메뉴 건너뛰기




Volumn 8, Issue 1, 1996, Pages 59-67

Processing and delivery of peptides presented by MHC class I molecules

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; EPITOPE; GAMMA INTERFERON; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PEPTIDE; PROTEASOME;

EID: 0029917002     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0952-7915(96)80106-3     Document Type: Article
Times cited : (153)

References (84)
  • 1
    • 0028904787 scopus 로고
    • Supply and transport of peptides presented by class I MHC molecules
    • Howard JC: Supply and transport of peptides presented by class I MHC molecules. Curr Opin Immunol 1995, 7:69-76.
    • (1995) Curr Opin Immunol , vol.7 , pp. 69-76
    • Howard, J.C.1
  • 2
    • 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, Bastin J, Gould K, Brownlee G, Andrew M, Coupar B, Boyle D, Chan S, Smith G: 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    Bastin, J.2    Gould, K.3    Brownlee, G.4    Andrew, M.5    Coupar, B.6    Boyle, D.7    Chan, S.8    Smith, G.9
  • 3
    • 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
  • 4
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Ȧ resolution
    • Löwe J, Stock D, Jap B, Zwickl P, Baumeister W, Huber R: Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Ȧ resolution. Science 1995, 268:533-539. Describes the X-ray cristallographic analysis of an archaebacterium 20S proteasome. The binding of a peptide aldehyde inhibitor identifies the active site on the β subunit in the central cavity of the protease complex.
    • (1995) Science , vol.268 , pp. 533-539
    • Löwe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 5
    • 0028985861 scopus 로고
    • Conformational constraints in protein degradation by the 20S proteasome
    • Wenzel T, Baumeister W: Conformational constraints in protein degradation by the 20S proteasome. Struct Biol 1995, 2:199-204. This paper shows that complete unfolding of α-lactalbumin is required for its access to the orifice of the proteasome peptide channel and subsequent degradation.
    • (1995) Struct Biol , vol.2 , pp. 199-204
    • Wenzel, T.1    Baumeister, W.2
  • 6
    • 0029060166 scopus 로고
    • Proteasome from Thermoplasma acidophilum: A threonine protease
    • Seemüller E, Lupas A, Stock D, Löwe J, Huber R, Baumeister W: Proteasome from Thermoplasma acidophilum: a threonine protease. Science 1995, 268:579-582. Site-directed mutagenesis on the 20S proteasome shows it to be a threonine protease. Deletion of the β subunit amino-terminal threonine, or mutation to an alanine, inactivates the enzyme.
    • (1995) Science , vol.268 , pp. 579-582
    • Seemüller, E.1    Lupas, A.2    Stock, D.3    Löwe, J.4    Huber, R.5    Baumeister, W.6
  • 7
    • 0028150688 scopus 로고
    • Inhibition of the proteolytic activity of the multicatalytic proteinase complex (proteasome) by substrate-related peptide aldehydes
    • Vinitsky A, Cardozo C, Sepp-Lorenzino L, Michaud C, Orlowski M: Inhibition of the proteolytic activity of the multicatalytic proteinase complex (proteasome) by substrate-related peptide aldehydes. J Biol Chem 1994, 269:29860-29866.
    • (1994) J Biol Chem , vol.269 , pp. 29860-29866
    • Vinitsky, A.1    Cardozo, C.2    Sepp-Lorenzino, L.3    Michaud, C.4    Orlowski, M.5
  • 9
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany G, Standaert RF, Lane WS, Choi S, Corey EJ, Schreiber SL: Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 1995, 268:726-731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 12
    • 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
    • Kuckeihom LJ, Frentzel S, Kraft R, Kostka S, Groettrup M, Kloetzel PM: 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
    • Kuckeihom, L.J.1    Frentzel, S.2    Kraft, R.3    Kostka, S.4    Groettrup, M.5    Kloetzel, P.M.6
  • 13
    • 0026442415 scopus 로고
    • Proteasome subunits encoded in the MHC are not generally required for the processing of peptides bound by MHC class I molecules
    • Arnold D, Driscoll P, Androlewicz M, Hughes E, Cresswell P, Spies TA: Proteasome subunits encoded in the MHC are not generally required for the processing of peptides bound by MHC class I molecules. Nature 1992, 360:171-173.
