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Volumn 49, Issue 3, 2001, Pages 195-201

Peptide loading of nascent MHC class I molecules

Author keywords

Antigen processing; CD8+ cells; Cytotoxic T lymphocytes; MHC class I; TAP

Indexed keywords

ABC TRANSPORTER; HLA ANTIGEN CLASS 1; TAP1 PROTEIN, HUMAN;

EID: 0035230392     PISSN: 0004069X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (4)

References (74)
  • 1
    • 0027424659 scopus 로고
    • Evidence that transporters associated with antigen processing translocate a major histocompatibility complex class I-binding peptide into the endoplasmic reticulum in an ATP-dependent manner
    • ANDROLEWICZ M. J., ANDERSON K. S. and CRESSWELL P. (1993): Evidence that transporters associated with antigen processing translocate a major histocompatibility complex class I-binding peptide into the endoplasmic reticulum in an ATP-dependent manner. Proc. Natl. Acad. Sci. USA, 90, 9130-9134.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9130-9134
    • Androlewicz, M.J.1    Anderson, K.S.2    Cresswell, P.3
  • 2
    • 0028408339 scopus 로고
    • Human transporters associated with antigen processing possess a promiscuous peptide-binding site
    • ANDROLEWICZ M. J. and CRESSWELL P. (1994): Human transporters associated with antigen processing possess a promiscuous peptide-binding site. Immunity, 1, 7-14.
    • (1994) Immunity , vol.1 , pp. 7-14
    • Androlewicz, M.J.1    Cresswell, P.2
  • 3
    • 0028606109 scopus 로고
    • Characteristics of peptide and major histocompatibility complex class I/β2-microglobulin binding to the transporters associated with antigen processing (TAP1 and TAP2)
    • ANDROLEWICZ M. J., ORTMANN B., VAN ENDERT P. M., SPIES T. and CRESSWELL P. (1994): Characteristics of peptide and major histocompatibility complex class I/β2-microglobulin binding to the transporters associated with antigen processing (TAP1 and TAP2). Proc. Natl. Acad. Sci. USA, 91, 12716-12720.
    • (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
  • 5
    • 0033060098 scopus 로고    scopus 로고
    • The N-terminal region of tapasin is required to stabilize the MHC class I loading complex
    • BANGIA N., LEHNER P. J., HUGHES E. A., SURMAN M. and CRESSWELL P. (1999): The N-terminal region of tapasin is required to stabilize the MHC class I loading complex. Eur. J. Immunol., 29, 1858-1870.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 1858-1870
    • Bangia, N.1    Lehner, P.J.2    Hughes, E.A.3    Surman, M.4    Cresswell, P.5
  • 6
    • 0028858641 scopus 로고
    • TAP associates with a unique class I conformation, whereas calnexin associates with multiple class I forms in mouse and man
    • CARRENO B. M., SOLHEIM J. C., HARRIS M., STROYNOWSKI I., CONNOLLY J. M. and HANSEN T. H. (1995): TAP associates with a unique class I conformation, whereas calnexin associates with multiple class I forms in mouse and man. J. Immunol., 155, 4726-4733.
    • (1995) J. Immunol. , vol.155 , pp. 4726-4733
    • Carreno, B.M.1    Solheim, J.C.2    Harris, M.3    Stroynowski, I.4    Connolly, J.M.5    Hansen, T.H.6
  • 7
    • 0029867236 scopus 로고    scopus 로고
    • Natural killer cell receptors specific for MHC class I molecules
    • COLONNA M. (1996): Natural killer cell receptors specific for MHC class I molecules. Curr. Opin. Immunol., 8, 101-107.
    • (1996) Curr. Opin. Immunol. , vol.8 , pp. 101-107
    • Colonna, M.1
  • 8
    • 0025208391 scopus 로고
    • Recognition by CD8 on cytotoxic T lymphocytes is ablated by several substitutions in the class I α3 domain: CD8 and the T-cell receptor recognize the same class I molecule
    • CONNOLY J., HANSEN T. H., INGOLD A. L. and POTTER T. A. (1990): Recognition by CD8 on cytotoxic T lymphocytes is ablated by several substitutions in the class I α3 domain: CD8 and the T-cell receptor recognize the same class I molecule. Proc. Natl. Acad. Sci. USA, 87, 2137-2141.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2137-2141
    • Connoly, J.1    Hansen, T.H.2    Ingold, A.L.3    Potter, T.A.4
  • 9
    • 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 J. H., GALARDY P., BENNINK J. R. and YEWDELL J. W. (1995): Presentation of endogenous and exogenous antigens is not affected by inactivation of E1 ubiquitin activating enzyme in temperature-sensitive cell lines. J. Immunol., 154, 511-519.
