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Volumn 288, Issue 44, 2013, Pages 31784-31794

The same major histocompatibility complex polymorphism involved in control of HIV influences peptide binding in the mouse H-2Ld system

Author keywords

[No Author keywords available]

Indexed keywords

ALLELIC VARIANTS; CELL ACTIVITY; DISEASE PROGRESSION; ENHANCED STABILITY; GAIN INSIGHT; HIGH AFFINITY; MAJOR HISTOCOMPATIBILITY COMPLEX; PEPTIDE BINDING;

EID: 84887050727     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.478412     Document Type: Article
Times cited : (4)

References (65)
  • 3
    • 14944346245 scopus 로고    scopus 로고
    • How T cells "see" antigen
    • Krogsgaard, M., and Davis, M. M. (2005) How T cells "see" antigen. Nat. Immunol. 6, 239-245
    • (2005) Nat. Immunol. , vol.6 , pp. 239-245
    • Krogsgaard, M.1    Davis, M.M.2
  • 4
    • 0023720148 scopus 로고
    • T-cell antigen receptor genes and T-cell recognition
    • Davis, M. M., and Bjorkman, P. J. (1988) T-cell antigen receptor genes and T-cell recognition. Nature 334, 395-402
    • (1988) Nature , vol.334 , pp. 395-402
    • Davis, M.M.1    Bjorkman, P.J.2
  • 5
    • 0030176270 scopus 로고    scopus 로고
    • Evidence that a single peptide-MHC complex on a target cell can elicit a cytolytic T cell response
    • DOI 10.1016/S1074-7613(00)80483-5
    • Sykulev, Y., Joo, M., Vturina, I., Tsomides, T. J., and Eisen, H. N. (1996) Evidence that a single peptide-MHC complex on a target cell can elicit a cytolytic T cell response. Immunity 4, 565-571 (Pubitemid 26233310)
    • (1996) Immunity , vol.4 , Issue.6 , pp. 565-571
    • Sykulev, Y.1    Joo, M.2    Vturina, I.3    Tsomides, T.J.4    Eisen, H.N.5
  • 9
    • 78650084232 scopus 로고    scopus 로고
    • The major genetic determinants of HIV-1 control affect HLA class I peptide presentation
    • International HIV Controllers Study
    • International HIV Controllers Study, Pereyra, F., Jia, X., McLaren, P. J., Telenti, A., de Bakker, P. I., Walker, B. D., Ripke, S., Brumme, C. J., Pulit, S. L., Carrington, M., Kadie, C.M., Carlson, J.M., Heckerman, D., Graham, R. R., Plenge, R. M., Deeks, S. G., Gianniny, L., Crawford, G., Sullivan, J., Gonzalez, E., Davies, L., Camargo, A., Moore, J. M., Beattie, N., Gupta, S., Crenshaw, A., Burtt, N. P., Guiducci, C., Gupta, N., Gao, X., Qi, Y., Yuki, Y., Piechocka-Trocha, A., Cutrell, E., Rosenberg, R., Moss, K. L., Lemay, P., O'Leary, J., Schaefer, T., Verma, P., Toth, I., Block, B., Baker, B., Rothchild, A., Lian, J., Proudfoot, J., Alvino, D. M., Vine, S., Addo, M. M., Allen, T. M., Altfeld, M., Henn, M. R., Le Gall, S., Streeck, H., Haas, D. W., Kuritzkes, D. R., Robbins, G. K., Shafer, R. W., Gulick, R. M., Shikuma, C. M., Haubrich, R., Riddler, S., Sax, P. E., Daar, E. S., Ribaudo, H. J., Agan, B., Agarwal, S., Ahern, R. L., Allen, B. L., Altidor, S., Altschuler, E. L., Ambardar, S., Anastos, K., Anderson, B., Anderson, V., Andrady, U., Antoniskis, D., Bangsberg, D., Barbaro, D., Barrie, W., Bartczak, J., Barton, S., Basden, P., Basgoz, N., Bazner, S., Bellos, N. C., Benson, A. M., Berger, J., Bernard, N. F., Bernard, A.M., Birch, C., Bodner, S.J., Bolan, R. K., Boudreaux, E. T., Bradley, M., Braun, J. F., Brndjar, J. E., Brown, S. J., Brown, K., Brown, S. T., Burack, J., Bush, L. M., Cafaro, V., Campbell, O., Campbell, J., Carlson, R. H., Carmichael, J. K., Casey, K.K., Cavacuiti, C., Celestin, G., Chambers, S. T., Chez, N., Chirch, L. M., Cimoch, P. J., Cohen, D., Cohn, L. E., Conway, B., Cooper, D. A., Cornelson, B., Cox, D. T., Cristofano, M. V., Cuchural, G., Jr., Czartoski, J. L., Dahman, J. M., Daly, J. S., Davis, B. T., Davis, K., Davod, S.M., DeJesus, E., Dietz, C.A., Dunham, E., Dunn, M.E., Ellerin, T. B., Eron, J. J., Fangman, J. J., Farel, C. E., Ferlazzo, H., Fidler, S., Fleenor-Ford, A., Frankel, R., Freedberg, K. A., French, N. K., Fuchs, J. D., Fuller, J. D., Gaberman, J., Gallant, J. E., Gandhi, R. T., Garcia, E., Garmon, D., Gathe, J. C., Jr., Gaultier, C. R., Gebre, W., Gilman, F. D., Gilson, I., Goepfert, P. A., Gottlieb, M.S., Goulston, C., Groger, R.K., Gurley, T. D., Haber, S., Hardwicke, R., Hardy, W. D., Harrigan, P. R., Hawkins, T. N., Heath, S., Hecht, F. M., Henry, W. K., Hladek, M., Hoffman, R.P., Horton, J. M., Hsu, R. K., Huhn, G. D., Hunt, P., Hupert, M. J., Illeman, M. L., Jaeger, H., Jellinger, R. M., John, M., Johnson, J. A., Johnson, K. L., Johnson, H., Johnson, K., Joly, J., Jordan, W. C., Kauffman, C. A., Khanlou, H., Killian, R. K., Kim, A. Y., Kim, D. D., Kinder, C. A., Kirchner, J. T., Kogelman, L., Kojic, E. M., Korthuis, P. T., Kurisu, W., Kwon, D. S., LaMar, M., Lampiris, H., Lanzafame, M., Lederman, M. M., Lee, D. M., Lee, J. M., Lee, M. J., Lee, E. T., Lemoine, J., Levy, J. A., Llibre, J. M., Liguori, M. A., Little, S. J., Liu, A. Y., Lopez, A. J., Loutfy, M. R., Loy, D., Mohammed, D. Y., Man, A., Mansour, M. K., Marconi, V.C., Markowitz, M., Marques, R., Martin, J. N., Martin, H. L., Jr., Mayer, K.H., McElrath, M.J., McGhee, T.A., McGovern, B. H., McGowan, K., McIntyre, D., McLeod, G. X., Menezes, P., Mesa, G., Metroka, C. E., Meyer-Olson, D., Miller, A. O., Montgomery, K., Mounzer, K. C., Nagami, E. H., Nagin, I., Nahass, R. G., Nelson, M. O., Nielsen, C., Norene, D. L., O'Connor, D. H., Ojikutu, B. O., Okulicz, J., Oladehin, O. O., Oldfield, E. C., 3rd, Olender, S. A., Ostrowski, M., Owen, W. F., Jr., Pae, E., Parsonnet, J., Pavlatos, A. M., Perlmutter, A. M., Pierce, M. N., Pincus, J. M., Pisani, L., Price, L. J., Proia, L., Prokesch, R. C., Pujet, H. C., Ramgopal, M., Rathod, A., Rausch, M., Ravishankar, J., Rhame, F. S., Richards, C. S., Richman, D. D., Rodes, B., Rodriguez, M., Rose, R. C., 3rd, Rosenberg, E. S., Rosenthal, D., Ross, P. E., Rubin, D. S., Rumbaugh, E., Saenz, L., Salvaggio, M. R., Sanchez, W. C., Sanjana, V. M., Santiago, S., Schmidt, W., Schuitemaker, H., Sestak, P. M., Shalit, P., Shay, W., Shirvani, V. N., Silebi, V. I., Sizemore, J. M., Jr., Skolnik, P. R., Sokol-Anderson, M., Sosman, J. M., Stabile, P., Stapleton, J. T., Starrett, S., Stein, F., Stellbrink, H. J., Sterman, F. L., Stone, V. E., Stone, D. R., Tambussi, G., Taplitz, R. A., Tedaldi, E. M., Telenti, A., Theisen, W., Torres, R., Tosiello, L., Tremblay, C., Tribble, M. A., Trinh, P. D., Tsao, A., Ueda, P., Vaccaro, A., Valadas, E., Vanig, T. J., Vecino, I., Vega, V. M., Veikley, W., Wade, B. H., Walworth, C., Wanidworanun, C., Ward, D. J., Warner, D. A., Weber, R. D., Webster, D., Weis, S., Wheeler, D. A., White, D. J., Wilkins, E., Winston, A., Wlodaver, C. G., van't Wout, A., Wright, D. P., Yang, O. O., Yurdin, D. L., Zabukovic, B. W., Zachary, K. C., Zeeman, B., and Zhao, M. (2010) The major genetic determinants of HIV-1 control affect HLA class I peptide presentation. Science 330, 1551-1557
    • (2010) Science , vol.330 , pp. 1551-1557
    • Pereyra, F.1    Jia, X.2    McLaren, P.J.3    Telenti, A.4    De Bakker, P.I.5    Walker, B.D.6    Ripke, S.7    Brumme, C.J.8    Pulit, S.L.9    Carrington, M.10    Kadie, C.M.11    Carlson, J.M.12    Heckerman, D.13    Graham, R.R.14    Plenge, R.M.15    Deeks, S.G.16    Gianniny, L.17    Crawford, G.18    Sullivan, J.19    Gonzalez, E.20    more..