    • (1992) Nature , vol.360 , pp. 171-173
    • Arnold, D.1    Driscoll, P.2    Androlewicz, M.3    Hughes, E.4    Cresswell, P.5    Spies, T.A.6
  • 15
    • 0028346277 scopus 로고
    • MHC-encoded proteasome subunits LMP-2 and LMP-7 are not required for efficient antigen presentation
    • Yewdell J, Lapham C, Bacik I, Spies T, Bennink J: MHC-encoded proteasome subunits LMP-2 and LMP-7 are not required for efficient antigen presentation. J Immunol 1994, 152:1163-1170.
    • (1994) J Immunol , vol.152 , pp. 1163-1170
    • Yewdell, J.1    Lapham, C.2    Bacik, I.3    Spies, T.4    Bennink, J.5
  • 16
    • 0028500190 scopus 로고
    • Proteasome components with reciprocal expression to that of the MHC-encoded LMP proteins
    • Belich MP, Glynne RJ, Senger G, Sheer D, Trowsdale J: Proteasome components with reciprocal expression to that of the MHC-encoded LMP proteins. Curr Biol 1994, 4:769-776.
    • (1994) Curr Biol , vol.4 , pp. 769-776
    • Belich, M.P.1    Glynne, R.J.2    Senger, G.3    Sheer, D.4    Trowsdale, J.5
  • 17
    • 0028241569 scopus 로고
    • Displacement of housekeeping proteasome subunits by MHC-encoded LMPs-a newly discovered mechanism for modulating the multlcatalytlc proteinase complex
    • Früh K, Gossen M, Wang KN, Bujard H, Peterson PA, Yang Y: Displacement of housekeeping proteasome subunits by MHC-encoded LMPs-a newly discovered mechanism for modulating the multlcatalytlc proteinase complex. EMBO J 1994, 13:3236-3244.
    • (1994) EMBO J , vol.13 , pp. 3236-3244
    • Früh, K.1    Gossen, M.2    Wang, K.N.3    Bujard, H.4    Peterson, P.A.5    Yang, Y.6
  • 18
    • 0027214605 scopus 로고
    • Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes
    • Gaczynska M, Rock K, Goldberg A: Gamma-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.2    Goldberg, A.3
  • 19
    • 0028136465 scopus 로고
    • Peptidase activities of proteasomes are differentially regulated by the major histocompatibility complex-encoded genes for LMP-2 and LMP-7
    • Gaczynska M, Rock KL, Spies T, Goldberg AL: Peptidase activities of proteasomes are differentially regulated by the major histocompatibility complex-encoded genes for LMP-2 and LMP-7. 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
  • 20
    • 0027223877 scopus 로고
    • MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
    • Driscoll J, Brown M, Finley D, Monaco J: MHC-linked LMP gene products specifically alter peptidase activities of the proteasome. Nature 1993, 365:252-264.
    • (1993) Nature , vol.365 , pp. 252-264
    • Driscoll, J.1    Brown, M.2    Finley, D.3    Monaco, J.4
  • 21
    • 0028097823 scopus 로고
    • Interferon γ stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes
    • Boes B, Hengel H, Ruppert T, Multhaup G, Koszinowski UH, Kloetzel PM: Interferon γ stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes. 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
  • 22
    • 0027493870 scopus 로고
    • PA2B, an activator of the 20S proteasome, is inactivated by proteolytic modification at its carboxyl terminus
    • Chu-Ping M, Willy PJ, Slaughter CA, DeMartino GN: PA2B, an activator of the 20S proteasome, is inactivated by proteolytic modification at its carboxyl terminus. J Biol Chem 1993, 268:22514-22519.
    • (1993) J Biol Chem , vol.268 , pp. 22514-22519
    • Chu-Ping, M.1    Willy, P.J.2    Slaughter, C.A.3    DeMartino, G.N.4
  • 23
    • 0027983803 scopus 로고
    • Molecular cloning and expression of γ-interferon-inducible activator of the multicatalytic protease
    • •] this paper suggests that the IFN-γ induced effects on peptide cleavage may be a combined response to LMP2, LMP7 and the 11S regulator.
