메뉴 건너뛰기




Volumn 64, Issue 12, 2003, Pages 1123-1143

A Novel MHCp Binding Prediction Model

Author keywords

Amino acids; MHC; Peptide binding; Prediction; Property matrix

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN; PEPTIDE;

EID: 0344420229     PISSN: 01988859     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.humimm.2003.08.343     Document Type: Article
Times cited : (24)

References (102)
  • 1
    • 0035884987 scopus 로고    scopus 로고
    • Crystal structures of two closely related but antigenically distinct HLA-A2/melanocyte-melanoma tumor-antigen peptide complexes
    • Sliz P, Michielin O, Cerottini JC, Luescher I, Romero P, Karplus M, Wiley DC: Crystal structures of two closely related but antigenically distinct HLA-A2/melanocyte-melanoma tumor-antigen peptide complexes. J Immunol 167:3276, 2001.
    • (2001) J Immunol , vol.167 , pp. 3276
    • Sliz, P.1    Michielin, O.2    Cerottini, J.C.3    Luescher, I.4    Romero, P.5    Karplus, M.6    Wiley, D.C.7
  • 2
    • 0033579885 scopus 로고    scopus 로고
    • Structural evidence of T cell xeno-reactivity in the absence of molecular mimicry
    • Zhao R, Loftus DJ, Appella E, Collins EJ: Structural evidence of T cell xeno-reactivity in the absence of molecular mimicry. J Exp Med 189:359, 1999.
    • (1999) J Exp Med , vol.189 , pp. 359
    • Zhao, R.1    Loftus, D.J.2    Appella, E.3    Collins, E.J.4
  • 3
    • 0035861753 scopus 로고    scopus 로고
    • T cell activity correlates with oligomeric peptide-major histocompatibility complex binding on T cell surface
    • Buslepp J, Zhao R, Donnini D, Loftus D, Saad M, Appella E, Collins EJ: T cell activity correlates with oligomeric peptide-major histocompatibility complex binding on T cell surface. J Biol Chem 276:47320, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 47320
    • Buslepp, J.1    Zhao, R.2    Donnini, D.3    Loftus, D.4    Saad, M.5    Appella, E.6    Collins, E.J.7
  • 4
    • 0033601293 scopus 로고    scopus 로고
    • The structural basis for the increased immunogenicity of two HIV-reverse transcriptase peptide variant/class-I major histocompatibility complexes
    • Kirksey TJ, Pogue-Caley RR, Frelinger JA, Collins EJ: The structural basis for the increased immunogenicity of two HIV-reverse transcriptase peptide variant/class-I major histocompatibility complexes. J Biol Chem 274:37259, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 37259
    • Kirksey, T.J.1    Pogue-Caley, R.R.2    Frelinger, J.A.3    Collins, E.J.4
  • 5
    • 0027525106 scopus 로고
    • The antigenic identity of peptide-MHC complexes: A comparison of the conformations of five viral peptides presented by HLA-A2
    • Madden DR, Garboczi DN, Wiley DC: The antigenic identity of peptide-MHC complexes: a comparison of the conformations of five viral peptides presented by HLA-A2. Cell 75:693, 1993.
    • (1993) Cell , vol.75 , pp. 693
    • Madden, D.R.1    Garboczi, D.N.2    Wiley, D.C.3
  • 7
    • 0033165928 scopus 로고    scopus 로고
    • Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical
    • Ding YH, Baker BM, Garboczi DN, Biddison WE, Wiley DC: Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical. Immunity 11:45, 1999.
    • (1999) Immunity , vol.11 , pp. 45
    • Ding, Y.H.1    Baker, B.M.2    Garboczi, D.N.3    Biddison, W.E.4    Wiley, D.C.5
  • 8
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • Garboczi DN, Ghosh P, Utz U, Fan QR, Biddison WE, Wiley DC: Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 384:134, 1996.
    • (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
  • 9
    • 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 YH, Smith KJ, Garboczi DN, Utz U, Biddison WE, Wiley DC: Two human T cell receptors bind in a similar diagonal mode to the HLA-A2/tax peptide complex using different TCR amino acids. Immunity 8:403, 1998.
