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Volumn 62, Issue 5, 2001, Pages 539-556

Towards the MHC-peptide combinatorics

Author keywords

Binding pattern; Binding value; MHC peptide interface; Residue preference

Indexed keywords

HLA ANTIGEN CLASS 1; HLA ANTIGEN CLASS 2; MAJOR HISTOCOMPATIBILITY ANTIGEN;

EID: 0035020158     PISSN: 01988859     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0198-8859(01)00219-1     Document Type: Article
Times cited : (16)

References (74)
  • 2
    • 0034614546 scopus 로고    scopus 로고
    • Immunology: Improving on nature in the twenty first century
    • Abbas A.K., Janeway C.A. Immunology improving on nature in the twenty first century . Cell. 100:2000;129.
    • (2000) Cell , vol.100 , pp. 129
    • Abbas, A.K.1    Janeway, C.A.2
  • 3
    • 0033980075 scopus 로고    scopus 로고
    • Rational antigen modification as a strategy to upregulate or downregulate antigen recognition
    • Abrams S.I., Schlom J. Rational antigen modification as a strategy to upregulate or downregulate antigen recognition. Curr Opin Immunol. 12:2000;85.
    • (2000) Curr Opin Immunol , vol.12 , pp. 85
    • Abrams, S.I.1    Schlom, J.2
  • 4
    • 0031895637 scopus 로고    scopus 로고
    • Mechanisms of MHC class I restricted antigen processing: Annu
    • Pamer E., Cresswell P. Mechanisms of MHC class I restricted antigen processing Annu . Rev. Immunol. 16:1998;323.
    • (1998) Rev. Immunol , vol.16 , pp. 323
    • Pamer, E.1    Cresswell, P.2
  • 5
    • 0030821945 scopus 로고    scopus 로고
    • Peptide binding and antigen presentation by class II histocompatibility glycoproteins
    • Jensen P.E. Peptide binding and antigen presentation by class II histocompatibility glycoproteins. Biopolymers. 43:1997;303.
    • (1997) Biopolymers , vol.43 , pp. 303
    • Jensen, P.E.1
  • 6
    • 0034603779 scopus 로고    scopus 로고
    • A three step kinetic mechanism for peptide binding to MHC class II proteins
    • Joshi R.V., Zarutslie J.A., Stern L.J. A three step kinetic mechanism for peptide binding to MHC class II proteins. Biochemistry. 39:2000;3751.
    • (2000) Biochemistry , vol.39 , pp. 3751
    • Joshi, R.V.1    Zarutslie, J.A.2    Stern, L.J.3
  • 8
    • 0033120523 scopus 로고    scopus 로고
    • Stable peptide binding to MHC class II molecule is rapid and is determined by a receptive conformation shaped by prior association with low affinity peptides
    • Natarajan S.K., Assadi M., Nasseri S.S. Stable peptide binding to MHC class II molecule is rapid and is determined by a receptive conformation shaped by prior association with low affinity peptides. J Immunol. 162:1999;4030.
    • (1999) J Immunol , vol.162 , pp. 4030
    • Natarajan, S.K.1    Assadi, M.2    Nasseri, S.S.3
  • 9
    • 0345516047 scopus 로고    scopus 로고
    • Fast association rates suggest a conformational change in the MHC class I molecule H-2Db upon peptide binding
    • Springer S., Doring K., Skipper J.C., Townsend A.R., Cerundolo V. Fast association rates suggest a conformational change in the MHC class I molecule H-2Db upon peptide binding. Biochemistry. 37:1998;3001.
    • (1998) Biochemistry , vol.37 , pp. 3001
    • Springer, S.1    Doring, K.2    Skipper, J.C.3    Townsend, A.R.4    Cerundolo, V.5
  • 10
    • 0030760565 scopus 로고    scopus 로고
    • Peptide binding by class I and class II MHC molecules
    • Batalia M.A., Collins E.J. Peptide binding by class I and class II MHC molecules. Biopolymers. 43:1997;281.
    • (1997) Biopolymers , vol.43 , pp. 281
    • Batalia, M.A.1    Collins, E.J.2
  • 12
    • 0343205907 scopus 로고    scopus 로고
    • http://www.anthonynolan.org.uk.