  • 11
    • 33846988640 scopus 로고    scopus 로고
    • In the absence of aminopeptidase ERAAP, MHC class I molecules present many unstable and highly immunogenic peptides
    • DOI 10.1038/ni1409, PII NI1409
    • Hammer, G. E., Gonzalez, F., James, E., Nolla, H., and Shastri, N. (2007) In the absence of aminopeptidase ERAAP, MHC class I molecules present many unstable and highly immunogenic peptides. Nat. Immunol. 8, 101-108 (Pubitemid 46242364)
    • (2007) Nature Immunology , vol.8 , Issue.1 , pp. 101-108
    • Hammer, G.E.1    Gonzalez, F.2    James, E.3    Nolla, H.4    Shastri, N.5
  • 12
    • 29244461714 scopus 로고    scopus 로고
    • The aminopeptidase ERAAP shapes the peptide repertoire displayed by major histocompatibility complex class I molecules
    • DOI 10.1038/ni1286, PII N1286
    • Hammer, G. E., Gonzalez, F., Champsaur, M., Cado, D., and Shastri, N. (2006) The aminopeptidase ERAAP shapes the peptide repertoire displayed by major histocompatibility complex class I molecules. Nat Immunol. 7, 103-112 (Pubitemid 41823874)
    • (2006) Nature Immunology , vol.7 , Issue.1 , pp. 103-112
    • Hammer, G.E.1    Gonzalez, F.2    Champsaur, M.3    Cado, D.4    Shastri, N.5
  • 13
    • 84855957129 scopus 로고    scopus 로고
    • How the TCR balances sensitivity and specificity for the recognition of self and pathogens
    • Morris, G. P., and Allen, P. M. (2012) How the TCR balances sensitivity and specificity for the recognition of self and pathogens. Nat. Immunol. 13, 121-128
    • (2012) Nat. Immunol. , vol.13 , pp. 121-128
    • Morris, G.P.1    Allen, P.M.2
  • 16
    • 0032540502 scopus 로고    scopus 로고
    • Proteases, processing, and thymic selection (see comments)
    • Cresswell, P. (1998) Proteases, processing, and thymic selection (see comments). Science 280, 394-395
    • (1998) Science , vol.280 , pp. 394-395
    • Cresswell, P.1
  • 18
    • 0037083299 scopus 로고    scopus 로고
    • Recruitment of MHC class I molecules by tapasin into the transporter associated with antigen processing-associated complex is essential for optimal peptide loading
    • Tan, P., Kropshofer, H., Mandelboim, O., Bulbuc, N., Hämmerling, G. J., and Momburg, F. (2002) Recruitment of MHC class I molecules by tapasin into the transporter associated with antigen processing-associated complex is essential for optimal peptide loading. J. Immunol. 168, 1950-1960 (Pubitemid 34135798)
    • (2002) Journal of Immunology , vol.168 , Issue.4 , pp. 1950-1960
    • Tan, P.1    Kropshofer, H.2    Mandelboim, O.3    Bulbuc, N.4    Hammerling, G.J.5    Momburg, F.6
  • 19
    • 0028024224 scopus 로고
    • Comparison of cell lines deficient in antigen presentation reveals a functional role for TAP-1 alone in antigen processing
    • Gabathuler, R., Reid, G., Kolaitis, G., Driscoll, J., and Jefferies, W. A. (1994) Comparison of cell lines deficient in antigen presentation reveals a functional role for TAP-1 alone in antigen processing. J. Exp. Med. 180, 1415-1425 (Pubitemid 24289615)
    • (1994) Journal of Experimental Medicine , vol.180 , Issue.4 , pp. 1415-1425
    • Gabathuler, R.1    Reid, G.2    Kolaitis, G.3    Driscoll, J.4    Jefferies, W.A.5
  • 21
    • 74049160009 scopus 로고    scopus 로고
    • Mechanisms maintaining peripheral tolerance
    • Mueller, D. L. (2010) Mechanisms maintaining peripheral tolerance. Nat. Immunol. 11, 21-27
    • (2010) Nat. Immunol. , vol.11 , pp. 21-27
    • Mueller, D.L.1
  • 24
