메뉴 건너뛰기




Volumn 1824, Issue 1, 2012, Pages 3-13

Intracellular protein degradation: From a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting

Author keywords

Diseases; Lysosome; Proteasome; Proteolysis; Ubiquitin

Indexed keywords

ADENOSINE TRIPHOSPHATE; BOVINE SERUM ALBUMIN; CARRIER PROTEIN; CATHEPSIN B; CELL PROTEIN; GLOBIN; LYSOSOME ENZYME; MEMBRANE PROTEIN; PROTEASOME; SUMO PROTEIN; TRANSCRIPTION FACTOR; TRITIUM; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME;

EID: 82755187338     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2011.03.007     Document Type: Review
Times cited : (110)

References (83)
  • 1
    • 0012135624 scopus 로고
    • Impressions of an organic chemist in biochemistry
    • H.T. Clarke Impressions of an organic chemist in biochemistry Annu. Rev. Biochem. 27 1958 1 14
    • (1958) Annu. Rev. Biochem. , vol.27 , pp. 1-14
    • Clarke, H.T.1
  • 2
    • 0035900693 scopus 로고    scopus 로고
    • Hitler's gift and the era of biosynthesis
    • E.P. Kennedy Hitler's gift and the era of biosynthesis J. Biol. Chem. 276 2001 42619 42631
    • (2001) J. Biol. Chem. , vol.276 , pp. 42619-42631
    • Kennedy, E.P.1
  • 3
    • 0037077319 scopus 로고    scopus 로고
    • The use of isotope tracers to study intermediary metabolism: Rudolf Schoenheimer
    • (available on-line at:)
    • R.D. Simoni, R.L. Hill, and M. Vaughan The use of isotope tracers to study intermediary metabolism: Rudolf Schoenheimer J. Biol. Chem. 277 issue 43 2002 e1 e3 (available on-line at: http://www.jbc.org)
    • (2002) J. Biol. Chem. , vol.277 , Issue.43
    • Simoni, R.D.1    Hill, R.L.2    Vaughan, M.3
  • 4
    • 0344850801 scopus 로고
    • Studies in protein metabolism: VII. The metabolism of tyrosine
    • R. Schoenheimer, S. Ratner, and D. Rittenberg Studies in protein metabolism: VII. The metabolism of tyrosine J. Biol. Chem. 127 1939 333 344
    • (1939) J. Biol. Chem. , vol.127 , pp. 333-344
    • Schoenheimer, R.1    Ratner, S.2    Rittenberg, D.3
  • 5
    • 23944504696 scopus 로고
    • Studies in protein metabolism: XIV. The chemical interaction of dietary glycine and body proteins in rats
    • S. Ratner, D. Rittenberg, A.S. Keston, and R. Schoenheimer Studies in protein metabolism: XIV. The chemical interaction of dietary glycine and body proteins in rats J. Biol. Chem. 134 1940 665 676
    • (1940) J. Biol. Chem. , vol.134 , pp. 665-676
    • Ratner, S.1    Rittenberg, D.2    Keston, A.S.3    Schoenheimer, R.4
  • 7
    • 0002865516 scopus 로고
    • Studies on the induced synthesis of β-galactosidase in Escherichia coli: The kinetics and mechanism of sulfur incorporation
    • D.S. Hogness, M. Cohn, and J. Monod Studies on the induced synthesis of β-galactosidase in Escherichia coli: the kinetics and mechanism of sulfur incorporation Biochim. Biophys. Acta 16 1955 99 116
    • (1955) Biochim. Biophys. Acta , vol.16 , pp. 99-116
    • Hogness, D.S.1    Cohn, M.2    Monod, J.3
  • 9
    • 78651047890 scopus 로고
    • Tissue fractionation studies 4 comparative study of the binding of acid phosphatase, β-glucoronidase and cathepsin by rat liver particles
    • R. Gianetto, and C. DeDuve Tissue fractionation studies 4 comparative study of the binding of acid phosphatase, β-glucoronidase and cathepsin by rat liver particles Biochem. J. 59 1955 433 438
    • (1955) Biochem. J. , vol.59 , pp. 433-438
    • Gianetto, R.1    Deduve, C.2
  • 10
    • 77049143850 scopus 로고
    • The release of labeled amino acids from proteins in liver slices
    • M.V. Simpson The release of labeled amino acids from proteins in liver slices J. Biol. Chem. 201 1953 143 154