  • 13
    • 0342771225 scopus 로고    scopus 로고
    • http://www.ebi.ac.uk/imgt/hla.
  • 14
    • 0032483463 scopus 로고    scopus 로고
    • Structural principles that govern the peptide binding motifs of class I MHC molecules
    • Zhang C., Anderson A., DeLisi C. Structural principles that govern the peptide binding motifs of class I MHC molecules. J Mol Biol. 281:1998;929.
    • (1998) J Mol Biol , vol.281 , pp. 929
    • Zhang, C.1    Anderson, A.2    Delisi, C.3
  • 15
    • 0033118895 scopus 로고    scopus 로고
    • Description and prediction of peptide-MHC binding: The "human MHC project."
    • Buus S. Description and prediction of peptide-MHC binding the "human MHC project." Curr Opin Immunol. 11:1999;209.
    • (1999) Curr Opin Immunol , vol.11 , pp. 209
    • Buus, S.1
  • 17
    • 0032402418 scopus 로고    scopus 로고
    • From peptides to peptidomimetics: Design of nonpeptide ligands for major histocompatibility proteins
    • Krebs S., Rognan D. From peptides to peptidomimetics design of nonpeptide ligands for major histocompatibility proteins . Pharm Acta Helv. 73:1998;173.
    • (1998) Pharm Acta Helv , vol.73 , pp. 173
    • Krebs, S.1    Rognan, D.2
  • 18
    • 0344721480 scopus 로고    scopus 로고
    • The MHC Sequencing Consortium: Complete sequence and gene map of a human major histocompatibility complex
    • The MHC Sequencing Consortium: Complete sequence and gene map of a human major histocompatibility complex. Nature 401:921, 1999.
    • (1999) Nature , vol.401 , pp. 921
  • 19
    • 0031455540 scopus 로고    scopus 로고
    • A structure-based algorithm to predict potential binding peptides to MHC molecules with hydrophobic binding pockets
    • Altuvia Y., Sette A., Sidney J., Southwood S., Margalit H. A structure-based algorithm to predict potential binding peptides to MHC molecules with hydrophobic binding pockets. Hum Immunol. 58:1997;1.
    • (1997) Hum Immunol , vol.58 , pp. 1
    • Altuvia, Y.1    Sette, A.2    Sidney, J.3    Southwood, S.4    Margalit, H.5
  • 20
    • 0032441130 scopus 로고    scopus 로고
    • Knowledge-based structure prediction of MHC class I bound peptides: A study of 23 complexes
    • Schueler-Furman O., Elber R., Margalit H. Knowledge-based structure prediction of MHC class I bound peptides a study of 23 complexes . Fold Des. 3:1998;549.
    • (1998) Fold des , vol.3 , pp. 549
    • Schueler-Furman, O.1    Elber, R.2    Margalit, H.3
  • 24
    • 0032387825 scopus 로고    scopus 로고
    • Predicting peptides that bind to MHC molecules using supervised learning of hidden Markov models
    • Mamitsuka H. Predicting peptides that bind to MHC molecules using supervised learning of hidden Markov models. Proteins. 33:1998;460.
    • (1998) Proteins , vol.33 , pp. 460
    • Mamitsuka, H.1
  • 25
    • 0029043976 scopus 로고
    • Peptide binding to MHC class I molecules: Implications for antigenic peptide prediction
    • Parker K.C., Shields M., DiBrino M., Brooks A., Coligan J.E. Peptide binding to MHC class I molecules implications for antigenic peptide prediction . Immunol Res. 14:1995;34.
    • (1995) Immunol Res , vol.14 , pp. 34
    • Parker, K.C.1    Shields, M.2    Dibrino, M.3    Brooks, A.4    Coligan, J.E.5
  • 26
    • 0032210911 scopus 로고    scopus 로고
    • Prediction of well-conserved HIV-1 ligands using a matrix-based algorithm, EpiMatrix
    • Schafer J.R., Jesdale B.M., George J.A., Kouttab N.M., De Groot A.S. Prediction of well-conserved HIV-1 ligands using a matrix-based algorithm, EpiMatrix. Vaccine. 16:1998;1880.