    • (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
  • 10
    • 0034660206 scopus 로고    scopus 로고
    • The structure and stability of an HLA-A*0201/octameric tax peptide complex with an empty conserved peptide-N-terminal binding site
    • Khan AR, Baker BM, Ghosh P, Biddison WE, Wiley DC: The structure and stability of an HLA-A*0201/octameric tax peptide complex with an empty conserved peptide-N-terminal binding site. J Immunol 164:6398, 2000.
    • (2000) J Immunol , vol.164 , pp. 6398
    • Khan, A.R.1    Baker, B.M.2    Ghosh, P.3    Biddison, W.E.4    Wiley, D.C.5
  • 11
    • 0035811033 scopus 로고    scopus 로고
    • Antigen presentation subverted: Structure of the human cytomegalovirus protein Us2 bound to the class I molecule HLA-A 2
    • Gewurz BE, Gaudet R, Tortorella D, Wang EW, Ploegh HL, Wiley DC: Antigen presentation subverted: structure of the human cytomegalovirus protein Us2 bound to the class I molecule HLA-A2. Proc Nat Acad Sci USA 98:6794, 2001.
    • (2001) Proc Nat Acad Sci USA , vol.98 , pp. 6794
    • Gewurz, B.E.1    Gaudet, R.2    Tortorella, D.3    Wang, E.W.4    Ploegh, H.L.5    Wiley, D.C.6
  • 12
    • 0026794581 scopus 로고
    • The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggest a general mechanism for tight peptide binding to MHC
    • Madden DR, Gorga JC, Strominger JL, Wiley DC: The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggest a general mechanism for tight peptide binding to MHC. Cell 70:1035, 1992.
    • (1992) Cell , vol.70 , pp. 1035
    • Madden, D.R.1    Gorga, J.C.2    Strominger, J.L.3    Wiley, D.C.4
  • 14
    • 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 285:645, 1999.
    • (1999) J Mol Biol , vol.285 , pp. 645
    • Menssen, R.1    Orth, P.2    Ziegler, A.3    Saenger, W.4
  • 15
    • 0034665104 scopus 로고    scopus 로고
    • Non-standard peptide binding revealed by crystal structures of HLA-B* 5101 complexed with HIV immunodominant epitopes
    • Maenaka K, Maenaka T, Tomiyama H, Takiguchi M, Stuart DI, Jones EY: Non-standard peptide binding revealed by crystal structures of HLA-B*5101 complexed with HIV immunodominant epitopes. J Immunol 165:3260, 2000.
    • (2000) J Immunol , vol.165 , pp. 3260
    • Maenaka, K.1    Maenaka, T.2    Tomiyama, H.3    Takiguchi, M.4    Stuart, D.I.5    Jones, E.Y.6
  • 16
    • 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-B 53
    • Smith KJ, Reid SW, Harlos K, McMichael AJ, Stuart DI, Bell JI, Jones EY: Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53. Immunity 4:215, 1996.
    • (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
  • 17
    • 0034213423 scopus 로고    scopus 로고
    • Structure of an NK cell immunoglobulin-like receptor in complex with its class-I MHC ligand
    • Boyington JC, Motyka SA, Schuck P, Brooks AG, Sun PD: Structure of an NK cell immunoglobulin-like receptor in complex with its class-I MHC ligand. Nature 405:537, 2000.
    • (2000) Nature , vol.405 , pp. 537
    • Boyington, J.C.1    Motyka, S.A.2    Schuck, P.3    Brooks, A.G.4    Sun, P.D.5
  • 18
    • 0035344199 scopus 로고    scopus 로고
    • Crystal structure of the human natural killer cell inhibitory receptor KIR2DL1-HLA-Cw4 complex
    • Fan QR, Long EO, Wiley DC: Crystal structure of the human natural killer cell inhibitory receptor KIR2DL1-HLA-Cw4 complex. Nat Immunol 2:452, 2001.
    • (2001) Nat Immunol , vol.2 , pp. 452
    • Fan, Q.R.1    Long, E.O.2    Wiley, D.C.3
  • 19
    • 0032402264 scopus 로고    scopus 로고
    • Recognition of a novel naturally processed, A2 restricted, HCV-NS4 epitope triggers IFN-gamma release in absence of detectable cytopathicity
    • Alexander J, Del Guercio MF, Fikes JD, Chesnut RW, Chisari FV, Chang KM, Appella E, Sette A: Recognition of a novel naturally processed, A2 restricted, HCV-NS4 epitope triggers IFN-gamma release in absence of detectable cytopathicity. Hum Immunol 59:776, 1998.