    • (1953) J. Biol. Chem. , vol.201 , pp. 143-154
    • Simpson, M.V.1
  • 11
    • 0023065242 scopus 로고
    • Intracellular protein catabolism and its control during nutrient deprivation and supply
    • G.E. Mortimore, and A.R. Poso Intracellular protein catabolism and its control during nutrient deprivation and supply Annu. Rev. Nutr. 7 1987 539 564
    • (1987) Annu. Rev. Nutr. , vol.7 , pp. 539-564
    • Mortimore, G.E.1    Poso, A.R.2
  • 12
    • 0000730374 scopus 로고
    • Cytoplasmic components in hepatic cell lysosomes
    • T.P. Ashford, and K.R. Porter Cytoplasmic components in hepatic cell lysosomes J. Cell Biol. 12 1962 198 202
    • (1962) J. Cell Biol. , vol.12 , pp. 198-202
    • Ashford, T.P.1    Porter, K.R.2
  • 13
    • 0014892983 scopus 로고
    • Control of enzyme levels in animal tissues
    • R.T. Schimke, and D. Doyle Control of enzyme levels in animal tissues Annu. Rev. Biochem. 39 1970 929 976
    • (1970) Annu. Rev. Biochem. , vol.39 , pp. 929-976
    • Schimke, R.T.1    Doyle, D.2
  • 14
    • 0016908233 scopus 로고
    • Intracellular protein degradation in mammalian and bacterial cells: Part 2
    • A.L. Goldberg, and A.C. St John 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
  • 15
    • 0016140019 scopus 로고
    • Relationship between degradation rates of proteins in vivo and their susceptibility to lysosomal proteases
    • H.L. Segal, J.R. Winkler, and M.P. Miyagi Relationship between degradation rates of proteins in vivo and their susceptibility to lysosomal proteases J. Biol. Chem. 249 1974 6364 6365
    • (1974) J. Biol. Chem. , vol.249 , pp. 6364-6365
    • Segal, H.L.1    Winkler, J.R.2    Miyagi, M.P.3
  • 16
    • 0015257324 scopus 로고
    • Some characteristics of the alanine-aminotransferase and arginase-inactivating system of lysosomes
    • M. Haider, and H.L. Segal Some characteristics of the alanine-aminotransferase and arginase-inactivating system of lysosomes Arch. Biochem. Biophys. 148 1972 228 237
    • (1972) Arch. Biochem. Biophys. , vol.148 , pp. 228-237
    • Haider, M.1    Segal, H.L.2
  • 17
    • 0017613741 scopus 로고
    • Lysosomes and protein degradation
    • R.T. Dean Lysosomes and protein degradation Acta Biol. Med. Ger. 36 1977 1815 1820 (Pubitemid 8378370)
    • (1977) Acta Biologica et Medica Germanica , vol.36 , Issue.11-12 , pp. 1815-1820
    • Dean, R.T.1
  • 18
    • 0019497190 scopus 로고
    • Immunochemical studies on catabolite inactivation of phosphoenolpyruvate carboxykinase in Saccharomyces cerevisiae
    • M. Müller, H. Müller, and H. Holzer Immunochemical studies on catabolite inactivation of phosphoenolpyruvate carboxykinase in Saccharomyces cerevisiae J. Biol. Chem. 256 1981 723 727 (Pubitemid 11151445)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.2 , pp. 723-727
    • Mueller, M.1    Mueller, H.2    Holzer, H.3
  • 19
    • 0024832940 scopus 로고
    • Proteolytic catabolite inactivation in Saccharomyces cerevisiae
    • H. Holzer Proteolytic catabolite inactivation in Saccharomyces cerevisiae Revis. Biol. Celular 21 1989 305 319
    • (1989) Revis. Biol. Celular , vol.21 , pp. 305-319
    • Holzer, H.1
  • 21
    • 0031883733 scopus 로고    scopus 로고
    • Lysosomes, a meeting point of proteins, chaperones, and proteases
    • A.M. Cuervo, and J.F. Dice Lysosomes, a meeting point of proteins, chaperones, and proteases J. Mol. Med. 76 1998 6 12 (Pubitemid 28085056)
    • (1998) Journal of Molecular Medicine , vol.76 , Issue.1 , pp. 6-12
    • Cuervo, A.M.1    Dice, J.F.2
  • 22
    • 0015814665 scopus 로고