    • (1995) J. Immunol. , vol.154 , pp. 511-519
    • Cox, J.H.1    Galardy, P.2    Bennink, J.R.3    Yewdell, J.W.4
  • 10
    • 0030851901 scopus 로고    scopus 로고
    • How does TAP associate with MHC class I molecules
    • ELLIOTT T. (1997): How does TAP associate with MHC class I molecules. Immunol. Today, 18, 375-379.
    • (1997) Immunol. Today , vol.18 , pp. 375-379
    • Elliott, T.1
  • 11
    • 0028925556 scopus 로고
    • Processing of major histocompatibility class I-restricted antigens in the endoplasmic reticulum
    • ELLIOTT T., WILLIS A., CERUNDOLO V. and TOWNSEND A. (1995): Processing of major histocompatibility class I-restricted antigens in the endoplasmic reticulum. J. Exp. Med., 181, 1481-1491.
    • (1995) J. Exp. Med. , vol.181 , pp. 1481-1491
    • Elliott, T.1    Willis, A.2    Cerundolo, V.3    Townsend, A.4
  • 12
    • 0025855156 scopus 로고
    • Allele-specific motifs revealed by sequencing of self-peptides eluted from mhc molecules
    • FALK K., ROTZSCHKE O., STEVANOVIC S., JUNG G. and RAMMENSEE H.-G. (1991): Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules. Nature, 351, 290-296.
    • (1991) Nature , vol.351 , pp. 290-296
    • Falk, K.1    Rotzschke, O.2    Stevanovic, S.3    Jung, G.4    Rammensee, H.-G.5
  • 13
    • 0032555922 scopus 로고    scopus 로고
    • Major histocompatibility complex class I viral antigen processing in the secretory pathway defined by the trans-Golgi network protease furin
    • GIL-TORREGROSA B. C., RAUL CASTANO A. and DEL VAL M. (1998): Major histocompatibility complex class I viral antigen processing in the secretory pathway defined by the trans-Golgi network protease furin. J. Exp. Med., 188, 1105-1116.
    • (1998) J. Exp. Med. , vol.188 , pp. 1105-1116
    • Gil-Torregrosa, B.C.1    Raul Castano, A.2    Del Val, M.3
  • 14
    • 0032499199 scopus 로고    scopus 로고
    • A proteolytic system that compensate for loss of proteasome function
    • GLAS R., BOGYO M., MCMASTER J. S., GACZYNSKA M. and PLOEGH H. L. (1998): A proteolytic system that compensate for loss of proteasome function. Nature, 392, 618-622.
    • (1998) Nature , vol.392 , pp. 618-622
    • Glas, R.1    Bogyo, M.2    McMaster, J.S.3    Gaczynska, M.4    Ploegh, H.L.5
  • 15
    • 0028817950 scopus 로고
    • Dependence of peptide binding by MHC class I molecules on their interaction with TAP
    • GRANDEA A. G., ANDROLEWICZ M. J., ATHWAL R. S., GERAGHTY D. E. and SPIES T. (1995): Dependence of peptide binding by MHC class I molecules on their interaction with TAP. Science, 270, 105-108.
    • (1995) Science , vol.270 , pp. 105-108
    • Grandea, A.G.1    Androlewicz, M.J.2    Athwal, R.S.3    Geraghty, D.E.4    Spies, T.5
  • 17
    • 0029120173 scopus 로고
    • Rate of antigen degradation by the ubiquitin-proteasome pathway influences MHC class I presentation
    • GRANT E. P., MICHALEK M. T., GOLDBERG A. L. and ROCK K. L. (1995): Rate of antigen degradation by the ubiquitin-proteasome pathway influences MHC class I presentation. J. Immunol., 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
  • 18
    • 0032101943 scopus 로고    scopus 로고
    • Calreticulin and calnexin interact with different protein and glycan determinants during the assembly of MHC class I
    • HARRIS M. R., YU Y. Y., KINDLE C. S., HANSEN T. H. and SOLHEIM J. C. (1998): Calreticulin and calnexin interact with different protein and glycan determinants during the assembly of MHC class I. J. Immunol., 160, 5404-5409.