    • (1998) Hum Immunol , vol.59 , pp. 776
    • Alexander, J.1    Del Guercio, M.F.2    Fikes, J.D.3    Chesnut, R.W.4    Chisari, F.V.5    Chang, K.M.6    Appella, E.7    Sette, A.8
  • 20
    • 0031937298 scopus 로고    scopus 로고
    • Multi-epitope approach for immunotherapy for cancer: Identification of several CTL epitopes from various tumor-associated antigens expressed on solid epithelial tumors
    • Kawashima I, Hudson SJ, Tsai V, Southwood S, Takesako K, Appella E, Sette A, Celis E: Multi-epitope approach for immunotherapy for cancer: identification of several CTL epitopes from various tumor-associated antigens expressed on solid epithelial tumors. Hum Immunol 59:1, 1998.
    • (1998) Hum Immunol , vol.59 , pp. 1
    • Kawashima, I.1    Hudson, S.J.2    Tsai, V.3    Southwood, S.4    Takesako, K.5    Appella, E.6    Sette, A.7    Celis, E.8
  • 21
    • 0033555410 scopus 로고    scopus 로고
    • Identification of HLA-A3 and HLA-B7-restricted CTL response to hepatitis C virus in patients with acute and chronic hepatitis C
    • Chang KM, Gruener NH, Southwood S, Sidney J, Pape GR, Chisari FV, Sette A: Identification of HLA-A3 and HLA-B7-restricted CTL response to hepatitis C virus in patients with acute and chronic hepatitis C. J Immunol 162:1156, 1999.
    • (1999) J Immunol , vol.162 , pp. 1156
    • Chang, K.M.1    Gruener, N.H.2    Southwood, S.3    Sidney, J.4    Pape, G.R.5    Chisari, F.V.6    Sette, A.7
  • 22
    • 0037461027 scopus 로고    scopus 로고
    • MHCBN: A comprehensive database of MHC binding and non-binding peptides
    • Bashin M, Singh H, Raghava PS: MHCBN: a comprehensive database of MHC binding and non-binding peptides. Bioinformatics 19:665, 2003.
    • (2003) Bioinformatics , vol.19 , pp. 665
    • Bashin, M.1    Singh, H.2    Raghava, P.S.3
  • 23
    • 0036211926 scopus 로고    scopus 로고
    • JenPep: A database of quantitative functional peptide data for immunology
    • Blythe MJ, Doytchinova IA, Flower DR: JenPep: a database of quantitative functional peptide data for immunology. Bioinformatics 18:434, 2002.
    • (2002) Bioinformatics , vol.18 , pp. 434
    • Blythe, M.J.1    Doytchinova, I.A.2    Flower, D.R.3
  • 24
    • 0034603779 scopus 로고    scopus 로고
    • A three-step kinetic mechanism for peptide binding to MHC class II proteins
    • Joshi RV, Zarutskie JA, Stern LJ: A three-step kinetic mechanism for peptide binding to MHC class II proteins. Biochemistry 39:3751, 2000.
    • (2000) Biochemistry , vol.39 , pp. 3751
    • Joshi, R.V.1    Zarutskie, J.A.2    Stern, L.J.3
  • 26
    • 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 SK, Assadi M, Sadegh-Nasseri 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 162:4030, 1999.
    • (1999) J Immunol , vol.162 , pp. 4030
    • Natarajan, S.K.1    Assadi, M.2    Sadegh-Nasseri, S.3
  • 27
    • 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 JC, Townsend AR, Cerundolo V: Fast association rates suggest a conformational change in the MHC class I molecule H-2Db upon peptide binding. Biochemistry 37:3001, 1998.
    • (1998) Biochemistry , vol.37 , pp. 3001
    • Springer, S.1    Doring, K.2    Skipper, J.C.3    Townsend, A.R.4    Cerundolo, V.5
  • 31
    • 0037029674 scopus 로고    scopus 로고
    • Structural comparison of allogeneic and syngeneic T cell receptor-pepride major histocompatibility complex complexes: A buried alloreactive mutation subtly alters peptide presentation substantially increasing V(beta) Interactions
    • Luz JG, Huang M, Garcia KC, Rudolph MG, Apostolopoulos V, Teyton L, Wilson IA: Structural comparison of allogeneic and syngeneic T cell. receptor-pepride major histocompatibility complex complexes: a buried alloreactive mutation subtly alters peptide presentation substantially increasing V(beta) Interactions. J Exp Med 195:1175, 2002.
