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Volumn 18, Issue 3, 1999, Pages 743-753

Retention of empty MHC class I molecules by tapasin is essential to reconstitute antigen presentation in invertebrate cells

Author keywords

Antigen presentation; Chaperone; MHC; Proteasome; Transpsrter associated with antigen processing

Indexed keywords

GLYCOPROTEIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1;

EID: 0344096462     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.3.743     Document Type: Article
Times cited : (100)

References (57)
  • 1
    • 0030016036 scopus 로고    scopus 로고
    • Molecular mechanism and species specificity of TAP inhibition by herpes simplex virus protein ICP47
    • Ahn, K., Meyer, T.H., Uebel, S., Sempé, P., Djaballah, H., Yang, Y., Peterson, P.A., Früh, K. and Tampé, R. (1996) Molecular mechanism and species specificity of TAP inhibition by herpes simplex virus protein ICP47. EMBO J., 15, 3247-3255.
    • (1996) EMBO J. , vol.15 , pp. 3247-3255
    • Ahn, K.1    Meyer, T.H.2    Uebel, S.3    Sempé, P.4    Djaballah, H.5    Yang, Y.6    Peterson, P.A.7    Früh, K.8    Tampé, R.9
  • 3
    • 0025879780 scopus 로고
    • Endogenously synthesized peptide with an endoplasmic reticulum signal sequence sensitizes antigen processing mutant cells to class I-restricted cell-mediated lysis
    • Anderson, K., Cresswell, P., Gammon, M., Hermes, J., Williamson, A. and Zweerink, H. (1991) Endogenously synthesized peptide with an endoplasmic reticulum signal sequence sensitizes antigen processing mutant cells to class I-restricted cell-mediated lysis. J. Exp. Med., 174, 489-492.
    • (1991) J. Exp. Med. , vol.174 , pp. 489-492
    • Anderson, K.1    Cresswell, P.2    Gammon, M.3    Hermes, J.4    Williamson, A.5    Zweerink, H.6
  • 4
    • 0022403592 scopus 로고
    • Impaired intracellular transport of class I MHC antigens as a possible means for adenoviruses to evade immune surveillance
    • Andersson, M., Pääbo, S., Nilsson, T. and Peterson, P.A. (1985) Impaired intracellular transport of class I MHC antigens as a possible means for adenoviruses to evade immune surveillance. Cell, 43, 215-222.
    • (1985) Cell , vol.43 , pp. 215-222
    • Andersson, M.1    Pääbo, S.2    Nilsson, T.3    Peterson, P.A.4
  • 5
    • 0032563221 scopus 로고    scopus 로고
    • Interferon-γ can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase
    • Beninga, J., Rock, K.L. and Goldberg, A.L. (1998) Interferon-γ can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase. J. Biol. Chem., 273, 18734-18742.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18734-18742
    • Beninga, J.1    Rock, K.L.2    Goldberg, A.L.3
  • 6
    • 0031953508 scopus 로고    scopus 로고
    • Structural characterization of a soluble and partially folded class I major histocompatibility heavy chain/β2m heterodimer
    • Bouvier, M. and Wiley, D.C. (1998) Structural characterization of a soluble and partially folded class I major histocompatibility heavy chain/β2m heterodimer. Nature Struct. Biol., 5, 377-384.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 377-384
    • Bouvier, M.1    Wiley, D.C.2
  • 7
    • 0029906583 scopus 로고    scopus 로고
    • Transfected Drosophila cells as a probe for defining the minimal requirements for stimulating unprimed CD8+ T cells
    • Cai, Z., Brunmark, A., Jackson, M.R., Loh, D., Peterson, P.A. and Sprent, J. (1996) Transfected Drosophila cells as a probe for defining the minimal requirements for stimulating unprimed CD8+ T cells. Proc. Natl Acad. Sci. USA, 93, 14736-14741.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14736-14741
    • Cai, Z.1    Brunmark, A.2    Jackson, M.R.3    Loh, D.4    Peterson, P.A.5    Sprent, J.6
  • 8
    • 0024583817 scopus 로고
    • Induction of ovalbumin-specific cytotoxic T cells by in vivo peptide immunization
    • Carbone, F.R. and Bevan, M.J. (1989) Induction of ovalbumin-specific cytotoxic T cells by in vivo peptide immunization. J. Exp. Med., 169, 603-612.
