메뉴 건너뛰기




Volumn , Issue , 2005, Pages 3-11

MHC Class I

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84882819439     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012455900-4/50263-4     Document Type: Chapter
Times cited : (1)

References (67)
  • 1
    • 0242331619 scopus 로고    scopus 로고
    • Early phagosomes in dendritic cells form a cellular compartment sufficient for cross presentation of exogenous antigens
    • Ackerman A.L., Kyritsis C., Tampe R., Cresswell P. Early phagosomes in dendritic cells form a cellular compartment sufficient for cross presentation of exogenous antigens. PNAS 2003, 100:12889-12894.
    • (2003) PNAS , vol.100 , pp. 12889-12894
    • Ackerman, A.L.1    Kyritsis, C.2    Tampe, R.3    Cresswell, P.4
  • 2
    • 0028606109 scopus 로고
    • Characteristics of peptide and major histocompatibility complex class I/{beta}2-microglobulin binding to the transporters associated with antigen processing (TAP1 and TAP2)
    • Androlewicz M., Ortmann B., Endert P., Spies T., Cresswell P. Characteristics of peptide and major histocompatibility complex class I/{beta}2-microglobulin binding to the transporters associated with antigen processing (TAP1 and TAP2). PNAS 1994, 91:12716-12720.
    • (1994) PNAS , vol.91 , pp. 12716-12720
    • Androlewicz, M.1    Ortmann, B.2    Endert, P.3    Spies, T.4    Cresswell, P.5
  • 3
    • 0034894893 scopus 로고    scopus 로고
    • Molecular typing of HLA-A, -B, and DRB using a high throughput micro array format
    • Balazs I., Beekman J., Neuweiler J., Liu H., Watson E., Ray B. Molecular typing of HLA-A, -B, and DRB using a high throughput micro array format. Hum Immunol 2001, 62:850-857.
    • (2001) Hum Immunol , vol.62 , pp. 850-857
    • Balazs, I.1    Beekman, J.2    Neuweiler, J.3    Liu, H.4    Watson, E.5    Ray, B.6
  • 4
    • 0034575122 scopus 로고    scopus 로고
    • The human major histocompatability complex: lessons from the DNA sequence
    • Beck S., Trowsdale J. The human major histocompatability complex: lessons from the DNA sequence. Annu Rev Genomics Hum Genet 2000, 1:117-137.
    • (2000) Annu Rev Genomics Hum Genet , vol.1 , pp. 117-137
    • Beck, S.1    Trowsdale, J.2
  • 5
    • 0023187442 scopus 로고
    • The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens
    • Bjorkman P., Saper M., Samraoui B., Bennett W., Strominger J., Wiley D. The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens. Nature 1987, 329:512-518.
    • (1987) Nature , vol.329 , pp. 512-518
    • Bjorkman, P.1    Saper, M.2    Samraoui, B.3    Bennett, W.4    Strominger, J.5    Wiley, D.6
  • 7
    • 0038325750 scopus 로고    scopus 로고
    • Induction of immune responses by attenuated isogenic mutant strains of Listeria monocytogenes
    • Darji A., Mohamed W., Domann E., Chakraborty T. Induction of immune responses by attenuated isogenic mutant strains of Listeria monocytogenes. Vaccine 2003, 21:S102-S109.
    • (2003) Vaccine , vol.21
    • Darji, A.1    Mohamed, W.2    Domann, E.3    Chakraborty, T.4
  • 8
    • 0022373781 scopus 로고
    • Mutations that impair a posttranscriptional step in expression of HLA-A and -B antigens
    • DeMars R., Rudersdorf R., Chang C., et al. Mutations that impair a posttranscriptional step in expression of HLA-A and -B antigens. Proc Natl Acad Sci USA 1985, 82:8183-8187.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 8183-8187
    • DeMars, R.1    Rudersdorf, R.2    Chang, C.3
  • 9
    • 0033529596 scopus 로고    scopus 로고
    • The proteasome, a novel protease regulated by multiple mechanisms
    • DeMartino G.N., Slaughter C.A. The proteasome, a novel protease regulated by multiple mechanisms. J Biol Chem 1999, 274:22123-22126.