    • (2002) J Exp Med , vol.195 , pp. 1175
    • Luz, J.G.1    Huang, M.2    Garcia, K.C.3    Rudolph, M.G.4    Apostolopoulos, V.5    Teyton, L.6    Wilson, I.A.7
  • 33
    • 0034329441 scopus 로고    scopus 로고
    • Structure of a covalently stabilized complex of a human alpha beta T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1
    • Hennecke J, Carfi A, Wiley DC: Structure of a covalently stabilized complex of a human alpha beta T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1. EMBO J 19:5611, 2000.
    • (2000) EMBO J , vol.19 , pp. 5611
    • Hennecke, J.1    Carfi, A.2    Wiley, D.C.3
  • 34
    • 0037018102 scopus 로고    scopus 로고
    • Structure of a complex of the human alpha/beta T cell receptor (TCR) Ha17, Influenza hemagglutinin peptide, and major histocompatibility complex class II molecule: HLA-DR4 (DRA*0101 and DRB*10401). Insight into TCR cross-restriction and alloreactivity
    • Hennecke J, Wiley DC: Structure of a complex of the human alpha/beta T cell receptor (TCR) Ha17, Influenza hemagglutinin peptide, and major histocompatibility complex class II molecule: HLA-DR4 (DRA*0101 and DRB*10401). Insight into TCR cross-restriction and alloreactivity. J Exp Med 195:571, 2002.
    • (2002) J Exp Med , vol.195 , pp. 571
    • Hennecke, J.1    Wiley, D.C.2
  • 41
    • 17644444485 scopus 로고    scopus 로고
    • Antibodies to the junctional adhesion molecule cause disruption of endothelial cells and do not prevent leukocyte influx into the meninges after viral or bacterial infection
    • Lechner F, Wong DK, Dunbar PR, Chapman R, Chung RT, Dohrenwend P, Robbins G, Phillips R, Klenerman P, Walker BD: Antibodies to the junctional adhesion molecule cause disruption of endothelial cells and do not prevent leukocyte influx into the meninges after viral or bacterial infection. J Exp Med 191:1499, 2000.
    • (2000) J Exp Med , vol.191 , pp. 1499
    • Lechner, F.1    Wong, D.K.2    Dunbar, P.R.3    Chapman, R.4    Chung, R.T.5    Dohrenwend, P.6    Robbins, G.7    Phillips, R.8    Klenerman, P.9    Walker, B.D.10
  • 43
    • 0035887910 scopus 로고    scopus 로고
    • Differential evolution and stability of epitope specific CD8 (+) T cell responses in EBV infection
    • Catalina MD, Sullivan JL, Bak KR, Luzuriaga K: Differential evolution and stability of epitope specific CD8 (+) T cell responses in EBV infection. J Immunol 167:4450, 2001.
    • (2001) J Immunol , vol.167 , pp. 4450
    • Catalina, M.D.1    Sullivan, J.L.2    Bak, K.R.3    Luzuriaga, K.4
  • 45
    • 0036534769 scopus 로고    scopus 로고
    • Epitope-specific evolution of human CD8(+) T cell responses from primary to persistent phases of Epstein Barr virus infection
    • Hislop AD, Annels NE, Gudgeon NH, Leese AM, Rickinson AB: Epitope-specific evolution of human CD8(+) T cell responses from primary to persistent phases of Epstein Barr virus infection. J Exp Med 195:893, 2002.
    • (2002) J Exp Med , vol.195 , pp. 893
    • Hislop, A.D.1    Annels, N.E.2    Gudgeon, N.H.3    Leese, A.M.4    Rickinson, A.B.5
  • 48
    • 0034672107 scopus 로고    scopus 로고
    • Direct detection and magnetic isolation of Chlamydia trachomatis major outer membrane protein-specific CD8+ CTLs with HLA class I tetramers
    • Kim SK, Devine L, Angevine M, DeMars R, Kavathas PB: Direct detection and magnetic isolation of Chlamydia trachomatis major outer membrane protein-specific CD8+ CTLs with HLA class I tetramers. J Immunol 165:7285, 2000.
