메뉴 건너뛰기




Volumn 7, Issue 5, 2007, Pages 403-410

Rethinking peptide supply to MHC class I molecules

Author keywords

[No Author keywords available]

Indexed keywords

ANTITHROMBIN; EPITOPE; HEAT SHOCK PROTEIN; HEMOGLOBIN; JANUS KINASE 1; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MUTANT PROTEIN; PEPTIDE; PREALBUMIN; PROTEASOME INHIBITOR; PROTEIN S; SMAD4 PROTEIN; SUPEROXIDE DISMUTASE; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 34247585533     PISSN: 14741733     EISSN: None     Source Type: Journal    
DOI: 10.1038/nri2077     Document Type: Review
Times cited : (32)

References (90)
  • 1
    • 26244455510 scopus 로고    scopus 로고
    • Mechanisms of MHC class I-restricted antigen processing and cross-presentation
    • Cresswell, P., Ackerman, A. L., Giodini, A., Peaper, D. R. & Wearsch, P. A. Mechanisms of MHC class I-restricted antigen processing and cross-presentation. Immunol. Rev. 207, 145-157 (2005).
    • (2005) Immunol. Rev , vol.207 , pp. 145-157
    • Cresswell, P.1    Ackerman, A.L.2    Giodini, A.3    Peaper, D.R.4    Wearsch, P.A.5
  • 2
    • 30344451087 scopus 로고    scopus 로고
    • The ins and outs of intracellular peptides and antigen presentation by MHC class I molecules
    • Groothuis, T. & Neefjes, J. The ins and outs of intracellular peptides and antigen presentation by MHC class I molecules. Curr. Top. Microbiol. Immunol. 300, 127-148 (2005).
    • (2005) Curr. Top. Microbiol. Immunol , vol.300 , pp. 127-148
    • Groothuis, T.1    Neefjes, J.2
  • 3
    • 30044438884 scopus 로고    scopus 로고
    • Processing and presentation of tumor antigens and vaccination strategies
    • van der Bruggen, P. & Van den Eynde, B. J. Processing and presentation of tumor antigens and vaccination strategies. Curr. Opin. Immunol. 18, 98-104 (2006).
    • (2006) Curr. Opin. Immunol , vol.18 , pp. 98-104
    • van der Bruggen, P.1    Van den Eynde, B.J.2
  • 4
    • 2542574206 scopus 로고    scopus 로고
    • + T cell cross-priming via transfer of proteasome substrates
    • + T cell cross-priming via transfer of proteasome substrates. Science 304, 1318-1321 (2004).
    • (2004) Science , vol.304 , pp. 1318-1321
    • Norbury, C.C.1
  • 5
    • 33746908527 scopus 로고    scopus 로고
    • Cross-priming utilizes antigen not available to the direct presentation pathway
    • Donohue, K. B. et al. Cross-priming utilizes antigen not available to the direct presentation pathway. Immunology 119, 63-73 (2006).
    • (2006) Immunology , vol.119 , pp. 63-73
    • Donohue, K.B.1
  • 6
    • 0030239693 scopus 로고    scopus 로고
    • Defective ribosomal products (DRIPs): A major source of antigenic peptides for MHC class I molecules?
    • Yewdell, J. W., Antón, L. C. & Bennink, J. R. Defective ribosomal products (DRIPs): a major source of antigenic peptides for MHC class I molecules? J. Immunol. 157, 1823-1826 (1996).
    • (1996) J. Immunol , vol.157 , pp. 1823-1826
    • Yewdell, J.W.1    Antón, L.C.2    Bennink, J.R.3
  • 8
    • 0015529509 scopus 로고
    • Biosynthesis of hemoglobin Ann Arbor: Evidence for catabolic and feedback regulation
    • Adams, J. G. 3rd, Winter, W. P., Rucknagel, D. L. & Spencer, H. H. Biosynthesis of hemoglobin Ann Arbor: evidence for catabolic and feedback regulation. Science 176, 1427-1429 (1972).
    • (1972) Science , vol.176 , pp. 1427-1429
    • Adams 3rd, J.G.1    Winter, W.P.2    Rucknagel, D.L.3    Spencer, H.H.4
  • 10
    • 0016815244 scopus 로고
    • Rapid postsynthetic destruction of unstable haemoglobin Bushwick
    • Rieder, R. F., Wolf, D. J., Clegg, J. B. & Lee, S. L. Rapid postsynthetic destruction of unstable haemoglobin Bushwick. Nature 254, 725-727 (1975).
