메뉴 건너뛰기




Volumn 96, Issue 1, 2011, Pages 110-118

The impact of human leukocyte antigen (HLA) micropolymorphism on ligand specificity within the HLA-B*41 allotypic family

Author keywords

HLA B*41; Micropolymorphism; Peptide motif; X ray crystallography

Indexed keywords

GLUTAMIC ACID; HLA B ANTIGEN; LEUCINE; PROLINE; VALINE;

EID: 78650992438     PISSN: 03906078     EISSN: 15928721     Source Type: Journal    
DOI: 10.3324/haematol.2010.030924     Document Type: Article
Times cited : (42)

References (56)
  • 1
    • 0029956865 scopus 로고    scopus 로고
    • A roadmap for HLA-A, HLA-B, and HLA-C peptide binding specificities
    • Chelvanayagam G. A roadmap for HLA-A, HLA-B, and HLA-C peptide binding specificities. Immunogenetics. 1996;45(1):15-26.
    • (1996) Immunogenetics , vol.45 , Issue.1 , pp. 15-26
    • Chelvanayagam, G.1
  • 2
    • 48749092592 scopus 로고    scopus 로고
    • The known unknowns of antigen processing and presentation
    • Vyas JM, Van der Veen AG, Ploegh HL. The known unknowns of antigen processing and presentation. Nat Rev Immunol. 2008;8 (8):607-18.
    • (2008) Nat Rev Immunol , vol.8 , Issue.8 , pp. 607-618
    • Vyas, J.M.1    van der Veen, A.G.2    Ploegh, H.L.3
  • 3
    • 71949096416 scopus 로고    scopus 로고
    • Derivation of an amino acid similarity matrix for peptide: MHC binding and its application as a Bayesian prior
    • Kim Y, Sidney J, Pinilla C, Sette A, Peters B. Derivation of an amino acid similarity matrix for peptide: MHC binding and its application as a Bayesian prior. BMC Bioinformatics. 2009;10:394.
    • (2009) BMC Bioinformatics , vol.10 , pp. 394
    • Kim, Y.1    Sidney, J.2    Pinilla, C.3    Sette, A.4    Peters, B.5
  • 4
    • 0035881251 scopus 로고    scopus 로고
    • Combinatorial peptide libraries and biometric score matrices permit the quantitative analysis of specific and degenerate interactions between clonotypic TCR and MHC peptide ligands
    • Zhao Y, Gran B, Pinilla C, Markovic-Plese S, Hemmer B, Tzou A, et al. Combinatorial peptide libraries and biometric score matrices permit the quantitative analysis of specific and degenerate interactions between clonotypic TCR and MHC peptide ligands. J Immunol. 2001;167(4):2130-41.
    • (2001) J Immunol , vol.167 , Issue.4 , pp. 2130-2141
    • Zhao, Y.1    Gran, B.2    Pinilla, C.3    Markovic-Plese, S.4    Hemmer, B.5    Tzou, A.6
  • 5
    • 33750978455 scopus 로고    scopus 로고
    • Optimally-connected hidden Markov models for predicting MHC-binding peptides
    • Zhang C, Bickis MG, Wu FX, Kusalik AJ. Optimally-connected hidden Markov models for predicting MHC-binding peptides. J Bioinform Comput Biol. 2006;4(5):959-80.
    • (2006) J Bioinform Comput Biol , vol.4 , Issue.5 , pp. 959-980
    • Zhang, C.1    Bickis, M.G.2    Wu, F.X.3    Kusalik, A.J.4
  • 6
    • 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. 1998;33(4):460-74.
    • (1998) Proteins , vol.33 , Issue.4 , pp. 460-474
    • Mamitsuka, H.1
  • 7
    • 70449359806 scopus 로고    scopus 로고
    • An artificial neural network-based alignment algorithm for MHC class II peptide binding prediction
    • Nielsen M, Lund O. NN-align. An artificial neural network-based alignment algorithm for MHC class II peptide binding prediction. BMC Bioinformatics. 2009;10:296.