    • (1998) J. Immunol. , vol.160 , pp. 5404-5409
    • Harris, M.R.1    Yu, Y.Y.2    Kindle, C.S.3    Hansen, T.H.4    Solheim, J.C.5
  • 21
    • 0032482384 scopus 로고    scopus 로고
    • The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex
    • HUGHES E. A. and CRESSWELL P. (1998): The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex. Curr. Biol., 8, 709-712.
    • (1998) Curr. Biol. , vol.8 , pp. 709-712
    • Hughes, E.A.1    Cresswell, P.2
  • 23
    • 0026632968 scopus 로고
    • Requirement for CD8-major histocompatibility complex class I interaction in positive and negative selection of developing T cells
    • KILLEEN N., MORIARTY A., TEH H.-S. and LITTMAN D. R. (1992): Requirement for CD8-major histocompatibility complex class I interaction in positive and negative selection of developing T cells. J. Exp. Med., 176, 89-97.
    • (1992) J. Exp. Med. , vol.176 , pp. 89-97
    • Killeen, N.1    Moriarty, A.2    Teh, H.-S.3    Littman, D.R.4
  • 24
    • 0342894676 scopus 로고    scopus 로고
    • Generation, intracellular transport and loading of peptides associated with MHC class I molecules
    • KOOPMANN J.-O., HAMMERLING G. J. and MOMBURG F. (1997): Generation, intracellular transport and loading of peptides associated with MHC class I molecules. Curr. Opin. Immunol., 9, 80-88.
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 80-88
    • Koopmann, J.-O.1    Hammerling, G.J.2    Momburg, F.3
  • 25
    • 0026486418 scopus 로고
    • Intrahepatic cytotoxic T lymphocytes specific for hepatitis C virus in persons with chronic hepatitis
    • KOZIEL M. J., DUDLEY D., WONG J. T., DIENSTAG J., HOUGHTON M., RALSTON R. and WALKER B. D. (1992): Intrahepatic cytotoxic T lymphocytes specific for hepatitis C virus in persons with chronic hepatitis. J. Immunol., 149, 3339-3344.
    • (1992) J. Immunol. , vol.149 , pp. 3339-3344
    • Koziel, M.J.1    Dudley, D.2    Wong, J.T.3    Dienstag, J.4    Houghton, M.5    Ralston, R.6    Walker, B.D.7
  • 26
    • 0032536790 scopus 로고    scopus 로고
    • Physical and functional association of the MHC class I heavy chain α3 domain with the transporter associated with antigen processing
    • KULIG K., NANDI D., BACIK I., MONACO J. J. and VUKMANOVIĆ S. (1998): Physical and functional association of the MHC class I heavy chain α3 domain with the transporter associated with antigen processing. J. Exp. Med., 187, 865-874.
    • (1998) J. Exp. Med. , vol.187 , pp. 865-874
    • Kulig, K.1    Nandi, D.2    Bacik, I.3    Monaco, J.J.4    Vukmanović, S.5
  • 27
    • 0028867421 scopus 로고
    • The membrane-bound and soluble forms of HLA-G bind identical sets of endogenous peptides but differ with respect to TAP association
    • LEE N., MALACKO A. R., ISHITANI A., CHEN M.-C., BAJORATH J., MARQUARDT H. and GERAGHTY D. E. (1995): The membrane-bound and soluble forms of HLA-G bind identical sets of endogenous peptides but differ with respect to TAP association. Immunity, 3, 591-600.
    • (1995) Immunity , vol.3 , pp. 591-600
    • Lee, N.1    Malacko, A.R.2    Ishitani, A.3    Chen, M.-C.4    Bajorath, J.5    Marquardt, H.6    Geraghty, D.E.7
  • 28
    • 0032005348 scopus 로고    scopus 로고
    • Soluble tapasin restores MHC class I expression and function in the tapasin-negative cell line. 220
    • LEHNER P. J., SURMAN M. J. and CRESSWELL P. (1998): Soluble tapasin restores MHC class I expression and function in the tapasin-negative cell line. 220. Immunity, 8, 221-231.