    • (1994) J Biol Chem , vol.269 , pp. 20727-20732
    • Realini, C.1    Dubiel, W.2    Pratt, G.3    Ferroll, K.4    Rechsteiner, M.5
  • 25
    • 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
  • 26
    • 0028890880 scopus 로고
    • Effects of Interferon γ and major histocompatibility complex-encoded subunits on peptidase activities of human multicatalytic proteases
    • Ustrell V, Pratt G, Rechsteiner M. Effects of Interferon γ and major histocompatibility complex-encoded subunits on peptidase activities of human multicatalytic proteases. 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
  • 28
    • 0025900181 scopus 로고
    • Efficient processing of an antigenic sequence for presentation by MHC class I molecules depends on its neighboring residues in the protein
    • Del Val M, Schlicht H-J, Ruppert T, Reddehase MJ, Koszinowski UH: Efficient processing of an antigenic sequence for presentation by MHC class I molecules depends on its neighboring residues in the protein. Cell 1991, 66:1145-1153.
    • (1991) Cell , vol.66 , pp. 1145-1153
    • Del Val, M.1    Schlicht, H.-J.2    Ruppert, T.3    Reddehase, M.J.4    Koszinowski, U.H.5
  • 29
    • 0026599764 scopus 로고
    • Flanking sequences influence the presentation of an endogenously synthesized peptide to cytotoxic T lymphocytes
    • Eisenlohr LC, Yewdell JL, Bennink J: Flanking sequences influence the presentation of an endogenously synthesized peptide to cytotoxic T lymphocytes. J Exp Med 1992, 175:481-487
    • (1992) J Exp Med , vol.175 , pp. 481-487
    • Eisenlohr, L.C.1    Yewdell, J.L.2    Bennink, J.3
  • 30
    • 0026667455 scopus 로고
    • + T cell recognition of an endogenously processed epitope is regulated primarily by residues within the epitope
    • + T cell recognition of an endogenously processed epitope is regulated primarily by residues within the epitope. J Exp Med 1992, 176:1335-1341.
    • (1992) J Exp Med , vol.176 , pp. 1335-1341
    • Hahn, Y.S.1    Hahn, C.S.2    Braciale, V.L.3    Braciale, T.J.4    Rice, C.M.5
  • 31
    • 0028817874 scopus 로고
    • The cleavage preference of the proteasome governs the yield of antigenic peptides
    • Eggers M, Boes-Fabian B, Ruppert T, Kloetzel P-M, Koszinowski UH: The cleavage preference of the proteasome governs the yield of antigenic peptides. J Exp Med 1995, 182:1865-1870.
    • (1995) J Exp Med , vol.182 , pp. 1865-1870
    • Eggers, M.1    Boes-Fabian, B.2    Ruppert, T.3    Kloetzel, P.-M.4    Koszinowski, U.H.5
  • 32
    • 0028968217 scopus 로고
    • Contribution of proteasome-mediated proteolysis to the hierarchy of epitopes presented by major histocompatibillty complex class I molecules
    • Niedermann G, Butz S, Ihlenfeldt HG, Grimm R, Lucchiari M, Hoschützky H, Jung G, Maier B, Eichmann, K: Contribution of proteasome-mediated proteolysis to the hierarchy of epitopes presented by major histocompatibillty complex class I molecules. Immunity 1995, 2:289-299.
    • (1995) Immunity , vol.2 , pp. 289-299
    • Niedermann, G.1    Butz, S.2    Ihlenfeldt, H.G.3    Grimm, R.4    Lucchiari, M.5    Hoschützky, H.6    Jung, G.7    Maier, B.8    Eichmann, K.9
  • 33
    • 0028501143 scopus 로고
    • Efficiency of MHC class I antigen processing: A quantitative analysis
    • Villanueva MS, Fischer P, Feen K, Pamer EG: Efficiency of MHC class I antigen processing: a quantitative analysis. Immunity 1994, 1:479-489. The first accurate quantitation of the efficiency of class I restricted antigen processing.