    • (1975) Nature , vol.254 , pp. 725-727
    • Rieder, R.F.1    Wolf, D.J.2    Clegg, J.B.3    Lee, S.L.4
  • 11
    • 0015292247 scopus 로고
    • Degradation of abnormal proteins in Escherichia coli (protein breakdown-protein structure-mistranslation-amino acid analogs-puromycin)
    • Goldberg, A. L. Degradation of abnormal proteins in Escherichia coli (protein breakdown-protein structure-mistranslation-amino acid analogs-puromycin). Proc. Natl Acad. Sci. USA 69, 422-426 (1972).
    • (1972) Proc. Natl Acad. Sci. USA , vol.69 , pp. 422-426
    • Goldberg, A.L.1
  • 12
    • 0016151680 scopus 로고
    • Degradation of abnormal proteins in Escherichia coli: Relative susceptibility of canavanyl proteins and puromycin peptides to proteolysis in vitro
    • Kemshead, J. T. & Hipkiss, A. R. Degradation of abnormal proteins in Escherichia coli: relative susceptibility of canavanyl proteins and puromycin peptides to proteolysis in vitro. Eur. J. Biochem. 45, 535-540 (1974).
    • (1974) Eur. J. Biochem , vol.45 , pp. 535-540
    • Kemshead, J.T.1    Hipkiss, A.R.2
  • 13
    • 0016612063 scopus 로고
    • Increased degradation rates of protein synthesized in hepatoma cells in the presence of amino acid analogues
    • Knowles, S. E., Gunn, J. M., Hanson, R. W. & Ballard, F. J. Increased degradation rates of protein synthesized in hepatoma cells in the presence of amino acid analogues. Biochem. J. 146, 595-600 (1975).
    • (1975) Biochem. J , vol.146 , pp. 595-600
    • Knowles, S.E.1    Gunn, J.M.2    Hanson, R.W.3    Ballard, F.J.4
  • 14
    • 0019218158 scopus 로고
    • Kinetics of degradation of 'short-' and 'long-lived' proteins in cultured mammalian cells
    • Wheatley, D. N., Giddings, M. R. & Inglis, M. S. Kinetics of degradation of 'short-' and 'long-lived' proteins in cultured mammalian cells. Cell Biol. Int. Rep. 4, 1081-1090 (1980).
    • (1980) Cell Biol. Int. Rep , vol.4 , pp. 1081-1090
    • Wheatley, D.N.1    Giddings, M.R.2    Inglis, M.S.3
  • 15
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • Schubert, U. et al. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404, 770-774 (2000).
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1
  • 16
    • 29144458032 scopus 로고    scopus 로고
    • Quantifying the contribution of defective ribosomal products to antigen production: A model-based computational analysis
    • Bulik, S., Peters, B. & Holzhutter, H. G. Quantifying the contribution of defective ribosomal products to antigen production: a model-based computational analysis. J. Immunol. 175, 7957-7964 (2005).
    • (2005) J. Immunol , vol.175 , pp. 7957-7964
    • Bulik, S.1    Peters, B.2    Holzhutter, H.G.3
  • 17
    • 29344464782 scopus 로고    scopus 로고
    • Protein synthesis upon acute nutrient restriction relies on proteasome function
    • Vabulas, R. M. & Hartl, F. U. Protein synthesis upon acute nutrient restriction relies on proteasome function. Science 310, 1960-1963 (2005).
    • (2005) Science , vol.310 , pp. 1960-1963
    • Vabulas, R.M.1    Hartl, F.U.2
  • 18
    • 33745833084 scopus 로고    scopus 로고
    • The DRiP hypothesis decennial: Support, controversy, refinement and extension
    • Yewdell, J. W. & Nicchitta, C. V. The DRiP hypothesis decennial: support, controversy, refinement and extension. Trends Immunol. 27, 368-373 (2006).
    • (2006) Trends Immunol , vol.27 , pp. 368-373
    • Yewdell, J.W.1    Nicchitta, C.V.2
  • 19
    • 0033214423 scopus 로고    scopus 로고
    • The induction of virus-specific CTL as a function of increasing epitope expression: Responses rise steadily until excessively high levels of epitope are attained
    • Wherry, E. J., Puorro, K. A., Porgador, A. & Eisenlohr, L. C. The induction of virus-specific CTL as a function of increasing epitope expression: responses rise steadily until excessively high levels of epitope are attained. J. Immunol. 163, 3735-3745 (1999).