    • (1998) Immunity , vol.8 , pp. 221-231
    • Lehner, P.J.1    Surman, M.J.2    Cresswell, P.3
  • 29
    • 0030198868 scopus 로고    scopus 로고
    • Point mutations in the a2 domain of HLA-A2.1 define a functionally relevant interaction with TAP
    • LEWIS J. W., NEISIG A., NEEFJES J. and ELLIOTT T. (1996): Point mutations in the a2 domain of HLA-A2.1 define a functionally relevant interaction with TAP. Curr. Biol., 6, 873-883.
    • (1996) Curr. Biol. , vol.6 , pp. 873-883
    • Lewis, J.W.1    Neisig, A.2    Neefjes, J.3    Elliott, T.4
  • 30
    • 0030871305 scopus 로고    scopus 로고
    • Cloning and functional characterization of a subunit of the transporter associated with antigen processing
    • LI S., SJOGREN H.-O., HELLMAN U., PETTERSSON R. F. and WANG P. (1997): Cloning and functional characterization of a subunit of the transporter associated with antigen processing. Proc. Natl. Acad. Sci. USA, 94, 8708-8713.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8708-8713
    • Li, S.1    Sjogren, H.-O.2    Hellman, U.3    Pettersson, R.F.4    Wang, P.5
  • 31
    • 0025880648 scopus 로고
    • MHC class I deficiency: Susceptibility to natural killer (NK) cells and impaired NK activity
    • LIAO N.-S., BIX M., ZIJLSTRA M., JAENISCH R. and RAULET D. (1991): MHC class I deficiency: susceptibility to natural killer (NK) cells and impaired NK activity. Science, 253, 199-202.
    • (1991) Science , vol.253 , pp. 199-202
    • Liao, N.-S.1    Bix, M.2    Zijlstra, M.3    Jaenisch, R.4    Raulet, D.5
  • 32
    • 0032522392 scopus 로고    scopus 로고
    • ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly
    • LINDQUIST J. A., JENSEN O. N., MANN M. and HAMMERLING G. J. (1998): ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly. EMBO J., 17, 2186-2195.
    • (1998) EMBO J. , vol.17 , pp. 2186-2195
    • Lindquist, J.A.1    Jensen, O.N.2    Mann, M.3    Hammerling, G.J.4
  • 33
    • 0027263157 scopus 로고
    • A role for the ubiquitin-dependent proteolytic pathway in MHC class I restricted antigen processing
    • MICHALEK M. T., GRANT E. P., GRAMM C., GOLDBERG A. L. and ROCK K. L. (1993): A role for the ubiquitin-dependent proteolytic pathway in MHC class I restricted antigen processing. Nature, 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
  • 34
    • 0029987724 scopus 로고    scopus 로고
    • Chemical denaturation and modification of ovalbumin alters its dependence on the ubiquitin conjugation for class I antigen presentation
    • MICHALEK M. T., GRANT E. P. and ROCK K. L. (1996): Chemical denaturation and modification of ovalbumin alters its dependence on the ubiquitin conjugation for class I antigen presentation. J. Immunol., 157, 617-624.
    • (1996) J. Immunol. , vol.157 , pp. 617-624
    • Michalek, M.T.1    Grant, E.P.2    Rock, K.L.3
  • 35
    • 0026524392 scopus 로고
    • A molecular model of MHC class-I-restricted antigen processing
    • MONACO J. J. (1992): A molecular model of MHC class-I-restricted antigen processing. Immunol. Today, 13, 173-179.
    • (1992) Immunol. Today , vol.13 , pp. 173-179
    • Monaco, J.J.1
  • 36
    • 0027239749 scopus 로고
    • Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter
    • NEEFJES J. J., MOMBURG F. and HAMMERLING G. J. (1993): Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter. Science, 261, 769-771.
    • (1993) Science , vol.261 , pp. 769-771
    • Neefjes, J.J.1    Momburg, F.2    Hammerling, G.J.3
  • 37
    • 0029974597 scopus 로고    scopus 로고
    • Allele-specific differences in the interaction of MHC class I molecules with transporters associated with antigen processing
    • NEISIG A., WUBBOLTS R., ZANG X., MELIEF C. and NEEFJES J. (1996): Allele-specific differences in the interaction of MHC class I molecules with transporters associated with antigen processing. J. Immunol., 156, 3196-3206.
