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Volumn 163, Issue , 1998, Pages 161-176

The MHC class I ligand-generating system: Roles of immunoproteasomes and the interferon-γ-inducible proteasome activator PA28

Author keywords

[No Author keywords available]

Indexed keywords

GAMMA INTERFERON; LIGAND; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PROTEASOME;

EID: 0031819536     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1600-065X.1998.tb01195.x     Document Type: Review
Times cited : (271)

References (127)
  • 1
    • 0027468145 scopus 로고
    • The biochemistry and cell biology of antigen processing and presentation
    • Germain RN, Margulies DH. The biochemistry and cell biology of antigen processing and presentation. Annu Rev Immunol 1993;11:403-450.
    • (1993) Annu Rev Immunol , vol.11 , pp. 403-450
    • Germain, R.N.1    Margulies, D.H.2
  • 2
    • 0029001515 scopus 로고
    • Generation, translocation, and presentation of MHC class I-restricted peptides
    • Heemels M-T, Ploegh H. Generation, translocation, and presentation of MHC class I-restricted peptides. Annu Rev Biochem 1995;64:463-491.
    • (1995) Annu Rev Biochem , vol.64 , pp. 463-491
    • Heemels, M.-T.1    Ploegh, H.2
  • 3
    • 0029591482 scopus 로고
    • The genetics of proteasomes and antigen processing
    • Monaco JJ, Nandi D. The genetics of proteasomes and antigen processing. Annu Rev Genet 1995;29:729-754.
    • (1995) Annu Rev Genet , vol.29 , pp. 729-754
    • Monaco, J.J.1    Nandi, D.2
  • 4
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux O, Tanaka K, Goldberg AL. Structure and functions of the 20S and 26S proteasomes. Annu Rev Biochem 1996;65:801-847.
    • (1996) Annu Rev Biochem , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 6
    • 0026764311 scopus 로고
    • Proteolysis, proteasomes and antigen presentation
    • Goldberg AL, Rock KL. Proteolysis, proteasomes and antigen presentation. Nature 1992;357:375-379.
    • (1992) Nature , vol.357 , pp. 375-379
    • Goldberg, A.L.1    Rock, K.L.2
  • 7
    • 0029920469 scopus 로고    scopus 로고
    • Antigen processing and presentation by the class I major histocompatibility complex
    • York IA, Rock KL. Antigen processing and presentation by the class I major histocompatibility complex. Annu Rev Immunol 1996;14:369-396.
    • (1996) Annu Rev Immunol , vol.14 , pp. 369-396
    • York, I.A.1    Rock, K.L.2
  • 8
    • 0030248766 scopus 로고    scopus 로고
    • Peptide antigen production by the proteasome: Complexity provides efficiency
    • Groettrup M, Soza A, Kuckelkorn U, Kloetzel P-M. Peptide antigen production by the proteasome: complexity provides efficiency. Immunol Today 1996;17:429-435.
    • (1996) Immunol Today , vol.17 , pp. 429-435
    • Groettrup, M.1    Soza, A.2    Kuckelkorn, U.3    Kloetzel, P.-M.4
  • 10
    • 0029830046 scopus 로고    scopus 로고
    • Chromosomal localization of the proteasome Z subunit gene reveals an ancient chromosomal duplication involving the major histocompatibility complex
    • Kasahara M, et al. Chromosomal localization of the proteasome Z subunit gene reveals an ancient chromosomal duplication involving the major histocompatibility complex. Proc Natl Acad Sci USA 1996;93:9096-9101.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9096-9101
    • Kasahara, M.1
  • 11
    • 0030200759 scopus 로고    scopus 로고
    • How selective is the transporter associated with antigen processing?
    • Androlewicz MJ, Cresswell P. How selective is the transporter associated with antigen processing? Immunity 1996;5:1-5.
    • (1996) Immunity , vol.5 , pp. 1-5
    • Androlewicz, M.J.1    Cresswell, P.2
  • 12
    • 0342894676 scopus 로고    scopus 로고
    • Generation, intracellular transport and loading of peptides associated with MHC class I molecules
    • Koopmann J-O, Hämmerling GJ, Momburg F. Generation, intracellular transport and loading of peptides associated with MHC class I molecules. Curr Opin Immunol 1997;9:80-88.
    • (1997) Curr Opin Immunol , vol.9 , pp. 80-88
    • Koopmann, J.-O.1    Hämmerling, G.J.2    Momburg, F.3
  • 13
    • 0028965533 scopus 로고
    • Molecular chaperones in antigen presentation
    • Williams DB, Watts TH. Molecular chaperones in antigen presentation. Curr Opin Immunol 1995;7:77-84.
    • (1995) Curr Opin Immunol , vol.7 , pp. 77-84
    • Williams, D.B.1    Watts, T.H.2
  • 14
    • 0028366212 scopus 로고
    • Heat shock proteins transfer peptides during antigen processing and CTL priming
    • Srivastava PK, Udono H, Blachere NE, Li Z. Heat shock proteins transfer peptides during antigen processing and CTL priming. Immunogenetics 1994;39:93-98.
    • (1994) Immunogenetics , vol.39 , pp. 93-98
    • Srivastava, P.K.1    Udono, H.2    Blachere, N.E.3    Li, Z.4
  • 15
    • 0028979675 scopus 로고
    • A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptide
    • Suto R, Srivastava PK. A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptide. Science 1995;269:1585-1588.
    • (1995) Science , vol.269 , pp. 1585-1588
    • Suto, R.1    Srivastava, P.K.2
  • 16
    • 0030800342 scopus 로고    scopus 로고
    • Influences of transporter associated with antigen processing (TAP) on the repertoire of peptides associated with the endoplasmic reticulum-resident stress protein gp96
    • Arnold D, Wahl C, Faath S, Rammensee HG, Schild H. Influences of transporter associated with antigen processing (TAP) on the repertoire of peptides associated with the endoplasmic reticulum-resident stress protein gp96. J Exp Med 1997;186:461-466.
    • (1997) J Exp Med , vol.186 , pp. 461-466
    • Arnold, D.1    Wahl, C.2    Faath, S.3    Rammensee, H.G.4    Schild, H.5
  • 17
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser M. Ubiquitin-dependent protein degradation. Annu Rev Genet 1996;30:405-439.
    • (1996) Annu Rev Genet , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 18
    • 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 1988;168:1211-1224.
    • (1988) J Exp Med , vol.168 , pp. 1211-1224
    • Townsend, A.1
  • 19
    • 0027263157 scopus 로고
    • A role for the ubiquitin-dependent proteolytic pathway in MHC class I-restricted antigen presentation
    • Michalek MT, Grant EP, Gramm C, Goldberg AL, Rock KL. A role for the ubiquitin-dependent proteolytic pathway in MHC class I-restricted antigen presentation. Nature 1993;363:552-554.