    • Effect of ATP on protein degradation in rat liver lysosomes
    • M. Hayashi, Y. Hiroi, and Y. Natori Effect of ATP on protein degradation in rat liver lysosomes Nature New Biol. 242 1973 163 166
    • (1973) Nature New Biol. , vol.242 , pp. 163-166
    • Hayashi, M.1    Hiroi, Y.2    Natori, Y.3
  • 23
    • 0019887961 scopus 로고
    • ATP-dependent acidification of intact and disrupted lysosomes: Evidence for an ATP-driven proton pump
    • D.L. Schneider ATP-dependent acidification of intact and disrupted lysosomes: evidence for an ATP-driven proton pump J. Biol. Chem. 256 1981 3858 3864
    • (1981) J. Biol. Chem. , vol.256 , pp. 3858-3864
    • Schneider, D.L.1
  • 25
    • 78651144607 scopus 로고
    • Characteristics of the inhibition of hemoglobin synthesis in rabbit reticulocytes by threo-α-amino-β-chlorobutyric acid
    • M. Rabinovitz, and J.M. Fisher Characteristics of the inhibition of hemoglobin synthesis in rabbit reticulocytes by threo-α-amino-β- chlorobutyric acid Biochim. Biophys. Acta 91 1964 313 322
    • (1964) Biochim. Biophys. Acta , vol.91 , pp. 313-322
    • Rabinovitz, M.1    Fisher, J.M.2
  • 26
    • 0014498225 scopus 로고
    • The unstable haemoglobin haemolytic anaemias
    • R.W. Carrell, and H. Lehmann The unstable haemoglobin haemolytic anaemias Semin. Hematol. 6 1969 116 132
    • (1969) Semin. Hematol. , vol.6 , pp. 116-132
    • Carrell, R.W.1    Lehmann, H.2
  • 27
    • 0014545506 scopus 로고
    • Diseases of function and stability of haemoglobin
    • E.R. Huehns, and A.J. Bellingham Diseases of function and stability of haemoglobin Br. J. Haematol. 17 1969 1 10
    • (1969) Br. J. Haematol. , vol.17 , pp. 1-10
    • Huehns, E.R.1    Bellingham, A.J.2
  • 29
    • 0010579588 scopus 로고
    • Mode of degradation of abnormal globin chains in rabbit reticulocytes
    • H.L. Segal, D.J. Doyle, Academic Press New York
    • A. Hershko, H. Heller, D. Ganoth, and A. Ciechanover Mode of degradation of abnormal globin chains in rabbit reticulocytes H.L. Segal, D.J. Doyle, Protein Turnover and Lysosome Function 1978 Academic Press New York 149 169
    • (1978) Protein Turnover and Lysosome Function , pp. 149-169
    • Hershko, A.1    Heller, H.2    Ganoth, D.3    Ciechanover, A.4
  • 30
    • 0017062911 scopus 로고
    • Selective control of the degradation of normal and aberrant proteins in Reuber H35 hepatoma cells
    • S.E. Knowles, and F.J. Ballard Selective control of the degradation of normal and aberrant proteins in Reuber H35 hepatoma cells Biochem. J. 156 1976 609 617
    • (1976) Biochem. J. , vol.156 , pp. 609-617
    • Knowles, S.E.1    Ballard, F.J.2
  • 31
    • 0018570404 scopus 로고
    • The effect of protease inhibitors and decreased temperature on the degradation of different classes of proteins in cultured hepatocytes
    • N.T. Neff, G.N. DeMartino, and A.L. Goldberg The effect of protease inhibitors and decreased temperature on the degradation of different classes of proteins in cultured hepatocytes J. Cell. Physiol. 101 1979 439 457
    • (1979) J. Cell. Physiol. , vol.101 , pp. 439-457
    • Neff, N.T.1    Demartino, G.N.2    Goldberg, A.L.3
  • 32
    • 0017574395 scopus 로고
    • The accumulation of weakly basic substances in lysosomes and the inhibition of intracellular protein degradation
    • B. Poole, S. Ohkuma, and M.J. Warburton The accumulation of weakly basic substances in lysosomes and the inhibition of intracellular protein degradation Acta Biol. Med. Germ. 36 1977 1777 1788 (Pubitemid 8378367)
    • (1977) Acta Biologica et Medica Germanica , vol.36 , Issue.11-12 , pp. 1777-1788