    • (2000) J Immunol , vol.165 , pp. 7285
    • Kim, S.K.1    Devine, L.2    Angevine, M.3    DeMars, R.4    Kavathas, P.B.5
  • 49
    • 0034879022 scopus 로고    scopus 로고
    • Ex vivo stimulation and expansion of both CD4(+) and CD8(+) T cells from peripheral blood mononuclear cells of human cytomegalovirus sero-positive blood donors by using a soluble recombinant chimeric protein, IE1-pp65
    • Vaz Santiago J, Lule J, Rohrlich P, Jacquier C, Gibert N, Le Roy E, Betbeder D, Davignon JL, Davrinche C: Ex vivo stimulation and expansion of both CD4(+) and CD8(+) T cells from peripheral blood mononuclear cells of human cytomegalovirus sero-positive blood donors by using a soluble recombinant chimeric protein, IE1-pp65. J Virol 75:7840, 2001.
    • (2001) J Virol , vol.75 , pp. 7840
    • Vaz Santiago, J.1    Lule, J.2    Rohrlich, P.3    Jacquier, C.4    Gibert, N.5    Le Roy, E.6    Betbeder, D.7    Davignon, J.L.8    Davrinche, C.9
  • 51
    • 0032846215 scopus 로고    scopus 로고
    • Longitudinal phenotypic analysis of human immunodeficiency virus type-1 specific cytotoxic T lymphocytes: Correlation with disease progression
    • Ogg GS, Kostense S, Klein MR, Jurriaans S, Hamann D, McMichael AJ, Miedema F: Longitudinal phenotypic analysis of human immunodeficiency virus type-1 specific cytotoxic T lymphocytes: correlation with disease progression. J Virol 73:9153, 1999.
    • (1999) J Virol , vol.73 , pp. 9153
    • Ogg, G.S.1    Kostense, S.2    Klein, M.R.3    Jurriaans, S.4    Hamann, D.5    McMichael, A.J.6    Miedema, F.7
  • 52
    • 0034330698 scopus 로고    scopus 로고
    • Longitudinal phenotypic analysis of human immunodeficiency virus type-1 specific cytotoxic T lymphocytes: Correlation with disease progression
    • Shankar P, Russo M, Harnisch B, Patterson M, Skolnik P, Lieberman J: Longitudinal phenotypic analysis of human immunodeficiency virus type-1 specific cytotoxic T lymphocytes: correlation with disease progression. Blood 96:3094, 2000.
    • (2000) Blood , vol.96 , pp. 3094
    • Shankar, P.1    Russo, M.2    Harnisch, B.3    Patterson, M.4    Skolnik, P.5    Lieberman, J.6
  • 53
    • 0033852737 scopus 로고    scopus 로고
    • Human immunodeficiency virus specific circulating CD8(+) T lymphocytes have down modulated CD3 zeta and CD28, key signaling molecules for T-cell activation
    • Trimble LA, Shankar P, Patterson M, Daily JP, Lieberman J: Human immunodeficiency virus specific circulating CD8(+) T lymphocytes have down modulated CD3 zeta and CD28, key signaling molecules for T-cell activation. J Virol 74:7320, 2000.
    • (2000) J Virol , vol.74 , pp. 7320
    • Trimble, L.A.1    Shankar, P.2    Patterson, M.3    Daily, J.P.4    Lieberman, J.5
  • 58
    • 0035200721 scopus 로고    scopus 로고
    • Visual demonstration of hepatitis C virus specific memory CD8(+) T-cell expansion in patients with acute hepatitis C
    • Sobao Y, Tomiyama H, Nakamura S, Sekihara H, Tanaka K, Takiguchi M: Visual demonstration of hepatitis C virus specific memory CD8(+) T-cell expansion in patients with acute hepatitis C. Hepatology 33:287, 2001.
    • (2001) Hepatology , vol.33 , pp. 287
    • Sobao, Y.1    Tomiyama, H.2    Nakamura, S.3    Sekihara, H.4    Tanaka, K.5    Takiguchi, M.6
  • 63
    • 0014251127 scopus 로고
    • 51Cr labelled allogeneic target cells in vitro: Inhibition by isoantibody and by drugs
    • 51Cr labelled allogeneic target cells in vitro: inhibition by isoantibody and by drugs. Immunology 14:181, 1968.
    • (1968) Immunology , vol.14 , pp. 181
    • Brunner, K.T.1    Mauel, J.2    Cerottini, J.C.3    Chapuis, B.4
  • 64
    • 0016017070 scopus 로고
    • Cell-mediated cytotoxicity, allograft rejection, and tumor immunity
    • Cerottini JC, Brunner KT: Cell-mediated cytotoxicity, allograft rejection, and tumor immunity. Adv Immunol 18:67, 1974.