    • (1999) J. Immunol , vol.163 , pp. 3735-3745
    • Wherry, E.J.1    Puorro, K.A.2    Porgador, A.3    Eisenlohr, L.C.4
  • 20
    • 0024095276 scopus 로고
    • Defective presentation to class I-restricted cytotoxic T lymphocytes in vaccinia-infected cells is overcome by enhanced degradation of antigen
    • Townsend, A. et al. Defective presentation to class I-restricted cytotoxic T lymphocytes in vaccinia-infected cells is overcome by enhanced degradation of antigen. J. Exp. Med. 168, 1211-1224 (1988).
    • (1988) J. Exp. Med , vol.168 , pp. 1211-1224
    • Townsend, A.1
  • 21
    • 0026766091 scopus 로고
    • The N-end rule
    • Varshavsky, A. The N-end rule. Cell 69, 725-735 (1992).
    • (1992) Cell , vol.69 , pp. 725-735
    • Varshavsky, A.1
  • 22
    • 26244435436 scopus 로고    scopus 로고
    • The seven dirty little secrets of major histocompatibility complex class I antigen processing
    • Yewdell, J. W. The seven dirty little secrets of major histocompatibility complex class I antigen processing. Immunol. Rev. 207, 8-18 (2005).
    • (2005) Immunol. Rev , vol.207 , pp. 8-18
    • Yewdell, J.W.1
  • 23
    • 0034643348 scopus 로고    scopus 로고
    • The major substrates for TAP in vivo are derived from newly synthesized proteins
    • Reits, E. A., Vos, J. C., Gromme, M. & Neefjes, J. The major substrates for TAP in vivo are derived from newly synthesized proteins. Nature 404, 774-778 (2000).
    • (2000) Nature , vol.404 , pp. 774-778
    • Reits, E.A.1    Vos, J.C.2    Gromme, M.3    Neefjes, J.4
  • 24
    • 0037342270 scopus 로고    scopus 로고
    • Quantitating protein synthesis, degradation, and endogenous antigen processing
    • Princiotta, M. F. et al. Quantitating protein synthesis, degradation, and endogenous antigen processing. Immunity 18, 343-354 (2003).
    • (2003) Immunity , vol.18 , pp. 343-354
    • Princiotta, M.F.1
  • 25
    • 0034703437 scopus 로고    scopus 로고
    • Detecting and measuring cotranslational protein degradation in vivo
    • Turner, G. C. & Varshavsky, A. Detecting and measuring cotranslational protein degradation in vivo. Science 289, 2117-2120 (2000).
    • (2000) Science , vol.289 , pp. 2117-2120
    • Turner, G.C.1    Varshavsky, A.2
  • 26
    • 0041822089 scopus 로고    scopus 로고
    • Cell biology: Join the crowd
    • Ellis, R. J. & Minton, A. P. Cell biology: join the crowd. Nature 425, 27-28 (2003).
    • (2003) Nature , vol.425 , pp. 27-28
    • Ellis, R.J.1    Minton, A.P.2
  • 27
    • 0032842870 scopus 로고    scopus 로고
    • The fundamentals of protein folding: Bringing together theory and experiment
    • Dobson, C. M. & Karplus, M. The fundamentals of protein folding: bringing together theory and experiment. Curr. Opin. Struct. Biol. 9, 92-101 (1999).
    • (1999) Curr. Opin. Struct. Biol , vol.9 , pp. 92-101
    • Dobson, C.M.1    Karplus, M.2
  • 28
    • 0032822103 scopus 로고    scopus 로고
    • Principles of protein folding in the cellular environment
    • Ellis, R. J. & Hartl, F. U. Principles of protein folding in the cellular environment. Curr. Opin. Struct. Biol. 9, 102-110 (1999).
    • (1999) Curr. Opin. Struct. Biol , vol.9 , pp. 102-110
    • Ellis, R.J.1    Hartl, F.U.2
  • 29
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: Folding, refolding, and degrading proteins
    • Wickner, S., Maurizi, M. R. & Gottesman, S. Posttranslational quality control: folding, refolding, and degrading proteins. Science 286, 1888-1893 (1999).
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 30
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman, J. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 70, 603-647 (2001).
    • (2001) Annu. Rev. Biochem , vol.70 , pp. 603-647
    • Frydman, J.1
  • 31
    • 10044252090 scopus 로고    scopus 로고
    • Protein folding, misfolding, and aggregation. Formation of inclusion bodies and aggresomes
    • Markossian, K. A. & Kurganov, B. I. Protein folding, misfolding, and aggregation. Formation of inclusion bodies and aggresomes. Biochemistry Mosc. 69, 971-984 (2004).
    • (2004) Biochemistry Mosc , vol.69 , pp. 971-984
    • Markossian, K.A.1    Kurganov, B.I.2
  • 32
    • 25444522227 scopus 로고    scopus 로고
    • Molecular chaperones in protein quality control
    • Lee, S. & Tsai, F. T. Molecular chaperones in protein quality control. J. Biochem. Mol. Biol. 38, 259-265 (2005).