    • (1996) J. Immunol. , vol.156 , pp. 3196-3206
    • Neisig, A.1    Wubbolts, R.2    Zang, X.3    Melief, C.4    Neefjes, J.5
  • 39
    • 0030589291 scopus 로고    scopus 로고
    • Multiple regions of the transporter associated with antigen processing (TAP) contribute to its binding site
    • NIJENHIUS M. and HAMMERLING G. J. (1997): Multiple regions of the transporter associated with antigen processing (TAP) contribute to its binding site. J. Immunol., 157, 5467-5477.
    • (1997) J. Immunol. , vol.157 , pp. 5467-5477
    • Nijenhius, M.1    Hammerling, G.J.2
  • 40
    • 0024393728 scopus 로고
    • The structure of HLA-B35 suggests that it is derived from HLA-Bw58 by two genetic mechanisms
    • OOBA T., HAYASHI H., KARAKI S., TANABE M., KANO K. and TAKIGUCHI M. (1989): The structure of HLA-B35 suggests that it is derived from HLA-Bw58 by two genetic mechanisms. Immunogenetics, 30, 76-80.
    • (1989) Immunogenetics , vol.30 , pp. 76-80
    • Ooba, T.1    Hayashi, H.2    Karaki, S.3    Tanabe, M.4    Kano, K.5    Takiguchi, M.6
  • 41
    • 0028282108 scopus 로고
    • MHC class I/β2-microglobulin complexes associate with TAP transporters before peptide binding
    • ORTMANN B., ANDROLEWICZ M. and CRESSWELL P. (1994): MHC class I/β2-microglobulin complexes associate with TAP transporters before peptide binding. Nature, 368, 864-867.
    • (1994) Nature , vol.368 , pp. 864-867
    • Ortmann, B.1    Androlewicz, M.2    Cresswell, P.3
  • 44
    • 0031895637 scopus 로고    scopus 로고
    • Mechanisms of MHC class I-restricted antigen processing
    • PAMER E. and CRESSWELL P. (1998): Mechanisms of MHC class I-restricted antigen processing. Annu. Rev. Immunol., 16, 323-358.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 323-358
    • Pamer, E.1    Cresswell, P.2
  • 45
    • 0030152620 scopus 로고    scopus 로고
    • A point mutation in HLA-A*0201 results in failure to bind the TAP complex and to present virus-derived peptides to CTL
    • PEACE-BREWER A. L., TUSSEY L. G., MATSUI M., LI G., QUINN D. G. and FRELINGER J. A. (1996): A point mutation in HLA-A*0201 results in failure to bind the TAP complex and to present virus-derived peptides to CTL. Immunity, 4, 505-514.
    • (1996) Immunity , vol.4 , pp. 505-514
    • Peace-Brewer, A.L.1    Tussey, L.G.2    Matsui, M.3    Li, G.4    Quinn, D.G.5    Frelinger, J.A.6
  • 46
    • 0032503029 scopus 로고    scopus 로고
    • Viral strategies of immune evasion
    • PLOEGH H. L. (1998): Viral strategies of immune evasion. Science, 280, 248-253.
    • (1998) Science , vol.280 , pp. 248-253
    • Ploegh, H.L.1
  • 47
    • 0024595609 scopus 로고
    • Substitution at residue 227 of H-2 class I molecules abrogates recognition by CD8-dependent, but not CD8-independent, cytotoxic T lymphocytes
    • POTTER T. A., RAJAN T. V., DICK R. F. II and BLUESTONE J. A. (1989): Substitution at residue 227 of H-2 class I molecules abrogates recognition by CD8-dependent, but not CD8-independent, cytotoxic T lymphocytes. Nature, 337, 73-75.
    • (1989) Nature , vol.337 , pp. 73-75
    • Potter, T.A.1    Rajan, T.V.2    Dick R.F. II3    Bluestone, J.A.4
  • 48
    • 0032971227 scopus 로고    scopus 로고
    • Degradation of cell proteins and the generation of MHC class I-presented peptides
    • ROCK K. L. and GOLDBERG A. L. (1999): Degradation of cell proteins and the generation of MHC class I-presented peptides. Ann. Rev. Immunol., 17, 739-779.