    • (1974) Adv Immunol , vol.18 , pp. 67
    • Cerottini, J.C.1    Brunner, K.T.2
  • 65
    • 0028077007 scopus 로고
    • Efficient MHC class-I peptide binding is required but does not ensure MHC class-I restricted immunogenicity
    • Feltkamp MC, Vierboom MP, Kast WM, Melief CJ: Efficient MHC class-I peptide binding is required but does not ensure MHC class-I restricted immunogenicity. Mol Immunol 31:1391, 1994.
    • (1994) Mol Immunol , vol.31 , pp. 1391
    • Feltkamp, M.C.1    Vierboom, M.P.2    Kast, W.M.3    Melief, C.J.4
  • 66
  • 67
    • 85030937838 scopus 로고    scopus 로고
    • http.//www.ebi.ac.uk/imgt/hla
  • 69
    • 0026706746 scopus 로고
    • Identification of a motif for HLA-DR1 binding peptides using M13 display libraries
    • Hammer J, Takacs B, Sinigaglia F: Identification of a motif for HLA-DR1 binding peptides using M13 display libraries. J Exp Med 176:1007, 1992.
    • (1992) J Exp Med , vol.176 , pp. 1007
    • Hammer, J.1    Takacs, B.2    Sinigaglia, F.3
  • 70
    • 0027937713 scopus 로고
    • Precise prediction of major histocompatibility complex class II peptide interaction based on peptide side chain scanning
    • Hammer J, Bono E, Gallazzi F, Belunis C, Nagy Z, Sinigaglia F: Precise prediction of major histocompatibility complex class II peptide interaction based on peptide side chain scanning. J Exp Med 180:2353, 1994.
    • (1994) J Exp Med , vol.180 , pp. 2353
    • Hammer, J.1    Bono, E.2    Gallazzi, F.3    Belunis, C.4    Nagy, Z.5    Sinigaglia, F.6
  • 71
    • 0033021020 scopus 로고    scopus 로고
    • Generation of tissue-specific and promiscuous HLA ligand databases using DNA microarrays and virtual HLA class II matrices
    • Sturniolo T, Bono E, Ding J, Raddrizzani L, Tuereci O, Sahin U: Generation of tissue-specific and promiscuous HLA ligand databases using DNA microarrays and virtual HLA class II matrices. Nat Biotechnol 17:555, 1999.
    • (1999) Nat Biotechnol , vol.17 , pp. 555
    • Sturniolo, T.1    Bono, E.2    Ding, J.3    Raddrizzani, L.4    Tuereci, O.5    Sahin, U.6
  • 72
    • 0036137241 scopus 로고    scopus 로고
    • ProPred: Prediction of HLA-DR binding sites
    • Singh H, Raghava GPs: ProPred: prediction of HLA-DR binding sites. Bioinformatics 17:1236, 2001.
    • (2001) Bioinformatics , vol.17 , pp. 1236
    • Singh, H.1    Raghava, G.Ps.2
  • 73
    • 0037606124 scopus 로고    scopus 로고
    • ProPredl: Prediction of promiscuous MHC class-I binding sites
    • Singh H, Raghava GPs: ProPredl: prediction of promiscuous MHC class-I binding sites. Bioinformatics 19:1009, 2003.
    • (2003) Bioinformatics , vol.19 , pp. 1009
    • Singh, H.1    Raghava, G.Ps.2
  • 74
    • 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 152:163, 1994.
    • (1994) J Immunol , vol.152 , pp. 163
    • Parker, K.C.1    Bednarek, M.A.2    Coligan, J.E.3
  • 76
    • 0037245593 scopus 로고    scopus 로고
    • HLA-A3 supermotif defined by quantitative structure-activity relationship analysis
    • Guan PP, Doytchinova IA, Flower DR: HLA-A3 supermotif defined by quantitative structure-activity relationship analysis. Protein Eng 16:11, 2003.