    • (1994) Immunity , vol.1 , pp. 479-489
    • Villanueva, M.S.1    Fischer, P.2    Feen, K.3    Pamer, E.G.4
  • 34
    • 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
  • 35
    • 0028872334 scopus 로고
    • Presentation of endogenous and exogenous antigens is not affected by inactivation of E1 ubiquitin-activating enzyme in temperature-sensitive cell lines
    • Cox JH, Galardy P, Bennink JR, Yewdell JW: Presentation of endogenous and exogenous antigens is not affected by inactivation of E1 ubiquitin-activating enzyme in temperature-sensitive cell lines. J Immunol 1995, 154:511-519. This paper, in contrast to [34], finds no evidence for antigen-processing defects in two mutant cell lines with temperature-sensitive E1 proteins. Temperature-sensitive cell lines are shown to maintain the capacity to ubiquitinate proteins at non-permissive temperatures.
    • (1995) J Immunol , vol.154 , pp. 511-519
    • Cox, J.H.1    Galardy, P.2    Bennink, J.R.3    Yewdell, J.W.4
  • 36
    • 0029120173 scopus 로고
    • Rate of antigen degradation by the ubiquitin-protease pathway influences MHC class I presentation
    • Grant EP, Michalek MT, Goldberg AL, Rock KL: Rate of antigen degradation by the ubiquitin-protease 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
  • 37
    • 0025155682 scopus 로고
    • Cellular peptide composition governed by major histocompatibility complex class I molecules
    • Falk K, Rötzschke O, Rammensee HG: Cellular peptide composition governed by major histocompatibility complex class I molecules. Nature 1990, 348:248-251.
    • (1990) Nature , vol.348 , pp. 248-251
    • Falk, K.1    Rötzschke, O.2    Rammensee, H.G.3
  • 39
    • 0028131363 scopus 로고
    • Importance of peptide amino and carboxyl termini to the stability of MHC class I molecules
    • Bouvier M, Wiley DC: Importance of peptide amino and carboxyl termini to the stability of MHC class I molecules. Science 1994, 265:398-402.
    • (1994) Science , vol.265 , pp. 398-402
    • Bouvier, M.1    Wiley, D.C.2
  • 40
    • 0026455159 scopus 로고
    • Expression of a membrane protease enhances presentation of endogenous antigens to MHC class I-restricted T lymphocytes
    • Eisenlohr LC, Bacik I, Bennink JR, Bernstein K, Yewdell JW: Expression of a membrane protease enhances presentation of endogenous antigens to MHC class I-restricted T lymphocytes. Cell 1992, 71:963-972.
    • (1992) Cell , vol.71 , pp. 963-972
    • Eisenlohr, L.C.1    Bacik, I.2    Bennink, J.R.3    Bernstein, K.4    Yewdell, J.W.5
  • 41
    • 0026576422 scopus 로고
    • HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides
    • Wei ML, Cresswell P: HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides. Nature 1992, 356:443-446.
    • (1992) Nature , vol.356 , pp. 443-446
    • Wei, M.L.1    Cresswell, P.2
  • 43
    • 0028096715 scopus 로고
    • Trimming of antigenic peptides in an early secretory compartment
    • Snyder HL, Yewdell JW, Bennink JR: Trimming of antigenic peptides in an early secretory compartment J Exp Med 1994, 180:2389-2394.
    • (1994) J Exp Med , vol.180 , pp. 2389-2394
    • Snyder, H.L.1    Yewdell, J.W.2    Bennink, J.R.3
  • 44
    • 0028925556 scopus 로고
    • Processing of major histocompatibility class I-restricted antigens in the endoplasmic reticulum
    • Elliott T, Willis A, Cerundolo V, Townsend A: Processing of major histocompatibility class I-restricted antigens in the endoplasmic reticulum. J Exp Med 1995, 181:1481-1491.
    • (1995) J Exp Med , vol.181 , pp. 1481-1491
    • Elliott, T.1    Willis, A.2    Cerundolo, V.3    Townsend, A.4
  • 45
    • 0027943180 scopus 로고
    • Trimming of TAP-translocated peptides in the endoplasmic reticulum and in the cytosol during recycling
    • Roelse J, Grommé M, Momburg F, Hämmerling G, Neefjes J: Trimming of TAP-translocated peptides in the endoplasmic reticulum and in the cytosol during recycling. J Exp Med 1994, 180:1591-1597. This paper shows that peptides translocated into the ER, which do not bind class I, are released from the ER by an ATP-dependent, TAP-independent mechanism.