    • (1998) Vaccine , vol.16 , pp. 1880
    • Schafer, J.R.1    Jesdale, B.M.2    George, J.A.3    Kouttab, N.M.4    De Groot, A.S.5
  • 29
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S., Thornton J.M. Principles of protein-protein interactions. Proc Natl Acad Sci USA. 93:1996;13.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13
    • Jones, S.1    Thornton, J.M.2
  • 31
    • 0343641497 scopus 로고    scopus 로고
    • http://www.rcsb.org/pdb.
  • 33
    • 0027525106 scopus 로고
    • The antigenic identity of peptide-MHC complexes: A comparison of the conformations of five viral peptides presented by HLA-A2
    • Madden D.R., Garboczi D.N., Wiley D.C. The antigenic identity of peptide-MHC complexes a comparison of the conformations of five viral peptides presented by HLA-A2 . Cell. 75:1993;693.
    • (1993) Cell , vol.75 , pp. 693
    • Madden, D.R.1    Garboczi, D.N.2    Wiley, D.C.3
  • 35
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • Garboczi D.N., Ghosh P., Utz U., Fan Q.R., Biddison W.E., Wiley D.C. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature. 384:1996;134.
    • (1996) Nature , vol.384 , pp. 134
    • Garboczi, D.N.1    Ghosh, P.2    Utz, U.3    Fan, Q.R.4    Biddison, W.E.5    Wiley, D.C.6
  • 36
    • 18344405559 scopus 로고    scopus 로고
    • Two human T cell receptors bind in a similar diagonal mode to the HLA-A2/Tax peptide complex using different TCR amino acids
    • Ding Y.H., Smith K.J., Garboczi D.N., Utz U., Biddison W.E., Wiley D.C. Two human T cell receptors bind in a similar diagonal mode to the HLA-A2/Tax peptide complex using different TCR amino acids. Immunity. 8:1998;403.
    • (1998) Immunity , vol.8 , pp. 403
    • Ding, Y.H.1    Smith, K.J.2    Garboczi, D.N.3    Utz, U.4    Biddison, W.E.5    Wiley, D.C.6
  • 37
    • 0033579885 scopus 로고    scopus 로고
    • Structural evidence of T cell xeno-reactivity in the absence of molecular mimicry
    • Zhao R., Loftus D.J., Appella E., Collins E.J. Structural evidence of T cell xeno-reactivity in the absence of molecular mimicry. J Exp Med. 189:1999;359.
    • (1999) J Exp Med , vol.189 , pp. 359
    • Zhao, R.1    Loftus, D.J.2    Appella, E.3    Collins, E.J.4
  • 38
    • 0032189076 scopus 로고    scopus 로고
    • Crystal structures of HLA-A*0201 complexed with antigenic peptides with either the amino or carboxyl-terminal group substituted by a methyl group
    • Bouvier M., Guo H.C., Smith K.J., Wiley D.C. Crystal structures of HLA-A*0201 complexed with antigenic peptides with either the amino or carboxyl-terminal group substituted by a methyl group. Proteins. 33:1998;97.
    • (1998) Proteins , vol.33 , pp. 97
    • Bouvier, M.1    Guo, H.C.2    Smith, K.J.3    Wiley, D.C.4
  • 39
    • 0028150789 scopus 로고
    • Three-dimensional structure of a peptide extending from one end of a class I MHC binding site
    • Collins E.J., Garboczi D.N., Wiley D.C. Three-dimensional structure of a peptide extending from one end of a class I MHC binding site. Nature. 371:1994;626.
    • (1994) Nature , vol.371 , pp. 626
    • Collins, E.J.1    Garboczi, D.N.2    Wiley, D.C.3
  • 40
    • 0028871148 scopus 로고
    • The three-dimensional structure of a class I major histocompatibility complex molecule missing the alpha 3 domain of the heavy chain
    • Collins E.J., Garboczi D.N., Karpusas M.N., Wiley D.C. The three-dimensional structure of a class I major histocompatibility complex molecule missing the alpha 3 domain of the heavy chain. Proc Natl Acad Sci USA. 92:1995;1218.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1218
    • Collins, E.J.1    Garboczi, D.N.2    Karpusas, M.N.3    Wiley, D.C.4
  • 42
    • 0026794581 scopus 로고
    • The three-dimensional structure of HLA-B27 at 2: 1 A resolution suggests a general mechanism for tight peptide binding to MHC
    • Madden D.R., Gorga J.C., Strominger J.L., Wiley D.C. The three-dimensional structure of HLA-B27 at 2 1 A resolution suggests a general mechanism for tight peptide binding to MHC . Cell. 70:1992;1035.