    • (1999) J Biol Chem , vol.274 , pp. 22123-22126
    • DeMartino, G.N.1    Slaughter, C.A.2
  • 10
    • 0035253721 scopus 로고    scopus 로고
    • A role for calnexin in the assembly of the MHC class I loading complex in the endoplasmic reticulum
    • Diedrich G., Bangia N., Pan M., Cresswell P. A role for calnexin in the assembly of the MHC class I loading complex in the endoplasmic reticulum. J Immunol 2001, 166:1703-1709.
    • (2001) J Immunol , vol.166 , pp. 1703-1709
    • Diedrich, G.1    Bangia, N.2    Pan, M.3    Cresswell, P.4
  • 11
    • 0025855156 scopus 로고
    • Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules
    • Falk K., Rotzschke O., Stevanovic S., Jung G., Rammensee H. Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules. Nature 1991, 351:290-296.
    • (1991) Nature , vol.351 , pp. 290-296
    • Falk, K.1    Rotzschke, O.2    Stevanovic, S.3    Jung, G.4    Rammensee, H.5
  • 12
    • 0029901736 scopus 로고    scopus 로고
    • Direct binding of a soluble natural killer cell inhibitory receptor to a soluble human leukocyte antigen-Cw4 class I major histocompatibility complex molecule
    • Fan Q.R., Garboczi D.N., Winter C.C., Wagtmann N., Long E.O., Wiley D.C. Direct binding of a soluble natural killer cell inhibitory receptor to a soluble human leukocyte antigen-Cw4 class I major histocompatibility complex molecule. PNAS 1996, 93:7178-7183.
    • (1996) PNAS , vol.93 , pp. 7178-7183
    • Fan, Q.R.1    Garboczi, D.N.2    Winter, C.C.3    Wagtmann, N.4    Long, E.O.5    Wiley, D.C.6
  • 13
    • 0038899636 scopus 로고    scopus 로고
    • Antigen presentation by MHC class I and its regulation by interferon gamma
    • Fruh K., Yang Y. Antigen presentation by MHC class I and its regulation by interferon gamma. Curr Opin Immunol 1999, 11:76-81.
    • (1999) Curr Opin Immunol , vol.11 , pp. 76-81
    • Fruh, K.1    Yang, Y.2
  • 14
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • Garboczi D., Ghosh P., Utz U., et al. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 1996, 384:134-141.
    • (1996) Nature , vol.384 , pp. 134-141
    • Garboczi, D.1    Ghosh, P.2    Utz, U.3
  • 15
    • 0035825154 scopus 로고    scopus 로고
    • The phagosome proteome: insight into phagosome functions
    • Garin J., Diez R., Kieffer S., et al. The phagosome proteome: insight into phagosome functions. J Cell Biol 2001, 152:165-180.
    • (2001) J Cell Biol , vol.152 , pp. 165-180
    • Garin, J.1    Diez, R.2    Kieffer, S.3
  • 16
    • 0024345149 scopus 로고
    • Specificity pockets for the side chains of peptide antigens in HLA-Aw68
    • Garrett T., Saper M., Bjorkman P., et al. Specificity pockets for the side chains of peptide antigens in HLA-Aw68. Nature 1989, 342:692-696.
    • (1989) Nature , vol.342 , pp. 692-696
    • Garrett, T.1    Saper, M.2    Bjorkman, P.3
  • 17
    • 1642353588 scopus 로고    scopus 로고
    • Control of cross-presentation during dendritic cell maturation
    • Gil-Torregrosa B., Lennon-Dumenil A., Kessler B., et al. Control of cross-presentation during dendritic cell maturation. Eur J Immunol 2004, 34:398-407.
    • (2004) Eur J Immunol , vol.34 , pp. 398-407
    • Gil-Torregrosa, B.1    Lennon-Dumenil, A.2    Kessler, B.3
  • 18
    • 0041672389 scopus 로고    scopus 로고
    • The antigen processing machinery of class I human leukocyte antigens: linked patterns of gene expression in neoplastic cells
    • Giorda E., Sibilio L., Martayan A., et al. The antigen processing machinery of class I human leukocyte antigens: linked patterns of gene expression in neoplastic cells. Cancer Res 2003, 63:4119-4127.