    • 84866490075 scopus 로고    scopus 로고
    • HIV and HLA class I. An evolving relationship
    • Goulder, P. J., and Walker, B. D. (2012) HIV and HLA class I. An evolving relationship. Immunity 37, 426-440
    • (2012) Immunity , vol.37 , pp. 426-440
    • Goulder, P.J.1    Walker, B.D.2
  • 25
    • 0016345568 scopus 로고
    • Restriction of in vitro T cell-mediated cytotoxicity in lymphocytic choriomeningitis within a syngeneic or semiallogeneic system
    • Zinkernagel, R. M., and Doherty, P. C. (1974) Restriction of in vitro T cell-mediated cytotoxicity in lymphocytic choriomeningitis within a syngeneic or semiallogeneic system. Nature 248, 701-702
    • (1974) Nature , vol.248 , pp. 701-702
    • Zinkernagel, R.M.1    Doherty, P.C.2
  • 26
    • 0025970895 scopus 로고
    • The specific binding of peptide ligand to ld class I major histocompatibility complex molecules determines their antigenic structure
    • Lie, W. R., and Myers., N. B., Connolly, J. M., Gorka, J., Lee, D. R., and Hansen, T. H. (1991) The specific binding of peptide ligand to Ld class I major histocompatibility complex molecules determines their antigenic structure. J. Exp. Med. 173, 449-459
    • (1991) J. Exp. Med. , vol.173 , pp. 449-459
    • Lie, W.R.1    Myers, N.B.2    Connolly, J.M.3    Gorka, J.4    Lee, D.R.5    Hansen, T.H.6
  • 28
  • 29
    • 0031674527 scopus 로고    scopus 로고
    • 2- microglobulin: Interactions with murine MHC I molecules
    • DOI 10.1016/S0161-5890(98)00083-2, PII S0161589098000832
    • Shields, M. J., and Moffat., L. E., and Ribaudo, R. K. (1998) Functional comparison of bovine, murine, and human β2-microglobulin. Interactions with murine MHC I molecules. Mol. Immunol. 35, 919-928 (Pubitemid 28563358)
    • (1998) Molecular Immunology , vol.35 , Issue.14-15 , pp. 919-928
    • Shields, M.J.1    Moffat, L.E.2    Ribaudo, R.K.3
  • 30
    • 0019408126 scopus 로고
    • Flow microfluorometric analysis of H-2L expression
    • Potter, T. A., Hansen, T. H, Habbersett, R., Ozato, K., and Ahmed, A. (1981) Flow microfluorometric analysis of H-2L expression. J. Immunol. 127, 580-584 (Pubitemid 11054669)
    • (1981) Journal of Immunology , vol.127 , Issue.2 , pp. 580-584
    • Potter, T.A.1    Hansen, T.H.2    Habbersett, R.3
  • 31
    • 70450240779 scopus 로고    scopus 로고
    • d to generate T cell specificity directed against their respective bound peptides
    • d to generate T cell specificity directed against their respective bound peptides. J. Biol. Chem. 284, 32551-32561
    • (2009) J. Biol. Chem. , vol.284 , pp. 32551-32561
    • Bowerman, N.A.1    Colf, L.A.2    Garcia, K.C.3    Kranz, D.M.4
  • 32
    • 0037105397 scopus 로고    scopus 로고
    • 2- microglobulin
    • Smith, R. A., and Myers., N. B., Robinson, M., Hansen, T. H., and Lee, D. R. (2002) Polymorphism at position 97 in MHC class I molecules affects peptide specificity, cell surface stability, and affinity for β2-microglobulin. J. Immunol. 169, 3105-3111 (Pubitemid 35013155)
    • (2002) Journal of Immunology , vol.169 , Issue.6 , pp. 3105-3111
    • Smith, R.A.1    Myers, N.B.2    Robinson, M.3    Hansen, T.H.4    Lee, D.R.5
  • 36
    • 33947726614 scopus 로고    scopus 로고
    • How a Single T Cell Receptor Recognizes Both Self and Foreign MHC
    • DOI 10.1016/j.cell.2007.01.048, PII S0092867407003133
    • Colf, L. A., and Bankovich., A. J., Hanick, N. A., Bowerman, N. A., and Jones., L. L., Kranz, D. M., and Garcia, K. C. (2007) How a single T cell receptor recognizes both self and foreign MHC. Cell 129, 135-146 (Pubitemid 46507586)