    • (1989) J. Exp. Med. , vol.169 , pp. 603-612
    • Carbone, F.R.1    Bevan, M.J.2
  • 9
    • 0026719025 scopus 로고
    • T cell receptor alpha-chain pairing determines the specificity of residue 262 within the Kb-restricted, ovalbumin 257-264 determinant
    • Carbone, F.R., Sterry, S.J., Butler, J., Rodda, S. and Moore, M.W. (1992) T cell receptor alpha-chain pairing determines the specificity of residue 262 within the Kb-restricted, ovalbumin 257-264 determinant. Int. Immunol., 4, 861-867.
    • (1992) Int. Immunol. , vol.4 , pp. 861-867
    • Carbone, F.R.1    Sterry, S.J.2    Butler, J.3    Rodda, S.4    Moore, M.W.5
  • 10
    • 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., Connally, 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    Connally, J.M.5    Hansen, T.H.6
  • 11
    • 0030923682 scopus 로고    scopus 로고
    • Nucleotide sequence of a Drosophila melanogaster cDNA encoding a calnexin homolog
    • Christodoulou, S., Lockyer, A.E., Foster, J.M., Hoheisel, J.D. and Roberts, D.B. (1997) Nucleotide sequence of a Drosophila melanogaster cDNA encoding a calnexin homolog. Gene, 191, 143-148.
    • (1997) Gene , vol.191 , pp. 143-148
    • Christodoulou, S.1    Lockyer, A.E.2    Foster, J.M.3    Hoheisel, J.D.4    Roberts, D.B.5
  • 12
    • 0030886208 scopus 로고    scopus 로고
    • Two distinct proteolytic processes in the generation of a major histocompatibility complex class I-presented peptide
    • Craiu, A., Akopian, T., Goldberg, A. and Rock, K.L. (1997) Two distinct proteolytic processes in the generation of a major histocompatibility complex class I-presented peptide. Proc. Natl Acad. Sci. USA, 94, 10850-10855.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10850-10855
    • Craiu, A.1    Akopian, T.2    Goldberg, A.3    Rock, K.L.4
  • 13
    • 0032529393 scopus 로고    scopus 로고
    • Assembly of MHC class I molecules with biosynthesized endoplasmic reticulum-targeted peptides is inefficient in insect cells and can be enhanced by protease inhibitors
    • Deng, Y. et al. (1998) Assembly of MHC class I molecules with biosynthesized endoplasmic reticulum-targeted peptides is inefficient in insect cells and can be enhanced by protease inhibitors. J. Immunol., 161, 1677-1685.
    • (1998) J. Immunol. , vol.161 , pp. 1677-1685
    • Deng, Y.1
  • 14
    • 0028981178 scopus 로고
    • HLA-DM induces CLIP dissociation from MHC class II ab dimers and facilitates peptide loading
    • Denzin, L.K. and Cresswell, P. (1995) HLA-DM induces CLIP dissociation from MHC class II ab dimers and facilitates peptide loading. Cell, 82, 155-165.
    • (1995) Cell , vol.82 , pp. 155-165
    • Denzin, L.K.1    Cresswell, P.2
  • 15
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany, G., Standaert, R.F., Lane, W.S., Choi, S., Corey, E.J. and Schreiber, S.L. (1995) Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science, 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
  • 16
    • 0038899636 scopus 로고    scopus 로고
    • Regulation of MHC class I antigen presentation by interferon gamma
    • in press
    • Früh, K. and Yang, Y. (1999) Regulation of MHC class I antigen presentation by interferon gamma. Curr. Opin. Immunol., in press.
    • (1999) Curr. Opin. Immunol.