    • (2003) Cancer Res , vol.63 , pp. 4119-4127
    • Giorda, E.1    Sibilio, L.2    Martayan, A.3
  • 19
    • 0036777957 scopus 로고    scopus 로고
    • The importance of the proteasome and subsequent proteolytic steps in the generation of antigenic peptides
    • Goldberg A.L., Cascio P., Saric T., Rock K.L. The importance of the proteasome and subsequent proteolytic steps in the generation of antigenic peptides. Mol Immunol 2002, 39:147-164.
    • (2002) Mol Immunol , vol.39 , pp. 147-164
    • Goldberg, A.L.1    Cascio, P.2    Saric, T.3    Rock, K.L.4
  • 20
    • 0031973736 scopus 로고    scopus 로고
    • Immunoprotea-some assembly: cooperative incorporation of interferon gamma (IFN-gamma)-inducible subunits
    • Griffin T.A., Nandi D., Cruz M., et al. Immunoprotea-some assembly: cooperative incorporation of interferon gamma (IFN-gamma)-inducible subunits. J Exp Med 1998, 187:97-104.
    • (1998) J Exp Med , vol.187 , pp. 97-104
    • Griffin, T.A.1    Nandi, D.2    Cruz, M.3
  • 21
    • 0141707939 scopus 로고    scopus 로고
    • ER-phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells
    • Guermonprez P., Saveanu L., Kleijmeer M., Davoust J., Van Endert P., Amigorena S. ER-phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells. Nature 2003, 425:397-402.
    • (2003) Nature , vol.425 , pp. 397-402
    • Guermonprez, P.1    Saveanu, L.2    Kleijmeer, M.3    Davoust, J.4    Van Endert, P.5    Amigorena, S.6
  • 22
    • 0033301948 scopus 로고    scopus 로고
    • Oligonucleotide arrays for high resolution HLA typing
    • Guo Z., Hood L., Petersdorf E. Oligonucleotide arrays for high resolution HLA typing. Rev Immunogenet 1999, 1:220-230.
    • (1999) Rev Immunogenet , vol.1 , pp. 220-230
    • Guo, Z.1    Hood, L.2    Petersdorf, E.3
  • 23
    • 1142269466 scopus 로고    scopus 로고
    • Immune recognition of a human renal cancer antigen through post-translational protein splicing
    • Hanada K., Yewdell J., Yang J. Immune recognition of a human renal cancer antigen through post-translational protein splicing. Nature 2004, 427:252-256.
    • (2004) Nature , vol.427 , pp. 252-256
    • Hanada, K.1    Yewdell, J.2    Yang, J.3
  • 24
    • 0141819094 scopus 로고    scopus 로고
    • A CTL epitope from human cytomegalovirus IE1 defined by combining prediction of HLA binding and proteasomal processing is the target of dominant immune responses in patients after allogeneic stem cell transplantation 1
    • Hebart H., Rauser G., Stevanovic S., et al. A CTL epitope from human cytomegalovirus IE1 defined by combining prediction of HLA binding and proteasomal processing is the target of dominant immune responses in patients after allogeneic stem cell transplantation 1. Exp Hematol 2003, 31:966-973.
    • (2003) Exp Hematol , vol.31 , pp. 966-973
    • Hebart, H.1    Rauser, G.2    Stevanovic, S.3
  • 25
    • 0027715856 scopus 로고
    • Peptide translocation by variants of the transporter associated with antigen processing
    • Heemels M., Schumacher T., Wonigeit K., Ploegh H. Peptide translocation by variants of the transporter associated with antigen processing. Science 1993, 262:2059-2063.
    • (1993) Science , vol.262 , pp. 2059-2063
    • Heemels, M.1    Schumacher, T.2    Wonigeit, K.3    Ploegh, H.4
  • 26
    • 0026471097 scopus 로고
    • Molecular analysis of the association of HLA-B53 and resistance to severe malaria
    • Hill A., Elvin J., Willis A., et al. Molecular analysis of the association of HLA-B53 and resistance to severe malaria. Nature 1992, 360:434-439.