    • (2007) Cell , vol.129 , Issue.1 , pp. 135-146
    • Colf, L.A.1    Bankovich, A.J.2    Hanick, N.A.3    Bowerman, N.A.4    Jones, L.L.5    Kranz, DavidM.6    Garcia, K.C.7
  • 37
    • 56749095210 scopus 로고    scopus 로고
    • Different thermodynamic binding mechanisms and peptide fine specificities associated with a panel of structurally similar high-affinity T cell receptors
    • Jones, L. L., and Colf., L. A., Bankovich, A. J., Stone, J. D., and Gao., Y. G., Chan, C. M., Huang, R. H., Garcia, K. C, and Kranz, D. M. (2008) Different thermodynamic binding mechanisms and peptide fine specificities associated with a panel of structurally similar high-affinity T cell receptors. Biochemistry 47, 12398-12408
    • (2008) Biochemistry , vol.47 , pp. 12398-12408
    • Jones, L.L.1    Colf, L.A.2    Bankovich, A.J.3    Stone, J.D.4    Gao, Y.G.5    Chan, C.M.6    Huang, R.H.7    Garcia, K.C.8    Kranz, D.M.9
  • 39
    • 0025343473 scopus 로고
    • Peptide ligand-induced conformation and surface expression of the ld class I MHC molecule
    • Lie, W. R., and Myers., N. B., Gorka, J., Rubocki, R. J., and Connolly., J. M., and Hansen, T. H. (1990) Peptide ligand-induced conformation and surface expression of the Ld class I MHC molecule. Nature 344, 439-441
    • (1990) Nature , vol.344 , pp. 439-441
    • Lie, W.R.1    Myers, N.B.2    Gorka, J.3    Rubocki, R.J.4    Connolly, J.M.5    Hansen, T.H.6
  • 40
    • 0037331525 scopus 로고    scopus 로고
    • Quantitative analysis of the contribution of TCR/pepMHC affinity and CD8 to T cell activation
    • DOI 10.1016/S1074-7613(03)00019-0
    • Holler, P. D., and Kranz, D. M. (2003) Quantitative analysis of the contribution of TCR/pep-MHC affinity and CD8 to T cell activation. Immunity 18, 255-264 (Pubitemid 36263000)
    • (2003) Immunity , vol.18 , Issue.2 , pp. 255-264
    • Holler, P.D.1    Kranz, D.M.2
  • 41
    • 68749096889 scopus 로고    scopus 로고
    • Engineering the binding properties of the T cell receptor: Peptide: MHC ternary complex that governs T cell activity
    • Bowerman, N. A., and Crofts., T. S., Chlewicki, L., Do, P., Baker, B. M., Christopher Garcia, K., and Kranz, D. M. (2009) Engineering the binding properties of the T cell receptor: peptide: MHC ternary complex that governs T cell activity. Mol. Immunol. 46, 3000-3008
    • (2009) Mol. Immunol. , vol.46 , pp. 3000-3008
    • Bowerman, N.A.1    Crofts, T.S.2    Chlewicki, L.3    Do, P.4    Baker, B.M.5    Christopher Garcia, K.6    Kranz, D.M.7
  • 42
    • 0037407551 scopus 로고    scopus 로고
    • Homology between an alloantigen and a self MHC allele calibrates the avidity of the alloreactive T cell repertoire independent of TCR affinity
    • Hornell, T. M., Myers, N, Hansen, T. H, and Connolly, J. M. (2003) Homology between an alloantigen and a self-MHC allele calibrates the avidity of the alloreactive T cell repertoire independent of TCR affinity. J. Immunol. 170, 4506-4514 (Pubitemid 36519955)
    • (2003) Journal of Immunology , vol.170 , Issue.9 , pp. 4506-4514
    • Hornell, T.M.C.1    Myers, N.2    Hansen, T.H.3    Connolly, J.M.4
  • 46
    • 0025113525 scopus 로고
    • Peptide feeding and cellular cookery
    • DOI 10.1038/346793a0
    • Parham, P. (1990) Antigen presentation. Peptide feeding and cellular cookery. Nature 346, 793-795 (Pubitemid 20272095)