    • (1993) Nature , vol.363 , pp. 552-554
    • Michalek, M.T.1    Grant, E.P.2    Gramm, C.3    Goldberg, A.L.4    Rock, K.L.5
  • 20
    • 0029120173 scopus 로고
    • Rate of antigen degradation by the ubiquitin-proteasome pathway influences MHC class I presentation
    • Grant EP, Michalek MT, Goldberg AL, Rock KL. Rate of antigen degradation by the ubiquitin-proteasome pathway influences MHC class I presentation. J Immunol 1995;155:3750-3758.
    • (1995) J Immunol , vol.155 , pp. 3750-3758
    • Grant, E.P.1    Michalek, M.T.2    Goldberg, A.L.3    Rock, K.L.4
  • 21
    • 0030977234 scopus 로고    scopus 로고
    • Targeting of HIV-1 antigens for rapid intracellular degradation enhances cytotoxic T lymphocyte (CTL) recognition and the induction of de novo CTL responses in vivo after immunization
    • Tobery TW, Siliciano RF. Targeting of HIV-1 antigens for rapid intracellular degradation enhances cytotoxic T lymphocyte (CTL) recognition and the induction of de novo CTL responses in vivo after immunization. J Exp Med 1997;185:909-920.
    • (1997) J Exp Med , vol.185 , pp. 909-920
    • Tobery, T.W.1    Siliciano, R.F.2
  • 22
    • 0026766091 scopus 로고
    • The N-end rule
    • Varshavsky A. The N-end rule. Cell 1992;69:725-735.
    • (1992) Cell , vol.69 , pp. 725-735
    • Varshavsky, A.1
  • 23
    • 0030774939 scopus 로고    scopus 로고
    • Production of a specific major histocompatibility complex class I-restricted epitope by ubiquitin-dependent degradation of modified ovalbumin in lymphocyte lysate
    • Ben-Shahar S, Cassouto B, Novak L, Porgador A, Reiss Y. Production of a specific major histocompatibility complex class I-restricted epitope by ubiquitin-dependent degradation of modified ovalbumin in lymphocyte lysate. J Biol Chem 1997;272:21060-21066.
    • (1997) J Biol Chem , vol.272 , pp. 21060-21066
    • Ben-Shahar, S.1    Cassouto, B.2    Novak, L.3    Porgador, A.4    Reiss, Y.5
  • 24
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most proteins and the generation of peptides presented on MHC class I molecules
    • Rock KL, et al. Inhibitors of the proteasome block the degradation of most proteins and the generation of peptides presented on MHC class I molecules. Cell 1994;78:761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1
  • 25
    • 0029123827 scopus 로고
    • Novel dipeptide aldehydes are proteasome inhibitors and block the MHC-I antigen-processing pathway
    • Harding CV, et al. Novel dipeptide aldehydes are proteasome inhibitors and block the MHC-I antigen-processing pathway. J Immunol 1995;155:1767-1775.
    • (1995) J Immunol , vol.155 , pp. 1767-1775
    • Harding, C.V.1
  • 26
    • 0030926777 scopus 로고    scopus 로고
    • Lactacystin and clasto-lactacystin β-lactone modify multiple proteasome β-subunits and inhibit protein degradation and major histocompatibility complex class I antigen presentation
    • Craiu A, et al. Lactacystin and clasto-lactacystin β-lactone modify multiple proteasome β-subunits and inhibit protein degradation and major histocompatibility complex class I antigen presentation. J Biol Chem 1997;272:13437-13445.
    • (1997) J Biol Chem , vol.272 , pp. 13437-13445
    • Craiu, A.1
  • 27
    • 0031032422 scopus 로고    scopus 로고
    • The proteasome-specific inhibitor lactacystin blocks presentation of cytotoxic T lymphocyte epitopes in human and murine cells
    • Cerundolo V, et al. The proteasome-specific inhibitor lactacystin blocks presentation of cytotoxic T lymphocyte epitopes in human and murine cells. Eur J Immunol 1997;27:336-341.
    • (1997) Eur J Immunol , vol.27 , pp. 336-341
    • Cerundolo, V.1
  • 28
    • 0027991677 scopus 로고
    • MHC class I expression in mice lacking the proteasome subunit LMP
    • Fehling HJ, et al. MHC class I expression in mice lacking the proteasome subunit LMP. Science 1994;265:1234-1237.
    • (1994) Science , vol.265 , pp. 1234-1237
    • Fehling, H.J.1
  • 29
    • 0028519275 scopus 로고
    • Altered peptidase and viral specific T cell response in LMP2 mutant mice
    • Van Kaer L, et al. Altered peptidase and viral specific T cell response in LMP2 mutant mice. Immunity 1994;1:533-541.
    • (1994) Immunity , vol.1 , pp. 533-541
    • Van Kaer, L.1
  • 30
    • 0028097823 scopus 로고
    • Interferon γ stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasome
    • Boes B, Hengel H, Ruppert T, Multhaup G, Koszinowski UH, Kloetzel P-M. Interferon γ stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasome. J Exp Med 1994;179:901-909.
    • (1994) J Exp Med , vol.179 , pp. 901-909
    • Boes, B.1    Hengel, H.2    Ruppert, T.3    Multhaup, G.4    Koszinowski, U.H.5    Kloetzel, P.-M.6
  • 31
    • 0028968217 scopus 로고
    • Contribution of proteasome-mediated proteolysis to the hierarchy of epitopes presented by major histocompatibility complex class I molecules
    • Niedermann G, et al. Contribution of proteasome-mediated proteolysis to the hierarchy of epitopes presented by major histocompatibility complex class I molecules. Immunity 1995;2:289-299.
    • (1995) Immunity , vol.2 , pp. 289-299
    • Niedermann, G.1
  • 32
    • 0029781734 scopus 로고    scopus 로고
    • The proteolytic fragments generated by vertebrate proteasomes: Structural relationships to major histocompatibility complex class I binding peptides
    • Niedermann G, et al. The proteolytic fragments generated by vertebrate proteasomes: structural relationships to major histocompatibility complex class I binding peptides. Proc Natl Acad Sci USA 1996;93:8572-8577.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8572-8577
    • Niedermann, G.1
  • 33
    • 16044372545 scopus 로고    scopus 로고
    • A single residue exchange within a viral CTL epitope alters proteasome-mediated degradation resulting in lack of antigen presentation
    • Ossendorp F, et al. A single residue exchange within a viral CTL epitope alters proteasome-mediated degradation resulting in lack of antigen presentation. Immunity 1996;5:115-124.