    • Poole, B.1    Ohkuma, S.2    Warburton, M.J.3
  • 33
    • 0344361332 scopus 로고
    • Some aspects of the intracellular breakdown of exogenous and endogenous proteins
    • H.L. Segal, D.J. Doyle, Academic Press New York
    • B. Poole, S. Ohkuma, and M.J. Warburton Some aspects of the intracellular breakdown of exogenous and endogenous proteins H.L. Segal, D.J. Doyle, Protein Turnover and Lysosome Function 1978 Academic Press New York 43 58
    • (1978) Protein Turnover and Lysosome Function , pp. 43-58
    • Poole, B.1    Ohkuma, S.2    Warburton, M.J.3
  • 34
    • 0000478070 scopus 로고
    • Turnover of protein in growing and non-growing populations of Escherichia coli
    • J. Mandelstam Turnover of protein in growing and non-growing populations of Escherichia coli Biochem. J. 69 1958 110 119
    • (1958) Biochem. J. , vol.69 , pp. 110-119
    • Mandelstam, J.1
  • 35
    • 18844365161 scopus 로고
    • Observations on intracellular protein catabolism studied in vitro
    • D. Steinberg, and M. Vaughan Observations on intracellular protein catabolism studied in vitro Arch. Biochem. Biophys. 65 1956 93 105
    • (1956) Arch. Biochem. Biophys. , vol.65 , pp. 93-105
    • Steinberg, D.1    Vaughan, M.2
  • 36
    • 0015217107 scopus 로고
    • Studies on the degradation of tyrosine aminotransferase in hepatoma cells in culture: Influence of the composition of the medium and adenosine triphosphate dependence
    • A. Hershko, and G.M. Tomkins Studies on the degradation of tyrosine aminotransferase in hepatoma cells in culture: influence of the composition of the medium and adenosine triphosphate dependence J. Biol. Chem. 246 1971 710 714
    • (1971) J. Biol. Chem. , vol.246 , pp. 710-714
    • Hershko, A.1    Tomkins, G.M.2
  • 37
    • 11244299845 scopus 로고
    • Studies on the selectivity and mechanisms of intracellular protein degradation
    • D.W. Ribbons, K. Brew, Academic Press New York
    • A.L. Goldberg, J.D. Kowit, and J.D. Etlinger Studies on the selectivity and mechanisms of intracellular protein degradation D.W. Ribbons, K. Brew, Proteolysis and Physiological Regulation 1976 Academic Press New York 313 337
    • (1976) Proteolysis and Physiological Regulation , pp. 313-337
    • Goldberg, A.L.1    Kowit, J.D.2    Etlinger, J.D.3
  • 38
    • 0018187738 scopus 로고
    • A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes
    • DOI 10.1016/0006-291X(78)91249-4
    • A. Ciechanover, Y. Hod, and A. Hershko A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes Biochem. Biophys. Res. Common. 81 1978 1100 1105 (Pubitemid 8331462)
    • (1978) Biochemical and Biophysical Research Communications , vol.81 , Issue.4 , pp. 1100-1105
    • Ciehanover, A.1    Hod, Y.2    Hershko, A.3
  • 39
    • 0018992813 scopus 로고
    • ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation
    • A. Ciechanover, H. Heller, S. Elias, A.L. Haas, and A. Hershko ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation Proc. Natl Acad. Sci. U.S.A. 77 1980 1365 1368
    • (1980) Proc. Natl Acad. Sci. U.S.A. , vol.77 , pp. 1365-1368
    • Ciechanover, A.1    Heller, H.2    Elias, S.3    Haas, A.L.4    Hershko, A.5
  • 40
    • 0019000271 scopus 로고
    • Proposed role of ATP in protein breakdown: Conjugation of proteins with multiple chains of the polypeptide of ATP-dependent proteolysis
    • A. Hershko, A. Ciechanover, H. Heller, A.L. Haas, and I.A. Rose Proposed role of ATP in protein breakdown: conjugation of proteins with multiple chains of the polypeptide of ATP-dependent proteolysis Proc. Natl Acad. Sci. U.S.A. 77 1980 1783 1786