    • (1992) Nature , vol.360 , pp. 434-439
    • Hill, A.1    Elvin, J.2    Willis, A.3
  • 27
    • 0028181429 scopus 로고
    • Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90)
    • Jackson M., Cohen-Doyle M., Peterson P., Williams D. Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90). Science 1994, 263:384-387.
    • (1994) Science , vol.263 , pp. 384-387
    • Jackson, M.1    Cohen-Doyle, M.2    Peterson, P.3    Williams, D.4
  • 28
    • 1342289031 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 subtype C Gag virus-like particle boost substantially improves the immune response to a subtype C gag DNA vaccine in mice
    • Jaffray A., Shephard E., van Harmelen J., Williamson C., Williamson A.-L., Rybicki E.P. Human immunodeficiency virus type 1 subtype C Gag virus-like particle boost substantially improves the immune response to a subtype C gag DNA vaccine in mice. J Gen Virol 2004, 85:409-413.
    • (2004) J Gen Virol , vol.85 , pp. 409-413
    • Jaffray, A.1    Shephard, E.2    van Harmelen, J.3    Williamson, C.4    Williamson, A.-L.5    Rybicki, E.P.6
  • 29
    • 0031950268 scopus 로고    scopus 로고
    • Inhibition of major histocompatibility complex class I antigen presentation in pig and primate cells by herpes simplex virus type 1 and 2 ICP47
    • Jugovic P., Hill A.M., Tomazin R., Ploegh H., Johnson D.C. Inhibition of major histocompatibility complex class I antigen presentation in pig and primate cells by herpes simplex virus type 1 and 2 ICP47. J Virol 1998, 72:5076-5084.
    • (1998) J Virol , vol.72 , pp. 5076-5084
    • Jugovic, P.1    Hill, A.M.2    Tomazin, R.3    Ploegh, H.4    Johnson, D.C.5
  • 30
    • 0035915772 scopus 로고    scopus 로고
    • TAP1 down-regulation in primary melanoma lesions: an independent marker of poor prognosis
    • Kamarashev J., Ferrone S., Seifert B., et al. TAP1 down-regulation in primary melanoma lesions: an independent marker of poor prognosis. Int J Cancer 2001, 95:23-28.
    • (2001) Int J Cancer , vol.95 , pp. 23-28
    • Kamarashev, J.1    Ferrone, S.2    Seifert, B.3
  • 31
    • 0028910938 scopus 로고
    • A phagosometo-cytosol pathway for exogenous antigens presented on MHC class I molecules
    • Kovascovics-Bankowski M., Rock K. A phagosometo-cytosol pathway for exogenous antigens presented on MHC class I molecules. Science 1995, 267:243-246.
    • (1995) Science , vol.267 , pp. 243-246
    • Kovascovics-Bankowski, M.1    Rock, K.2
  • 32
    • 0035214302 scopus 로고    scopus 로고
    • Bipartite regulation of different components of the MHC class I antigen-processing machinery during dendritic cell maturation
    • Li J., Schuler-Thurner B., Schuler G., Huber C., Seliger B. Bipartite regulation of different components of the MHC class I antigen-processing machinery during dendritic cell maturation. Int Immunol 2001, 13:1515-1523.
    • (2001) Int Immunol , vol.13 , pp. 1515-1523
    • Li, J.1    Schuler-Thurner, B.2    Schuler, G.3    Huber, C.4    Seliger, B.5
  • 33
    • 0027263157 scopus 로고
    • A role for the ubiquitin-dependent proteolytic pathway in MHC class I-restricted antigen presentation
    • Michalek M., Grant E., Gramm C., Goldberg A.L., Rock K. 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.1    Grant, E.2    Gramm, C.3    Goldberg, A.L.4    Rock, K.5
  • 34
    • 0037378093 scopus 로고    scopus 로고
    • Induction of protective immunity to Listeria monocytogenes with dendritic cells retrovirally transduced with a cytotoxic T lymphocyte epitope minigene
    • Nakamura Y., Suda T., Nagata T., et al. Induction of protective immunity to Listeria monocytogenes with dendritic cells retrovirally transduced with a cytotoxic T lymphocyte epitope minigene. Infect Immun 2003, 71:1748-1754.