    • (2005) J. Biochem. Mol. Biol , vol.38 , pp. 259-265
    • Lee, S.1    Tsai, F.T.2
  • 33
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani, M. & Dobson, C. M. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 81, 678-699 (2003).
    • (2003) J. Mol. Med , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 34
    • 9644280977 scopus 로고    scopus 로고
    • Cooperation of molecular chaperones with the ubiquitin/proteasome system
    • Esser, C., Alberti, S. & Hohfeld, J. Cooperation of molecular chaperones with the ubiquitin/proteasome system. Biochim. Biophys. Acta 1695, 171-188 (2004).
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 171-188
    • Esser, C.1    Alberti, S.2    Hohfeld, J.3
  • 35
  • 36
  • 37
    • 28844478925 scopus 로고    scopus 로고
    • Molecular guardians for newborn proteins: Ribosome-associated chaperones and their role in protein folding
    • Wegrzyn, R. D. & Deuerling, E. Molecular guardians for newborn proteins: ribosome-associated chaperones and their role in protein folding. Cell. Mol. Life Sci. 62, 2727-2738 (2005).
    • (2005) Cell. Mol. Life Sci , vol.62 , pp. 2727-2738
    • Wegrzyn, R.D.1    Deuerling, E.2
  • 38
    • 33646354930 scopus 로고    scopus 로고
    • A conserved motif is prerequisite for the interaction of NAC with ribosomal protein L23 and nascent chains
    • Wegrzyn, R. D. et al. A conserved motif is prerequisite for the interaction of NAC with ribosomal protein L23 and nascent chains. J. Biol. Chem. 281, 2847-2857 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 2847-2857
    • Wegrzyn, R.D.1
  • 39
    • 22544445528 scopus 로고    scopus 로고
    • The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex
    • Otto, H. et al. The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex. Proc. Natl Acad. Sci. USA 102, 10064-10069 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 10064-10069
    • Otto, H.1
  • 40
    • 31444452768 scopus 로고    scopus 로고
    • The battle of the fold: Chaperones take on prions
    • True, H. L. The battle of the fold: chaperones take on prions. Trends Genet. 22, 110-117 (2006).
    • (2006) Trends Genet , vol.22 , pp. 110-117
    • True, H.L.1
  • 41
    • 0026035205 scopus 로고
    • Relative activities and stabilities of mutant Escherichia coli tryptophan synthase ? subunits
    • Lim, W. K., Shin, H. J., Milton, D. L. & Hardman, J. K. Relative activities and stabilities of mutant Escherichia coli tryptophan synthase ? subunits. J. Bacteriol. 173, 1886-1893 (1991).
    • (1991) J. Bacteriol , vol.173 , pp. 1886-1893
    • Lim, W.K.1    Shin, H.J.2    Milton, D.L.3    Hardman, J.K.4
  • 42
    • 0345580617 scopus 로고    scopus 로고
    • Characterization of novel cathepsin K mutations in the pro and mature polypeptide regions causing pycnodysostosis
    • Hou, W. S. et al. Characterization of novel cathepsin K mutations in the pro and mature polypeptide regions causing pycnodysostosis. J. Clin. Invest. 103, 731-738 (1999).
    • (1999) J. Clin. Invest , vol.103 , pp. 731-738
    • Hou, W.S.1
  • 43
    • 0037108875 scopus 로고    scopus 로고
    • The functional consequences of mis-sense mutations affecting an intra-molecular salt bridge in arylsulphatase A
    • Schestag, F. et al. The functional consequences of mis-sense mutations affecting an intra-molecular salt bridge in arylsulphatase A. Biochem. J. 367, 499-504 (2002).
    • (2002) Biochem. J , vol.367 , pp. 499-504
    • Schestag, F.1
  • 44
    • 23044467754 scopus 로고    scopus 로고
    • Characterization of four variant forms of human propionyl-CoA carboxylase expressed in Escherichia coli
    • Jiang, H., Rao, K. S., Yee, V. C. & Kraus, J. P. Characterization of four variant forms of human propionyl-CoA carboxylase expressed in Escherichia coli. J. Biol. Chem. 280, 27719-27727 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 27719-27727
    • Jiang, H.1    Rao, K.S.2    Yee, V.C.3    Kraus, J.P.4
  • 45
    • 14044270751 scopus 로고    scopus 로고
    • The impact of misfolding versus targeted degradation on the efficiency of the MHC class I-restricted antigen processing
    • Golovina, T. N., Morrison, S. E. & Eisenlohr, L. C. The impact of misfolding versus targeted degradation on the efficiency of the MHC class I-restricted antigen processing. J. Immunol. 174, 2763-2769 (2005).
