메뉴 건너뛰기




Volumn 156, Issue 1, 2006, Pages 72-83

Proteasomes and their associated ATPases: A destructive combination

Author keywords

19S; 20S; 26S; Archaea; ATP; ATP S; ATPase; Brownian; Brownian ratchet; Degradation; Electron microscopy; EM; Gate; HbYX; LFP; PAN; Proteasomal ATPases; Proteasome; Proteasome activating nucleotidase; Protein; Protein degradation; RPT; Translocation; Turnover; YDR

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ENZYME; GLOBULAR PROTEIN; NUCLEOTIDE; PROTEASOME; PROTEASOME ACTIVATING NUCLEOTIDASE; UNCLASSIFIED DRUG;

EID: 33749234748     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2006.04.012     Document Type: Review
Times cited : (99)

References (78)
  • 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. Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum. J. Biol. Chem. 272 (1997) 1791-1798
    • (1997) J. Biol. Chem. , vol.272 , pp. 1791-1798
    • Akopian, T.N.1    Kisselev, A.F.2    Goldberg, A.L.3
  • 2
    • 0038686574 scopus 로고    scopus 로고
    • Proteasome disassembly and downregulation is correlated with viability during stationary phase
    • Bajorek M., Finley D., and Glickman M.H. Proteasome disassembly and downregulation is correlated with viability during stationary phase. Curr. Biol. 13 (2003) 1140-1144
    • (2003) Curr. Biol. , vol.13 , pp. 1140-1144
    • Bajorek, M.1    Finley, D.2    Glickman, M.H.3
  • 4
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: paradigm of a self-compartmentalizing protease
    • Baumeister W., Walz J., Zuhl F., and Seemuller 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    Zuhl, F.3    Seemuller, E.4
  • 5
    • 0033769733 scopus 로고    scopus 로고
    • PAN, the proteasome activating nucleotidase from archaebacteria, is a molecular chaperone which unfolds protein substrate
    • Benaroudj N., and Goldberg A.L. PAN, the proteasome activating nucleotidase from archaebacteria, is a molecular chaperone which unfolds protein substrate. Nat. Cell Biol. 2 (2000) 833-839
    • (2000) Nat. Cell Biol. , vol.2 , pp. 833-839
    • Benaroudj, N.1    Goldberg, A.L.2
  • 6
    • 0035067597 scopus 로고    scopus 로고
    • The unfolding of substrates and ubiquitin-independent protein degradation by proteasomes
    • Benaroudj N., Tarcsa E., Cascio P., and Goldberg A.L. The unfolding of substrates and ubiquitin-independent protein degradation by proteasomes. Biochimie 83 (2001) 311-318
    • (2001) Biochimie , vol.83 , pp. 311-318
    • Benaroudj, N.1    Tarcsa, E.2    Cascio, P.3    Goldberg, A.L.4
  • 7
    • 0037248908 scopus 로고    scopus 로고
    • ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation
    • Benaroudj N., Zwickl P., Seemuller E., Baumeister W., and Goldberg A.L. ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation. Mol. Cell 11 (2003) 69-78
    • (2003) Mol. Cell , vol.11 , pp. 69-78
    • Benaroudj, N.1    Zwickl, P.2    Seemuller, E.3    Baumeister, W.4    Goldberg, A.L.5
  • 11
    • 0037013955 scopus 로고    scopus 로고
    • Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes
    • Cascio P., Call M., Petre B.M., Walz T., and Goldberg A.L. Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes. EMBO J. 21 (2002) 2636-2645
    • (2002) EMBO J. , vol.21 , pp. 2636-2645
    • Cascio, P.1    Call, M.2    Petre, B.M.3    Walz, T.4    Goldberg, A.L.5
  • 12
    • 0013533949 scopus 로고
    • The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La
    • Chung C.H., and Goldberg A.L. The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La. Proc. Natl. Acad. Sci. USA 78 (1981) 4931-4935