    • (2009) BMC Bioinformatics , vol.10 , pp. 296
    • Nielsen, M.1    Nn-Align Lund, O.2
  • 8
    • 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 HG. Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules. Nature. 1991;351(6324):290-6.
    • (1991) Nature , vol.351 , Issue.6324 , pp. 290-296
    • Falk, K.1    Rotzschke, O.2    Stevanovic, S.3    Jung, G.4    Rammensee, H.G.5
  • 11
    • 48449106045 scopus 로고    scopus 로고
    • NetMHC-3.0: Accurate web accessible predictions of human, mouse and monkey MHC class I affinities for peptides of length 8-11
    • Web Server issue
    • Lundegaard C, Lamberth K, Harndahl M, Buus S, Lund O, Nielsen M. NetMHC-3.0: accurate web accessible predictions of human, mouse and monkey MHC class I affinities for peptides of length 8-11. Nucleic Acids Res. 2008;36(Web Server issue):W509-12.
    • (2008) Nucleic Acids Res , vol.36
    • Lundegaard, C.1    Lamberth, K.2    Harndahl, M.3    Buus, S.4    Lund, O.5    Nielsen, M.6
  • 12
    • 5444249860 scopus 로고    scopus 로고
    • Enhancement to the RANKPEP resource for the prediction of peptide binding to MHC molecules using profiles
    • Reche PA, Glutting JP, Zhang H, Reinherz EL. Enhancement to the RANKPEP resource for the prediction of peptide binding to MHC molecules using profiles. Immunogenetics. 2004;56(6):405-19.
    • (2004) Immunogenetics , vol.56 , Issue.6 , pp. 405-419
    • Reche, P.A.1    Glutting, J.P.2    Zhang, H.3    Reinherz, E.L.4
  • 13
    • 44649087765 scopus 로고    scopus 로고
    • Implementing the modular MHC model for predicting peptide binding
    • DeLuca DS, Blasczyk R. Implementing the modular MHC model for predicting peptide binding. Methods Mol Biol. 2007;409: 261-71.
    • (2007) Methods Mol Biol , vol.409 , pp. 261-271
    • de Luca, D.S.1    Blasczyk, R.2
  • 14
    • 0028052724 scopus 로고
    • Scheme for ranking potential HLA-A2 binding peptides based on independent binding of individual peptide side-chains
    • Parker KC, Bednarek MA, Coligan JE. Scheme for ranking potential HLA-A2 binding peptides based on independent binding of individual peptide side-chains. J Immunol. 1994;152(1):163-75.
    • (1994) J Immunol , vol.152 , Issue.1 , pp. 163-175
    • Parker, K.C.1    Bednarek, M.A.2    Coligan, J.E.3
  • 15
    • 30544452130 scopus 로고    scopus 로고
    • Have we cut ourselves too short in mapping CTL epitopes?
    • Burrows SR, Rossjohn J, McCluskey J. Have we cut ourselves too short in mapping CTL epitopes? Trends Immunol. 2006;27(1):11-6.
    • (2006) Trends Immunol , vol.27 , Issue.1 , pp. 11-16
    • Burrows, S.R.1    Rossjohn, J.2    McCluskey, J.3
  • 16
    • 27544446623 scopus 로고    scopus 로고
    • T cell receptor recognition of a 'super-bulged' major histocompatibility complex class Ibound peptide
    • Tynan FE, Burrows SR, Buckle AM, Clements CS, Borg NA, Miles JJ, et al. T cell receptor recognition of a 'super-bulged' major histocompatibility complex class Ibound peptide. Nat Immunol. 2005;6(11): 1114-22.