    • (2005) J. Immunol , vol.174 , pp. 2763-2769
    • Golovina, T.N.1    Morrison, S.E.2    Eisenlohr, L.C.3
  • 46
    • 0033485429 scopus 로고    scopus 로고
    • Generation of an immunodominant CTL epitope is affected by proteasome subunit composition and stability of the antigenic protein
    • Gileadi, U. et al. Generation of an immunodominant CTL epitope is affected by proteasome subunit composition and stability of the antigenic protein. J. Immunol. 163, 6045-6052 (1999).
    • (1999) J. Immunol , vol.163 , pp. 6045-6052
    • Gileadi, U.1
  • 47
    • 4344657752 scopus 로고    scopus 로고
    • An evaluation of enforced rapid proteasomal degradation as a means of enhancing vaccine-induced CTL responses
    • Wong, S. B., Buck, C. B., Shen, X. & Siliciano, R. F. An evaluation of enforced rapid proteasomal degradation as a means of enhancing vaccine-induced CTL responses. J. Immunol. 173, 3073-3083 (2004).
    • (2004) J. Immunol , vol.173 , pp. 3073-3083
    • Wong, S.B.1    Buck, C.B.2    Shen, X.3    Siliciano, R.F.4
  • 48
    • 0141861067 scopus 로고    scopus 로고
    • Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: Which way to go?
    • Uversky, V. N. Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: which way to go? Cell. Mol. Life Sci. 60, 1852-1871 (2003).
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 1852-1871
    • Uversky, V.N.1
  • 49
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C. L., Omura, S. & Kopito, R. R. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83, 121-127 (1995).
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 50
    • 20344378216 scopus 로고    scopus 로고
    • Most F508del-CFTR is targeted to degradation at an early folding checkpoint and independently of calnexin
    • Farinha, C. M. & Amaral, M. D. Most F508del-CFTR is targeted to degradation at an early folding checkpoint and independently of calnexin. Mol. Cell. Biol. 25, 5242-5252 (2005).
    • (2005) Mol. Cell. Biol , vol.25 , pp. 5242-5252
    • Farinha, C.M.1    Amaral, M.D.2
  • 51
    • 14244262456 scopus 로고    scopus 로고
    • Destabilization of the transmembrane domain induces misfolding in a phenotypic mutant of cystic fibrosis transmembrane conductance regulator
    • Choi, M. Y. et al. Destabilization of the transmembrane domain induces misfolding in a phenotypic mutant of cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 280, 4968-4974 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 4968-4974
    • Choi, M.Y.1
  • 52
    • 0019857705 scopus 로고
    • Properties of abnormal proteins degraded rapidly in reticulocytes. Intracellular aggregation of the globin molecules prior to hydrolysis
    • Klemes, Y., Etlinger, J. D. & Goldberg, A. L. Properties of abnormal proteins degraded rapidly in reticulocytes. Intracellular aggregation of the globin molecules prior to hydrolysis. J. Biol. Chem. 256, 8436-8444 (1981).
    • (1981) J. Biol. Chem , vol.256 , pp. 8436-8444
    • Klemes, Y.1    Etlinger, J.D.2    Goldberg, A.L.3
  • 53
  • 54
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau, B., Weissman, J. & Horwich, A. Molecular chaperones and protein quality control. Cell 125, 443-451 (2006).
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 55
    • 33644872508 scopus 로고    scopus 로고
    • Characterization of rapidly degraded polypeptides in mammalian cells reveals a novel layer of nascent protein quality control
    • Qian, S. B., Princiotta, M. F., Bennink, J. R. & Yewdell, J. W. Characterization of rapidly degraded polypeptides in mammalian cells reveals a novel layer of nascent protein quality control. J. Biol. Chem. 281, 392-400 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 392-400
    • Qian, S.B.1    Princiotta, M.F.2    Bennink, J.R.3    Yewdell, J.W.4
  • 56
    • 0030052923 scopus 로고    scopus 로고
    • Ornithine decarboxylase antizyme: A novel type of regulatory protein
    • Hayashi, S.-i., Murakami, Y. & Matsufuji, S. Ornithine decarboxylase antizyme: a novel type of regulatory protein. Trends Biochem. Sci. 21, 27-30 (1996).