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4931-4935
    • Chung, C.H.1    Goldberg, A.L.2
  • 13
    • 11244309014 scopus 로고    scopus 로고
    • Proteolysis: from the lysosome to ubiquitin and the proteasome
    • Ciechanover A. Proteolysis: from the lysosome to ubiquitin and the proteasome. Nat. Rev. Mol. Cell Biol. 6 (2005) 79-87
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 79-87
    • Ciechanover, A.1
  • 14
    • 0029328549 scopus 로고
    • A 200-amino acid ATPase module in search of a basic function
    • Confalonieri F., and Duguet M. A 200-amino acid ATPase module in search of a basic function. Bioessays 17 (1995) 639-650
    • (1995) Bioessays , vol.17 , pp. 639-650
    • Confalonieri, F.1    Duguet, M.2
  • 15
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux O., Tanaka K., and 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
  • 16
    • 0024972956 scopus 로고
    • The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteria
    • Dahlmann B., Kopp F., Kuehn L., Niedel B., Pfeifer G., Hegerl R., and Baumeister W. The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteria. FEBS Lett. 251 (1989) 125-131
    • (1989) FEBS Lett. , vol.251 , pp. 125-131
    • Dahlmann, B.1    Kopp, F.2    Kuehn, L.3    Niedel, B.4    Pfeifer, G.5    Hegerl, R.6    Baumeister, W.7
  • 17
    • 0342265782 scopus 로고
    • A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes
    • Etlinger J.D., and Goldberg A.L. A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes. Proc. Natl. Acad. Sci. USA 74 (1977) 54-58
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 54-58
    • Etlinger, J.D.1    Goldberg, A.L.2
  • 18
    • 0033976299 scopus 로고    scopus 로고
    • Regulatory subunit interactions of the 26S proteasome, a complex problem [Review]
    • Ferrell K., Wilkinson C.R.M., Dubiel W., and Gordon C. Regulatory subunit interactions of the 26S proteasome, a complex problem [Review]. Trends Biochem. Sci. 25 (2000) 83-88
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 83-88
    • Ferrell, K.1    Wilkinson, C.R.M.2    Dubiel, W.3    Gordon, C.4
  • 19
    • 19444387760 scopus 로고    scopus 로고
    • The 1.9 Å structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions
    • Forster A., Masters E.I., Whitby F.G., Robinson H., and Hill C.P. The 1.9 Å structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions. Mol. Cell 18 (2005) 589-599
    • (2005) Mol. Cell , vol.18 , pp. 589-599
    • Forster, A.1    Masters, E.I.2    Whitby, F.G.3    Robinson, H.4    Hill, C.P.5
  • 20
    • 0043192299 scopus 로고    scopus 로고
    • The pore of activated 20S proteasomes has an ordered 7-fold symmetric conformation
    • Forster A., Whitby F.G., and Hill C.P. The pore of activated 20S proteasomes has an ordered 7-fold symmetric conformation. EMBO J. 22 (2003) 4356-4364
    • (2003) EMBO J. , vol.22 , pp. 4356-4364
    • Forster, A.1    Whitby, F.G.2    Hill, C.P.3
  • 21
    • 30044443816 scopus 로고    scopus 로고
    • VAT, the thermoplasma homolog of mammalian p97/VCP, is an N domain-regulated protein unfoldase
    • Gerega A., Rockel B., Peters J., Tamura T., Baumeister W., and Zwickl P. VAT, the thermoplasma homolog of mammalian p97/VCP, is an N domain-regulated protein unfoldase. J. Biol. Chem. 280 (2005) 42856-42862
    • (2005) J. Biol. Chem. , vol.280 , pp. 42856-42862
    • Gerega, A.1    Rockel, B.2    Peters, J.3    Tamura, T.4    Baumeister, W.5    Zwickl, P.6
  • 22
    • 0028834046 scopus 로고
    • Can Hsp70 proteins act as force-generating motors?