    • (2005) Nat Immunol , vol.6 , Issue.11 , pp. 1114-1122
    • Tynan, F.E.1    Burrows, S.R.2    Buckle, A.M.3    Clements, C.S.4    Borg, N.A.5    Miles, J.J.6
  • 17
    • 4644272170 scopus 로고    scopus 로고
    • Potent T cell response to a class I-binding 13-mer viral epitope and the influence of HLA micropolymorphism in controlling epitope length
    • Green KJ, Miles JJ, Tellam J, van Zuylen WJ, Connolly G, Burrows SR. Potent T cell response to a class I-binding 13-mer viral epitope and the influence of HLA micropolymorphism in controlling epitope length. Eur J Immunol. 2004;34(9):2510-9.
    • (2004) Eur J Immunol , vol.34 , Issue.9 , pp. 2510-2519
    • Green, K.J.1    Miles, J.J.2    Tellam, J.3    van Zuylen, W.J.4    Connolly, G.5    Burrows, S.R.6
  • 18
    • 2942529423 scopus 로고    scopus 로고
    • A single amino-acid polymorphism in pocket A of HLA-A*6602 alters the auxiliary anchors compared with HLA-A*6601 ligands
    • Bade-Doeding C, Elsner HA, Eiz-Vesper B, Seltsam A, Holtkamp U, Blasczyk R. A single amino-acid polymorphism in pocket A of HLA-A*6602 alters the auxiliary anchors compared with HLA-A*6601 ligands. Immunogenetics. 2004;56(2):83-8.
    • (2004) Immunogenetics , vol.56 , Issue.2 , pp. 83-88
    • Bade-Doeding, C.1    Elsner, H.A.2    Eiz-Vesper, B.3    Seltsam, A.4    Holtkamp, U.5    Blasczyk, R.6
  • 19
    • 0018154865 scopus 로고
    • Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens-new tools for genetic analysis
    • Barnstable CJ, Bodmer WF, Brown G, Galfre G, Milstein C, Williams AF, et al. Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens-new tools for genetic analysis. Cell. 1978;14(1):9-20.
    • (1978) Cell , vol.14 , Issue.1 , pp. 9-20
    • Barnstable, C.J.1    Bodmer, W.F.2    Brown, G.3    Galfre, G.4    Milstein, C.5    Williams, A.F.6
  • 21
    • 0027286502 scopus 로고
    • MASCOT: Multiple alignment system for protein sequences based on threeway dynamic programming
    • Hirosawa M, Hoshida M, Ishikawa M, Toya T. MASCOT: multiple alignment system for protein sequences based on threeway dynamic programming. Comput Appl Biosci. 1993;9(2):161-7.
    • (1993) Comput Appl Biosci , vol.9 , Issue.2 , pp. 161-167
    • Hirosawa, M.1    Hoshida, M.2    Ishikawa, M.3    Toya, T.4
  • 23
    • 0037063316 scopus 로고    scopus 로고
    • Identification of a dominant self-ligand bound to three HLA B44 alleles and the preliminary crystallographic analysis of recombinant forms of each complex
    • Macdonald W, Williams DS, Clements CS, Gorman JJ, Kjer-Nielsen L, Brooks AG, et al. Identification of a dominant self-ligand bound to three HLA B44 alleles and the preliminary crystallographic analysis of recombinant forms of each complex. FEBS Lett. 2002;527(1-3):27-32.
    • (2002) FEBS Lett , vol.527 , Issue.1-3 , pp. 27-32
    • Macdonald, W.1    Williams, D.S.2    Clements, C.S.3    Gorman, J.J.4    Kjer-Nielsen, L.5    Brooks, A.G.6
  • 24
    • 43249126282 scopus 로고    scopus 로고
    • Impact of clonal competition for peptide-MHC complexes on the CD8+ T-cell repertoire selection in a persistent viral infection
    • Wynn KK, Fulton Z, Cooper L, Silins SL, Gras S, Archbold JK, et al. Impact of clonal competition for peptide-MHC complexes on the CD8+ T-cell repertoire selection in a persistent viral infection. Blood. 2008;111 (8):4283-92.
    • (2008) Blood , vol.111 , Issue.8 , pp. 4283-4292
    • Wynn, K.K.1    Fulton, Z.2    Cooper, L.3    Silins, S.L.4    Gras, S.5    Archbold, J.K.6
  • 25
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Cryst. 1993;26:795-800.