    • (1980) Proc. Natl Acad. Sci. U.S.A. , vol.77 , pp. 1783-1786
    • Hershko, A.1    Ciechanover, A.2    Heller, H.3    Haas, A.L.4    Rose, I.A.5
  • 41
    • 0019225640 scopus 로고
    • Characterization of the heatstable polypeptide of the ATP-dependent proteolytic system from reticulocytes
    • A. Ciechanover, S. Elias, H. Heller, S. Ferber, and A. Hershko Characterization of the heat-stable polypeptide of the ATP-dependent proteolytic system from reticulocytes J. Biol. Chem. 255 1980 7525 7528 (Pubitemid 11239454)
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.16 , pp. 7525-7528
    • Ciechanover, A.1    Elias, S.2    Heller, H.3
  • 42
    • 0019174693 scopus 로고
    • Ubiquitin is the ATP-dependent proteolysis factor I of rabbit reticulocytes
    • K.D. Wilkinson, M.K. Urban, and A.L. Haas Ubiquitin is the ATP-dependent proteolysis factor I of rabbit reticulocytes J. Biol. Chem. 255 1980 7529 7532 (Pubitemid 11239455)
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.16 , pp. 7529-7532
    • Wilkinson, K.D.1    Urban, M.K.2    Haas, A.L.3
  • 43
    • 0015950074 scopus 로고
    • Isolation of bovine thymin, a polypeptide hormone of the thymus
    • G. Goldstein Isolation of bovine thymin, a polypeptide hormone of the thymus Nature (London) 247 1974 11 14
    • (1974) Nature (London) , vol.247 , pp. 11-14
    • Goldstein, G.1
  • 44
    • 2442437350 scopus 로고
    • Isolation of a polypeptide that has lymphocyte-differentiating properties and is probably represented universally in living cells
    • G. Goldstein, M. Scheid, U. Hammerling, D.H. Schlesinger, H.D. Niall, and E.A. Boyse Isolation of a polypeptide that has lymphocyte-differentiating properties and is probably represented universally in living cells Proc. Natl Acad. Sci. U.S.A. 72 1975 11 15
    • (1975) Proc. Natl Acad. Sci. U.S.A. , vol.72 , pp. 11-15
    • Goldstein, G.1    Scheid, M.2    Hammerling, U.3    Schlesinger, D.H.4    Niall, H.D.5    Boyse, E.A.6
  • 45
    • 0016798328 scopus 로고
    • The complete amino acid sequence of ubiquitin, an adenylate cyclase stimulating polypeptide probably universal in living cells
    • D.H. Schlessinger, G. Goldstein, and H.D. Niall The complete amino acid sequence of ubiquitin, an adenylate cyclase stimulating polypeptide probably universal in living cells Biochemistry 14 1975 2214 2218
    • (1975) Biochemistry , vol.14 , pp. 2214-2218
    • Schlessinger, D.H.1    Goldstein, G.2    Niall, H.D.3
  • 46
    • 0018412317 scopus 로고
    • 1
    • T.L.K. Low, and A.L. Goldstein The chemistry and biology of thymosin: amino acid analysis of thymosin α1 and polypeptide β1 J. Biol. Chem. 254 1979 987 995 (Pubitemid 9145947)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.3 , pp. 987-995
    • Low, T.L.K.1    Goldstein, A.L.2
  • 47
    • 0016712824 scopus 로고
    • Remarkable similarities of peptide fingerprints of histone 2A and non-histone chromosomal protein A24
    • I.L. Goldknopf, and H. Busch Remarkable similarities of peptide fingerprints of histone 2A and non-histone chromosomal protein A24 Biochem. Biophys. Res. Commun. 65 1975 951 955
    • (1975) Biochem. Biophys. Res. Commun. , vol.65 , pp. 951-955
    • Goldknopf, I.L.1    Busch, H.2
  • 49
    • 0017327721 scopus 로고
    • Amino terminal sequence identity of ubiquitin and the nonhistone component of nuclear protein A24
    • DOI 10.1016/0006-291X(77)90352-7
    • L.T. Hunt, and M.O. Dayhoff Amino-terminal sequence identity of ubiquitin and the non-histone component of nuclear protein A24 Biochim. Biophys. Res. Commun. 74 1977 650 655 (Pubitemid 8022254)