    • Glick B.S. Can Hsp70 proteins act as force-generating motors?. Cell 80 (1995) 11-14
    • (1995) Cell , vol.80 , pp. 11-14
    • Glick, B.S.1
  • 23
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
    • Glickman M.H., and Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82 (2002) 373-428
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 24
    • 13244298289 scopus 로고    scopus 로고
    • Nobel committee tags ubiquitin for distinction
    • Goldberg A.L. Nobel committee tags ubiquitin for distinction. Neuron 45 (2005) 339-344
    • (2005) Neuron , vol.45 , pp. 339-344
    • Goldberg, A.L.1
  • 25
    • 0016908233 scopus 로고
    • Intracellular protein degradation in mammalian and bacterial cells: part 2
    • Goldberg A.L., and St. John A.C. Intracellular protein degradation in mammalian and bacterial cells: part 2. Annu. Rev. Biochem. 45 (1976) 747-803
    • (1976) Annu. Rev. Biochem. , vol.45 , pp. 747-803
    • Goldberg, A.L.1    St. John, A.C.2
  • 26
    • 0033119210 scopus 로고    scopus 로고
    • Assembly of the regulatory complex of the 26S proteasome
    • Gorbea C., Taillandier D., and Rechsteiner M. Assembly of the regulatory complex of the 26S proteasome. Mol. Biol. Rep. 26 (1999) 15-19
    • (1999) Mol. Biol. Rep. , vol.26 , pp. 15-19
    • Gorbea, C.1    Taillandier, D.2    Rechsteiner, M.3
  • 27
    • 0030444320 scopus 로고    scopus 로고
    • Proteases and their targets in Escherichia coli
    • Gottesman S. Proteases and their targets in Escherichia coli. Annu. Rev. Genet. 30 (1996) 465-506
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 465-506
    • Gottesman, S.1
  • 28
    • 0032079329 scopus 로고    scopus 로고
    • The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system
    • Gottesman S., Roche E., Zhou Y., and Sauer R.T. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev. 12 (1998) 1338-1347
    • (1998) Genes Dev. , vol.12 , pp. 1338-1347
    • Gottesman, S.1    Roche, E.2    Zhou, Y.3    Sauer, R.T.4
  • 30
    • 0037436376 scopus 로고    scopus 로고
    • Investigations on the maturation and regulation of archaebacterial proteasomes
    • Groll M., Brandstetter H., Bartunik H., Bourenkow G., and Huber R. Investigations on the maturation and regulation of archaebacterial proteasomes. J. Mol. Biol. 327 (2003) 75-83
    • (2003) J. Mol. Biol. , vol.327 , pp. 75-83
    • Groll, M.1    Brandstetter, H.2    Bartunik, H.3    Bourenkow, G.4    Huber, R.5
  • 32
    • 0037401695 scopus 로고    scopus 로고
    • Substrate access and processing by the 20S proteasome core particle
    • Groll M., and Huber R. Substrate access and processing by the 20S proteasome core particle. Int. J. Biochem. Cell Biol. 35 (2003) 606-616
    • (2003) Int. J. Biochem. Cell Biol. , vol.35 , pp. 606-616
    • Groll, M.1    Huber, R.2
  • 33
    • 0023655017 scopus 로고
    • Purification of two high molecular weight proteases from rabbit reticulocyte lysate
    • Hough R., Pratt G., and Rechsteiner M. Purification of two high molecular weight proteases from rabbit reticulocyte 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
  • 34
    • 0030881850 scopus 로고    scopus 로고
    • Proteolytic activity of the ATP-dependent protease HslVU can be uncoupled from ATP hydrolysis
    • Huang H., and Goldberg A.L. Proteolytic activity of the ATP-dependent protease HslVU can be uncoupled from ATP hydrolysis. J. Biol. Chem. 272 (1997) 21364-21372
    • (1997) J. Biol. Chem. , vol.272 , pp. 21364-21372
    • Huang, H.1    Goldberg, A.L.2
  • 35
    • 0037147328 scopus 로고    scopus 로고
    • What curves alpha-solenoids? Evidence for an alpha-helical toroid structure of Rpn1 and Rpn2 proteins of the 26 S proteasome
    • Kajava A.V. What curves alpha-solenoids? Evidence for an alpha-helical toroid structure of Rpn1 and Rpn2 proteins of the 26 S proteasome. J. Biol. Chem. 277 (2002) 49791-49798
    • (2002) J. Biol. Chem. , vol.277 , pp. 49791-49798
    • Kajava, A.V.1
  • 36
    • 0042329502 scopus 로고    scopus 로고
    • Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine
    • Kenniston J.A., Baker T.A., Fernandez J.M., and Sauer R.T. Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine. Cell 114 (2003) 511-520
    • (2003) Cell , vol.114 , pp. 511-520
    • Kenniston, J.A.1    Baker, T.A.2    Fernandez, J.M.3    Sauer, R.T.4
  • 38
    • 0031892541 scopus 로고    scopus 로고
    • Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes
    • Kisselev A.F., Akopian T.N., and Goldberg A.L. Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes. J. Biol. Chem. 273 (1998) 1982-1989
    • (1998) J. Biol. Chem. , vol.273 , pp. 1982-1989
    • Kisselev, A.F.1    Akopian, T.N.2    Goldberg, A.L.3
  • 39
    • 0034685889 scopus 로고    scopus 로고
    • Why does threonine, and not serine, function as the active site nucleophile in proteasomes
    • Kisselev A.F., Songyang Z., and Goldberg A.L. Why does threonine, and not serine, function as the active site nucleophile in proteasomes. J. Biol. Chem. 275 (2000) 14831-14837
    • (2000) J. Biol. Chem. , vol.275 , pp. 14831-14837
    • Kisselev, A.F.1    Songyang, Z.2    Goldberg, A.L.3
  • 40
    • 0034964524 scopus 로고    scopus 로고
    • The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release
    • Kohler A., Cascio P., Leggett D.S., Woo K.M., Goldberg A.L., and Finley D. The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release. Mol. Cell 7 (2001) 1143-1152
    • (2001) Mol. Cell , vol.7 , pp. 1143-1152
    • Kohler, A.1    Cascio, P.2    Leggett, D.S.3    Woo, K.M.4    Goldberg, A.L.5    Finley, D.6
  • 41
    • 0035266072 scopus 로고    scopus 로고
    • ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
    • Lee C., Schwartz M.P., Prakash S., Iwakura M., and Matouschek A. ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol. Cell 7 (2001) 627-637
    • (2001) Mol. Cell , vol.7 , pp. 627-637
    • Lee, C.1    Schwartz, M.P.2    Prakash, S.3    Iwakura, M.4    Matouschek, A.5
  • 43
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution
    • Lowe J., Stock D., Jap B., Zwickl P., Baumeister W., and Huber R. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science 268 (1995) 533-539
    • (1995) Science , vol.268 , pp. 533-539
    • Lowe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 45
    • 0027493870 scopus 로고
    • PA28, an activator of the 20 S proteasome, is inactivated by proteolytic modification at its carboxyl terminus
    • Ma C.P., Willy P.J., Slaughter C.A., and DeMartino G.N. PA28, an activator of the 20 S proteasome, is inactivated by proteolytic modification at its carboxyl terminus. J. Biol. Chem. 268 (1993) 22514-22519
    • (1993) J. Biol. Chem. , vol.268 , pp. 22514-22519
    • Ma, C.P.1    Willy, P.J.2    Slaughter, C.A.3    DeMartino, G.N.4
  • 46
    • 0033612302 scopus 로고    scopus 로고
    • BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane
    • Matlack K.E., Misselwitz B., Plath K., and Rapoport T.A. BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane. Cell 97 (1999) 553-564
    • (1999) Cell , vol.97 , pp. 553-564
    • Matlack, K.E.1    Misselwitz, B.2    Plath, K.3    Rapoport, T.A.4
  • 47
    • 0037308999 scopus 로고    scopus 로고
    • Protein unfolding-an important process in vivo?
    • Matouschek A. Protein unfolding-an important process in vivo?. Curr. Opin. Struct. Biol. 13 (2003) 98-109
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 98-109
    • Matouschek, A.1
  • 48
    • 0032568504 scopus 로고    scopus 로고
    • Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and clpP
    • Maurizi M.R., Singh S.K., Thompson M.W., Kessel M., and Ginsburg A. Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and clpP. Biochemistry 37 (1998) 7778-7786
    • (1998) Biochemistry , vol.37 , pp. 7778-7786
    • Maurizi, M.R.1    Singh, S.K.2    Thompson, M.W.3    Kessel, M.4    Ginsburg, A.5
  • 49
    • 0018676915 scopus 로고
    • Protein degradation is stimulated by ATP in extracts of Escherichia coli
    • Murakami K., Voellmy R., and Goldberg A.L. Protein degradation is stimulated by ATP in extracts of Escherichia coli. J. Biol. Chem. 254 (1979) 8194-8200
    • (1979) J. Biol. Chem. , vol.254 , pp. 8194-8200
    • Murakami, K.1    Voellmy, R.2    Goldberg, A.L.3
  • 51
    • 0035694696 scopus 로고    scopus 로고
    • Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome
    • Navon A., and Goldberg A.L. Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome. Mol. Cell 8 (2001) 1339-1349
    • (2001) Mol. Cell , vol.8 , pp. 1339-1349
    • Navon, A.1    Goldberg, A.L.2
  • 52
    • 33749249447 scopus 로고    scopus 로고
    • Navon, A., Goodman, A., Goldberg, A.L., 2006. The terminal sequences of a protein determine the direction of translocation into the proteasome and whether a distant globular domain is degraded (Manuscript in preparation).