    • (1992) Cell , vol.70 , pp. 1035
    • Madden, D.R.1    Gorga, J.C.2    Strominger, J.L.3    Wiley, D.C.4
  • 43
    • 0029965954 scopus 로고    scopus 로고
    • An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501
    • Smith K.J., Reid S.W., Stuart D.I., McMichael A.J., Jones E.Y., Bell J.I. An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. Immunity. 4:1996;203.
    • (1996) Immunity , vol.4 , pp. 203
    • Smith, K.J.1    Reid, S.W.2    Stuart, D.I.3    McMichael, A.J.4    Jones, E.Y.5    Bell, J.I.6
  • 44
    • 0033556246 scopus 로고    scopus 로고
    • Decamer like conformation of a nona-peptide bound to HLA-B*3501 due to non-standard positioning of the C terminus
    • Menssen R., Orth P., Ziegler A., Saenger W. Decamer like conformation of a nona-peptide bound to HLA-B*3501 due to non-standard positioning of the C terminus. J Mol Biol. 285:1999;645.
    • (1999) J Mol Biol , vol.285 , pp. 645
    • Menssen, R.1    Orth, P.2    Ziegler, A.3    Saenger, W.4
  • 45
    • 0029969665 scopus 로고    scopus 로고
    • Bound water structure and polymorphic 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., Jones E.Y. Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53. Immunity. 4:1996;215.
    • (1996) Immunity , vol.4 , pp. 215
    • 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
  • 47
    • 0026673724 scopus 로고
    • Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb
    • Fremont D.H., Matsumura M., Stura E.A., Peterson P.A., Wilson I.A. Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb. Science. 257:1992;919.
    • (1992) Science , vol.257 , pp. 919
    • Fremont, D.H.1    Matsumura, M.2    Stura, E.A.3    Peterson, P.A.4    Wilson, I.A.5
  • 48
    • 0033024354 scopus 로고    scopus 로고
    • Crystal structure of an MHC class I presented glycopeptide that generates carbohydrate-specific CTL
    • Speir J.A., Abdel-Motal U.M., Jondal M., Wilson I.A. Crystal structure of an MHC class I presented glycopeptide that generates carbohydrate-specific CTL. Immunity. 10:1999;51.
    • (1999) Immunity , vol.10 , pp. 51
    • Speir, J.A.1    Abdel-Motal, U.M.2    Jondal, M.3    Wilson, I.A.4
  • 49
    • 0028987213 scopus 로고
    • Crystal structure of an H-2Kb-ovalbumin peptide complex reveals the interplay of primary and secondary anchor positions in the major histocompatibility complex binding groove
    • Fremont D.H., Stura E.A., Matsumura M., Peterson P.A., Wilson I.A. Crystal structure of an H-2Kb-ovalbumin peptide complex reveals the interplay of primary and secondary anchor positions in the major histocompatibility complex binding groove. Proc Natl Acad Sci USA. 92:1995;2479.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2479
    • Fremont, D.H.1    Stura, E.A.2    Matsumura, M.3    Peterson, P.A.4    Wilson, I.A.5
  • 50
    • 0033579885 scopus 로고    scopus 로고
    • Structural evidence of T cell xeno-reactivity in the absence of molecular mimicry
    • Zhao R., Loftus D.J., Appella E., Collins E.J. Structural evidence of T cell xeno-reactivity in the absence of molecular mimicry. J Exp Med. 189:1999;359.
    • (1999) J Exp Med , vol.189 , pp. 359
    • Zhao, R.1    Loftus, D.J.2    Appella, E.3    Collins, E.J.4
  • 52
    • 0032143985 scopus 로고    scopus 로고
    • The crystal structure of H-2Dd MHC class I complexed with the HIV-1-derived peptide P18-110 at 2: 4 A resolution: Implications for T cell and NK cell recognition
    • Achour A., Persson K., Harris R.A., Sundback J., Sentman C.L., Lindqvist Y., Schneider G., Karre K. The crystal structure of H-2Dd MHC class I complexed with the HIV-1-derived peptide P18-110 at 2 4 A resolution: implications for T cell and NK cell recognition . Immunity. 9:1998;199.