    • (1993) J. Appl. Cryst , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 27
    • 2942753075 scopus 로고    scopus 로고
    • Natural HLA class I polymorphism controls the pathway of antigen presentation and susceptibility to viral evasion
    • Zernich D, Purcell AW, Macdonald WA, Kjer-Nielsen L, Ely LK, Laham N, et al. Natural HLA class I polymorphism controls the pathway of antigen presentation and susceptibility to viral evasion. J Exp Med. 2004;200(1):13-24.
    • (2004) J Exp Med , vol.200 , Issue.1 , pp. 13-24
    • Zernich, D.1    Purcell, A.W.2    Macdonald, W.A.3    Kjer-Nielsen, L.4    Ely, L.K.5    Laham, N.6
  • 28
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr. 1997;53(Pt 3):240-55.
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , Issue.PART 3 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 30
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr A. 1991;47 (Pt 2):110-9.
    • (1991) Acta Crystallogr A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 31
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • PART 1
    • Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 12 Pt 1):2126-32.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 33
    • 0033152783 scopus 로고    scopus 로고
    • Expanding the model: Anisotropic displacement parameters in protein structure refinement
    • Merritt EA. Expanding the model: anisotropic displacement parameters in protein structure refinement. Acta Crystallogr D Biol Crystallogr. 1999;55(Pt 6):1109-17.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , Issue.PART 6 , pp. 1109-1117
    • Merritt, E.A.1
  • 34
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine AA, Richelle J, Wodak SJ. SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr D Biol Crystallogr. 1999;55(Pt 1):191-205.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , Issue.PART 1 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 35
    • 0028070557 scopus 로고
    • Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement
    • Torsion angle dynamics: reduced variable conformational sampling enhances crystallographic structure refinement. Proteins. 1994;19(4):277-90.
    • (1994) Proteins , vol.19 , Issue.4 , pp. 277-290
  • 36
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the Crystallography and NMR system
    • Brunger AT. Version 1.2 of the Crystallography and NMR system. Nat Protoc. 2007;2(11):2728-33.
    • (2007) Nat Protoc , vol.2 , Issue.11 , pp. 2728-2733
    • Brunger, A.T.1
  • 37
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Web Server issue
    • Davis IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, Wang X, et al. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 2007;35(Web Server issue): W375-83.
    • (2007) Nucleic Acids Res , vol.35
    • Davis, I.W.1    Leaver-Fay, A.2    Chen, V.B.3    Block, J.N.4    Kapral, G.J.5    Wang, X.6
  • 38
    • 23144457576 scopus 로고    scopus 로고
    • H++: A server for estimating pKas and adding missing hydrogens to macromolecules
    • Web Server issue
    • Gordon JC, Myers JB, Folta T, Shoja V, Heath LS, Onufriev A. H++: a server for estimating pKas and adding missing hydrogens to macromolecules. Nucleic Acids Res. 2005;33(Web Server issue):W368-71.
    • (2005) Nucleic Acids Res , vol.33
    • Gordon, J.C.1    Myers, J.B.2    Folta, T.3    Shoja, V.4    Heath, L.S.5    Onufriev, A.6
  • 39
    • 33847785568 scopus 로고    scopus 로고
    • Amino acid 95 causes strong alteration of peptide position Pomega in HLA-B*41 variants
    • Bade-Doeding C, DeLuca DS, Seltsam A, Blasczyk R, Eiz-Vesper B. Amino acid 95 causes strong alteration of peptide position Pomega in HLA-B*41 variants. Immunogenetics. 2007;59(4):253-9.
    • (2007) Immunogenetics , vol.59 , Issue.4 , pp. 253-259
    • Bade-Doeding, C.1    Deluca, D.S.2    Seltsam, A.3    Blasczyk, R.4    Eiz-Vesper, B.5
  • 40
    • 0345059376 scopus 로고    scopus 로고
    • Announcing the worldwide Protein Data Bank
    • Berman H, Henrick K, Nakamura H. Announcing the worldwide Protein Data Bank. Nat Struct Biol. 2003;10(12):980.