  • 53
    • 0036798857 scopus 로고    scopus 로고
    • Chemomechanical coupling of the forward and backward steps of single kinesin molecules
    • Nishiyama M., Higuchi H., and Yanagida T. Chemomechanical coupling of the forward and backward steps of single kinesin molecules. Nat. Cell Biol. 4 (2002) 790-797
    • (2002) Nat. Cell Biol. , vol.4 , pp. 790-797
    • Nishiyama, M.1    Higuchi, H.2    Yanagida, T.3
  • 54
    • 0037249434 scopus 로고    scopus 로고
    • Dissecting various ATP-dependent steps involved in proteasomal degradation
    • Ogura T., and Tanaka K. Dissecting various ATP-dependent steps involved in proteasomal degradation. Mol. Cell 11 (2003) 3-5
    • (2003) Mol. Cell , vol.11 , pp. 3-5
    • Ogura, T.1    Tanaka, K.2
  • 55
    • 0031973716 scopus 로고    scopus 로고
    • The AAA team: related ATPases with diverse functions
    • Patel S., and Latterich M. The AAA team: related ATPases with diverse functions. Trends Cell Biol. 8 (1998) 65-71
    • (1998) Trends Cell Biol. , vol.8 , pp. 65-71
    • Patel, S.1    Latterich, M.2
  • 56
    • 0029240213 scopus 로고
    • Protein sorting. Pulling in the proteins
    • Pfanner N., and Meijer M. Protein sorting. Pulling in the proteins. Curr. Biol. 5 (1995) 132-135
    • (1995) Curr. Biol. , vol.5 , pp. 132-135
    • Pfanner, N.1    Meijer, M.2
  • 57
    • 4344559454 scopus 로고    scopus 로고
    • An unstructured initiation site is required for efficient proteasome-mediated degradation
    • Prakash S., Tian L., Ratliff K.S., Lehotzky R.E., and Matouschek A. An unstructured initiation site is required for efficient proteasome-mediated degradation. Nat. Struct. Mol. Biol. 11 (2004) 830-837
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 830-837
    • Prakash, S.1    Tian, L.2    Ratliff, K.S.3    Lehotzky, R.E.4    Matouschek, A.5
  • 58
    • 0036091848 scopus 로고    scopus 로고
    • Taking a bite: proteasomal protein processing
    • Rape M., and Jentsch S. Taking a bite: proteasomal protein processing. Nat. Cell Biol. 4 (2002) E113-E116
    • (2002) Nat. Cell Biol. , vol.4
    • Rape, M.1    Jentsch, S.2
  • 60
    • 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. Active site mutants in the six regulatory particle 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
  • 61
    • 6044274345 scopus 로고    scopus 로고
    • Interstitial collagenase is a Brownian ratchet driven by proteolysis of collagen
    • Saffarian S., Collier I.E., Marmer B.L., Elson E.L., and Goldberg G. Interstitial collagenase is a Brownian ratchet driven by proteolysis of collagen. Science 306 (2004) 108-111
    • (2004) Science , vol.306 , pp. 108-111
    • Saffarian, S.1    Collier, I.E.2    Marmer, B.L.3    Elson, E.L.4    Goldberg, G.5
  • 63
    • 28444452611 scopus 로고    scopus 로고
    • ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins
    • Smith D.M., Kafri G., Cheng Y., Ng D., Walz T., and Goldberg A.L. ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins. Mol. Cell 20 (2005) 687-698
    • (2005) Mol. Cell , vol.20 , pp. 687-698
    • Smith, D.M.1    Kafri, G.2    Cheng, Y.3    Ng, D.4    Walz, T.5    Goldberg, A.L.6
  • 65
    • 0033681249 scopus 로고    scopus 로고
    • Crystal and solution structures of an HslUV protease-chaperone complex
    • Sousa M.C., Trame C.B., Tsuruta H., Wilbanks S.M., Reddy V.S., and McKay D.B. Crystal and solution structures of an HslUV protease-chaperone complex. Cell 103 (2000) 633-643
    • (2000) Cell , vol.103 , pp. 633-643
    • Sousa, M.C.1    Trame, C.B.2    Tsuruta, H.3    Wilbanks, S.M.4    Reddy, V.S.5    McKay, D.B.6
  • 66
    • 0034090632 scopus 로고    scopus 로고
    • Recognition of misfolding proteins by PA700, the regulatory subcomplex of the 26 S proteasome