    • (1996) Trends Biochem. Sci , vol.21 , pp. 27-30
    • Hayashi, S.-I.1    Murakami, Y.2    Matsufuji, S.3
  • 57
  • 58
    • 14644446056 scopus 로고    scopus 로고
    • 20S proteasomal degradation of ornithine decarboxylase is regulated by NQO1
    • Asher, G., Bercovich, Z., Tsvetkov, P., Shaul, Y. & Kahana, C. 20S proteasomal degradation of ornithine decarboxylase is regulated by NQO1. Mol. Cell 17, 645-655 (2005).
    • (2005) Mol. Cell , vol.17 , pp. 645-655
    • Asher, G.1    Bercovich, Z.2    Tsvetkov, P.3    Shaul, Y.4    Kahana, C.5
  • 59
    • 0032488219 scopus 로고    scopus 로고
    • Association between HTLV-1 Tax and IκBα is dependent on the IκBα phosphorylation state
    • Petropoulos, L. & Hiscott, J. Association between HTLV-1 Tax and IκBα is dependent on the IκBα phosphorylation state. Virology 252, 189-199 (1998).
    • (1998) Virology , vol.252 , pp. 189-199
    • Petropoulos, L.1    Hiscott, J.2
  • 60
    • 0037834898 scopus 로고    scopus 로고
    • Ubiquitin-independent proteolytic functions of the proteasome
    • Orlowski, M. & Wilk, S. Ubiquitin-independent proteolytic functions of the proteasome. Arch. Biochem. Biophys. 415, 1-5 (2003).
    • (2003) Arch. Biochem. Biophys , vol.415 , pp. 1-5
    • Orlowski, M.1    Wilk, S.2
  • 61
    • 0035872863 scopus 로고    scopus 로고
    • A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 α-subunit of the 20S proteasome
    • Touitou, R. et al. A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 α-subunit of the 20S proteasome. EMBO J. 20, 2367-2375 (2001).
    • (2001) EMBO J , vol.20 , pp. 2367-2375
    • Touitou, R.1
  • 62
    • 0035370123 scopus 로고    scopus 로고
    • Binding and regulation of HIF-1α by a subunit of the proteasome complex, PSMA7
    • Cho, S. et al. Binding and regulation of HIF-1α by a subunit of the proteasome complex, PSMA7. FEBS Lett. 498, 62-66 (2001).
    • (2001) FEBS Lett , vol.498 , pp. 62-66
    • Cho, S.1
  • 63
    • 4143131114 scopus 로고    scopus 로고
    • 20S proteasome prevents aggregation of heat-denatured proteins without PA700 regulatory subcomplex like a molecular chaperone
    • Yano, M., Koumoto, Y., Kanesaki, Y., Wu, X. & Kido, H. 20S proteasome prevents aggregation of heat-denatured proteins without PA700 regulatory subcomplex like a molecular chaperone. Biomacromolecules 5, 1465-1469 (2004).
    • (2004) Biomacromolecules , vol.5 , pp. 1465-1469
    • Yano, M.1    Koumoto, Y.2    Kanesaki, Y.3    Wu, X.4    Kido, H.5
  • 65
    • 33745301876 scopus 로고    scopus 로고
    • Tight linkage between translation and MHC class I peptide ligand generation implies specialized antigen processing for defective ribosomal products
    • Qian, S. B. et al. Tight linkage between translation and MHC class I peptide ligand generation implies specialized antigen processing for defective ribosomal products. J. Immunol. 177, 227-233 (2006).
    • (2006) J. Immunol , vol.177 , pp. 227-233
    • Qian, S.B.1
  • 67
    • 0036806274 scopus 로고    scopus 로고
    • Three-state equilibrium of Escherichia coli trigger factor
    • Patzelt, H. et al. Three-state equilibrium of Escherichia coli trigger factor. Biol. Chem. 383, 1611-1619 (2002).
    • (2002) Biol. Chem , vol.383 , pp. 1611-1619
    • Patzelt, H.1
  • 68
    • 22144451849 scopus 로고    scopus 로고
    • Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli
    • Rauch, T. et al. Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli. Mol. Microbiol. 57, 357-365 (2005).
    • (2005) Mol. Microbiol , vol.57 , pp. 357-365
    • Rauch, T.1
  • 69
    • 0021153961 scopus 로고
    • Intracellular protein degradation: Basis of a self-regulating mechanism for the proteolysis of endogenous proteins
    • Wheatley, D. N. Intracellular protein degradation: basis of a self-regulating mechanism for the proteolysis of endogenous proteins. J. Theor. Biol. 107, 127-149 (1984).
    • (1984) J. Theor. Biol , vol.107 , pp. 127-149
    • Wheatley, D.N.1
  • 70
    • 0033549496 scopus 로고    scopus 로고
    • Intracellular localization of proteasomal degradation of a viral antigen
    • Antón, L. C. et al. Intracellular localization of proteasomal degradation of a viral antigen. J. Cell. Biol. 146, 113-124 (1999).