    • (2003) Nat Struct Biol , vol.10 , Issue.12 , pp. 980
    • Berman, H.1    Henrick, K.2    Nakamura, H.3
  • 41
    • 6344272484 scopus 로고    scopus 로고
    • Conformational restraints and flexibility of 14-meric peptides in complex with HLAB* 3501
    • Probst-Kepper M, Hecht HJ, Herrmann H, Janke V, Ocklenburg F, Klempnauer J, et al. Conformational restraints and flexibility of 14-meric peptides in complex with HLAB* 3501. J Immunol. 2004;173(9): 5610-6.
    • (2004) J Immunol , vol.173 , Issue.9 , pp. 5610-5616
    • Probst-Kepper, M.1    Hecht, H.J.2    Herrmann, H.3    Janke, V.4    Ocklenburg, F.5    Klempnauer, J.6
  • 42
    • 33750832289 scopus 로고    scopus 로고
    • TCR alpha genes direct MHC restriction in the potent human T cell response to a class I-bound viral epitope
    • Miles JJ, Borg NA, Brennan RM, Tynan FE, Kjer-Nielsen L, Silins SL, et al. TCR alpha genes direct MHC restriction in the potent human T cell response to a class I-bound viral epitope. J Immunol. 2006;177(10): 6804-14.
    • (2006) J Immunol , vol.177 , Issue.10 , pp. 6804-6814
    • Miles, J.J.1    Borg, N.A.2    Brennan, R.M.3    Tynan, F.E.4    Kjer-Nielsen, L.5    Silins, S.L.6
  • 43
    • 34247154800 scopus 로고    scopus 로고
    • A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule
    • Tynan FE, Reid HH, Kjer-Nielsen L, Miles JJ, Wilce MC, Kostenko L, et al. A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule. Nat Immunol. 2007;8(3):268-76.
    • (2007) Nat Immunol , vol.8 , Issue.3 , pp. 268-276
    • Tynan, F.E.1    Reid, H.H.2    Kjer-Nielsen, L.3    Miles, J.J.4    Wilce, M.C.5    Kostenko, L.6
  • 44
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 1983;22(12):2577-637.
    • (1983) Biopolymers , vol.22 , Issue.12 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 45
    • 77950374922 scopus 로고    scopus 로고
    • Constraints within major histocompatibility complex class I restricted peptides: Presentation and consequences for T-cell recognition
    • Theodossis A, Guillonneau C, Welland A, Ely LK, Clements CS, Williamson NA, et al. Constraints within major histocompatibility complex class I restricted peptides: presentation and consequences for T-cell recognition. Proc Natl Acad Sci USA. 2010;107 (12):5534-9.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.12 , pp. 5534-5539
    • Theodossis, A.1    Guillonneau, C.2    Welland, A.3    Ely, L.K.4    Clements, C.S.5    Williamson, N.A.6
  • 46
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • Web Server issue
    • Dundas J, Ouyang Z, Tseng J, Binkowski A, Turpaz Y, Liang J. CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acids Res. 2006;34(Web Server issue): W116-8.
    • (2006) Nucleic Acids Res , vol.34
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 47
    • 0036708467 scopus 로고    scopus 로고
    • Relationship between ion pair geometries and electrostatic strengths in proteins
    • Kumar S, Nussinov R. Relationship between ion pair geometries and electrostatic strengths in proteins. Biophys J. 2002;83(3):1595-612.
    • (2002) Biophys J , vol.83 , Issue.3 , pp. 1595-1612
    • Kumar, S.1    Nussinov, R.2
  • 48
    • 0029655676 scopus 로고    scopus 로고
    • Alloreactive cytotoxic T-lymphocytedefined HLA-B7 subtypes differ in peptide antigen presentation
    • Smith KD, Epperson DF, Lutz CT. Alloreactive cytotoxic T-lymphocytedefined HLA-B7 subtypes differ in peptide antigen presentation. Immunogenetics. 1996;43(1-2):27-37.