    • (1977) Biochemical and Biophysical Research Communications , vol.74 , Issue.2 , pp. 650-655
    • Hunt, L.T.1    Dayhoff, M.O.2
  • 50
    • 0019887743 scopus 로고
    • Identification of the active amino acid residue of the polypeptide of ATP-dependent protein breakdown
    • A. Hershko, A. Ciechanover, and I.A. Rose Identification of the active amino acid residue of the polypeptide of ATP-dependent protein breakdown J. Biol. Chem. 256 1981 1525 1528
    • (1981) J. Biol. Chem. , vol.256 , pp. 1525-1528
    • Hershko, A.1    Ciechanover, A.2    Rose, I.A.3
  • 51
    • 0021813071 scopus 로고
    • Occurrence of a polyubiquitin structure in ubiquitin-protein conjugates
    • A. Hershko, and H. Heller Occurrence of a polyubiquitin structure in ubiquitin-protein conjugates Biochem. Biophys. Res. Common. 128 1985 1079 1086 (Pubitemid 15008255)
    • (1985) Biochemical and Biophysical Research Communications , vol.128 , Issue.3 , pp. 1079-1086
    • Hershko, A.1    Heller, H.2
  • 52
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • V. Chau, J.W. Tobias, A. Bachmair, D. Mariott, D. Ecker, D.K. Gonda, and A. Varshavsky A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein Science 243 1989 1576 1583 (Pubitemid 19090506)
    • (1989) Science , vol.243 , Issue.4898 , pp. 1576-1583
    • Chau, V.1    Tobias, J.W.2    Bachmair, A.3    Marriott, D.4    Ecker, D.J.5    Gonda, D.K.6    Varshavsky, A.7
  • 53
    • 1442323729 scopus 로고    scopus 로고
    • N-terminal ubiquitination: More protein substrates join in
    • DOI 10.1016/j.tcb.2004.01.004, PII S0962892404000236
    • A. Ciechanover, and R. Ben-Saadon N-terminal ubiquitination: more protein substrates join in Trends Cell Biol. 14 2004 103 106 (Pubitemid 38293450)
    • (2004) Trends in Cell Biology , vol.14 , Issue.3 , pp. 103-106
    • Ciechanover, A.1    Ben-Saadon, R.2
  • 54
    • 0037335034 scopus 로고    scopus 로고
    • How the ubiquitin-proteasome system controls transcription
    • DOI 10.1038/nrm1049
    • M. Muratani, and W.P. Tansey How the ubiquitin-proteasome system controls transcription Nat. Rev. Mol. Cell Biol. 4 2003 192 201 (Pubitemid 36288041)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.3 , pp. 192-201
    • Muratani, M.1    Tansey, W.P.2
  • 55
    • 0344442779 scopus 로고    scopus 로고
    • Transcriptional regulation by histone ubiquitination and deubiquitination
    • DOI 10.1101/gad.1156403
    • Y. Zhang Transcriptional regulation by histone ubiquitination and deubiquitination Genes Dev. 17 2003 2733 2740 (Pubitemid 37463282)
    • (2003) Genes and Development , vol.17 , Issue.22 , pp. 2733-2740
    • Zhang, Y.1
  • 57
    • 0015209453 scopus 로고
    • Attempts to map a process evolution of peptide biosynthesis
    • F. Lipman Attempts to map a process evolution of peptide biosynthesis Science 173 1971 875 884
    • (1971) Science , vol.173 , pp. 875-884
    • Lipman, F.1
  • 58
    • 0020478687 scopus 로고
    • "Covalent affinity" purification of ubiquitin-activating enzyme
    • A. Ciechanover, S. Elias, H. Heller, and A. Hershko "Covalent affinity" purification of ubiquitin-activating enzyme J. Biol. Chem. 257 1982 2537 2542
    • (1982) J. Biol. Chem. , vol.257 , pp. 2537-2542
    • Ciechanover, A.1    Elias, S.2    Heller, H.3    Hershko, A.4
  • 59
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system: Resolution, affinity purification and role in protein breakdown
    • A. Hershko, H. Heller, S. Elias, and A. Ciechanover Components of ubiquitin-protein ligase system: resolution, affinity purification and role in protein breakdown J. Biol. Chem. 258 1983 8206 8214