    • Strickland E., Hakala K., Thomas P.J., and DeMartino G.N. Recognition of misfolding proteins by PA700, the regulatory subcomplex of the 26 S proteasome. J. Biol. Chem. 275 (2000) 5565-5572
    • (2000) J. Biol. Chem. , vol.275 , pp. 5565-5572
    • Strickland, E.1    Hakala, K.2    Thomas, P.J.3    DeMartino, G.N.4
  • 67
    • 0020546084 scopus 로고
    • ATP serves two distinct roles in protein degradation in reticulocytes, one requiring and one independent of ubiquitin
    • Tanaka K., Waxman L., and Goldberg A.L. ATP serves two distinct roles in protein degradation in reticulocytes, one requiring and one independent of ubiquitin. J. Cell Biol. 96 (1983) 1580-1585
    • (1983) J. Cell Biol. , vol.96 , pp. 1580-1585
    • Tanaka, K.1    Waxman, L.2    Goldberg, A.L.3
  • 69
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: a molecular machine designed for controlled proteolysis
    • Voges D., Zwickl P., and Baumeister W. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68 (1999) 1015-1068
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 71
    • 0029739021 scopus 로고    scopus 로고
    • Mammalian Sug1 and C-Fos in the nuclear 26s proteasome
    • Wang W.L., Chevray P.M., and Nathans D. Mammalian Sug1 and C-Fos in the nuclear 26s proteasome. Proc. Natl. Acad. Sci. USA 93 (1996) 8236-8240
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8236-8240
    • Wang, W.L.1    Chevray, P.M.2    Nathans, D.3
  • 73
    • 0023664012 scopus 로고
    • Demonstration of two distinct high molecular weight proteases in rabbit reticulocytes, one of which degrades ubiquitin conjugates
    • Waxman L., Fagan J.M., and Goldberg A.L. Demonstration of two distinct high molecular weight proteases in rabbit reticulocytes, one of which degrades ubiquitin conjugates. J. Biol. Chem. 262 (1987) 2451-2457
    • (1987) J. Biol. Chem. , vol.262 , pp. 2451-2457
    • Waxman, L.1    Fagan, J.M.2    Goldberg, A.L.3
  • 74
    • 0033517351 scopus 로고    scopus 로고
    • Global unfolding of a substrate protein by the Hsp100 chaperone ClpA
    • Weber-Ban E.U., Reid B.G., Miranker A.D., and Horwich A.L. Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature 401 (1999) 90-93
    • (1999) Nature , vol.401 , pp. 90-93
    • Weber-Ban, E.U.1    Reid, B.G.2    Miranker, A.D.3    Horwich, A.L.4
  • 76
    • 0031577577 scopus 로고    scopus 로고
    • ATP binding, but not its hydrolysis, is required for assembly and proteolytic activity of the HslVU protease in Escherichia coli
    • Yoo S.J., Seol J.H., Seong I.S., Kang M.S., and Chung C.H. ATP binding, but not its hydrolysis, is required for assembly and proteolytic activity of the HslVU protease in Escherichia coli. Biochem. Biophys. Res. Commun. 238 (1997) 581-585
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 581-585
    • Yoo, S.J.1    Seol, J.H.2    Seong, I.S.3    Kang, M.S.4    Chung, C.H.5
  • 77
    • 1542305655 scopus 로고    scopus 로고
    • Repeat sequence of Epstein-Barr virus-encoded nuclear antigen 1 protein interrupts proteasome substrate processing
    • Zhang M., and Coffino P. Repeat sequence of Epstein-Barr virus-encoded nuclear antigen 1 protein interrupts proteasome substrate processing. J. Biol. Chem. 279 (2004) 8635-8641
    • (2004) J. Biol. Chem. , vol.279 , pp. 8635-8641
    • Zhang, M.1    Coffino, P.2
  • 78
    • 0033543648 scopus 로고    scopus 로고
    • An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26 S proteasome, activates protein breakdown by 20 S proteasomes
    • Zwickl P., Ng D., Woo K.M., Klenk H.P., and Goldberg A.L. An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26 S proteasome, activates protein breakdown by 20 S proteasomes. J. Biol. Chem. 274 (1999) 26008-26014
    • (1999) J. Biol. Chem. , vol.274 , pp. 26008-26014
    • Zwickl, P.1    Ng, D.2    Woo, K.M.3    Klenk, H.P.4    Goldberg, A.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.