    • (1996) Immunity , vol.5 , pp. 115-124
    • Ossendorp, F.1
  • 34
    • 0030602834 scopus 로고    scopus 로고
    • Coordinated dual cleavages induced by the proteasome regulator PA28 lead to dominant MHC ligands
    • Dick TP, et al. Coordinated dual cleavages induced by the proteasome regulator PA28 lead to dominant MHC ligands. Cell 1996;86:253-262.
    • (1996) Cell , vol.86 , pp. 253-262
    • Dick, T.P.1
  • 35
    • 2642676173 scopus 로고    scopus 로고
    • Double-cleavage production of the CTL epitope by proteasomes and PA28: Role of the flanking region
    • In press
    • Shimbara N, et al. Double-cleavage production of the CTL epitope by proteasomes and PA28: Role of the flanking region. Genes to Cells 1998;3 (In press).
    • (1998) Genes to Cells , vol.3
    • Shimbara, N.1
  • 36
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister W, Walz J, Zühl F, Seemüller E. The proteasome: Paradigm of a self-compartmentalizing protease. Cell 1998;92:367-380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zühl, F.3    Seemüller, E.4
  • 37
    • 0030897031 scopus 로고    scopus 로고
    • Structure of 20S proteasome from yeast at 2.4 Å resolution
    • Groll M, et al. Structure of 20S proteasome from yeast at 2.4 Å resolution. Nature 1997;386:463-471.
    • (1997) Nature , vol.386 , pp. 463-471
    • Groll, M.1
  • 38
    • 0030726159 scopus 로고    scopus 로고
    • Protein translocation channels in the proteasome and other protease
    • Larsen CN, Finley D. Protein translocation channels in the proteasome and other protease. Cell 1997;91:431-434.
    • (1997) Cell , vol.91 , pp. 431-434
    • Larsen, C.N.1    Finley, D.2
  • 39
    • 0031887332 scopus 로고    scopus 로고
    • Proteasomes: Structure and biology
    • In press
    • Tanaka K. Proteasomes: structure and biology. J Biochem 1998;123 (In press).
    • (1998) J Biochem , vol.123
    • Tanaka, K.1
  • 40
    • 0031973716 scopus 로고    scopus 로고
    • The AAA team: Related ATPases with diverse functions
    • Patel S, Latterich M. The AAA team: related ATPases with diverse functions. Trends Cell Biol 1998;8:65-71.
    • (1998) Trends Cell Biol , vol.8 , pp. 65-71
    • Patel, S.1    Latterich, M.2
  • 42
    • 0028037781 scopus 로고
    • cDNA cloning and interferon γ down-regulation of proteasomal subunits X and Y
    • Akiyama K, et al. cDNA cloning and interferon γ down-regulation of proteasomal subunits X and Y. Science 1994;265:1231-1234.
    • (1994) Science , vol.265 , pp. 1231-1234
    • Akiyama, K.1
  • 43
    • 0029911690 scopus 로고    scopus 로고
    • Newly identified pair of proteasomal subunits regulated reciprocally by interferon-γ
    • Hisamatsu H, et al. Newly identified pair of proteasomal subunits regulated reciprocally by interferon-γ. J Exp Med 1996;183:1807-1816.
    • (1996) J Exp Med , vol.183 , pp. 1807-1816
    • Hisamatsu, H.1
  • 44
    • 0028500190 scopus 로고
    • Proteasome components with reciprocal expression to that of the MHC-encoded LMP protein
    • Belich M, Glynne RJ, Senger G, Sheer D, Trowsdale J. Proteasome components with reciprocal expression to that of the MHC-encoded LMP protein. Curr Biol 1994;4:769-776.
    • (1994) Curr Biol , vol.4 , pp. 769-776
    • Belich, M.1    Glynne, R.J.2    Senger, G.3    Sheer, D.4    Trowsdale, J.5
  • 45
    • 0028241569 scopus 로고
    • Displacement of housekeeping proteasome subunits by MHC-encoded LMPs: A newly discovered mechanism for modulating the multicatalytic proteinase complex
    • Früh K, Gossen M, Wang K, Bujard H, Peterson PA, Yang Y. Displacement of housekeeping proteasome subunits by MHC-encoded LMPs: a newly discovered mechanism for modulating the multicatalytic proteinase complex. EMBO J 1994;13:3236-3244.
    • (1994) EMBO J , vol.13 , pp. 3236-3244
    • Früh, K.1    Gossen, M.2    Wang, K.3    Bujard, H.4    Peterson, P.A.5    Yang, Y.6
  • 46
    • 0029878931 scopus 로고    scopus 로고
    • Identification of MECL-1 (LMP-10) as the third IFN-γ-inducible proteasome subunit
    • Nandi D, Jiang H, Monaco JJ. Identification of MECL-1 (LMP-10) as the third IFN-γ-inducible proteasome subunit. J Immunol 1996;156:2361-2364.
    • (1996) J Immunol , vol.156 , pp. 2361-2364
    • Nandi, D.1    Jiang, H.2    Monaco, J.J.3
  • 48
    • 0031571887 scopus 로고    scopus 로고
    • The mouse genes encoding the third pair of β-type proteasome subunits regulated reciprocally by IFN-γ: Structural comparison, chromosomal localization, and analysis of the promoter
    • Hayashi M, Ishibashi T, Tanaka K, Kasahara M. The mouse genes encoding the third pair of β-type proteasome subunits regulated reciprocally by IFN-γ: structural comparison, chromosomal localization, and analysis of the promoter. J Immunol 1997;159:2760-2770.
    • (1997) J Immunol , vol.159 , pp. 2760-2770
    • Hayashi, M.1    Ishibashi, T.2    Tanaka, K.3    Kasahara, M.4
  • 49
    • 0028179233 scopus 로고
    • Interferon-γ induces different subunit organizations and functional diversity of proteasomes
    • Aki M, et al. Interferon-γ induces different subunit organizations and functional diversity of proteasomes. J Biochem 1993;115:257-269.
    • (1993) J Biochem , vol.115 , pp. 257-269
    • Aki, M.1
  • 50
    • 0030693111 scopus 로고    scopus 로고
    • Biogenesis of eukaryotic 20S proteasomes: The complex maturation pathway of a complex enzyme
    • Schmidt M, Kloetzel P-M. Biogenesis of eukaryotic 20S proteasomes: the complex maturation pathway of a complex enzyme. FASEB J 1997;11:1235-1243.