    • (2003) Infect Immun , vol.71 , pp. 1748-1754
    • Nakamura, Y.1    Suda, T.2    Nagata, T.3
  • 35
    • 0022652885 scopus 로고
    • An improved biochemical method for the analysis of HLA-class I antigens. Definition of new HLA-class I subtypes
    • Neefjes J., Breur-Vriesendorp B., van Seventer G., Ivanyi P., Ploegh H. An improved biochemical method for the analysis of HLA-class I antigens. Definition of new HLA-class I subtypes. Hum Immunol 1986, 16:169-181.
    • (1986) Hum Immunol , vol.16 , pp. 169-181
    • Neefjes, J.1    Breur-Vriesendorp, B.2    van Seventer, G.3    Ivanyi, P.4    Ploegh, H.5
  • 36
    • 0030865333 scopus 로고    scopus 로고
    • A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes
    • Ortmann B., Copeman J., Lehner P., et al. A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes. Science 1997, 277:1306-1309.
    • (1997) Science , vol.277 , pp. 1306-1309
    • Ortmann, B.1    Copeman, J.2    Lehner, P.3
  • 37
    • 0036756291 scopus 로고    scopus 로고
    • Definition of the immunogenic HLA epitopes based on an epitope prediction algorithm
    • Papassavas A.C., Stavropoulos-Giokas C. Definition of the immunogenic HLA epitopes based on an epitope prediction algorithm. Transplant Proc 2002, 34:2049-2052.
    • (2002) Transplant Proc , vol.34 , pp. 2049-2052
    • Papassavas, A.C.1    Stavropoulos-Giokas, C.2
  • 38
    • 0036206510 scopus 로고    scopus 로고
    • Mutant MHC class I molecules define interactions between components of the peptide-loading complex
    • Paquet M.-E., Williams D.B. Mutant MHC class I molecules define interactions between components of the peptide-loading complex. Int Immunol 2002, 14:347-358.
    • (2002) Int Immunol , vol.14 , pp. 347-358
    • Paquet, M.-E.1    Williams, D.B.2
  • 39
    • 0020971336 scopus 로고
    • Monoclonal antibodies against HLA products and their use in immunoaffinity purification
    • Parham P. Monoclonal antibodies against HLA products and their use in immunoaffinity purification. Methods Enzymol 1983, 92:110-138.
    • (1983) Methods Enzymol , vol.92 , pp. 110-138
    • Parham, P.1
  • 40
    • 0024344047 scopus 로고
    • Diversity and diversification of HLA-A,B,C alleles
    • Parham P., Lawlor D., Lomen C., Ennis P. Diversity and diversification of HLA-A,B,C alleles. J Immunol 1989, 142:3937-3950.
    • (1989) J Immunol , vol.142 , pp. 3937-3950
    • Parham, P.1    Lawlor, D.2    Lomen, C.3    Ennis, P.4
  • 41
    • 10744220328 scopus 로고    scopus 로고
    • Protection against mucosal Simian immunodeficiency virus SIVmac251 challenge by using replicating adenovirus-SIV multigene vaccine priming and subunit boosting
    • Patterson L.J., Malkevitch N., Venzon D., et al. Protection against mucosal Simian immunodeficiency virus SIVmac251 challenge by using replicating adenovirus-SIV multigene vaccine priming and subunit boosting. J Virol 2004, 78:2212-2221.
    • (2004) J Virol , vol.78 , pp. 2212-2221
    • Patterson, L.J.1    Malkevitch, N.2    Venzon, D.3
  • 42
    • 0141617555 scopus 로고    scopus 로고
    • Examining the independent binding assumption for binding of peptide epitopes to MHC-I molecules
    • Peters B., Tong W., Sidney J., Sette A., Weng Z. Examining the independent binding assumption for binding of peptide epitopes to MHC-I molecules. Bioinformatics 2003, 19:1765-1772.