    • (1999) J. Cell. Biol , vol.146 , pp. 113-124
    • Antón, L.C.1
  • 71
    • 1342324680 scopus 로고    scopus 로고
    • Toward a definition of self: Proteomic evaluation of the class I peptide repertoire
    • Hickman, H. D. et al. Toward a definition of self: proteomic evaluation of the class I peptide repertoire. J. Immunol. 172, 2944-2952 (2004).
    • (2004) J. Immunol , vol.172 , pp. 2944-2952
    • Hickman, H.D.1
  • 72
    • 1842290406 scopus 로고    scopus 로고
    • Introduction of a glycosylation site into a secreted protein provides evidence for an alternative antigen processing pathway: Transport of precursors of MHC class I restricted-peptides from the endoplasmic reticulum to the cytosol
    • Bacík, I. et al. Introduction of a glycosylation site into a secreted protein provides evidence for an alternative antigen processing pathway: transport of precursors of MHC class I restricted-peptides from the endoplasmic reticulum to the cytosol. J. Exp. Med. 186, 479-487 (1997).
    • (1997) J. Exp. Med , vol.186 , pp. 479-487
    • Bacík, I.1
  • 73
    • 0031973735 scopus 로고    scopus 로고
    • The class I antigen-processing pathway for the membrane protein tyrosinase involves translation in the endoplasmic reticulum and processing in the cytosol
    • Mosse, C. A. et al. The class I antigen-processing pathway for the membrane protein tyrosinase involves translation in the endoplasmic reticulum and processing in the cytosol. J. Exp. Med. 187, 37-48 (1998).
    • (1998) J. Exp. Med , vol.187 , pp. 37-48
    • Mosse, C.A.1
  • 75
    • 33747175431 scopus 로고    scopus 로고
    • Cotranslocational degradation protects the stressed endoplasmic reticulum from protein overload
    • Oyadomari, S. et al. Cotranslocational degradation protects the stressed endoplasmic reticulum from protein overload. Cell 126, 727-739 (2006).
    • (2006) Cell , vol.126 , pp. 727-739
    • Oyadomari, S.1
  • 76
    • 1142269466 scopus 로고    scopus 로고
    • Immune recognition of a human renal cancer antigen through post-translational protein splicing
    • Hanada, K., Yewdell, J. W. & Yang, J. C. Immune recognition of a human renal cancer antigen through post-translational protein splicing. Nature 427, 252-256 (2004).
    • (2004) Nature , vol.427 , pp. 252-256
    • Hanada, K.1    Yewdell, J.W.2    Yang, J.C.3
  • 77
    • 2142644458 scopus 로고    scopus 로고
    • An antigenic peptide produced by peptide splicing in the proteasome
    • Vigneron, N. et al. An antigenic peptide produced by peptide splicing in the proteasome. Science 304, 587-590 (2004).
    • (2004) Science , vol.304 , pp. 587-590
    • Vigneron, N.1
  • 78
    • 0041971307 scopus 로고    scopus 로고
    • Self-inhibition of synthesis and antigen presentation by Epstein-Barr virus-encoded EBNA1
    • Yin, Y., Manoury, B. & Fahraeus, R. Self-inhibition of synthesis and antigen presentation by Epstein-Barr virus-encoded EBNA1. Science 301, 1371-1374 (2003).
    • (2003) Science , vol.301 , pp. 1371-1374
    • Yin, Y.1    Manoury, B.2    Fahraeus, R.3
  • 79
    • 0029003999 scopus 로고
    • Inhibiton of antigen processing by the internal repeat region of the Epstein-Barr virus nuclear antigen-1
    • Levitskaya, J. et al. Inhibiton of antigen processing by the internal repeat region of the Epstein-Barr virus nuclear antigen-1. Nature 375, 685-688 (1995).
    • (1995) Nature , vol.375 , pp. 685-688
    • Levitskaya, J.1
  • 80
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair, A., Finley, D. & Varshavsky, A. In vivo half-life of a protein is a function of its amino-terminal residue. Science 234, 179-186 (1986).
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 81
    • 30444449969 scopus 로고    scopus 로고
    • Mitosis: A matter of getting rid of the right protein at the right time
    • Pines, J. Mitosis: a matter of getting rid of the right protein at the right time. Trends Cell. Biol. 16, 55-63 (2006).
