:1989;181-186.
    • (1989) Biochim. Biophys. Acta , vol.995 , pp. 181-186
    • McGuire, M.J.1    McCullough, M.L.2    Croall, D.E.3    Demartino, G.N.4
  • 31
    • 0023140474 scopus 로고
    • Ubiquitin is a component of paired helical filaments in Alzheimer disease
    • Mori H., Kondo J., Ihara Y. Ubiquitin is a component of paired helical filaments in Alzheimer disease. Science. 235:1987;1641-1644.
    • (1987) Science , vol.235 , pp. 1641-1644
    • Mori, H.1    Kondo, J.2    Ihara, Y.3
  • 32
    • 0027193036 scopus 로고
    • Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments
    • Morishima-Kawashima M., Hasegawa M., Takio K., Suzuki M., Titani K., Ihara Y. Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments. Neuron. 10:1993;1151-1160.
    • (1993) Neuron , vol.10 , pp. 1151-1160
    • Morishima-Kawashima, M.1    Hasegawa, M.2    Takio, K.3    Suzuki, M.4    Titani, K.5    Ihara, Y.6
  • 33
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
    • Morrissey J. Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Anal. Biochem. 117:1981;307-310.
    • (1981) Anal. Biochem. , vol.117 , pp. 307-310
    • Morrissey, J.1
  • 35
    • 0029051233 scopus 로고
    • Cell ubiquitination: The destructive end of mitosis
    • Murray A. Cell ubiquitination: the destructive end of mitosis. Cell. 81:1995;149-152.
    • (1995) Cell , vol.81 , pp. 149-152
    • Murray, A.1
  • 36
    • 0025727517 scopus 로고
    • Identification of an ubiquitin- And ATP-dependent protein degradation pathway in rat cerebral cortex
    • Okada M., Ishikawa M., Mizushima Y. Identification of an ubiquitin- and ATP-dependent protein degradation pathway in rat cerebral cortex. Biochim. Biophys. Acta. 1073:1991;514-520.
    • (1991) Biochim. Biophys. Acta , vol.1073 , pp. 514-520
    • Okada, M.1    Ishikawa, M.2    Mizushima, Y.3
  • 37
    • 0024351497 scopus 로고
    • Pituitary multicatalytic proteinase complex. Specificity of components and aspects of proteolytic activity
    • Orlowski M., Michaud C. Pituitary multicatalytic proteinase complex. Specificity of components and aspects of proteolytic activity. Biochemistry. 28:1989;9270-9278.
    • (1989) Biochemistry , vol.28 , pp. 9270-9278
    • Orlowski, M.1    Michaud, C.2
  • 38
    • 0025874019 scopus 로고
    • Regulation of the peptidylglutamyl-peptide hydrolyzing activity of the pituitary multicatalytic proteinase complex
    • Orlowski M., Cardozo C., Hidalgo M.C., Michaud C. Regulation of the peptidylglutamyl-peptide hydrolyzing activity of the pituitary multicatalytic proteinase complex. Biochemistry. 30:1991;5999-6005.
    • (1991) Biochemistry , vol.30 , pp. 5999-6005
    • Orlowski, M.1    Cardozo, C.2    Hidalgo, M.C.3    Michaud, C.4
  • 39
    • 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 aminoacids
    • Orlowski M., Cardozo C., Michaud C. 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 aminoacids. Biochemistry. 32:1993;1563-1572.
    • (1993) Biochemistry , vol.32 , pp. 1563-1572
    • Orlowski, M.1    Cardozo, C.2    Michaud, C.3
  • 40
    • 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., 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
  • 42
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the 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., Goldberg A.L. Inhibitors of the proteasome block the 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
  • 43
    • 0032168508 scopus 로고    scopus 로고
    • Active site mutants in the six regulatory particles ATPases reveal multiple roles for ATP in the proteasome
    • Rubin D.M., Glickman M.H., Larsen C.N., Dhruvakumar S., Finley D. Active site mutants in the six regulatory particles ATPases reveal multiple roles for ATP in the proteasome. EMBO J. 17:1998;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
  • 44
    • 0027442427 scopus 로고
    • Different ratios in 20S proteasomes and regulatory subunit complexes in two isoforms of the 26S proteasome purified from rabbit skeletal muscle
    • Sawada H.H., Muto K., Fujimuro M., Akaishi T., Sawada M.T., Yokosawa H., Goldberg A.L. Different ratios in 20S proteasomes and regulatory subunit complexes in two isoforms of the 26S proteasome purified from rabbit skeletal muscle. FEBS Lett. 335:1993;207-212.
    • (1993) FEBS Lett. , vol.335 , pp. 207-212
    • Sawada, H.H.1    Muto, K.2    Fujimuro, M.3    Akaishi, T.4    Sawada, M.T.5    Yokosawa, H.6    Goldberg, A.L.7
  • 45
    • 0033016291 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and pathogenesis of human diseases
    • Schwartz A.L., Ciechanover A. The ubiquitin-proteasome pathway and pathogenesis of human diseases. Annu. Rev. Med. 50:1999;57-74.
    • (1999) Annu. Rev. Med. , vol.50 , pp. 57-74
    • Schwartz, A.L.1    Ciechanover, A.2
  • 47
    • 0028267440 scopus 로고
    • Normal and abnormal biology of the beta-amyloid precursor protein
    • Selkoe D.J. Normal and abnormal biology of the beta-amyloid precursor protein. Annu. Rev. Neurosci. 17:1994;489-517.
    • (1994) Annu. Rev. Neurosci. , vol.17 , pp. 489-517
    • Selkoe, D.J.1
  • 48
    • 0021154990 scopus 로고
    • Immunoblotting and immunobinding current status and outlook
    • Towbin H., Gordon J. Immunoblotting and immunobinding current status and outlook. J. Immunol. Methods. 72:1984;313-340.
    • (1984) J. Immunol. Methods , vol.72 , pp. 313-340
    • Towbin, H.1    Gordon, J.2


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