    • (2003) Bioinformatics , vol.19 , pp. 1765-1772
    • Peters, B.1    Tong, W.2    Sidney, J.3    Sette, A.4    Weng, Z.5
  • 43
    • 0142180035 scopus 로고    scopus 로고
    • Virus evasion of MHC Class I molecule presentation
    • Petersen J.L., Morris C.R., Solheim J.C. Virus evasion of MHC Class I molecule presentation. J Immunol 2003, 171:4473-4478.
    • (2003) J Immunol , vol.171 , pp. 4473-4478
    • Petersen, J.L.1    Morris, C.R.2    Solheim, J.C.3
  • 44
    • 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., Deng Y., Bennink J., Germain R. Localization, quantitation, and in situ detection of specific peptide-MHC class I complexes using a monoclonal antibody. Immunity 1997, 6:715-726.
    • (1997) Immunity , vol.6 , pp. 715-726
    • Porgador, A.1    Yewdell, J.2    Deng, Y.3    Bennink, J.4    Germain, R.5
  • 45
    • 0029930418 scopus 로고    scopus 로고
    • The rat cim effect: TAP allele-dependent changes in a class I MHC anchor motif and evidence against C-terminal trimming of peptides in the ER
    • Powis S., Young L., Joly E., et al. The rat cim effect: TAP allele-dependent changes in a class I MHC anchor motif and evidence against C-terminal trimming of peptides in the ER. Immunity 1996, 4:159-165.
    • (1996) Immunity , vol.4 , pp. 159-165
    • Powis, S.1    Young, L.2    Joly, E.3
  • 46
    • 0032778516 scopus 로고    scopus 로고
    • Impaired immunoproteasome assembly and immune responses in PA28/ mice
    • Preckel T., Fung-Leung W.-P., Cai Z., et al. Impaired immunoproteasome assembly and immune responses in PA28/ mice. Science 1999, 286:2162-2165.
    • (1999) Science , vol.286 , pp. 2162-2165
    • Preckel, T.1    Fung-Leung, W.-P.2    Cai, Z.3
  • 47
    • 0037342270 scopus 로고    scopus 로고
    • Quantitating protein synthesis, degradation, and endogenous antigen processing
    • Princiotta M., Finzi D., et al. Quantitating protein synthesis, degradation, and endogenous antigen processing. Immunity 2003, 18:343-354.
    • (2003) Immunity , vol.18 , pp. 343-354
    • Princiotta, M.1    Finzi, D.2
  • 48
    • 0031954650 scopus 로고    scopus 로고
    • Peptide transport in human lymphoblastoid and tumor cells: effect of transporter associated with antigen presentation (TAP) polymorphism
    • Quadri S., Singal D. Peptide transport in human lymphoblastoid and tumor cells: effect of transporter associated with antigen presentation (TAP) polymorphism. Immunol Lett 1998, 61:25-31.
    • (1998) Immunol Lett , vol.61 , pp. 25-31
    • Quadri, S.1    Singal, D.2
  • 49
    • 2242469355 scopus 로고    scopus 로고
    • Identification of specific glycoforms of major histocompatibility complex class I heavy chains suggests that class I peptide loading is an adaptation of the quality control pathway involving calreticulin and ERp57
    • Radcliffe C.M., Diedrich G., Harvey D.J., Dwek R.A., Cresswell P., Rudd P.M. Identification of specific glycoforms of major histocompatibility complex class I heavy chains suggests that class I peptide loading is an adaptation of the quality control pathway involving calreticulin and ERp57. J Biol Chem 2002, 277:46415-46423.
    • (2002) J Biol Chem , vol.277 , pp. 46415-46423
    • Radcliffe, C.M.1    Diedrich, G.2    Harvey, D.J.3    Dwek, R.A.4    Cresswell, P.5    Rudd, P.M.6
  • 50
    • 0034643348 scopus 로고    scopus 로고
    • The major substrates for TAP in vivo are derived from newly synthesized proteins
    • Reits E., Vos J., Gromme M., Neefjes J. The major substrates for TAP in vivo are derived from newly synthesized proteins. Nature 2000, 404:774-778.