    • (1983) J. Biol. Chem. , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 61
    • 0020479850 scopus 로고
    • Immunochemical analysis of the turnover of ubiquitin-protein conjugates in intact cells: Relationship to the breakdown of abnormal proteins
    • A. Hershko, E. Eytan, A. Ciechanover, and A.L. Haas Immunochemical analysis of the turnover of ubiquitin-protein conjugates in intact cells: relationship to the breakdown of abnormal proteins J. Biol. Chem. 257 1982 13964 13970
    • (1982) J. Biol. Chem. , vol.257 , pp. 13964-13970
    • Hershko, A.1    Eytan, E.2    Ciechanover, A.3    Haas, A.L.4
  • 62
    • 0020676363 scopus 로고
    • Decrease in uH2A (protein A24) of a mouse temperature-sensitive mutant
    • DOI 10.1016/0014-5793(83)80359-7
    • Y. Matsumoto, H. Yasuda, T. Marunouchi, and M. Yamada Decrease in uH2A (protein A24) of a mouse temperature-sensitive mutant FEBS Lett. 151 1983 139 142 (Pubitemid 13139225)
    • (1983) FEBS Letters , vol.151 , Issue.1 , pp. 139-142
    • Matsumoto, Y.1    Yasuda, H.2    Marunouchi, T.3    Yamada, M.4
  • 63
    • 0021139080 scopus 로고
    • Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85
    • D. Finley, A. Ciechanover, and A. Varshavsky Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85 Cell 37 1984 43 55 (Pubitemid 14079835)
    • (1984) Cell , vol.37 , Issue.1 , pp. 43-55
    • Finley, D.1    Ciechanover, A.2    Varshavsky, A.3
  • 64
    • 0021140995 scopus 로고
    • Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85
    • A. Ciechanover, D. Finley, and A. Varshavsky Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85 Cell 37 1984 57 66 (Pubitemid 14079836)
    • (1984) Cell , vol.37 , Issue.1 , pp. 57-66
    • Ciechanover, A.1    Finley, D.2    Varshavsky, A.3
  • 65
    • 0020546084 scopus 로고
    • ATP serves two distinct roles in protein degradation in reticulocytes, one requiring and one independent of ubiquitin
    • K. Tanaka, L. Waxman, and A.L. Goldberg ATP serves two distinct roles in protein degradation in reticulocytes, one requiring and one independent of ATP J. Cell Biol. 96 1983 1580 1585 (Pubitemid 13034434)
    • (1983) Journal of Cell Biology , vol.96 , Issue.6 , pp. 1580-1585
    • Tanaka, K.1    Waxman, L.2    Goldberg, A.L.3
  • 67
    • 0022970210 scopus 로고
    • Ubiquitin-lysozyme conjugates. Identification and characterization of an ATP-dependent protease from rabbit reticulocyte lysates
    • R. Hough, G. Pratt, and M. Rechsteiner Ubiquitin-lysozyme conjugates. Identification and characterization of an ATP-dependent protease from rabbit reticulocyte lysates J. Biol. Chem. 261 1986 2400 2408 (Pubitemid 17205179)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.5 , pp. 2400-2408
    • Hough, R.1    Pratt, G.2    Rechsteiner, M.3
  • 68
    • 0023664012 scopus 로고
    • Demonstration of two distinct high molecular weight proteases in rabbit reticulocytes, one of which degrades ubiquitin conjugates
    • L. Waxman, J. Fagan, and A.L. Goldberg 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.2    Goldberg, A.L.3
  • 69
    • 0023655017 scopus 로고
    • Purification of two high molecular weight proteases from rabbit reticulocyte lysate
    • R. Hough, G. Pratt, and M. Rechsteiner 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
  • 70
    • 0019195859 scopus 로고
    • Cation-sensitive neutral endopeptidase: Isolation and specificity of the bovine pituitary enzyme
    • DOI 10.1111/j.1471-4159.1980.tb07873.x