    • (1999) Ann. Rev. Immunol. , vol.17 , pp. 739-779
    • Rock, K.L.1    Goldberg, A.L.2
  • 49
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • ROCK K. L., GRAMM C., ROTHSTEIN L., CLARK K., STEIN R., DICK L., HWANG D. and GOLDBERG A. L. (1994): Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell, 78, 761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 50
    • 0029552627 scopus 로고
    • Assembly, peptide loading, and transport of MHC class I in a calnexin-negative cell line
    • SADASIVAN B., CARIAPPA A., WANECK G. L. and CRESSWELL P. (1995): Assembly, peptide loading, and transport of MHC class I in a calnexin-negative cell line. Cold Spring Harbor Symp., 55, 267-275.
    • (1995) Cold Spring Harbor Symp. , vol.55 , pp. 267-275
    • Sadasivan, B.1    Cariappa, A.2    Waneck, G.L.3    Cresswell, P.4
  • 51
    • 0030217926 scopus 로고    scopus 로고
    • Roles of calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP
    • SADASIVAN B., LEHNER P. J., ORTMANN B., SPIES T. and CRESSWELL P. (1996): Roles of calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity, 5, 103-114.
    • (1996) Immunity , vol.5 , pp. 103-114
    • Sadasivan, B.1    Lehner, P.J.2    Ortmann, B.3    Spies, T.4    Cresswell, P.5
  • 52
    • 0025006862 scopus 로고
    • Direct binding of peptide to empty MHC class I molecules on intact cells and in vitro
    • SCHUMACHER T. N. M., HEEMELS M.-T., NEEFJES J. J., KAST W. M., MELIEF C. J. M. and PLOEGH H. L. (1990): Direct binding of peptide to empty MHC class I molecules on intact cells and in vitro. Cell, 62, 563-567.
    • (1990) Cell , vol.62 , pp. 563-567
    • Schumacher, T.N.M.1    Heemels, M.-T.2    Neefjes, J.J.3    Kast, W.M.4    Melief, C.J.M.5    Ploegh, H.L.6
  • 54
    • 0029009565 scopus 로고
    • MHC class I expression and transport in a calnexin-deficient cell line
    • SCOTT J. E. and DAWSON J. R. (1995): MHC class I expression and transport in a calnexin-deficient cell line. J. Immunol., 155, 143-148.
    • (1995) J. Immunol. , vol.155 , pp. 143-148
    • Scott, J.E.1    Dawson, J.R.2
  • 56
    • 0029969665 scopus 로고    scopus 로고
    • Bound water structure and polymorphyc amino acids act together to allow the binding of different peptides to MHC class I HLA-B53
    • SMITH K. J., REID S. W., HARLOS K., MCMICHAEL A. J., STUART D. I., BELL J. I. and JONES E. Y. (1996): Bound water structure and polymorphyc amino acids act together to allow the binding of different peptides to MHC class I HLA-B53. Immunity, 4, 215-228.
    • (1996) Immunity , vol.4 , pp. 215-228
    • Smith, K.J.1    Reid, S.W.2    Harlos, K.3    McMichael, A.J.4    Stuart, D.I.5    Bell, J.I.6    Jones, E.Y.7
  • 57
    • 0028096715 scopus 로고
    • Trimming of antigenic peptides in an early secretory compartment
    • SNYDER H. L., YEWDELL J. W. and BENNIK J. R. (1994): Trimming of antigenic peptides in an early secretory compartment. J. Exp. Med., 180, 2389-2394.
    • (1994) J. Exp. Med. , vol.180 , pp. 2389-2394
    • Snyder, H.L.1    Yewdell, J.W.2    Bennik, J.R.3
  • 58
    • 0031091739 scopus 로고    scopus 로고
    • Prominence of β2-microglobulin, class I heavy chain conformation, and tapasin in the interactions of class I heavy chain with calreticulin and the transporter associated with antigen processing
    • SOLHEIM J. C., HARRIS M. R., KINDLE C. S. and HANSEN T. H. (1997): Prominence of β2-microglobulin, class I heavy chain conformation, and tapasin in the interactions of class I heavy chain with calreticulin and the transporter associated with antigen processing. J. Immunol., 158, 2236-2241.