    • (2000) Nature , vol.404 , pp. 774-778
    • Reits, E.1    Vos, J.2    Gromme, M.3    Neefjes, J.4
  • 51
    • 0037767110 scopus 로고    scopus 로고
    • Attenuated Yersinia pseudotuberculosis carrier vaccine for simultaneous antigen-specific CD4 and CD8 T-cell induction
    • Russmann H., Gerdemann U., Igwe E.I., et al. Attenuated Yersinia pseudotuberculosis carrier vaccine for simultaneous antigen-specific CD4 and CD8 T-cell induction. Infect Immun 2003, 71:3463-3472.
    • (2003) Infect Immun , vol.71 , pp. 3463-3472
    • Russmann, H.1    Gerdemann, U.2    Igwe, E.I.3
  • 52
    • 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., Ortmann B., Spies T., Cresswell P. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 1996, 5:103-114.
    • (1996) Immunity , vol.5 , pp. 103-114
    • Sadasivan, B.1    Lehner, P.2    Ortmann, B.3    Spies, T.4    Cresswell, P.5
  • 53
    • 0022718930 scopus 로고
    • Impaired assembly and transport of HLA-A and -B antigens in a mutant TxB cell hybrid
    • Salter R., Cresswell P. Impaired assembly and transport of HLA-A and -B antigens in a mutant TxB cell hybrid. EMBO J 1986, 5:934-939.
    • (1986) EMBO J , vol.5 , pp. 934-939
    • Salter, R.1    Cresswell, P.2
  • 54
    • 0038350948 scopus 로고    scopus 로고
    • Predicting proteasomal cleavage sites: a comparison of available methods
    • Saxova P., Buus S., Brunak S., Kesmir C. Predicting proteasomal cleavage sites: a comparison of available methods. Int Immunol 2003, 15:781-787.
    • (2003) Int Immunol , vol.15 , pp. 781-787
    • Saxova, P.1    Buus, S.2    Brunak, S.3    Kesmir, C.4
  • 55
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • Schubert U., Anton L., Gibbs J., Norbury C., Yewdell J., Bennink J. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 2000, 404:770-774.
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1    Anton, L.2    Gibbs, J.3    Norbury, C.4    Yewdell, J.5    Bennink, J.6
  • 56
    • 0028670488 scopus 로고
    • Transporters from H-2b, H-2d, H-2s, H-2k, and H-2g7 (NOD/Lt) haplotype translocate similar sets of peptides
    • Schumacher T., Kantesaria D., Serreze D., Roopenian D., Ploegh H. Transporters from H-2b, H-2d, H-2s, H-2k, and H-2g7 (NOD/Lt) haplotype translocate similar sets of peptides. Proc Natl Acad Sci USA 1994, 91:13004-13008.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 13004-13008
    • Schumacher, T.1    Kantesaria, D.2    Serreze, D.3    Roopenian, D.4    Ploegh, H.5
  • 57
    • 0037015624 scopus 로고    scopus 로고
    • ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum
    • Serwold T., Gonzalez F., Kim J., Jacob R., Shastri N. ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum. Nature 2002, 419:480-483.
    • (2002) Nature , vol.419 , pp. 480-483
    • Serwold, T.1    Gonzalez, F.2    Kim, J.3    Jacob, R.4    Shastri, N.5
  • 58
    • 0033616715 scopus 로고    scopus 로고
    • Crystal structure of the HLA-Cw3 allotype-specific killer cell inhibitory receptor KIR2DL2
    • Snyder GA., Brooks A.G., Sun P.D. Crystal structure of the HLA-Cw3 allotype-specific killer cell inhibitory receptor KIR2DL2. PNAS 1999, 96:3864-3869.
    • (1999) PNAS , vol.96 , pp. 3864-3869
    • Snyder, G.A.1    Brooks, A.G.2    Sun, P.D.3
  • 59
    • 0034090632 scopus 로고    scopus 로고
    • Recognition of misfolding proteins by PA700, the regulatory subcomplex of the 26 S proteasome
    • Strickland E., Hakala K., Thomas P.J., DeMartino GN Recognition of misfolding proteins by PA700, the regulatory subcomplex of the 26 S proteasome. J Biol Chem 2000, 275:5565-5572.