    • (1990) Nature , vol.346 , Issue.6287 , pp. 793-795
    • Parham, P.1
  • 51
    • 78650165514 scopus 로고    scopus 로고
    • Genetics. First-class control of HIV-1
    • McMichael, A. J., and Jones, E. Y. (2010) Genetics. First-class control of HIV-1. Science 330, 1488-1490
    • (2010) Science , vol.330 , pp. 1488-1490
    • McMichael, A.J.1    Jones, E.Y.2
  • 55
    • 79955549816 scopus 로고    scopus 로고
    • Opposite effects of endogenous peptide-MHC class I on T cell activity in the presence and absence of CD8
    • Stone, J. D., Aggen, D. H, Chervin, A. S., Narayanan, S., and Schmitt., T. M., Greenberg, P.D., and Kranz, D.M. (2011) Opposite effects of endogenous peptide-MHC class I on T cell activity in the presence and absence of CD8. J. Immunol. 186, 5193-5200
    • (2011) J. Immunol. , vol.186 , pp. 5193-5200
    • Stone, J.D.1    Aggen, D.H.2    Chervin, A.S.3    Narayanan, S.4    Schmitt, T.M.5    Greenberg, P.D.6    Kranz, D.M.7
  • 56
    • 79954533158 scopus 로고    scopus 로고
    • Shifting the equilibrium in cancer immunoediting: From tumor tolerance to eradication
    • Quezada, S.A., Peggs, K. S., and Simpson., T. R., and Allison, J. P. (2011) Shifting the equilibrium in cancer immunoediting: from tumor tolerance to eradication. Immunol. Rev. 241, 104-118
    • (2011) Immunol. Rev. , vol.241 , pp. 104-118
    • Quezada, S.A.1    Peggs, K.S.2    Simpson, T.R.3    Allison, J.P.4
  • 57
    • 84866107338 scopus 로고    scopus 로고
    • Dynamics of major histocompatibility complex class I association with the human peptide-loading complex
    • Panter, M. S., Jain, A., Leonhardt, R. M., Ha, T., and Cresswell, P. (2012) Dynamics of major histocompatibility complex class I association with the human peptide-loading complex. J. Biol. Chem. 287, 31172-31184
    • (2012) J. Biol. Chem. , vol.287 , pp. 31172-31184
    • Panter, M.S.1    Jain, A.2    Leonhardt, R.M.3    Ha, T.4    Cresswell, P.5
  • 58
    • 58149215628 scopus 로고    scopus 로고
    • Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer
    • Dong, G., and Wearsch., P. A., Peaper, D. R., Cresswell, P., and Reinisch, K. M. (2009) Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer. Immunity 30, 21-32
    • (2009) Immunity , vol.30 , pp. 21-32
    • Dong, G.1    Wearsch, P.A.2    Peaper, D.R.3    Cresswell, P.4    Reinisch, K.M.5
  • 59
    • 82455192402 scopus 로고    scopus 로고
    • DRiPs solidify. Progress in understanding endogenous MHC class I antigen processing
    • Yewdell, J. W. (2011) DRiPs solidify. Progress in understanding endogenous MHC class I antigen processing. Trends Immunol. 32, 548-558
    • (2011) Trends Immunol. , vol.32 , pp. 548-558
    • Yewdell, J.W.1
  • 63
    • 0024537272 scopus 로고
    • A pentapeptide as minimal antigenic determinant for MHC class I-restricted T lymphocytes
    • DOI 10.1038/337651a0
    • Reddehase, M. J., and Rothbard., J. B., and Koszinowski, U. H. (1989) A penta-peptide as minimal antigenic determinant for MHC class I-restricted T lymphocytes. Nature 337, 651-653 (Pubitemid 19054293)
    • (1989) Nature , vol.337 , Issue.6208 , pp. 651-653
    • Reddehase, M.J.1    Rothbard, J.B.2    Koszinowski, U.H.3
  • 65
    • 0029993109 scopus 로고    scopus 로고
    • d ligands lacking the consensus P2 anchor
    • d ligands lacking the consensus P2 anchor. J. Immunol. 156, 4266-4273
    • (1996) J. Immunol. , vol.156 , pp. 4266-4273
    • Robinson, R.A.1    Lee, D.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.