    • (1998) Immunity , vol.9 , pp. 199
    • Achour, A.1    Persson, K.2    Harris, R.A.3    Sundback, J.4    Sentman, C.L.5    Lindqvist, Y.6    Schneider, G.7    Karre, K.8
  • 54
    • 0031572833 scopus 로고    scopus 로고
    • The class II MHC protein HLA-DR1 in complex with an endogenous peptide: Implications for the structural basis of the specificity of peptide binding
    • Murthy V.L., Stern L.J. The class II MHC protein HLA-DR1 in complex with an endogenous peptide implications for the structural basis of the specificity of peptide binding . Structure. 5:1997;1385.
    • (1997) Structure , vol.5 , pp. 1385
    • Murthy, V.L.1    Stern, L.J.2
  • 57
    • 0032547858 scopus 로고    scopus 로고
    • Crystal structure of HLA-DR2 (DRA*0101, DRB1*1501) complexed with a peptide from human myelin basic protein
    • Smith K.J., Pyrdol J., Gauthier L., Wiley D.C., Wucherpfennig K.W. Crystal structure of HLA-DR2 (DRA*0101, DRB1*1501) complexed with a peptide from human myelin basic protein. J Exp Med. 188:1998;1511.
    • (1998) J Exp Med , vol.188 , pp. 1511
    • Smith, K.J.1    Pyrdol, J.2    Gauthier, L.3    Wiley, D.C.4    Wucherpfennig, K.W.5
  • 58
    • 0028823585 scopus 로고
    • The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3
    • Ghosh P., Amaya M., Mellins E., Wiley D.C. The structure of an intermediate in class II MHC maturation CLIP bound to HLA-DR3 . Nature. 378:1995;457.
    • (1995) Nature , vol.378 , pp. 457
    • Ghosh, P.1    Amaya, M.2    Mellins, E.3    Wiley, D.C.4
  • 59
    • 0030701632 scopus 로고    scopus 로고
    • X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed with a peptide from human collagen II
    • Dessen A., Lawrence C.M., Cupo S., Zaller D.M., Wiley D.C. X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed with a peptide from human collagen II. Immunity. 7:1997;473.
    • (1997) Immunity , vol.7 , pp. 473
    • Dessen, A.1    Lawrence, C.M.2    Cupo, S.3    Zaller, D.M.4    Wiley, D.C.5
  • 60
    • 0032033678 scopus 로고    scopus 로고
    • Crystal structures of two I-Ad-peptide complexes reveal that high affinity can be achieved without large anchor residues
    • Scott C.A., Peterson P.A., Teyton L., Wilson I.A. Crystal structures of two I-Ad-peptide complexes reveal that high affinity can be achieved without large anchor residues. Immunity. 8:1998;319.
    • (1998) Immunity , vol.8 , pp. 319
    • Scott, C.A.1    Peterson, P.A.2    Teyton, L.3    Wilson, I.A.4
  • 61
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B., Richard F.M. The interpretation of protein structures estimation of static accessibility . J Mol Biol. 55:1971;379.
    • (1971) J Mol Biol , vol.55 , pp. 379
    • Lee, B.1    Richard, F.M.2
  • 62
    • 0342336249 scopus 로고
    • London: Department of Biochemistry and Molecular Biology, University College
    • Laskowski RA: SURFNET computer-program. London: Department of Biochemistry and Molecular Biology, University College, 1991.
    • (1991) SURFNET Computer-program
    • Laskowski, R.A.1
  • 63
    • 0028881975 scopus 로고
    • SURFNET: A program for visualizing molecular surfaces, cavities and intermolecular interactions
    • Laskowski R.A. SURFNET a program for visualizing molecular surfaces, cavities and intermolecular interactions . J Mol Graph. 13:1995;323.