    • Früh, K.1    Yang, Y.2
  • 17
    • 0026595367 scopus 로고
    • Alternative exon usage and processing of the major histocompatibility complex-encoded proteasome subunits
    • Früh, K., Yang, Y., Arnold, D., Chambers, J., Wu, L., Waters, J.B., Spies, T. and Peterson, P.A. (1992) Alternative exon usage and processing of the major histocompatibility complex-encoded proteasome subunits. J. Biol. Chem., 267, 22131-22140.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22131-22140
    • Früh, K.1    Yang, Y.2    Arnold, D.3    Chambers, J.4    Wu, L.5    Waters, J.B.6    Spies, T.7    Peterson, P.A.8
  • 18
    • 0032499199 scopus 로고    scopus 로고
    • A proteolytic system that compensates for loss of proteasome function
    • Glas, R., Bogyo, M., McMaster, J.S., Gaczynska, M. and Ploegh, H.L. (1998) A proteolytic system that compensates 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
  • 19
    • 0026764311 scopus 로고
    • Proteolysis, proteasomes and antigen presentation
    • Goldberg, A.L. and Rock, K.L. (1992) Proteolysis, proteasomes and antigen presentation. Nature, 357, 376-378.
    • (1992) Nature , vol.357 , pp. 376-378
    • Goldberg, A.L.1    Rock, K.L.2
  • 20
    • 0028817950 scopus 로고
    • Dependence of peptide binding by MHC class I molecules on their interaction with TAP
    • Grandea, A., III, 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. III1    Androlewicz, M.J.2    Athwal, R.S.3    Geraghty, D.E.4    Spies, T.5
  • 22
    • 0020170182 scopus 로고
    • Localization of allodeterminants on H-2Kb antigens determined with monoclonal antibodies and H-2 mutant mice
    • Hämmerling, G.J., Rusch, E., Tada, N., Kimura, S. and Hämmerling, U. (1982) Localization of allodeterminants on H-2Kb antigens determined with monoclonal antibodies and H-2 mutant mice. Proc. Natl Acad. Sci. USA, 79, 4737-4741.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 4737-4741
    • Hämmerling, G.J.1    Rusch, E.2    Tada, N.3    Kimura, S.4    Hämmerling, U.5
  • 23
    • 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.L., 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.L.2    Kindle, C.S.3    Hansen, T.H.4    Solheim, J.C.5
  • 24
    • 0029001515 scopus 로고
    • Generation, translocation and presentation of MHC class I-restricted peptides
    • Heemels, M. T. and Ploegh, H. (1995) Generation, translocation and presentation of MHC class I-restricted peptides. Annu. Rev. Biochem., 64, 463-491.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 463-491
    • Heemels, M.T.1    Ploegh, H.2
  • 26
    • 0032482384 scopus 로고    scopus 로고
    • The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex
    • Hughes, E. 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.1    Cresswell, P.2
  • 27
    • 0025184422 scopus 로고
    • Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum
    • Jackson, M.R., Nilsson, T. and Peterson, P.A. (1990) Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum. EMBO J., 9, 3153-3162.
    • (1990) EMBO J. , vol.9 , pp. 3153-3162
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 28
    • 0027048777 scopus 로고
    • Empty and peptide-containing conformers of class I major histocompatibility complex molecules expressed in Drosophila melanogaster cells
    • Jackson, M.R., Song, E.S., Young, Y. and Peterson, P.A. (1992) Empty and peptide-containing conformers of class I major histocompatibility complex molecules expressed in Drosophila melanogaster cells. Proc. Natl Acad. Sci. USA, 89, 12117-12121.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 12117-12121
    • Jackson, M.R.1    Song, E.S.2    Young, Y.3    Peterson, P.A.4
  • 29
    • 0028181429 scopus 로고
    • Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90)
    • Jackson, M.R., Cohen-Doyle, M.F., Peterson, P.A. and Williams, D.B. (1994) Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90). Science, 263, 384-387.
    • (1994) Science , vol.263 , pp. 384-387
    • Jackson, M.R.1    Cohen-Doyle, M.F.2    Peterson, P.A.3    Williams, D.B.4
  • 30
    • 0032536790 scopus 로고    scopus 로고
    • Physical and functional association of the major histocompatibility complex class I heavy chain α3 domain with the transporter associated with antigen processing
    • Kulig, K., Nandi, D., Bacik, I., Monaco, J.J. and Vukmanovic, S. (1998) Physical and functional association of the major histocompatibility complex 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    Vukmanovic, S.5
  • 31
    • 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
  • 32
    • 0032482319 scopus 로고    scopus 로고
    • Evidence for successive peptide binding and quality control stages during MHC class I assembly
    • Lewis, J.W. und Elliot, T. (1998) Evidence for successive peptide binding and quality control stages during MHC class I assembly. Curr. Biol., 8, 717-720.