    • (1997) J. Immunol. , vol.158 , pp. 2236-2241
    • Solheim, J.C.1    Harris, M.R.2    Kindle, C.S.3    Hansen, T.H.4
  • 59
    • 0026500826 scopus 로고
    • Presentation of viral antigen by mhc class i molecules is dependent on a putative peptide transporter heterodimer
    • SPIES T., CERUNDOLO V., COLONA M., CRESSWELL P., TOWNSEND A. and DEMARS R. (1992): Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer. Nature, 355, 644-646.
    • (1992) Nature , vol.355 , pp. 644-646
    • Spies, T.1    Cerundolo, V.2    Colona, M.3    Cresswell, P.4    Townsend, A.5    Demars, R.6
  • 60
    • 0031771008 scopus 로고    scopus 로고
    • Generation of the vesicular stomatitis virus nucleoprotein cytotoxic T lymphocyte epitope requires proteasome-dependent and -independent proteolytic activities
    • STOLTZE L., DICK T. P., DEEG M., POMMERL B., RAMMENSEE H. G. and SCHILD H. (1998): Generation of the vesicular stomatitis virus nucleoprotein cytotoxic T lymphocyte epitope requires proteasome-dependent and -independent proteolytic activities. Eur. J. Immunol., 28, 4029-4036.
    • (1998) Eur. J. Immunol. , vol.28 , pp. 4029-4036
    • Stoltze, L.1    Dick, T.P.2    Deeg, M.3    Pommerl, B.4    Rammensee, H.G.5    Schild, H.6
  • 61
    • 0033083288 scopus 로고    scopus 로고
    • Interaction of murine MHC class I molecules with tapasin and TAP enhances peptide loading and involves the heavy chain alpha3 domain
    • SUH W. K., DERBY M. A., COHEN-DOYLE M. F., SCHOENHALS G. J., FRUH K., BERZOFSKY J. A. and WILLIAMS D. B. (1999): Interaction of murine MHC class I molecules with tapasin and TAP enhances peptide loading and involves the heavy chain alpha3 domain. J. Immunol., 162, 1530-1540.
    • (1999) J. Immunol. , vol.162 , pp. 1530-1540
    • Suh, W.K.1    Derby, M.A.2    Cohen-Doyle, M.F.3    Schoenhals, G.J.4    Fruh, K.5    Berzofsky, J.A.6    Williams, D.B.7
  • 62
    • 0029813510 scopus 로고    scopus 로고
    • MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains
    • SUH W.-K., MITCHELL E. K., YANG Y., PETERSON P. A., WANECK G. L. and WILLIAMS D. B. (1996): MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains. J. Exp. Med., 184, 337-348.
    • (1996) J. Exp. Med. , vol.184 , pp. 337-348
    • Suh, W.-K.1    Mitchell, E.K.2    Yang, Y.3    Peterson, P.A.4    Waneck, G.L.5    Williams, D.B.6
  • 63
    • 0030873556 scopus 로고    scopus 로고
    • Differential requirements for survival and proliferation of CD8 naive or memory T cells
    • TANCHOT C., LEMONNIER F. A., PERARNAU B., FREITAS A. and ROCHA B. (1997): Differential requirements for survival and proliferation of CD8 naive or memory T cells. Science, 276, 2057-2062.
    • (1997) Science , vol.276 , pp. 2057-2062
    • Tanchot, C.1    Lemonnier, F.A.2    Perarnau, B.3    Freitas, A.4    Rocha, B.5
  • 64
    • 0029100978 scopus 로고
    • Calnexin influences folding of human class I histocompatibility proteins but not their assembly with beta 2-microglobulin
    • TECTOR M. and SALTER R. D. (1995): Calnexin influences folding of human class I histocompatibility proteins but not their assembly with beta 2-microglobulin. J. Biol. Chem., 270, 19638-19642.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19638-19642
    • Tector, M.1    Salter, R.D.2
  • 65
    • 0024324442 scopus 로고
    • Association of class I major histocompatibility heavy and light chains induced by viral peptides
    • TOWNSEND A., OHLEN C., BASTIN J., LJUNGREN H.-G., FOSTER L. and KARRE K. (1989): Association of class I major histocompatibility heavy and light chains induced by viral peptides. Nature, 340, 443-448.