    • (1994) J Exp Med , vol.180 , pp. 1591-1597
    • Roelse, J.1    Grommé, M.2    Momburg, F.3    Hämmerling, G.4    Neefjes, J.5
  • 46
    • 0028910938 scopus 로고
    • A phagosome-to-cytosol pathway for exogenous antigens presented on MHC class I molecules
    • •], this paper demonstrates a TAP-dependent mechanism by which phagocytosed antigen may gain access to the MHC class I pathway.
    • (1995) Science , vol.267 , pp. 243-246
    • Kovacsovics-Bankowski, M.1    Rock, K.L.2
  • 47
    • 0029149603 scopus 로고
    • Major histocompatibility complex class I presentation of peptides derived from soluble exogenous antigen by a subset of cells engaged in phagocytosis
    • •].
    • (1995) J Exp Med , vol.182 , pp. 841-851
    • Reis E Sousa, C.1    Germain, R.N.2
  • 50
    • 0026762981 scopus 로고
    • Measles virus transmembrane fusion protein synthesized de novo or presented in immunostimulating complexes is endogenously processed for HLA class I- And class II-restricted cytotoxic T cell recognition
    • Van Binnendijk RS, van Baalen CA, Poelen MC, De Vries P, Boes J, Cerundolo V, Osterhaus AD, UyteHaag FG: Measles virus transmembrane fusion protein synthesized de novo or presented in immunostimulating complexes is endogenously processed for HLA class I- and class II-restricted cytotoxic T cell recognition. J Exp Med 1992, 176:119-128.
    • (1992) J Exp Med , vol.176 , pp. 119-128
    • Van Binnendijk, R.S.1    Van Baalen, C.A.2    Poelen, M.C.3    De Vries, P.4    Boes, J.5    Cerundolo, V.6    Osterhaus, A.D.7    Uytehaag, F.G.8
  • 51
    • 0028606109 scopus 로고
    • Characteristics of peptide and class I/β2m binding to the transporters associated with antigen processing (TAP.1 and TAP.2)
    • Androlewicz MJ, Ortmann B, van Endert PM, Spies T, Cresswell P: Characteristics of peptide and class I/β2m binding to the transporters associated with antigen processing (TAP.1 and TAP.2). Proc Natl Acad Sci USA 1994, 91:12716-12720. Together with [63] this paper shows the association of MHC class I molecules with TAP1. A combinatorial peptide-binding site involving TAP1 and TAP2 is demonstrated.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12716-12720
    • Androlewicz, M.J.1    Ortmann, B.2    Van Endert, P.M.3    Spies, T.4    Cresswell, P.5
  • 52
    • 0028110959 scopus 로고
    • Functional expression and purification of the ABC transporter complex associated with antigen processing (TAP) in insect cells
    • Meyer TH, Van Endert PM, Uebel S, Ehring B, Tampé R: Functional expression and purification of the ABC transporter complex associated with antigen processing (TAP) in insect cells. FEBS Lett 1994, 351:443-447.
    • (1994) FEBS Lett , vol.351 , pp. 443-447
    • Meyer, T.H.1    Van Endert, P.M.2    Uebel, S.3    Ehring, B.4    Tampé, R.5
  • 53
    • 0028501327 scopus 로고
    • A sequential model for peptide binding and transport by the transporters associated with antigen processing
    • Van Endert P, Tampé R, Meyer TH, Tisch R, Bach J-F, McDevitt HO: A sequential model for peptide binding and transport by the transporters associated with antigen processing. Immunity 1994, 1:491-500.
    • (1994) Immunity , vol.1 , pp. 491-500
    • Van Endert, P.1    Tampé, R.2    Meyer, T.H.3    Tisch, R.4    Bach, J.-F.5    McDevitt, H.O.6
  • 54
    • 0029148985 scopus 로고
    • Requirements for peptide binding to the human transporter associated with antigen processing revealed by peptide scans and complex peptide libraries
    • Uebel S, Meyer TH, Kraas W, Kienle S, Jung G, Wiesmüller K-H, Tampé R; Requirements for peptide binding to the human transporter associated with antigen processing revealed by peptide scans and complex peptide libraries. J Biol Chem 1995, 270:18512-18516.