    • (2000) J Biol Chem , vol.275 , pp. 5565-5572
    • Strickland, E.1    Hakala, K.2    Thomas, P.J.3    DeMartino, G.N.4
  • 60
    • 0023372207 scopus 로고
    • Interferons increase transcription of a major histocompatibility class I gene via a 5' interferon consensus sequence
    • Sugita K., Miyazaki J., Appella E., Ozato K. Interferons increase transcription of a major histocompatibility class I gene via a 5' interferon consensus sequence. Mol Cell Biol 1987, 7:2625-2630.
    • (1987) Mol Cell Biol , vol.7 , pp. 2625-2630
    • Sugita, K.1    Miyazaki, J.2    Appella, E.3    Ozato, K.4
  • 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 {alpha}3 Domain
    • Suh W.K., Derby M.A., Cohen-Doyle M.F., et al. Interaction of murine MHC class I molecules with tapasin and TAP enhances peptide loading and involves the heavy chain {alpha}3 Domain. J Immunol 1999, 162:1530-1540.
    • (1999) J Immunol , vol.162 , pp. 1530-1540
    • Suh, W.K.1    Derby, M.A.2    Cohen-Doyle, M.F.3
  • 62
    • 0029100978 scopus 로고
    • Calnexin influences folding of human class I histocompatibility proteins but not their assembly with beta(2)-microglobulin
    • Tector M., Salter R.D. Calnexin influences folding of human class I histocompatibility proteins but not their assembly with beta(2)-microglobulin. J Biol Chem 1995, 270:19638-19642.
    • (1995) J Biol Chem , vol.270 , pp. 19638-19642
    • Tector, M.1    Salter, R.D.2
  • 63
    • 0025166228 scopus 로고
    • Isolation of an endogenously processed immunodominant viral peptide from the class I H-2Kb molecule
    • Van Bleek G., Nathenson S. Isolation of an endogenously processed immunodominant viral peptide from the class I H-2Kb molecule. Nature 1990, 348:213-216.
    • (1990) Nature , vol.348 , pp. 213-216
    • Van Bleek, G.1    Nathenson, S.2
  • 64
    • 10744232251 scopus 로고    scopus 로고
    • Modification to the capsid of the adenovirus vector that enhances dendritic cell infection and transgene-specific cellular immune responses
    • Worgall S., Busch A., Rivara M., et al. Modification to the capsid of the adenovirus vector that enhances dendritic cell infection and transgene-specific cellular immune responses. J Virol 2004, 78:2572-2580.
    • (2004) J Virol , vol.78 , pp. 2572-2580
    • Worgall, S.1    Busch, A.2    Rivara, M.3
  • 65
    • 0036884090 scopus 로고    scopus 로고
    • The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues
    • York I., Chang S., Saric T., et al. The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues. Nat Immunol 2002, 3:1177-1184.
    • (2002) Nat Immunol , vol.3 , pp. 1177-1184
    • York, I.1    Chang, S.2    Saric, T.3
  • 66
    • 10744222173 scopus 로고    scopus 로고
    • Tapasin is a facilitator, not an editor, of class I MHC peptide binding
    • Zarling A.L., Luckey C.J., Marto J.A., et al. Tapasin is a facilitator, not an editor, of class I MHC peptide binding. J Immunol 2003, 171:5287-5295.
    • (2003) J Immunol , vol.171 , pp. 5287-5295
    • Zarling, A.L.1    Luckey, C.J.2    Marto, J.A.3
  • 67
    • 0028906481 scopus 로고
    • Calnexin recognizes carbohydrate and protein determinants of class I major histocompatibility complex molecules
    • Zhang Q., Tector M., Salter R.D. Calnexin recognizes carbohydrate and protein determinants of class I major histocompatibility complex molecules. J Biol Chem 1995, 270:3944-3948.
    • (1995) J Biol Chem , vol.270 , pp. 3944-3948
    • Zhang, Q.1    Tector, M.2    Salter, R.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.