메뉴 건너뛰기




Volumn 6, Issue 4, 1999, Pages 197-204

Bifunctional inhibitors of the trypsin-like activity of eukaryotic proteasomes

Author keywords

Eukaryotic proteasome; Selective inhibition; Trypsin like activity; X ray analysis

Indexed keywords


EID: 0033117370     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(99)80036-2     Document Type: Article
Times cited : (66)

References (42)
  • 1
    • 0029347062 scopus 로고
    • New insights into proteasome function - from archaebacteria to drug development
    • Goldberg, A.L., Stein, R. & Adams, J. (1995). New insights into proteasome function - from archaebacteria to drug development. Chem. Biol. 2, 503-508.
    • (1995) Chem. Biol. , vol.2 , pp. 503-508
    • Goldberg, A.L.1    Stein, R.2    Adams, J.3
  • 2
    • 0028935165 scopus 로고
    • Ubiquitin, proteasomes, and the regulation of the intracellular protein degradation
    • Hochstrasser, M. (1995). Ubiquitin, proteasomes, and the regulation of the intracellular protein degradation. Curr. Opin. Cell Biol. 7, 215-223.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 215-223
    • Hochstrasser, M.1
  • 3
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., Tanaka, K. & Goldberg, A.L. (1996). Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 5
    • 0028999726 scopus 로고
    • Biogenesis, structure and function of the yeast 20S proteasome
    • Chen, P. & Hochstrasser, M. (1995). Biogenesis, structure and function of the yeast 20S proteasome. EMBO J. 14, 2620-2630.
    • (1995) EMBO J. , vol.14 , pp. 2620-2630
    • Chen, P.1    Hochstrasser, M.2
  • 6
    • 0030248766 scopus 로고    scopus 로고
    • Peptide antigen production by the proteasome: Complexity provides efficiency
    • Groettrup, M., Soza, A., Kuckelkorn, U. & Kloetzel. P.M. (1996). Peptide antigen production by the proteasome: Complexity provides efficiency. Immunol. Today 17, 429-435.
    • (1996) Immunol. Today , vol.17 , pp. 429-435
    • Groettrup, M.1    Soza, A.2    Kuckelkorn, U.3    Kloetzel, P.M.4
  • 7
    • 0029867623 scopus 로고    scopus 로고
    • Proteasomes: Destruction as a programme
    • Hilt, W. & Wolf, D.H. (1996). Proteasomes: Destruction as a programme. Trends Biochem. Sci. 21, 96-102.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 96-102
    • Hilt, W.1    Wolf, D.H.2
  • 8
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister, W., Walz, J., Zühl, F. & Seemüller, E. (1998). The proteasome: Paradigm of a self-compartmentalizing protease. Cell 92, 367-380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zühl, F.3    Seemüller, E.4
  • 9
    • 0030897031 scopus 로고    scopus 로고
    • Structure of 20S proteasome from yeast at 2.4 Å resolution
    • Groll, M., et al., & Huber, R. (1997). Structure of 20S proteasome from yeast at 2.4 Å resolution. Nature 386, 463-471.
    • (1997) Nature , vol.386 , pp. 463-471
    • Groll, M.1    Huber, R.2
  • 10
    • 0030774890 scopus 로고    scopus 로고
    • The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing
    • Heinemeyer, W., Fischer, M., Krimmer, T., Stachon, U. & Wolf, D.H. (1997). The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing. J. Biol. Chem. 272, 25200-25209.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25200-25209
    • Heinemeyer, W.1    Fischer, M.2    Krimmer, T.3    Stachon, U.4    Wolf, D.H.5
  • 11
    • 0032514684 scopus 로고    scopus 로고
    • Cleavage motifs of the yeast 20S proteasome β subunits deduced from digests of enolase I
    • Nussbaum, A.K., et al, & Schild, H. (1998). Cleavage motifs of the yeast 20S proteasome β subunits deduced from digests of enolase I. Proc. Natl Acad. Sci. USA 95, 12504-12509.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12504-12509
    • Nussbaum, A.K.1    Schild, H.2
  • 12
    • 0030737501 scopus 로고    scopus 로고
    • Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation
    • Arendt, C.S. & Hochstrasser M. (1997). Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation. Proc. Natl Acad. Sci. USA 94, 7156-7161.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 7156-7161
    • Arendt, C.S.1    Hochstrasser, M.2
  • 13
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologists
    • Lee, D.H. & Goldberg, A.L. (1998). Proteasome inhibitors: Valuable new tools for cell biologists. Trends Cell Biol. 8, 397-403.
    • (1998) Trends Cell Biol. , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 14
    • 0030012069 scopus 로고    scopus 로고
    • Design and synthesis of novel protease inhibitors: Tripeptide α', β'-epoxyketones as nanomolar inactivators of the proteasome