    • (1997) FASEB J , vol.11 , pp. 1235-1243
    • Schmidt, M.1    Kloetzel, P.-M.2
  • 51
    • 0029789918 scopus 로고    scopus 로고
    • Autocatalytic processing of the 20S proteasome
    • Seemüller E, Lupas A, Baumeister W. Autocatalytic processing of the 20S proteasome. Nature 1996;382:468-470.
    • (1996) Nature , vol.382 , pp. 468-470
    • Seemüller, E.1    Lupas, A.2    Baumeister, W.3
  • 52
    • 0030595329 scopus 로고    scopus 로고
    • Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly
    • Chen P, Hochstrasser M. Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly. Cell 1996;86:961-972.
    • (1996) Cell , vol.86 , pp. 961-972
    • Chen, P.1    Hochstrasser, M.2
  • 53
    • 0030481129 scopus 로고    scopus 로고
    • Analysis of mammalian 20S proteasome biogenesis: The maturation of β-subunits is an ordered two-step mechanism involving autocatalysis
    • Schmidtke G, et al. Analysis of mammalian 20S proteasome biogenesis: the maturation of β-subunits is an ordered two-step mechanism involving autocatalysis. EMBO J 1996;15:6887-6898.
    • (1996) EMBO J , vol.15 , pp. 6887-6898
    • Schmidtke, G.1
  • 54
    • 0030774890 scopus 로고    scopus 로고
    • The active sites of the eukaryotic 20S proteasome and their involvement in subunit precursor processing
    • Heinemeyer W, Fischer M, Krimmer T, Stachon U, Wolf DH. The active sites of the eukaryotic 20S proteasome and their involvement in subunit precursor processing. J Biol Chem 1997;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
  • 55
    • 0030793290 scopus 로고    scopus 로고
    • The subunits MECL-1 and LMP2 are mutually required for incorporation into the 20S proteasome
    • Groettrup M, Standera S, Stohwasser R, Kloetzel P-M. The subunits MECL-1 and LMP2 are mutually required for incorporation into the 20S proteasome. Proc Natl Acad Sci USA 1997;94:8970-8975.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8970-8975
    • Groettrup, M.1    Standera, S.2    Stohwasser, R.3    Kloetzel, P.-M.4
  • 56
    • 0030880547 scopus 로고    scopus 로고
    • Intermediates in the formation of mouse 20S proteasomes: Implications for the assembly of precursor β subunits
    • Nandi D, Woodward E, Ginsburg DB, Monaco JJ. Intermediates in the formation of mouse 20S proteasomes: implications for the assembly of precursor β subunits. EMBO J 1997;16:5363-5375.
    • (1997) EMBO J , vol.16 , pp. 5363-5375
    • Nandi, D.1    Woodward, E.2    Ginsburg, D.B.3    Monaco, J.J.4
  • 57
    • 0031973736 scopus 로고    scopus 로고
    • Immunoproteasome assembly: Cooperative incorporation of interferon γ (IFN-γ)-inducible subunits
    • Griffin TA, et al. Immunoproteasome assembly: cooperative incorporation of interferon γ (IFN-γ)-inducible subunits. J Exp Med 1998;187:97-104.
    • (1998) J Exp Med , vol.187 , pp. 97-104
    • Griffin, T.A.1
  • 58
    • 0027214605 scopus 로고
    • γ-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes
    • Gaczynska M, Rock KL, Goldberg AL. γ-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes. Nature 1993;365:264-267.
    • (1993) Nature , vol.365 , pp. 264-267
    • Gaczynska, M.1    Rock, K.L.2    Goldberg, A.L.3
  • 59
    • 0027223877 scopus 로고
    • MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
    • Driscoll J, Brown MG, Finley D, Monaco JJ. MHC-linked LMP gene products specifically alter peptidase activities of the proteasome. Nature 1993;365:262-264.
    • (1993) Nature , vol.365 , pp. 262-264
    • Driscoll, J.1    Brown, M.G.2    Finley, D.3    Monaco, J.J.4
  • 61
    • 0028136465 scopus 로고
    • Peptidase activities of proteasomes are differentially regulated by the major histocompatibility complex-encoded genes for LMP2 and LMP7
    • Gaczynska M, Rock KL, Spies T, Goldberg AL. Peptidase activities of proteasomes are differentially regulated by the major histocompatibility complex-encoded genes for LMP2 and LMP7. Proc Natl Acad Sci USA 1994;91:9213-9217.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9213-9217
    • Gaczynska, M.1    Rock, K.L.2    Spies, T.3    Goldberg, A.L.4
  • 62
    • 0030037846 scopus 로고    scopus 로고
    • Proteasome subunits X and Y alter peptidase activities in opposite ways to the interferon-γ-induced subunits LMP2 and LMP7
    • Gaczynska M, Goldberg AL, Tanaka K, Hendil KB, Rock KL. Proteasome subunits X and Y alter peptidase activities in opposite ways to the interferon-γ-induced subunits LMP2 and LMP7. J Biol Chem 1996,271:17275-17280.
    • (1996) J Biol Chem , vol.271 , pp. 17275-17280
    • Gaczynska, M.1    Goldberg, A.L.2    Tanaka, K.3    Hendil, K.B.4    Rock, K.L.5
  • 63
    • 0028890880 scopus 로고
    • Effects of interferon γ and major histocompatibility complex-encoded subunits on peptidase activities of human multicatalytic protease
    • Ustrell V, Pratt G, Rechsteiner M. Effects of interferon γ and major histocompatibility complex-encoded subunits on peptidase activities of human multicatalytic protease. Proc Natl Acad Sci USA 1995,92:584-588.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 584-588
    • Ustrell, V.1    Pratt, G.2    Rechsteiner, M.3
  • 64
    • 0029162601 scopus 로고
    • Incorporation of major histocompatibility complex-encoded subunits LMP2 and LMP7 changes the quality of the 20S proteasome polypeptide processing products independent of interferon-γ
    • Kuckelkorn U, Frentzel S, Kraft R, Kostka S, Groettrup M, Kloetzel P-M. Incorporation of major histocompatibility complex-encoded subunits LMP2 and LMP7 changes the quality of the 20S proteasome polypeptide processing products independent of interferon-γ. Eur J Immunol 1995;25:2605-2611.
    • (1995) Eur J Immunol , vol.25 , pp. 2605-2611
    • Kuckelkorn, U.1    Frentzel, S.2    Kraft, R.3    Kostka, S.4    Groettrup, M.5    Kloetzel, P.-M.6
  • 65
    • 0026600718 scopus 로고
    • Primary structure of the Thermoplasma proteasome and its implications for the structure, function, and evolution of the multicatalytic proteinase
    • Zwickl P, Grziwa A, Pühler G, Dihlmann B, Lottspeich F, Baumeister W. Primary structure of the Thermoplasma proteasome and its implications for the structure, function, and evolution of the multicatalytic proteinase. Biochemistry 1992;31:964-972.
