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Volumn 7, Issue , 2006, Pages

EpiJen: A server for multistep T cell epitope prediction

Author keywords

[No Author keywords available]

Indexed keywords

DIFFERENT PROPORTIONS; ENDOPLASMIC RETICULUM; EPITOPE PREDICTIONS; IDENTIFICATION METHOD; INTEGRATED APPROACH; INTEGRATED METHOD; QUANTITATIVE MATRICES; TRANSPORTER ASSOCIATED WITH ANTIGEN PROCESSING (TAP);

EID: 33645472169     PISSN: 14712105     EISSN: 14712105     Source Type: Journal    
DOI: 10.1186/1471-2105-7-131     Document Type: Article
Times cited : (148)

References (94)
  • 2
    • 0030886208 scopus 로고    scopus 로고
    • Two distinct proteolytic processes in the generation of a major histocompatibility complex class I-presented peptide
    • Craiu A, Akopian T, Goldberg A, Rock KL: Two distinct proteolytic processes in the generation of a major histocompatibility complex class I-presented peptide. Proc Natl Acad Sci USA 1997, 94:10850-10855.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10850-10855
    • Craiu, A.1    Akopian, T.2    Goldberg, A.3    Rock, K.L.4
  • 3
    • 0033486008 scopus 로고    scopus 로고
    • Distinct proteolytic processes generate the C and N termini of MHC class I-binding peptides
    • Mo XY, Cascio P, Lemerise K, Goldberg AL, Rock K: Distinct proteolytic processes generate the C and N termini of MHC class I-binding peptides. J Immunol 1999, 163:5851-5859.
    • (1999) J Immunol , vol.163 , pp. 5851-5859
    • Mo, X.Y.1    Cascio, P.2    Lemerise, K.3    Goldberg, A.L.4    Rock, K.5
  • 4
    • 0033561553 scopus 로고    scopus 로고
    • Specific proteolytic cleavages limit the diversity of the pool of peptides available to MHC class I molecules in living cells
    • Serwold T, Shastri N: Specific proteolytic cleavages limit the diversity of the pool of peptides available to MHC class I molecules in living cells. J Immunol 1999, 162:4712-4719.
    • (1999) J Immunol , vol.162 , pp. 4712-4719
    • Serwold, T.1    Shastri, N.2
  • 5
    • 0035873704 scopus 로고    scopus 로고
    • 26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide
    • Cascio P, Hilton C, Kisselev AF, Rock KL, Goldberg AL: 26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide. EMBO J 2001, 20:2357-2366.
    • (2001) EMBO J , vol.20 , pp. 2357-2366
    • Cascio, P.1    Hilton, C.2    Kisselev, A.F.3    Rock, K.L.4    Goldberg, A.L.5
  • 6
    • 0024351497 scopus 로고
    • Pituitary multicatalytic proteinase complex. Specificity of components and aspects of proteolitic activity
    • Orlowski M, Michaud C: Pituitary multicatalytic proteinase complex. Specificity of components and aspects of proteolitic activity. Biochemistry 1989, 28:9270-9278.
    • (1989) Biochemistry , vol.28 , pp. 9270-9278
    • Orlowski, M.1    Michaud, C.2
  • 7
    • 0026649077 scopus 로고
    • Use of serine-protease inhibitors as probes for the different proteolytic activities of the rat liver multicatalitic proteinase complex
    • Djaballah H, Harness JA, Savory PJ, Rivett AJ: Use of serine-protease inhibitors as probes for the different proteolytic activities of the rat liver multicatalitic proteinase complex. Eur J Biochem 1992, 209:629-634.
    • (1992) Eur J Biochem , vol.209 , pp. 629-634
    • Djaballah, H.1    Harness, J.A.2    Savory, P.J.3    Rivett, A.J.4
  • 8
    • 0027410433 scopus 로고
    • Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two components cleaving bonds on the carboxy side of branched chain and small neutral amino acids
    • Orlowski M, Cardozo C, Michaud C: Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two components cleaving bonds on the carboxy side of branched chain and small neutral amino acids. Biochemistry 1993, 32:1563-1572.
    • (1993) Biochemistry , vol.32 , pp. 1563-1572
    • Orlowski, M.1    Cardozo, C.2    Michaud, C.3
  • 9
    • 0031819536 scopus 로고    scopus 로고
    • The MHC class I ligand-generating system: Roles of immunoproteasomes and the interferon-γ-inducible proteasome activator PA28
    • Tanaka K, Kasahara M: The MHC class I ligand-generating system: roles of immunoproteasomes and the interferon-γ-inducible proteasome activator PA28. Immunol Rev 1998, 163:161-176.
    • (1998) Immunol Rev , vol.163 , pp. 161-176
    • Tanaka, K.1    Kasahara, M.2
  • 10
    • 0035314002 scopus 로고    scopus 로고
    • Differential processing of class-I-restricted epitopes by the standard proteasome and the immunoproteasome
    • Van den Eynde BJ, Morel S: Differential processing of class-I-restricted epitopes by the standard proteasome and the immunoproteasome. Curr Opin Immunol 2001, 13:147-153.
    • (2001) Curr Opin Immunol , vol.13 , pp. 147-153
    • Van den Eynde, B.J.1    Morel, S.2
  • 13
    • 0025646826 scopus 로고
    • Transport protein genes in the murine MHC - Possible implications for antigen processing
    • Monaco J, Cho S, Attaya M: Transport protein genes in the murine MHC - possible implications for antigen processing. Science 1990, 250:1723-1726.