    • (2006) Trends Cell. Biol , vol.16 , pp. 55-63
    • Pines, J.1
  • 82
    • 29244468279 scopus 로고    scopus 로고
    • Characterization of endoplasmic reticulum-associated degradation of a protein S mutant identified in a family of quantitative protein S deficiency
    • Tsuda, H., Tokunaga, F., Nagamitsu, H. & Koide, T. Characterization of endoplasmic reticulum-associated degradation of a protein S mutant identified in a family of quantitative protein S deficiency. Thromb. Res. 117, 323-331 (2006).
    • (2006) Thromb. Res , vol.117 , pp. 323-331
    • Tsuda, H.1    Tokunaga, F.2    Nagamitsu, H.3    Koide, T.4
  • 83
    • 32244448470 scopus 로고    scopus 로고
    • Quality control of a mutant plasma membrane ATPase: Ubiquitylation prevents cell-surface stability
    • Liu, Y. & Chang, A. Quality control of a mutant plasma membrane ATPase: ubiquitylation prevents cell-surface stability. J. Cell Sci. 119, 360-369 (2006).
    • (2006) J. Cell Sci , vol.119 , pp. 360-369
    • Liu, Y.1    Chang, A.2
  • 84
    • 33644636609 scopus 로고    scopus 로고
    • A novel mouse Smad4 mutation reduces protein stability and wild-type protein levels
    • Chen, Y., Yee, D. & Magnuson, T. A novel mouse Smad4 mutation reduces protein stability and wild-type protein levels. Mamm. Genome. 17, 211-219 (2006).
    • (2006) Mamm. Genome , vol.17 , pp. 211-219
    • Chen, Y.1    Yee, D.2    Magnuson, T.3
  • 85
    • 25444533096 scopus 로고    scopus 로고
    • Trapping of normal EB1 ligands in aggresomes formed by an EB1 deletion mutant
    • Riess, N. P. et al. Trapping of normal EB1 ligands in aggresomes formed by an EB1 deletion mutant. BMC Cell. Biol. 6, 17 (2005).
    • (2005) BMC Cell. Biol , vol.6 , pp. 17
    • Riess, N.P.1
  • 86
    • 17044402604 scopus 로고    scopus 로고
    • The biological and chemical basis for tissue-selective amyloid disease
    • Sekijima, Y. et al. The biological and chemical basis for tissue-selective amyloid disease. Cell 121, 73-85 (2005).
    • (2005) Cell , vol.121 , pp. 73-85
    • Sekijima, Y.1
  • 87
    • 0032815965 scopus 로고    scopus 로고
    • Variation in the biochemical/biophysical properties of mutant superoxide dismutase 1 enzymes and the rate of disease progression in familial amyotrophic lateral sclerosis kindreds
    • Ratovitski, T. et al. Variation in the biochemical/biophysical properties of mutant superoxide dismutase 1 enzymes and the rate of disease progression in familial amyotrophic lateral sclerosis kindreds. Hum. Mol. Genet. 8, 1451-1460 (1999).
    • (1999) Hum. Mol. Genet , vol.8 , pp. 1451-1460
    • Ratovitski, T.1
  • 88
    • 20144380189 scopus 로고    scopus 로고
    • Identification of a novel amino acid deletion mutation and a very rare single nucleotide variant in a Japanese family with type I antithrombin deficiency
    • Katayama, K. et al. Identification of a novel amino acid deletion mutation and a very rare single nucleotide variant in a Japanese family with type I antithrombin deficiency. Thromb. Res. 116, 215-221 (2005).
    • (2005) Thromb. Res , vol.116 , pp. 215-221
    • Katayama, K.1
  • 89
    • 4644272165 scopus 로고    scopus 로고
    • Trafficking defects of a novel autosomal recessive distal renal tubular acidosis mutant (S773P) of the human kidney anion exchanger (kAE1)
    • Kittanakom, S., Cordat, E., Akkarapatumwong, V., Yenchitsomanus, P. T. & Reithmeier, R. A. Trafficking defects of a novel autosomal recessive distal renal tubular acidosis mutant (S773P) of the human kidney anion exchanger (kAE1). J. Biol. Chem. 279, 40960-40971 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 40960-40971
    • Kittanakom, S.1    Cordat, E.2    Akkarapatumwong, V.3    Yenchitsomanus, P.T.4    Reithmeier, R.A.5
  • 90
    • 1542349213 scopus 로고    scopus 로고
    • Familial Parkinson's disease-associated L166P mutation disrupts DJ-1 protein folding and function
    • Olzmann, J. A. et al. Familial Parkinson's disease-associated L166P mutation disrupts DJ-1 protein folding and function. J. Biol. Chem. 279, 8506-8515 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 8506-8515
    • Olzmann, J.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.