    • (1992) Biochemistry , vol.31 , pp. 964-972
    • Zwickl, P.1    Grziwa, A.2    Pühler, G.3    Dihlmann, B.4    Lottspeich, F.5    Baumeister, W.6
  • 66
    • 0029867623 scopus 로고    scopus 로고
    • Proteasomes: Destruction as a programme
    • Hilt W, Wolf DH. Proteasomes: destruction as a programme. Trends Biochem Sci 1996;21:96-102.
    • (1996) Trends Biochem Sci , vol.21 , pp. 96-102
    • Hilt, W.1    Wolf, D.H.2
  • 67
    • 0026595367 scopus 로고
    • Alternative exon usage and processing of the major histocompatibility complex-encoded proteasome subunits
    • Früh K, et al. Alternative exon usage and processing of the major histocompatibility complex-encoded proteasome subunits. J Biol Chem 1992;267:22131-22140.
    • (1992) J Biol Chem , vol.267 , pp. 22131-22140
    • Früh, K.1
  • 68
    • 0027370768 scopus 로고
    • Genomic organization of the mouse Lmp-2 gene and characteristic structure of its promoter
    • Kishi F, Suminami Y, Monaco JJ. Genomic organization of the mouse Lmp-2 gene and characteristic structure of its promoter. Gene 1993;133:243-248.
    • (1993) Gene , vol.133 , pp. 243-248
    • Kishi, F.1    Suminami, Y.2    Monaco, J.J.3
  • 69
    • 0027308710 scopus 로고
    • Genomic organization and tissue expression of mouse proteasome gene Lmp-2
    • Zhou P, Zanelli E, Smart M, David C. Genomic organization and tissue expression of mouse proteasome gene Lmp-2. Genomics 1993;16:664-668.
    • (1993) Genomics , vol.16 , pp. 664-668
    • Zhou, P.1    Zanelli, E.2    Smart, M.3    David, C.4
  • 70
    • 0029005476 scopus 로고
    • Characterization and mapping of the gene encoding mouse proteasome subunit DELTA (Lmp19)
    • Woodward EC, Monaco JJ. Characterization and mapping of the gene encoding mouse proteasome subunit DELTA (Lmp19). Immunogenetics 1995;42:28-34.
    • (1995) Immunogenetics , vol.42 , pp. 28-34
    • Woodward, E.C.1    Monaco, J.J.2
  • 71
    • 0030044440 scopus 로고    scopus 로고
    • Genomic organization of a mouse MHC class II region including the H2-M and Lmp2 loci
    • Péléraux A, Karlsson L, Chambers J, Peterson PA. Genomic organization of a mouse MHC class II region including the H2-M and Lmp2 loci. Immunogenetics 1996;43:204-214.
    • (1996) Immunogenetics , vol.43 , pp. 204-214
    • Péléraux, A.1    Karlsson, L.2    Chambers, J.3    Peterson, P.A.4
  • 72
    • 0031281868 scopus 로고    scopus 로고
    • DNA sequence chromosomal localization, and tissue expression of the mouse proteasome subunit Lmp10 (Psmb10) gene
    • Cruz M, Elenich LA, Smolarek TA, Menon AG, Monaco JJ. DNA sequence chromosomal localization, and tissue expression of the mouse proteasome subunit Lmp10 (Psmb10) gene. Genomics 1997;45:618-622.
    • (1997) Genomics , vol.45 , pp. 618-622
    • Cruz, M.1    Elenich, L.A.2    Smolarek, T.A.3    Menon, A.G.4    Monaco, J.J.5
  • 74
    • 0031474006 scopus 로고    scopus 로고
    • Structural analysis and chromosomal localization of the Psmb5 gene coding for the constitutively expressed β-type proteasome subunit
    • Kohda K, Matsuda Y, Ishibashi T, Tanaka K, Kasahara M. Structural analysis and chromosomal localization of the Psmb5 gene coding for the constitutively expressed β-type proteasome subunit. Immunogenetics 1997;47:77-87.
    • (1997) Immunogenetics , vol.47 , pp. 77-87
    • Kohda, K.1    Matsuda, Y.2    Ishibashi, T.3    Tanaka, K.4    Kasahara, M.5
  • 75
    • 0027415561 scopus 로고
    • Genomic structure and function in the MHC
    • Trowsdale J. Genomic structure and function in the MHC. Trends Genet 1993;9:117-122.
    • (1993) Trends Genet , vol.9 , pp. 117-122
    • Trowsdale, J.1
  • 76
    • 0030200739 scopus 로고    scopus 로고
    • Paralogy mapping: Identification of a region in the human MHC triplicated onto human chromosomes 1 and 9 allows the prediction and isolation of novel PBX and NOTCH loci
    • Katsanis N, Fitzgibbon J, Fischer EMC. Paralogy mapping: identification of a region in the human MHC triplicated onto human chromosomes 1 and 9 allows the prediction and isolation of novel PBX and NOTCH loci. Genomics 1996;35:101-108.
    • (1996) Genomics , vol.35 , pp. 101-108
    • Katsanis, N.1    Fitzgibbon, J.2    Fischer, E.M.C.3
  • 78
    • 0027404163 scopus 로고
    • Phylogenetic diversification of immunoglobulin genes and the antibody repertoire
    • Litman GW, et al. Phylogenetic diversification of immunoglobulin genes and the antibody repertoire. Mol Biol Evol 1993;10:60-72.
    • (1993) Mol Biol Evol , vol.10 , pp. 60-72
    • Litman, G.W.1
  • 80
    • 0028867419 scopus 로고
    • New insights into V(D)J recombination and its role in the evolution of the immune system
    • Thompson CB. New insights into V(D)J recombination and its role in the evolution of the immune system. Immunity 1995;3:531-539.
    • (1995) Immunity , vol.3 , pp. 531-539
    • Thompson, C.B.1
  • 81
    • 0030732316 scopus 로고    scopus 로고
    • New insights into the genomic organization and origin of the major histocompatibility complex: Role of chromosomal (genome) duplication in the emergence of the adaptive immune system
    • Kasahara M. New insights into the genomic organization and origin of the major histocompatibility complex: role of chromosomal (genome) duplication in the emergence of the adaptive immune system. Hereditas 1997;127:59-65.