    • (1996) Immunogenetics , vol.43 , Issue.1-2 , pp. 27-37
    • Smith, K.D.1    Epperson, D.F.2    Lutz, C.T.3
  • 49
    • 27344445458 scopus 로고    scopus 로고
    • Analysis of memory T lymphocyte activity following stimulation with overlapping HLA-A*2402, A*0101 and Cw*0402 restricted CMV pp65 peptides
    • Ghei M, Stroncek DF, Provenzano M. Analysis of memory T lymphocyte activity following stimulation with overlapping HLA-A*2402, A*0101 and Cw*0402 restricted CMV pp65 peptides. J Transl Med. 2005;3:23.
    • (2005) J Transl Med , vol.3 , pp. 23
    • Ghei, M.1    Stroncek, D.F.2    Provenzano, M.3
  • 50
    • 0035825036 scopus 로고    scopus 로고
    • A 16- mer peptide (RQIKIWFQNRRMKWKK) from antennapedia preferentially targets the Class I pathway
    • Pietersz GA, Li W, Apostolopoulos V. A 16- mer peptide (RQIKIWFQNRRMKWKK) from antennapedia preferentially targets the Class I pathway. Vaccine. 2001;19(11-12):1397-405.
    • (2001) Vaccine , vol.19 , Issue.11-12 , pp. 1397-1405
    • Pietersz, G.A.1    Li, W.2    Apostolopoulos, V.3
  • 51
    • 0036830113 scopus 로고    scopus 로고
    • Comprehensive mapping of HLA-A0201- restricted CD8 T-cell epitopes on PDC-E2 in primary biliary cirrhosis
    • Matsumura S, Kita H, He XS, Ansari AA, Lian ZX, Van De Water J, et al. Comprehensive mapping of HLA-A0201- restricted CD8 T-cell epitopes on PDC-E2 in primary biliary cirrhosis. Hepatology. 2002;36(5):1125-34.
    • (2002) Hepatology , vol.36 , Issue.5 , pp. 1125-1134
    • Matsumura, S.1    Kita, H.2    He, X.S.3    Ansari, A.A.4    Lian, Z.X.5    van de Water, J.6
  • 53
    • 64149115648 scopus 로고    scopus 로고
    • The peptide length specificity of some HLA class I alleles is very broad and includes peptides of up to 25 amino acids in length
    • Bell MJ, Burrows JM, Brennan R, Miles JJ, Tellam J, McCluskey J, et al. The peptide length specificity of some HLA class I alleles is very broad and includes peptides of up to 25 amino acids in length. Mol Immunol. 2009;46(8-9):1911-7.
    • (2009) Mol Immunol , vol.46 , Issue.8-9 , pp. 1911-1917
    • Bell, M.J.1    Burrows, J.M.2    Brennan, R.3    Miles, J.J.4    Tellam, J.5    McCluskey, J.6
  • 54
    • 0025831493 scopus 로고
    • Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution
    • Saper MA, Bjorkman PJ, Wiley DC. Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution. J Mol Biol. 1991;219(2):277-319.
    • (1991) J Mol Biol , vol.219 , Issue.2 , pp. 277-319
    • Saper, M.A.1    Bjorkman, P.J.2    Wiley, D.C.3
  • 55
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Bailey S. The CCP4 suite: programs for protein crystallography. Acta Cryst. 1994;50(Pt 5):760-3.
    • (1994) Acta Cryst , vol.50 , Issue.PART 5 , pp. 760-763
    • Bailey, S.1
  • 56
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B, Richards FM. The interpretation of protein structures: estimation of static accessibility. J Mol Biol. 1971;55(3):379-400.
    • (1971) J Mol Biol , vol.55 , Issue.3 , pp. 379-400
    • Lee, B.1    Richards, F.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.