    • (1998) Curr. Biol. , vol.8 , pp. 717-720
    • Lewis, J.W.1    Elliot, T.2
  • 33
    • 0030198868 scopus 로고    scopus 로고
    • Point mutations in the alpha 2 domain of HLA-A2.1 define a functionally relevant interaction with TAP
    • Lewis, J.W., Neisig, A., Neefjes, J. and Elliot, T. (1996) Point mutations in the alpha 2 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    Elliot, T.4
  • 34
    • 0030871305 scopus 로고    scopus 로고
    • Cloning and functional characterization of a subunit of the transporter associated with antigen processing
    • Li, S., Sjoegren, 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    Sjoegren, H.-O.2    Hellman, U.3    Pettersson, R.F.4    Wang, P.5
  • 35
    • 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
  • 36
    • 0032482385 scopus 로고    scopus 로고
    • A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
    • Morrice, N.A. and Powis, S.A. (1998) A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules. Curr. Biol., 8, 713-716.
    • (1998) Curr. Biol. , vol.8 , pp. 713-716
    • Morrice, N.A.1    Powis, S.A.2
  • 37
    • 0027239749 scopus 로고
    • Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter
    • Neefjes, J.J., Momburg, F. and Hämmerling, 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    Hämmerling, G.J.3
  • 38
    • 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
    • 0030852963 scopus 로고    scopus 로고
    • Potential immunocompetence of proteolytic fragments produced by proteasomes before evolution of the vertebrate immune system
    • Niedermann, G. et al. (1997) Potential immunocompetence of proteolytic fragments produced by proteasomes before evolution of the vertebrate immune system. J. Exp. Med., 186, 209-220.
    • (1997) J. Exp. Med. , vol.186 , pp. 209-220
    • Niedermann, G.1
  • 40
    • 0028917887 scopus 로고
    • Species-specific differences in chaperone interaction of human and mouse major histocompatibility complex class I molecules
    • Noessner, E. and Parham, P. (1995) Species-specific differences in chaperone interaction of human and mouse major histocompatibility complex class I molecules. J. Exp. Med., 181, 327-337.
    • (1995) J. Exp. Med. , vol.181 , pp. 327-337
    • Noessner, E.1    Parham, P.2
  • 41
    • 0028282108 scopus 로고
    • MHC class I/β2-microglobulin complexes associate with TAP transporters before peptide binding
    • Ortmann, B., Androlewicz, M.J. 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.J.2    Cresswell, P.3
  • 42
    • 0030865333 scopus 로고    scopus 로고
    • A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes
    • Ortmann, B. et al. (1997) A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes. Science, 277, 1306-1309.
    • (1997) Science , vol.277 , pp. 1306-1309
    • Ortmann, B.1
  • 43
    • 0030152620 scopus 로고    scopus 로고
    • A point mutation in HLA-A *0201 results in failure to bind to 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 to 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
  • 44
    • 0032076171 scopus 로고    scopus 로고
    • HLA-B27-restricted antigen in the absence of tapasin reveals polymorphism in mechanisms of HLA class I peptide loading
    • Peh, C.A., Burrows, S.R., Barnden, M., Khanna, R., Cresswell, P., Moss, D.J. and McCluskey, J. (1998) HLA-B27-restricted antigen in the absence of tapasin reveals polymorphism in mechanisms of HLA class I peptide loading. Immunity, 8, 531-542.
    • (1998) Immunity , vol.8 , pp. 531-542
    • Peh, C.A.1    Burrows, S.R.2    Barnden, M.3    Khanna, R.4    Cresswell, P.5    Moss, D.J.6    McCluskey, J.7
  • 45
    • 0030849769 scopus 로고    scopus 로고
    • Localization, quantitation and in situ detection of specific peptide-MHC class I complexes using a monoclonal antibody
    • Porgador, A., Yewdell, J.W., Deng, Y., Bennink, J.R. and Germain, R.N. (1997) Localization, quantitation and in situ detection of specific peptide-MHC class I complexes using a monoclonal antibody. Immunity, 6, 715-726.