    • (1997) Hereditas , vol.127 , pp. 59-65
    • Kasahara, M.1
  • 82
    • 0026634168 scopus 로고
    • Evolution of the major histocompatibility complex: Isolation of class II A cDNA clones from the cartilaginous fish
    • Kasahara M, Vazquez M, Sato K, McKinney EC, Flajnik MF. Evolution of the major histocompatibility complex: Isolation of class II A cDNA clones from the cartilaginous fish. Proc Natl Acad Sci USA 1992;89:6688-6692.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6688-6692
    • Kasahara, M.1    Vazquez, M.2    Sato, K.3    McKinney, E.C.4    Flajnik, M.F.5
  • 83
    • 0026509498 scopus 로고
    • Identification of a shark sequence resembling the major histocompatibility complex class I α3 domain
    • Hashimoto K, Nakanishi T, Kurosawa Y. Identification of a shark sequence resembling the major histocompatibility complex class I α3 domain. Proc Natl Acad Sci USA 1992;89:2209-2212.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2209-2212
    • Hashimoto, K.1    Nakanishi, T.2    Kurosawa, Y.3
  • 84
    • 0029977015 scopus 로고    scopus 로고
    • Isolation of low molecular mass polypeptide complementary DNA clones from primitive vertebrates: Implications for the origin of MHC class I-restricted antigen presentation
    • Kandil E, et al. Isolation of low molecular mass polypeptide complementary DNA clones from primitive vertebrates: implications for the origin of MHC class I-restricted antigen presentation. J Immunol 1996;156:4245-4253.
    • (1996) J Immunol , vol.156 , pp. 4245-4253
    • Kandil, E.1
  • 85
    • 0031570872 scopus 로고    scopus 로고
    • Evolution of proteasome subunits δ and LMP2: Complementary DNA cloning and linkage analysis with MHC in lower vertebrates
    • Nonaka M, Namikawa-Yamada C, Sasaki M, Salter-Cid L, Flajnik MF. Evolution of proteasome subunits δ and LMP2: complementary DNA cloning and linkage analysis with MHC in lower vertebrates. J Immunol 1997;159:734-740.
    • (1997) J Immunol , vol.159 , pp. 734-740
    • Nonaka, M.1    Namikawa-Yamada, C.2    Sasaki, M.3    Salter-Cid, L.4    Flajnik, M.F.5
  • 86
    • 0030699351 scopus 로고    scopus 로고
    • The 20S proteasome gene family in Arabidopsis thalian
    • Parmentier Y, Bouchez D, Fleck J, Genschik P. The 20S proteasome gene family in Arabidopsis thalian. FEBS Lett 1997;416:281-285.
    • (1997) FEBS Lett , vol.416 , pp. 281-285
    • Parmentier, Y.1    Bouchez, D.2    Fleck, J.3    Genschik, P.4
  • 87
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins CF. ABC transporters: From microorganisms to man. Annu Rev Cell Biol 1992;8:67-113.
    • (1992) Annu Rev Cell Biol , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 88
    • 0030853591 scopus 로고    scopus 로고
    • Notch in vertebrates
    • Robey E. Notch in vertebrates. Curr Opin Genet Dev 1997;7:551-557.
    • (1997) Curr Opin Genet Dev , vol.7 , pp. 551-557
    • Robey, E.1
  • 89
    • 0025858492 scopus 로고
    • Evolution of the complement system
    • Farries TC, Atkinson JP. Evolution of the complement system. Immunol Today 1991;12:295-300.
    • (1991) Immunol Today , vol.12 , pp. 295-300
    • Farries, T.C.1    Atkinson, J.P.2
  • 90
    • 0030902728 scopus 로고    scopus 로고
    • Chromosomal duplication and the emergence of the adaptive immune system
    • Kasahara M, Nakaya J, Satta Y, Takahata N. Chromosomal duplication and the emergence of the adaptive immune system. Trends Genet 1997;13:90-92.
    • (1997) Trends Genet , vol.13 , pp. 90-92
    • Kasahara, M.1    Nakaya, J.2    Satta, Y.3    Takahata, N.4
  • 92
    • 0011354387 scopus 로고    scopus 로고
    • Conservation, duplication, and divergence of developmental genes during chordate evolution
    • Sharman AC, Holland PWH. Conservation, duplication, and divergence of developmental genes during chordate evolution. Neth J Zool 1996;46:47-67.
    • (1996) Neth J Zool , vol.46 , pp. 47-67
    • Sharman, A.C.1    Holland, P.W.H.2
  • 93
    • 0030473920 scopus 로고    scopus 로고
    • Gen(om)e duplications in the evolution of early vertebrates
    • Sidow A. Gen(om)e duplications in the evolution of early vertebrates. Curr Opin Genet Dev 1996;6:715-722.
    • (1996) Curr Opin Genet Dev , vol.6 , pp. 715-722
    • Sidow, A.1
  • 94
    • 0026669739 scopus 로고
    • Identification, purification, and characterization of a protein activator (PA28) of the 20S proteasome (macropain)
    • Ma C-P, Slaughter CA, DeMartino GN. Identification, purification, and characterization of a protein activator (PA28) of the 20S proteasome (macropain). J Biol Chem 1992;267:10515-10523.
    • (1992) J Biol Chem , vol.267 , pp. 10515-10523
    • Ma, C.-P.1    Slaughter, C.A.2    Demartino, G.N.3
  • 95
    • 0026498493 scopus 로고
    • Purification of an 11S regulator of the multicatalytic protease
    • Dubiel W, Pratt G, Ferrell K, Rechsteiner M. Purification of an 11S regulator of the multicatalytic protease. J Biol Chem 1992;267:22369-22377.
    • (1992) J Biol Chem , vol.267 , pp. 22369-22377
    • Dubiel, W.1    Pratt, G.2    Ferrell, K.3    Rechsteiner, M.4
  • 96
    • 0028300177 scopus 로고
    • PA28 activator protein forms regulatory caps on proteasome stacked rings
    • Gray CW, Slaughter CA, DeMartino GN. PA28 activator protein forms regulatory caps on proteasome stacked rings. J Mol Biol 1994;236:7-15.
    • (1994) J Mol Biol , vol.236 , pp. 7-15
    • Gray, C.W.1    Slaughter, C.A.2    DeMartino, G.N.3
  • 97
    • 0029000418 scopus 로고
    • Primary structures of two homologous subunits of PA28, a γ-interferon-inducible protein activator of the 20S proteasome
    • Ahn JY, et al. Primary structures of two homologous subunits of PA28, a γ-interferon-inducible protein activator of the 20S proteasome. FEBS Lett 1995;366:37-42.