    • (2003) Protein Eng , vol.16 , pp. 11
    • Guan, P.P.1    Doytchinova, I.A.2    Flower, D.R.3
  • 77
    • 0035950043 scopus 로고    scopus 로고
    • Toward the quantitative prediction of T-cell epitopes: coMFA and coMSIA studies of peptides with affinity for the class-I MHC molecule HLA-A*0201
    • Doytchinova IA, Flower DR: Toward the quantitative prediction of T-cell epitopes: coMFA and coMSIA studies of peptides with affinity for the class-I MHC molecule HLA-A*0201. J Med Chem 44:3572, 2001.
    • (2001) J Med Chem , vol.44 , pp. 3572
    • Doytchinova, I.A.1    Flower, D.R.2
  • 78
    • 0036589852 scopus 로고    scopus 로고
    • Additive method for the prediction of protein-peptide binding affinity. Application to the MHC class I molecule HLA-A*0201
    • Doytchinova IA, Blythe MJ, Flower DR: Additive method for the prediction of protein-peptide binding affinity. Application to the MHC class I molecule HLA-A*0201. J Proteome Res 1:263, 2002.
    • (2002) J Proteome Res , vol.1 , pp. 263
    • Doytchinova, I.A.1    Blythe, M.J.2    Flower, D.R.3
  • 79
    • 0031825709 scopus 로고    scopus 로고
    • Prediction of MHC class-II binding peptides using an evolutionary algorithm and artificial neural network
    • Brusic V, Rudy G, Honeyman MC, Hammer J, Harrison LC: Prediction of MHC class-II binding peptides using an evolutionary algorithm and artificial neural network. Bioinformatics 14:121, 1998.
    • (1998) Bioinformatics , vol.14 , pp. 121
    • Brusic, V.1    Rudy, G.2    Honeyman, M.C.3    Hammer, J.4    Harrison, L.C.5
  • 81
    • 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 33:460, 1998.
    • (1998) Proteins , vol.33 , pp. 460
    • Mamitsuka, H.1
  • 82
    • 0142174642 scopus 로고    scopus 로고
    • Prediction of MHC class I binding peptides, using SVMHC
    • Dönnes P, Elofsson A: Prediction of MHC class I binding peptides, using SVMHC. BMC Bioinformatics 3:25, 2002.
    • (2002) BMC Bioinformatics , vol.3 , pp. 25
    • Dönnes, P.1    Elofsson, A.2
  • 83
    • 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 3:549, 1998.
    • (1998) Fold Des , vol.3 , pp. 549
    • Schueler-Furman, O.1    Elber, R.2    Margalit, H.3
  • 84
    • 0033820208 scopus 로고    scopus 로고
    • Structure-based prediction of binding peptides to MHC class I molecules: Application to a broad range of MHC alleles
    • Schueler-Furman O, Altuvia Y, Sette A, Margalit H: Structure-based prediction of binding peptides to MHC class I molecules: application to a broad range of MHC alleles. Protein Sci 9:1838, 2000.
    • (2000) Protein Sci , vol.9 , pp. 1838
    • Schueler-Furman, O.1    Altuvia, Y.2    Sette, A.3    Margalit, H.4
  • 85
    • 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 SL, 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 42:4650, 1999.
    • (1999) J Med Chem , vol.42 , pp. 4650
    • Rognan, D.1    Lauemoller, S.L.2    Holm, A.3    Buus, S.4    Tschinke, V.5
  • 87
    • 0029159753 scopus 로고
    • A general model of invariant chain association with class II major histocompatibility complex proteins
    • Lee C, McConnell HM: A general model of invariant chain association with class II major histocompatibility complex proteins. Proc Natl Acad Sci USA 92:8269, 1995.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8269
    • Lee, C.1    McConnell, H.M.2
  • 88
    • 0029018773 scopus 로고
    • Ranking potential binding peptides to MHC molecules by a computational threading approach
    • Altuvia Y, Schueler O, Margalit H: Ranking potential binding peptides to MHC molecules by a computational threading approach. J Mol Biol 249:244, 1995.
    • (1995) J Mol Biol , vol.249 , pp. 244
    • Altuvia, Y.1    Schueler, O.2    Margalit, H.3
  • 89
    • 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 58:1, 1997.
    • (1997) Hum Immunol , vol.58 , pp. 1
    • Altuvia, Y.1    Sette, A.2    Sidney, J.3    Southwood, S.4    Margalit, H.5
  • 90
    • 0028135684 scopus 로고
    • Molecular dynamics simulation of MHC-peptide complexes as a tool for predicting potential T cell epitopes
    • Rognan D, Scapozza L, Folkers G, Daser A: Molecular dynamics simulation of MHC-peptide complexes as a tool for predicting potential T cell epitopes. Biochemistry 33:11476, 1994.