    • Spaltenstein, A., et al., & Crouch, R. (1996). Design and synthesis of novel protease inhibitors: Tripeptide α', β'-epoxyketones as nanomolar inactivators of the proteasome. Tetrahedron Lett. 37, 1343-1346.
    • (1996) Tetrahedron Lett. , vol.37 , pp. 1343-1346
    • Spaltenstein, A.1    Crouch, R.2
  • 15
    • 0030848702 scopus 로고    scopus 로고
    • Catalytic properties of 26S and 20S proteasomes and radiolabeling of MB1, LMP7 and C7 subunits associated with trypsin-like and chymotrypsin-like activities
    • Reidlinger, J., Pike, A.M., Savory, P.J., Murray, R.Z. & Rivett, A.J. (1997). Catalytic properties of 26S and 20S proteasomes and radiolabeling of MB1, LMP7 and C7 subunits associated with trypsin-like and chymotrypsin-like activities. J. Biol. Chem. 272, 24899-24905.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24899-24905
    • Reidlinger, J.1    Pike, A.M.2    Savory, P.J.3    Murray, R.Z.4    Rivett, A.J.5
  • 16
    • 0026648975 scopus 로고
    • 3,4-Dichloroisocumarin-induced activation of the degradation of beta casein by the bovine pituitary multicatalytic proteinase complex
    • Pereira, M.E., Nguyen, T., Wagner, B.J., Margolis, J.W., Yu, B. & Wilk, S. (1992). 3,4-Dichloroisocumarin-induced activation of the degradation of beta casein by the bovine pituitary multicatalytic proteinase complex. J. Biol. Chem. 267, 7949-7955.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7949-7955
    • Pereira, M.E.1    Nguyen, T.2    Wagner, B.J.3    Margolis, J.W.4    Yu, B.5    Wilk, S.6
  • 17
    • 0026712247 scopus 로고
    • A 3,4-Dichloroisocumarin-resistant component of the multicatalytic proteinase complex
    • Cardozo, C., Vinitsky, A., Hidalgo, M.C., Michaud, C. & Orlowski, M. (1992). A 3,4-Dichloroisocumarin-resistant component of the multicatalytic proteinase complex. Biochemistry 31, 7373-7380.
    • (1992) Biochemistry , vol.31 , pp. 7373-7380
    • Cardozo, C.1    Vinitsky, A.2    Hidalgo, M.C.3    Michaud, C.4    Orlowski, M.5
  • 18
    • 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. & Goldberg, A.L. (1997). Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum. J. Biol. Chem. 272, 1791-1798.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1791-1798
    • Akopian, T.N.1    Kisselev, A.F.2    Goldberg, A.L.3
  • 20
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany, G., Standaert, R.F., Lane, W.S., Choi, S., Corey, E.J. & Schreiber, S.L. (1995). Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268, 726-731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 21
    • 15644363581 scopus 로고    scopus 로고
    • Mechanistic studies on the inactivation of the proteasome by lactacystin in cultured cells
    • Dick L.R., et al., & Stein R.L. (1997). Mechanistic studies on the inactivation of the proteasome by lactacystin in cultured cells. J. Biol. Chem. 272, 182-188.
    • (1997) J. Biol. Chem. , vol.272 , pp. 182-188
    • Dick, L.R.1    Stein, R.L.2
  • 22
    • 0027493645 scopus 로고
    • Studies on the total synthesis of lactacystin: An improved aldol coupling reaction and a beta-lactone intermediate in thiol ester formation
    • Corey, E.J., Reichard, G.A. & Kania, R. (1993). Studies on the total synthesis of lactacystin: An improved aldol coupling reaction and a beta-lactone intermediate in thiol ester formation. Tetrahedron Lett. 34, 6977-6980.
    • (1993) Tetrahedron Lett. , vol.34 , pp. 6977-6980
    • Corey, E.J.1    Reichard, G.A.2    Kania, R.3
  • 23
    • 0032568514 scopus 로고    scopus 로고
    • Kinetic studies of the branched chain amino acid preferring activity of the 20S proteasome: Development of a continuous assay and inhibition by tripeptide aldehydes and clasto-lactacystin β-lactone
    • McCormack, T.A., et al., & Dick, L.R. (1998). Kinetic studies of the branched chain amino acid preferring activity of the 20S proteasome: Development of a continuous assay and inhibition by tripeptide aldehydes and clasto-lactacystin β-lactone. Biochemistry 37, 7792-7800.
    • (1998) Biochemistry , vol.37 , pp. 7792-7800
    • McCormack, T.A.1    Dick, L.R.2
  • 24
    • 0031010398 scopus 로고    scopus 로고
    • Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors
    • Bogyo, M., McMaster, J.S., Gaczynska, M., Tortorella, D., Goldberg, A.L. & Ploegh, H. (1997). Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors. Proc. Natl Acad. Sci. USA 90, 6629-6634.
    • (1997) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6629-6634
    • Bogyo, M.1    McMaster, J.S.2    Gaczynska, M.3    Tortorella, D.4    Goldberg, A.L.5    Ploegh, H.6