    • (1995) FEBS Lett , vol.366 , pp. 37-42
    • Ahn, J.Y.1
  • 98
    • 0025157203 scopus 로고
    • Cloning and nucleotide sequence of cDNA for Ki antigen, a highly conserved nuclear protein detected with sera from patients with systemic lupus erythematosus
    • Nikaido T, et al. Cloning and nucleotide sequence of cDNA for Ki antigen, a highly conserved nuclear protein detected with sera from patients with systemic lupus erythematosus. Clin Exp Immunol 1990;79:209-214.
    • (1990) Clin Exp Immunol , vol.79 , pp. 209-214
    • Nikaido, T.1
  • 99
    • 0031085545 scopus 로고    scopus 로고
    • Molecular properties of the proteasome activator PA28 family proteins and γ-interferon regulation
    • Tanahashi N, et al. Molecular properties of the proteasome activator PA28 family proteins and γ-interferon regulation. Genes to Cells 1997;2:195-211.
    • (1997) Genes to Cells , vol.2 , pp. 195-211
    • Tanahashi, N.1
  • 100
    • 0029921985 scopus 로고    scopus 로고
    • A model for the quaternary structure of the proteasome activator PA28
    • Song X, et al. A model for the quaternary structure of the proteasome activator PA28. J Biol Chem 1996;271:26410-26417.
    • (1996) J Biol Chem , vol.271 , pp. 26410-26417
    • Song, X.1
  • 101
    • 0030840661 scopus 로고    scopus 로고
    • Expression and subcellular localization of mouse 20S proteasome activator complex PA28
    • Soza A, Knuehl C, Groettrup M, Henklein P, Tanaka K, Kloetzel P-M. Expression and subcellular localization of mouse 20S proteasome activator complex PA28. FEBS Lett 1997;413:27-34.
    • (1997) FEBS Lett , vol.413 , pp. 27-34
    • Soza, A.1    Knuehl, C.2    Groettrup, M.3    Henklein, P.4    Tanaka, K.5    Kloetzel, P.-M.6
  • 102
    • 0027983803 scopus 로고
    • Molecular cloning and expression of a γ-interferon-inducible activator of the multicatalytic protease
    • Realini C, Dubiel W, Pratt G, Ferrell K, Rechsteiner M. Molecular cloning and expression of a γ-interferon-inducible activator of the multicatalytic protease. J Biol Chem 1994;269:20727-20732.
    • (1994) J Biol Chem , vol.269 , pp. 20727-20732
    • Realini, C.1    Dubiel, W.2    Pratt, G.3    Ferrell, K.4    Rechsteiner, M.5
  • 103
    • 0031456970 scopus 로고    scopus 로고
    • Structure of the proteasome activator REGα (PA28α)
    • Knowlton JR, et al. Structure of the proteasome activator REGα (PA28α). Nature 1997;390:639-643.
    • (1997) Nature , vol.390 , pp. 639-643
    • Knowlton, J.R.1
  • 104
    • 0030607248 scopus 로고    scopus 로고
    • Reconstruction of proteasome activator PA28 from isolated subunits: Optimal activity is associated with an α,β-heterodimer
    • Kuehn L, Dahimann B. Reconstruction of proteasome activator PA28 from isolated subunits: optimal activity is associated with an α,β-heterodimer. FEBS Lett 1996;394:183-186.
    • (1996) FEBS Lett , vol.394 , pp. 183-186
    • Kuehn, L.1    Dahimann, B.2
  • 105
    • 0030735087 scopus 로고    scopus 로고
    • Relative functions of the α and β subunits of the proteasome activator, PA28
    • Song X, von Kampen J, Slaughter CA, DeMartino GN. Relative functions of the α and β subunits of the proteasome activator, PA28. J Biol Chem 1997;272:27994-28000.
    • (1997) J Biol Chem , vol.272 , pp. 27994-28000
    • Song, X.1    Von Kampen, J.2    Slaughter, C.A.3    DeMartino, G.N.4
  • 106
    • 0030611045 scopus 로고    scopus 로고
    • Characterization of recombinant REGα, REGβ, and REGγ proteasome activators
    • Realini C, et al. Characterization of recombinant REGα, REGβ, and REGγ proteasome activators. J Biol Chem 1997;272:25483-25492.
    • (1997) J Biol Chem , vol.272 , pp. 25483-25492
    • Realini, C.1
  • 107
    • 0027139249 scopus 로고
    • Interferon-γ up-regulates a unique set of proteins in human keratinocytes. Molecular cloning and expression of the cDNA encoding the RGD-sequence-containing protein IGUP I-5111
    • Honoré B, Leffers H, Madsen P, Celis JE. Interferon-γ up-regulates a unique set of proteins in human keratinocytes. Molecular cloning and expression of the cDNA encoding the RGD-sequence-containing protein IGUP I-5111. Eur J Biochem 1993;218:421-430.
    • (1993) Eur J Biochem , vol.218 , pp. 421-430
    • Honoré, B.1    Leffers, H.2    Madsen, P.3    Celis, J.E.4
  • 108
    • 0030978919 scopus 로고    scopus 로고
    • Sequence and expression of mouse proteasome activator PA28 and the related autoantigen
    • Jiang H, Monaco JJ. Sequence and expression of mouse proteasome activator PA28 and the related autoantigen. Immunogenetics 1997;46:93-98.
    • (1997) Immunogenetics , vol.46 , pp. 93-98
    • Jiang, H.1    Monaco, J.J.2
  • 109
    • 0028970626 scopus 로고
    • The interferon-γ-inducible 11 S regulator (PA28) and the LMP2/LMP7 subunits govern the peptide production by the 20 S proteasome in vitro
    • Groettrup M, et al. The interferon-γ-inducible 11 S regulator (PA28) and the LMP2/LMP7 subunits govern the peptide production by the 20 S proteasome in vitro. J Biol Chem 1995;270:23808-23815.
    • (1995) J Biol Chem , vol.270 , pp. 23808-23815
    • Groettrup, M.1
  • 110
    • 0029918289 scopus 로고    scopus 로고
    • A role for the proteasome regulator PA28α in antigen presentation
    • Groettrup M, et al. A role for the proteasome regulator PA28α in antigen presentation. Nature 1996;381:166-168.
    • (1996) Nature , vol.381 , pp. 166-168
    • Groettrup, M.1
  • 111
    • 0030580291 scopus 로고    scopus 로고
    • A tick homologue of the human Ki nuclear autoantigen
    • Paesen GC, Nuttall PA. A tick homologue of the human Ki nuclear autoantigen. Biochim Biophys Acta 1996;1309:9-13.
    • (1996) Biochim Biophys Acta , vol.1309 , pp. 9-13
    • Paesen, G.C.1    Nuttall, P.A.2
  • 112
    • 0030858638 scopus 로고    scopus 로고
    • PA28 subunits of the mouse proteasome: Primary structures and chromosomal localization of the genes
    • Kandil E, Kohda K, Ishibashi T, Tanaka K, Kasahara M. PA28 subunits of the mouse proteasome: primary structures and chromosomal localization of the genes. Immunogenetics 1997;46:337-344.