    • (1995) J Biol Chem , vol.270 , pp. 18512-18516
    • Uebel, S.1    Meyer, T.H.2    Kraas, W.3    Kienle, S.4    Jung, G.5    Wiesmüller, K.-H.6    Tampé, R.7
  • 55
    • 0028136684 scopus 로고
    • Nucleotide binding of the C-terminal domains of the major histocompatibility complex-encoded transporter expressed in Drosophita melanogaster cells
    • Wang K, Früh K, Peterson PA, Yang Y: Nucleotide binding of the C-terminal domains of the major histocompatibility complex-encoded transporter expressed in Drosophita melanogaster cells. FEBS Lett 1994, 350:337-341.
    • (1994) FEBS Lett , vol.350 , pp. 337-341
    • Wang, K.1    Früh, K.2    Peterson, P.A.3    Yang, Y.4
  • 57
    • 0028829908 scopus 로고
    • Major differences in transporter associated with antigen presentation (TAP)-dependent translocation of MHC class I-presentable peptides and the effect of flanking sequences
    • Neisig A, Roelse J, Sijts AJAM, Ossendorp F, Feltkamp MCW, Kast WM, Melief CJM, Neefjes JJ: Major differences in transporter associated with antigen presentation (TAP)-dependent translocation of MHC class I-presentable peptides and the effect of flanking sequences. J Immunol 1995, 154:1273-1279.
    • (1995) J Immunol , vol.154 , pp. 1273-1279
    • Neisig, A.1    Roelse, J.2    Sijts, A.J.A.M.3    Ossendorp, F.4    Feltkamp, M.C.W.5    Kast, W.M.6    Melief, C.J.M.7    Neefjes, J.J.8
  • 59
    • 0026651895 scopus 로고
    • Electron microscopic localization of the multicatalytic proteinase complex in rat liver and in cultured cells
    • Rivett AJ, Palmer A, Knecht E: Electron microscopic localization of the multicatalytic proteinase complex in rat liver and in cultured cells. J Histochem Cytochem 1992, 40:1165-1172.
    • (1992) J Histochem Cytochem , vol.40 , pp. 1165-1172
    • Rivett, A.J.1    Palmer, A.2    Knecht, E.3
  • 60
    • 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
  • 61
    • 0028979675 scopus 로고
    • A mechanism for the specific immunogenlcity of heat shock protein-chaperoned peptides
    • Suto R, Srivastava PK: A mechanism for the specific immunogenlcity of heat shock protein-chaperoned peptides. Science 1995, 269:1585-1588.
    • (1995) Science , vol.269 , pp. 1585-1588
    • Suto, R.1    Srivastava, P.K.2
  • 62
    • 0028282108 scopus 로고
    • MHC class I/β2-microglobulin complexes associate with TAP transporters before peptide binding
    • Ortmann B, Androlewicz M, Cresswell P: MHC class I/β2-microglobulin complexes associate with TAP transporters before peptide binding. Nature 1994, 368:864-867.
    • (1994) Nature , vol.368 , pp. 864-867
    • Ortmann, B.1    Androlewicz, M.2    Cresswell, P.3
  • 63
    • 0028239443 scopus 로고
    • Interaction of MHC class I molecules with the transporter associated with antigen processing
    • Suh W-K, Cohen-Doyle MF, Früh K, Wang K, Peterson PA, Williams DB: Interaction of MHC class I molecules with the transporter associated with antigen processing. Science 1994, 264:1322-1326.
    • (1994) Science , vol.264 , pp. 1322-1326
    • Suh, W.-K.1    Cohen-Doyle, M.F.2    Früh, K.3    Wang, K.4    Peterson, P.A.5    Williams, D.B.6
  • 64
  • 67
    • 0028170597 scopus 로고
    • 2-microglobulin: Major histocompatibility complex class I heavy chain intermediate dissociates from calnexin and then is stablized by binding peptide
    • 2-microglobulin: major histocompatibility complex class I heavy chain intermediate dissociates from calnexin and then is stablized by binding peptide. J Exp Med 1994, 180:2163-2171.