    • (1997) Immunity , vol.6 , pp. 715-726
    • Porgador, A.1    Yewdell, J.W.2    Deng, Y.3    Bennink, J.R.4    Germain, R.N.5
  • 46
    • 0027399243 scopus 로고
    • Peptides naturally presented by MHC class I molecules
    • Rammensee, H.G., Falk, K. and Rötschke, O. (1993) Peptides naturally presented by MHC class I molecules. Annu. Rev. Immunol., 11, 213-244.
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 213-244
    • Rammensee, H.G.1    Falk, K.2    Rötschke, O.3
  • 47
    • 0032486251 scopus 로고    scopus 로고
    • A soluble major histocompatibility complex class I peptide-binding platform undergoes a conformational change in response to peptide epitopes
    • Rigney, E., Kojima, M., Glithero, A. and Elliott, T. (1998) A soluble major histocompatibility complex class I peptide-binding platform undergoes a conformational change in response to peptide epitopes. J. Biol. Chem., 273, 14200-14204.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14200-14204
    • Rigney, E.1    Kojima, M.2    Glithero, A.3    Elliott, T.4
  • 48
    • 0030217926 scopus 로고    scopus 로고
    • Roles for 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 for 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
  • 49
    • 0028300583 scopus 로고
    • In vivo regulation of the assembly and intracellular transport of class I major histocompatibility complex molecules
    • Song, E.S., Yang, Y., Jackson, M.R. and Peterson, P.A. (1994) In vivo regulation of the assembly and intracellular transport of class I major histocompatibility complex molecules. J. Biol. Chem., 269, 7024-7029.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7024-7029
    • Song, E.S.1    Yang, Y.2    Jackson, M.R.3    Peterson, P.A.4
  • 50
    • 0028239443 scopus 로고
    • Interaction of MHC class I molecules with the transporter associated with antigen processing
    • Suh, W.-K., Cohen-Doyle, M.F., Früh, K., Wang, K., Peterson, P.A. and Williams, D.B. (1994) Interaction of MHC class I molecules with the transporter associated with antigen processing. Science, 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
  • 51
    • 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
  • 52
    • 0027548728 scopus 로고
    • The transporters associated with antigen presentation
    • Townsend, A. and Trowsdale, J. (1993) The transporters associated with antigen presentation. Semin. Cell Biol., 4, 53-61.
    • (1993) Semin. Cell Biol. , vol.4 , pp. 53-61
    • Townsend, A.1    Trowsdale, J.2
  • 53
    • 0024324442 scopus 로고
    • Association of class I major histocompatihility heavy and light chains induced by viral peptides
    • Townsend, A., Öhlén, C., Bastin, J., Ljunggren, H.-G., Foster, L. and Kärre, K. (1989) Association of class I major histocompatihility heavy and light chains induced by viral peptides. Nature, 340, 443-448.
    • (1989) Nature , vol.340 , pp. 443-448
    • Townsend, A.1    Öhlén, C.2    Bastin, J.3    Ljunggren, H.-G.4    Foster, L.5    Kärre, K.6
  • 55
    • 0029925940 scopus 로고    scopus 로고
    • The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules
    • Vassilakos, A., Cohen-Doyle, M.F., 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, 1495-506.
    • (1996) EMBO J. , vol.15 , pp. 1495-1506
    • Vassilakos, A.1    Cohen-Doyle, M.F.2    Peterson, P.A.3    Jackson, M.R.4    Williams, D.B.5
  • 56
    • 0028136684 scopus 로고
    • Nucleotide binding of the C-terminal domains of the major histocompatibility complex-encoded transporter expressed in Drosophila melanogaster cells
    • Wang, K., Früh, K., Peterson, P.A. and Yang, Y. (1994) Nucleotide binding of the C-terminal domains of the major histocompatibility complex-encoded transporter expressed in Drosophila melanogaster cells. FEBS Lett., 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
    • 0029824101 scopus 로고    scopus 로고
    • Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA-DM
    • Weber, D.A., Evavold, B.D. and Jensen, P.E. (1996) Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA-DM. Science, 274, 618-620.
    • (1996) Science , vol.274 , pp. 618-620
    • Weber, D.A.1    Evavold, B.D.2    Jensen, P.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.