  • 25
    • 0032103006 scopus 로고    scopus 로고
    • Substrate binding and sequence preference of the proteasome revealed by active-site-directed affinity probes
    • Bogyo, M., Shin, S., McMaster, J.S. & Ploegh, H. (1998). Substrate binding and sequence preference of the proteasome revealed by active-site-directed affinity probes. Chem. Biol. 5, 307-320.
    • (1998) Chem. Biol. , vol.5 , pp. 307-320
    • Bogyo, M.1    Shin, S.2    McMaster, J.S.3    Ploegh, H.4
  • 26
    • 0001283831 scopus 로고    scopus 로고
    • Novel inhibitors of the proteasome and their therapeutic use in inflammation
    • Adams, J. & Stein, R. (1996). Novel inhibitors of the proteasome and their therapeutic use in inflammation. Annu. Rep. Med. Chem. 31, 279-288.
    • (1996) Annu. Rep. Med. Chem. , vol.31 , pp. 279-288
    • Adams, J.1    Stein, R.2
  • 27
    • 18744428952 scopus 로고    scopus 로고
    • Lactacystin, a specific inhibitor of the proteasome, inhibits human platelet lysosomal cathepsin A-like enzyme
    • Ostrowska, H., Omura, S., Wojcik, C. & Worowski, K. (1997). Lactacystin, a specific inhibitor of the proteasome, inhibits human platelet lysosomal cathepsin A-like enzyme. Biochem. Biophys. Res. Comm. 234, 729-732.
    • (1997) Biochem. Biophys. Res. Comm. , vol.234 , pp. 729-732
    • Ostrowska, H.1    Omura, S.2    Wojcik, C.3    Worowski, K.4
  • 28
    • 0024370674 scopus 로고
    • The multicatalytic proteinase
    • Rivett, A.J. (1989). The multicatalytic proteinase. J. Biol. Chem. 264, 12215-12219.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12215-12219
    • Rivett, A.J.1
  • 29
    • 0026775928 scopus 로고
    • Identification and localization of a cysteinyl residue critical for the trypsin-like catalytic activity of the proteasome
    • Dick, L.R., Moomaw, C.R., Pramanik, G.N., DeMartino, G.N. & Slaughter, C.A. (1992). Identification and localization of a cysteinyl residue critical for the trypsin-like catalytic activity of the proteasome. Biochemistry 31, 7347-7355.
    • (1992) Biochemistry , vol.31 , pp. 7347-7355
    • Dick, L.R.1    Moomaw, C.R.2    Pramanik, G.N.3    DeMartino, G.N.4    Slaughter, C.A.5
  • 30
    • 0001405626 scopus 로고
    • Thermodynamics of chelation. I. The statistical factor in chelate ring formation
    • Spike, C.G. & Parry, R.W. (1953). Thermodynamics of chelation. I. The statistical factor in chelate ring formation. J. Am. Chem. Soc. 75, 2726-2729.
    • (1953) J. Am. Chem. Soc. , vol.75 , pp. 2726-2729
    • Spike, C.G.1    Parry, R.W.2
  • 31
    • 0015313012 scopus 로고
    • The influence of polyvalency on the binding properties of antibodies
    • Crothers, D.M. & Metzger, H. (1972). The influence of polyvalency on the binding properties of antibodies. Immunochemistry 9, 341-357.
    • (1972) Immunochemistry , vol.9 , pp. 341-357
    • Crothers, D.M.1    Metzger, H.2
  • 33
    • 0027483808 scopus 로고
    • Lipophilic derivatization and its effect on the interaction of cholecystokinin (CCK) nonapeptide with phospholipids
    • Romano, R., Bayerl, T.M. & Moroder, L. (1993). Lipophilic derivatization and its effect on the interaction of cholecystokinin (CCK) nonapeptide with phospholipids. Biochim. Biophys. Acta 1151, 111-119.
    • (1993) Biochim. Biophys. Acta , vol.1151 , pp. 111-119
    • Romano, R.1    Bayerl, T.M.2    Moroder, L.3
  • 34
    • 0013770208 scopus 로고
    • Reactions of N-ethylmaleimide with peptides and amino acids
    • Smyth, D.G. (1964). Reactions of N-ethylmaleimide with peptides and amino acids. Biochem. J. 91, 589-595.
    • (1964) Biochem. J. , vol.91 , pp. 589-595
    • Smyth, D.G.1
  • 36
    • 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
  • 38
    • 0029886022 scopus 로고    scopus 로고
    • Kinetic characterization of the chymotryptic activity of the 20S proteasome
    • Stein, R.L., Melandri, F. & Dick, L. (1996). Kinetic characterization of the chymotryptic activity of the 20S proteasome. Biochemistry 35, 3899-3908.
    • (1996) Biochemistry , vol.35 , pp. 3899-3908
    • Stein, R.L.1    Melandri, F.2    Dick, L.3
  • 41
    • 0000356656 scopus 로고
    • A graphic model building and refinement system for macromolecules
    • Jones, T.A. (1978). A graphic model building and refinement system for macromolecules. J. Appl. Crystallogr. 11, 268-272.
    • (1978) J. Appl. Crystallogr. , vol.11 , pp. 268-272
    • Jones, T.A.1
  • 42
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R.A. & Huber, R. (1991 ). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A 47, 392-400.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.