    • (1994) J Exp Med , vol.180 , pp. 2163-2171
    • Sugita, M.1    Brenner, M.B.2
  • 68
    • 0028917887 scopus 로고
    • Species specific differences in chaperone interaction of human and mouse major histocompatibility complex class I molecules
    • Nöbner E, Parham P: Species specific differences in chaperone interaction of human and mouse major histocompatibility complex class I molecules. J Exp Med 1995, 181:327-337.
    • (1995) J Exp Med , vol.181 , pp. 327-337
    • Nöbner, E.1    Parham, P.2
  • 69
    • 0028858641 scopus 로고
    • TAP associates with a unique class I conformation, whereas calnexin associates with multiple class I forms in mouse and man
    • Carreno BM, Soiheim JC, Harris M, Stroynowski I, Connolly JM, Hansen TH: TAP associates with a unique class I conformation, whereas calnexin associates with multiple class I forms in mouse and man. J Immunol 1995, 155:4726-4753.
    • (1995) J Immunol , vol.155 , pp. 4726-4753
    • Carreno, B.M.1    Soiheim, J.C.2    Harris, M.3    Stroynowski, I.4    Connolly, J.M.5    Hansen, T.H.6
  • 70
    • 0029009565 scopus 로고
    • MHC class I expression and transport in a calnexin-deficient cell line
    • •], shows that MHC class I molecules can assemble and be transported in the absence of the chaperone, calnexin.
    • (1995) J Immunol , vol.155 , pp. 143-148
    • Scott, J.E.1    Dawson, J.F.2
  • 72
    • 0028955449 scopus 로고
    • Effect of TAP on the generation and intracellular trafficking of peptide-receptive major histocompatibility complex class I molecules
    • Day PM, Esquivel F, Lukszo J, Bennink JR, Yewdell JW: Effect of TAP on the generation and intracellular trafficking of peptide-receptive major histocompatibility complex class I molecules. Immunity 1995, 2:137-147.
    • (1995) Immunity , vol.2 , pp. 137-147
    • Day, P.M.1    Esquivel, F.2    Lukszo, J.3    Bennink, J.R.4    Yewdell, J.W.5
  • 73
    • 0028265113 scopus 로고
    • Endoplasmic reticulum signal sequence facilitated transport of peptide epitopes restores immunogenicity of an antigen processing defective tumour cell line
    • Khanna R, Burrows SR, Argaet V, Moss DJ: Endoplasmic reticulum signal sequence facilitated transport of peptide epitopes restores immunogenicity of an antigen processing defective tumour cell line, Int Immunol 1994, 6:639-645.
    • (1994) Int Immunol , vol.6 , pp. 639-645
    • Khanna, R.1    Burrows, S.R.2    Argaet, V.3    Moss, D.J.4
  • 74
    • 0029053611 scopus 로고
    • Restoration of endogenous antigen processing in Burkitt's lymphoma cells by Epstein-Barr virus latent membrane protein-1: Coordinate up-regulation of peptide transporters and HLA-class I antigen expression
    • Rowe M, Khanna R, Jacob CA, Argaet V, Kelly A, Powis S, Belich M, Croom-Carter D, Lee S, Burrows SR et al.: Restoration of endogenous antigen processing in Burkitt's lymphoma cells by Epstein-Barr virus latent membrane protein-1: coordinate up-regulation of peptide transporters and HLA-class I antigen expression. Eur J Immunol 1995, 25:1374-1384.
    • (1995) Eur J Immunol , vol.25 , pp. 1374-1384
    • Rowe, M.1    Khanna, R.2    Jacob, C.A.3    Argaet, V.4    Kelly, A.5    Powis, S.6    Belich, M.7    Croom-Carter, D.8    Lee, S.9    Burrows, S.R.10
  • 75
    • 0029003999 scopus 로고
    • Inhibition of antigen processing by the internal repeat region of the Epstein-Barr virus nuclear antigen-1
    • Levitskaya J, Coram M, Levitsky V, Imreh S, Steigerwald-Mullen PM, Klein G, Kurilla MG, Masucci MG: Inhibition of antigen processing by the internal repeat region of the Epstein-Barr virus nuclear antigen-1. Nature 1995, 375:685-688. The EBNA 1 protein is detected in all EBV-associated malignancies, but does not elicit a detectable CTL response. This paper suggests that the internal glycine-alanine repeat region of EBNA-1 prevents processing of epitopes from within the protein.