    • S. Wilk, and M. Orlowski Cation-sensitive neutral endopeptidase: isolation and specificity of the bovine pituitary enzyme J. Neurochem. 35 1980 1172 1182 (Pubitemid 11198291)
    • (1980) Journal of Neurochemistry , vol.35 , Issue.5 , pp. 1172-1182
    • Wilk, S.1    Orlowski, M.2
  • 72
    • 0025232804 scopus 로고
    • The proteasome (multicatalytic protease) is a component of the 1,500-kDa proteolytic complex which degrades ubiquitin-conjugated proteins
    • J. Driscoll, and A.L. Goldberg The proteasome (multicatalytic protease) is a component of the 1,500-kDa proteolytic complex which degrades ubiquitin-conjugated proteins J. Biol. Chem. 265 1990 4789 4792
    • (1990) J. Biol. Chem. , vol.265 , pp. 4789-4792
    • Driscoll, J.1    Goldberg, A.L.2
  • 73
    • 0026539795 scopus 로고
    • Multiple forms of the 20S multicatalytic and the 26S ubiquitin/ATP- dependent proteases from rabbit reticulocyte lysate
    • L. Hoffman, G. Pratt, and M. Rechsteiner Multiple forms of the 20S multicatalytic and the 26S ubiquitin/ATP-dependent proteases from rabbit reticulocyte 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
  • 75
    • 0025331090 scopus 로고
    • In vivo degradation of a transcriptional regulator: The yeast α2 repressor
    • M. Hochstrasser, and A. Varshavsky In vivo degradation of a transcriptional regulator: the yeast α2 repressor Cell 61 1990 697 708
    • (1990) Cell , vol.61 , pp. 697-708
    • Hochstrasser, M.1    Varshavsky, A.2
  • 76
    • 0025639158 scopus 로고
    • The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53
    • M. Scheffner, B.A. Werness, J.M. Huibregtse, A.J. Levine, and P.M. Howley The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53 Cell 63 1990 1129 1136 (Pubitemid 120035062)
    • (1990) Cell , vol.63 , Issue.6 , pp. 1129-1136
    • Scheffner, M.1    Werness, B.A.2    Huibregtse, J.M.3    Levine, A.J.4    Howley, P.M.5
  • 77
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • M. Glotzer, A.W. Murray, and M.W. Kirschner Cyclin is degraded by the ubiquitin pathway Nature 349 1991 132 138 (Pubitemid 21912025)
    • (1991) Nature , vol.349 , Issue.6305 , pp. 132-138
    • Glotzer, M.1    Murray, A.W.2    Kirschner, M.W.3
  • 80
    • 0037376230 scopus 로고    scopus 로고
    • Potential for proteasome inhibition in the treatment of cancer
    • DOI 10.1016/S1359-6446(03)02647-3, PII S1359644603026473
    • J. Adams Potential for proteasome inhibition in the treatment of cancer Drug Discov. Today 8 2003 307 315 (Pubitemid 36332222)
    • (2003) Drug Discovery Today , vol.8 , Issue.7 , pp. 307-315
    • Adams, J.1
  • 81
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • M.H. Glickman, and A. Ciechanover The ubiquitin-proteasome pathway: destruction for the sake of construction Physiol. Rev. 82 2002 373 428 (Pubitemid 34654457)
    • (2002) Physiological Reviews , vol.82 , Issue.2 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 82
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: Proteases in the machine age
    • DOI 10.1038/nrm1336
    • C.M. Pickart, and R.E. Cohen Proteasomes and their kin: proteases in the machine age Nature Rev. Mol. Cell Biol. 5 2004 177 187 (Pubitemid 38325799)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.3 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 83
    • 11244309014 scopus 로고    scopus 로고
    • From the lysosome to ubiquitin and the proteasome
    • A. Ciechanover From the lysosome to ubiquitin and the proteasome Nature Rev. Mol. Cell Biol. 6 2005 79 86
    • (2005) Nature Rev. Mol. Cell Biol. , vol.6 , pp. 79-86
    • Ciechanover, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.