    • (1997) Immunogenetics , vol.46 , pp. 337-344
    • Kandil, E.1    Kohda, K.2    Ishibashi, T.3    Tanaka, K.4    Kasahara, M.5
  • 113
    • 0032524958 scopus 로고    scopus 로고
    • Characterization of the mouse PA28 activator complex gene family: Complete organizations of the three member genes and a physical map of the ∼150-kb region containing the α- and β-subunit genes
    • Kohda K, Ishibashi T, Shimbara N, Tanaka K, Matsuda Y, Kasahara M. Characterization of the mouse PA28 activator complex gene family: complete organizations of the three member genes and a physical map of the ∼150-kb region containing the α- and β-subunit genes. J Immunol 1998;160:4923-4935.
    • (1998) J Immunol , vol.160 , pp. 4923-4935
    • Kohda, K.1    Ishibashi, T.2    Shimbara, N.3    Tanaka, K.4    Matsuda, Y.5    Kasahara, M.6
  • 114
    • 0027933150 scopus 로고
    • A physical map and candidate genes in the BRCA1 region on chromosome 17q12-21
    • Albertsen HM, et al. A physical map and candidate genes in the BRCA1 region on chromosome 17q12-21. Nat Genet 1994;7:472-479.
    • (1994) Nat Genet , vol.7 , pp. 472-479
    • Albertsen, H.M.1
  • 115
    • 0030697995 scopus 로고    scopus 로고
    • Genetic relationships of the genes encoding the human proteasome β subunits and the proteasome PA28 complex
    • McCusker D, Jones T, Sheer D, Trowsdale J. Genetic relationships of the genes encoding the human proteasome β subunits and the proteasome PA28 complex. Genomics 1997;45:362-367.
    • (1997) Genomics , vol.45 , pp. 362-367
    • McCusker, D.1    Jones, T.2    Sheer, D.3    Trowsdale, J.4
  • 116
    • 0028234529 scopus 로고
    • Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
    • Darnell JE Jr, Kerr IM, Stark GR. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science 1994;264:1415-1421.
    • (1994) Science , vol.264 , pp. 1415-1421
    • Darnell Jr., J.E.1    Kerr, I.M.2    Stark, G.R.3
  • 118
    • 0026468645 scopus 로고
    • Cytokines increase transporter in antigen processing-1 expression more rapidly than HLA class I expression in endothelial cells
    • Epperson DE, Arnold D, Spies T, Cresswell P, Pober JS, Johnson DR. Cytokines increase transporter in antigen processing-1 expression more rapidly than HLA class I expression in endothelial cells. J Immunol 1992;149:3297-3301.
    • (1992) J Immunol , vol.149 , pp. 3297-3301
    • Epperson, D.E.1    Arnold, D.2    Spies, T.3    Cresswell, P.4    Pober, J.S.5    Johnson, D.R.6
  • 119
    • 0029930581 scopus 로고    scopus 로고
    • Kinetically coordinated induction of TAP1 and HLA class I by IFN-γ: The rapid induction of TAP1 by IFN-γ is mediated by Stat1α
    • Min W, Pober JS, Johnson DR. Kinetically coordinated induction of TAP1 and HLA class I by IFN-γ: the rapid induction of TAP1 by IFN-γ is mediated by Stat1α. J Immunol 1996;156:3174-3183.
    • (1996) J Immunol , vol.156 , pp. 3174-3183
    • Min, W.1    Pober, J.S.2    Johnson, D.R.3
  • 120
    • 0028927841 scopus 로고
    • Coordinate regulation of the human TAP1 and LMP2 genes from a shared bidirectional promoter
    • Wright KL, White LC, Kelly A, Beck S, Trowsdale J, Ting JP-Y. Coordinate regulation of the human TAP1 and LMP2 genes from a shared bidirectional promoter. J Exp Med 1995;181:1459-1471.
    • (1995) J Exp Med , vol.181 , pp. 1459-1471
    • Wright, K.L.1    White, L.C.2    Kelly, A.3    Beck, S.4    Trowsdale, J.5    Ting, J.P.-Y.6
  • 121
    • 0030715295 scopus 로고    scopus 로고
    • Rapamycin inhibits proteasome activator expression and proteasome activity
    • Wang X, et al. Rapamycin inhibits proteasome activator expression and proteasome activity. Eur J Immunol 1997;27:2781-2786.
    • (1997) Eur J Immunol , vol.27 , pp. 2781-2786
    • Wang, X.1
  • 122
    • 0027812238 scopus 로고
    • Molecular characterization of the "26S" proteasome complex from rat liver
    • Yoshimura T, et al. Molecular characterization of the "26S" proteasome complex from rat liver. J Struct Biol 1993;111:200-211.
    • (1993) J Struct Biol , vol.111 , pp. 200-211
    • Yoshimura, T.1
  • 125
    • 0027529514 scopus 로고
    • The major histocompatibility complex-encoded proteasome component LMP7: Alternative first exons and post-translational processing
    • Glynne R, Kerr L-A, Mockridge I, Beck S, Kelly A, Trowsdale J. The major histocompatibility complex-encoded proteasome component LMP7: alternative first exons and post-translational processing. Eur J Immunol 1993;23:860-866.
    • (1993) Eur J Immunol , vol.23 , pp. 860-866
    • Glynne, R.1    Kerr, L.-A.2    Mockridge, I.3    Beck, S.4    Kelly, A.5    Trowsdale, J.6
  • 126
    • 0027261242 scopus 로고
    • Different genomic structure of mouse and human Lmp7 genes: Characterization of MHC-encoded proteasome genes
    • Meinhardt T, Gräf U, Hämmerling G. Different genomic structure of mouse and human Lmp7 genes: characterization of MHC-encoded proteasome genes. Immunogenetics 1993;38:373-379.
    • (1993) Immunogenetics , vol.38 , pp. 373-379
    • Meinhardt, T.1    Gräf, U.2    Hämmerling, G.3
  • 127
    • 0028291932 scopus 로고
    • KEKE motifs: Proposed roles in protein-protein association and presentation of peptides by MHC class I receptors
    • Realini C, Rogers SW, Rechsteiner M. KEKE motifs: Proposed roles in protein-protein association and presentation of peptides by MHC class I receptors. FEBS Lett 1994;348:109-113.
    • (1994) FEBS Lett , vol.348 , pp. 109-113
    • Realini, C.1    Rogers, S.W.2    Rechsteiner, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.