    • (1995) Nature , vol.375 , pp. 685-688
    • Levitskaya, J.1    Coram, M.2    Levitsky, V.3    Imreh, S.4    Steigerwald-Mullen, P.M.5    Klein, G.6    Kurilla, M.G.7    Masucci, M.G.8
  • 79
    • 0027505073 scopus 로고
    • Human cytomegalovirus down-regulates HLA class I expression by reducing the stability of class I H chains
    • Beersma MF, Bijlmakers MJ, Ploegh HL: Human cytomegalovirus down-regulates HLA class I expression by reducing the stability of class I H chains. J Immunol 1993, 151:4455-4464.
    • (1993) J Immunol , vol.151 , pp. 4455-4464
    • Beersma, M.F.1    Bijlmakers, M.J.2    Ploegh, H.L.3
  • 80
    • 0028224570 scopus 로고
    • Human cytomegalovirus-infected cells have unstable assembly of major histocompatibility complex class I complexes and are resistant to lysis by cytotoxic T lymphocytes
    • Warren AP, Ducroq DH, Lehner PJ, Borysiewicz LK: Human cytomegalovirus-infected cells have unstable assembly of major histocompatibility complex class I complexes and are resistant to lysis by cytotoxic T lymphocytes. J Virol 1994, 68:2822-2829.
    • (1994) J Virol , vol.68 , pp. 2822-2829
    • Warren, A.P.1    Ducroq, D.H.2    Lehner, P.J.3    Borysiewicz, L.K.4
  • 81
    • 0024356849 scopus 로고
    • Presentation of CMV immediate-early antigen to cytolytic T lymphocytes is selectively prevented by viral genes expressed in the early phase
    • Del Val M, Munch K, Reddehase MJ, Koszinowski UH: Presentation of CMV immediate-early antigen to cytolytic T lymphocytes is selectively prevented by viral genes expressed in the early phase. Cell 1989, 58:305-315.
    • (1989) Cell , vol.58 , pp. 305-315
    • Del Val, M.1    Munch, K.2    Reddehase, M.J.3    Koszinowski, U.H.4
  • 82
    • 0028798015 scopus 로고
    • Getting the inside out: The transporter associated with antigen processing (TAP) and the presentation of viral antigen
    • Hill A, Ploegh H: Getting the inside out: the transporter associated with antigen processing (TAP) and the presentation of viral antigen. Proc Natl Acad Sci USA 1995, 92:341-343.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 341-343
    • Hill, A.1    Ploegh, H.2
  • 83
    • 0029144277 scopus 로고
    • Identification of the mouse cytomegalovirus genomic region affecting major histocompatibility complex class I molecule transport
    • Thäle R, Szepan U, Hengel H, Geginat G, Lucin P, Koszinowski UH: Identification of the mouse cytomegalovirus genomic region affecting major histocompatibility complex class I molecule transport. J Virol 1995, 69:6098-6015. This paper identifies the mouse CMV genomic region causing ER retention of MHC class I molecules and identifies a late mechanism that downregulates MHC class I molecules.
    • (1995) J Virol , vol.69 , pp. 6098-16015
    • Thäle, R.1    Szepan, U.2    Hengel, H.3    Geginat, G.4    Lucin, P.5    Koszinowski, U.H.6
  • 84
    • 0029120480 scopus 로고
    • Up-regulation of MHC class I by flavivirus-induced peptide translocation into the endoplasmic reticulum
    • Müllbacher A, Lobigs M: Up-regulation of MHC class I by flavivirus-induced peptide translocation into the endoplasmic reticulum. Immunity 1995, 3:207-214.
    • (1995) Immunity , vol.3 , pp. 207-214
    • Müllbacher, A.1    Lobigs, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.