    • (1995) J Mol Graph , vol.13 , pp. 323
    • Laskowski, R.A.1
  • 64
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald I.K., Thornton J.M. Satisfying hydrogen bonding potential in proteins. J Mol Biol. 238:1994;777.
    • (1994) J Mol Biol , vol.238 , pp. 777
    • McDonald, I.K.1    Thornton, J.M.2
  • 67
    • 0033523959 scopus 로고    scopus 로고
    • Predicting binding affinities of protein ligands from three-dimensional models: Application to peptide binding to class I major histocompatibility proteins
    • Rognan D., Lauemoller S.L., Holm A., Buus S., Tschinke V. Predicting binding affinities of protein ligands from three-dimensional models application to peptide binding to class I major histocompatibility proteins . J Med Chem. 42:1999;4650.
    • (1999) J Med Chem , vol.42 , pp. 4650
    • Rognan, D.1    Lauemoller, S.L.2    Holm, A.3    Buus, S.4    Tschinke, V.5
  • 68
    • 0034677965 scopus 로고    scopus 로고
    • Structural genomics offers high-speed look at proteins
    • Service R.F. Structural genomics offers high-speed look at proteins. Science. 287:2000;1954.
    • (2000) Science , vol.287 , pp. 1954
    • Service, R.F.1
  • 70
    • 0033230777 scopus 로고    scopus 로고
    • Human transporters associated with antigen processing (TAPs) select epitope precursor peptides for processing in the endoplasmic reticulum and presentation to T cells
    • Lauvau G., Kakimi K., Niedermann G., Ostankovitch M., Yotnda P., Firat H., Chisari F.V., van Endert P.M. Human transporters associated with antigen processing (TAPs) select epitope precursor peptides for processing in the endoplasmic reticulum and presentation to T cells. J Exp Med. 190:1999;1227.
    • (1999) J Exp Med , vol.190 , pp. 1227
    • Lauvau, G.1    Kakimi, K.2    Niedermann, G.3    Ostankovitch, M.4    Yotnda, P.5    Firat, H.6    Chisari, F.V.7    Van Endert, P.M.8
  • 71
    • 0034087707 scopus 로고    scopus 로고
    • Human memory CTL response specific for influenza A virus is broad and multispecific
    • Gianfrani C., Oseroff C., Sidney J., Chesnut R.W., Sette A. Human memory CTL response specific for influenza A virus is broad and multispecific. Hum Immunol. 61:2000;438.
    • (2000) Hum Immunol , vol.61 , pp. 438
    • Gianfrani, C.1    Oseroff, C.2    Sidney, J.3    Chesnut, R.W.4    Sette, A.5
  • 72
    • 0032752883 scopus 로고    scopus 로고
    • Immunization with the HBV core 18-27 epitope elicits CTL responses in humans expressing different HLA-A2 supertype molecules
    • Livingston B.D., Crimi C., Fikes J., Chesnut R.W., Sidney J., Sette A. Immunization with the HBV core 18-27 epitope elicits CTL responses in humans expressing different HLA-A2 supertype molecules. Hum Immunol. 60:1999;1013.
    • (1999) Hum Immunol , vol.60 , pp. 1013
    • Livingston, B.D.1    Crimi, C.2    Fikes, J.3    Chesnut, R.W.4    Sidney, J.5    Sette, A.6
  • 73
    • 0027983589 scopus 로고
    • Determinant selection of major histocompatibility complex class I-restricted antigenic peptides is explained by class I-peptide affinity and is strongly influenced by nondominant anchor residues
    • Chen W., Khilko S., Fecondo J., Margulies D.H., McCluskey J. Determinant selection of major histocompatibility complex class I-restricted antigenic peptides is explained by class I-peptide affinity and is strongly influenced by nondominant anchor residues. J Exp Med. 180:1994;1471.
    • (1994) J Exp Med , vol.180 , pp. 1471
    • Chen, W.1    Khilko, S.2    Fecondo, J.3    Margulies, D.H.4    McCluskey, J.5
  • 74
    • 0033944416 scopus 로고    scopus 로고
    • From data to knowledge
    • Rechenmann F. From data to knowledge. Bioinformatics. 16:2000;411.
    • (2000) Bioinformatics , vol.16 , pp. 411
    • Rechenmann, F.1


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