    • (1989) Nature , vol.340 , pp. 443-448
    • Townsend, A.1    Ohlen, C.2    Bastin, J.3    Ljungren, H.-G.4    Foster, L.5    Karre, K.6
  • 68
    • 0030467255 scopus 로고    scopus 로고
    • Deglucosilation of N-linked glycans is an important step in the dissociation of calreticulin-class I-TAP complexes
    • VAN LEEUWEN J. E. M. and KEARSE K. P. (1996): Deglucosilation of N-linked glycans is an important step in the dissociation of calreticulin-class I-TAP complexes. Proc. Natl. Acad. Sci. USA, 93, 13997-14001.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13997-14001
    • Van Leeuwen, J.E.M.1    Kearse, K.P.2
  • 69
    • 0029925940 scopus 로고    scopus 로고
    • The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules
    • VASILLAKOS A., COHEN-DOYLE M., PETERSON P. A., JACKSON M. R. and WILLIAMS D. B. (1996): The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules. EMBO J., 15, 1495-1506.
    • (1996) EMBO J. , vol.15 , pp. 1495-1506
    • Vasillakos, A.1    Cohen-Doyle, M.2    Peterson, P.A.3    Jackson, M.R.4    Williams, D.B.5
  • 70
    • 0031570893 scopus 로고    scopus 로고
    • The generation of MHC class I-associated peptides is only partially inhibited by proteasome inhibitors
    • VINITSKY A., ANTON L. C., LINK SNYDER H., ORLOWSKY M., BENNINK J. R. and YEWDELL J. W. (1997): The generation of MHC class I-associated peptides is only partially inhibited by proteasome inhibitors. J. Immunol., 159, 554-564.
    • (1997) J. Immunol. , vol.159 , pp. 554-564
    • Vinitsky, A.1    Anton, L.C.2    Link Snyder, H.3    Orlowsky, M.4    Bennink, J.R.5    Yewdell, J.W.6
  • 71
    • 0025609606 scopus 로고
    • The role of β2-microglobulin in peptide binding by class I molecules
    • VITIELLO A., POTTER T. A. and SHERMAN L. A. (1990): The role of β2-microglobulin in peptide binding by class I molecules. Science, 250, 1423-1426.
    • (1990) Science , vol.250 , pp. 1423-1426
    • Vitiello, A.1    Potter, T.A.2    Sherman, L.A.3
  • 72
    • 0024502952 scopus 로고
    • Role of β2-microglobulin in the intracellular transport and surface expression of murine class I histocompatibility molecules
    • WILLIAMS D. B., BARBER B. H., FLAVELL R. A. and ALLEN H. (1989): Role of β2-microglobulin in the intracellular transport and surface expression of murine class I histocompatibility molecules. J. Immunol., 142, 2796-2806.
    • (1989) J. Immunol. , vol.142 , pp. 2796-2806
    • Williams, D.B.1    Barber, B.H.2    Flavell, R.A.3    Allen, H.4
  • 73
    • 0029920469 scopus 로고    scopus 로고
    • Antigen processing and presentation by the class I major histocompatibility complex
    • YORK I. A. and ROCK K. L. (1996): Antigen processing and presentation by the class I major histocompatibility complex. Ann. Rev. Immunol., 14, 369-396.
    • (1996) Ann. Rev. Immunol. , vol.14 , pp. 369-396
    • York, I.A.1    Rock, K.L.2
  • 74
    • 0032853308 scopus 로고    scopus 로고
    • An extensive region of an MHC class I alpha2 domain loop influences interaction with the assembly complex
    • YU Y. Y., TURNQUIST H. R., MYERS N. B., BALENDIRAN G. K., HANSEN T. H. and SOLHEIM J. C. (1999): An extensive region of an MHC class I alpha2 domain loop influences interaction with the assembly complex. J. Immunol., 163, 4427-4433.
    • (1999) J. Immunol. , vol.163 , pp. 4427-4433
    • Yu, Y.Y.1    Turnquist, H.R.2    Myers, N.B.3    Balendiran, G.K.4    Hansen, T.H.5    Solheim, J.C.6


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