    • (1994) Biochemistry , vol.33 , pp. 11476
    • Rognan, D.1    Scapozza, L.2    Folkers, G.3    Daser, A.4
  • 92
    • 0031576355 scopus 로고    scopus 로고
    • Do aligned sequences share the same fold?
    • Abagyan RA, Batalov S: Do aligned sequences share the same fold? J Mol Biol 273:355, 1997.
    • (1997) J Mol Biol , vol.273 , pp. 355
    • Abagyan, R.A.1    Batalov, S.2
  • 93
    • 34248398449 scopus 로고    scopus 로고
    • Types of inter-atomic interactions at the MHC-peptide interface: Identifying commonality from accumulated data
    • Adrian P, Rajaseger G, Mathura V, Sakharkar M, Kangueane P: Types of inter-atomic interactions at the MHC-peptide interface: identifying commonality from accumulated data. BMC Struct Biol 2:2, 2002.
    • (2002) BMC Struct Biol , vol.2 , pp. 2
    • Adrian, P.1    Rajaseger, G.2    Mathura, V.3    Sakharkar, M.4    Kangueane, P.5
  • 94
    • 33845377127 scopus 로고
    • Estimation of effective interresidue contact energies from protein crystal structure, quasi-chemical approximation
    • Miyazawa S, Jernigan RL: Estimation of effective interresidue contact energies from protein crystal structure, quasi-chemical approximation. Macromolecules 18:534, 1985.
    • (1985) Macromolecules , vol.18 , pp. 534
    • Miyazawa, S.1    Jernigan, R.L.2
  • 95
    • 0029919190 scopus 로고    scopus 로고
    • Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading
    • Miyazawa S, Jernigan RL: Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading. J Mol Biol 256:623, 1996.
    • (1996) J Mol Biol , vol.256 , pp. 623
    • Miyazawa, S.1    Jernigan, R.L.2
  • 96
    • 0037314055 scopus 로고    scopus 로고
    • MPID: MHC-peptide interaction database for sequence structure function information on peptides binding to MHC molecules
    • Govindarajan KR, Kangueane P, Tan TW, Ranganathan S: MPID: MHC-peptide interaction database for sequence structure function information on peptides binding to MHC molecules. Bioinformatics 19:309, 2003.
    • (2003) Bioinformatics , vol.19 , pp. 309
    • Govindarajan, K.R.1    Kangueane, P.2    Tan, T.W.3    Ranganathan, S.4
  • 97
    • 0033980451 scopus 로고    scopus 로고
    • Molecular modeling of the minor histocompatibility antigen HA-1 peptides binding to HLA-A alleles
    • Ren EC, Kangueane P, Kolatkar P, Lin MT, Tseng LH, Hansen JA: Molecular modeling of the minor histocompatibility antigen HA-1 peptides binding to HLA-A alleles. Tissue Antigens 55:24, 2000.
    • (2000) Tissue Antigens , vol.55 , pp. 24
    • Ren, E.C.1    Kangueane, P.2    Kolatkar, P.3    Lin, M.T.4    Tseng, L.H.5    Hansen, J.A.6
  • 99
    • 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 45:15, 1996.
    • (1996) Immunogenetics , vol.45 , pp. 15
    • Chelvanayagam, G.1
  • 100
    • 0031409658 scopus 로고    scopus 로고
    • A roadmap for HLA-DR peptide binding specificities
    • Chelvanayagam G: A roadmap for HLA-DR peptide binding specificities. Hum Immunol 58:61, 1997.
    • (1997) Hum Immunol , vol.58 , pp. 61
    • Chelvanayagam, G.1
  • 101
    • 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 281:929, 1998.
    • (1998) J Mol Biol , vol.281 , pp. 929
    • Zhang, C.1    Anderson, A.2    DeLisi, C.3
  • 102
    • 0035789124 scopus 로고    scopus 로고
    • New quantitative descriptor of amino acids based on multi-dimensional scaling of a large number of physical-chemical properties
    • Venkatarajan MS, Braun W: New quantitative descriptor of amino acids based on multi-dimensional scaling of a large number of physical-chemical properties. J Mol Model 7:445, 2001.
    • (2001) J Mol Model , vol.7 , pp. 445
    • Venkatarajan, M.S.1    Braun, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.