    • (1990) Science , vol.250 , pp. 1723-1726
    • Monaco, J.1    Cho, S.2    Attaya, M.3
  • 14
    • 0028110959 scopus 로고
    • Functional expression and purification of the ABC transporter complex associated with antigen processing (TAP) in insect cells
    • Meyer TH, van Endert PM, Uebel S, Ehring B, Tampé R: Functional expression and purification of the ABC transporter complex associated with antigen processing (TAP) in insect cells. FEBS Lett 1994, 351:443-447.
    • (1994) FEBS Lett , vol.351 , pp. 443-447
    • Meyer, T.H.1    van Endert, P.M.2    Uebel, S.3    Ehring, B.4    Tampé, R.5
  • 15
    • 0028150053 scopus 로고
    • Nucleotide binding to the hydrophilic C-terminal domain of the transporter associated with antigen processing (TAP)
    • Müller KM, Ebensperger C, Tampé R: Nucleotide binding to the hydrophilic C-terminal domain of the transporter associated with antigen processing (TAP). J Biol Chem 1994, 269:14032-14037.
    • (1994) J Biol Chem , vol.269 , pp. 14032-14037
    • Müller, K.M.1    Ebensperger, C.2    Tampé, R.3
  • 17
    • 0037386520 scopus 로고    scopus 로고
    • TAP-independent antigen presentation on MHC class I molecules: Lessons from Epstein-Barr virus
    • Lautscham G, Rickinson A, Blake N: TAP-independent antigen presentation on MHC class I molecules: lessons from Epstein-Barr virus. Microbes Infect 2003, 5:291-299.
    • (2003) Microbes Infect , vol.5 , pp. 291-299
    • Lautscham, G.1    Rickinson, A.2    Blake, N.3
  • 22
    • 0028130237 scopus 로고
    • T cell recognition of an HLA-A2-restricted epitope derived from a cleaved signal sequence
    • Guéguen M, Biddison W, Long EO: T cell recognition of an HLA-A2-restricted epitope derived from a cleaved signal sequence. J Exp Med 1994, 180:1989-1994.
    • (1994) J Exp Med , vol.180 , pp. 1989-1994
    • Guéguen, M.1    Biddison, W.2    Long, E.O.3
  • 23
    • 0029967745 scopus 로고    scopus 로고
    • Peptide-dependent expression of HLA-B7 on antigen processing-deficient T2 cells
    • Smith KD, Lutz CT: Peptide-dependent expression of HLA-B7 on antigen processing-deficient T2 cells. J Immunol 1996, 156:3755-3764.
    • (1996) J Immunol , vol.156 , pp. 3755-3764
    • Smith, K.D.1    Lutz, C.T.2
  • 24
    • 0030013725 scopus 로고    scopus 로고
    • Peptide transporter (TAP-1 and TAP-2)-independent endogenous processing of Epstein-Barr virus (EBV) latent membrane protein 2A: Implications for cytotoxic T-lymphocyte control of EBV-associated malignancies
    • Khanna R, Burrows SR, Moss DJ, Silins SL: Peptide transporter (TAP-1 and TAP-2)-independent endogenous processing of Epstein-Barr virus (EBV) latent membrane protein 2A: implications for cytotoxic T-lymphocyte control of EBV-associated malignancies. J Virol 1996, 70:5357-5362.
    • (1996) J Virol , vol.70 , pp. 5357-5362
    • Khanna, R.1    Burrows, S.R.2    Moss, D.J.3    Silins, S.L.4
  • 26
    • 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, 219:277-319.
    • (1991) J Mol Biol , vol.219 , pp. 277-319
    • Saper, M.A.1    Bjorkman, P.J.2    Wiley, D.C.3
  • 27
    • 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 KJ, Reid SW, Harlos K, McMichael AJ, Stuard 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 1996, 4:215-228.
    • (1996) Immunity , vol.4 , pp. 215-228
    • Smith, K.J.1    Reid, S.W.2    Harlos, K.3    McMichael, A.J.4    Stuard, D.I.5    Bell, J.I.6    Jones, E.Y.7
  • 28
    • 0033526774 scopus 로고    scopus 로고
    • Structure of human histocompatibility leukocyte antigen (HLA)-Cw4, a ligand for the KIR2D natural killer cell inhibitory receptor
    • Fan QR, Wiley DC: Structure of human histocompatibility leukocyte antigen (HLA)-Cw4, a ligand for the KIR2D natural killer cell inhibitory receptor. J Exp Med 1999, 190:113-123.
    • (1999) J Exp Med , vol.190 , pp. 113-123
    • Fan, Q.R.1    Wiley, D.C.2
  • 29
    • 0344309217 scopus 로고    scopus 로고
    • Towards in silico prediction of immunogenic epitopes
    • Flower DR: Towards in silico prediction of immunogenic epitopes. Trends Immunol 2003, 24:667-674.
    • (2003) Trends Immunol , vol.24 , pp. 667-674
    • Flower, D.R.1
  • 30
    • 0036777957 scopus 로고    scopus 로고
    • The importance of the proteasome and subsequent proteolitic steps in the generation of antigenic peptides
    • Golgberg AL, Cascio P, Saric T, Rock KL: The importance of the proteasome and subsequent proteolitic steps in the generation of antigenic peptides. Mol Immunol 2002, 39:147-164.
    • (2002) Mol Immunol , vol.39 , pp. 147-164
    • Golgberg, A.L.1    Cascio, P.2    Saric, T.3    Rock, K.L.4
  • 31
    • 0035500466 scopus 로고    scopus 로고
    • Combining computer algorithms with experimental approaches permits the rapid and accurate identification of T cell epitopes from defined antigens
    • Schirle M, Weinschenk T, Stevanović S: Combining computer algorithms with experimental approaches permits the rapid and accurate identification of T cell epitopes from defined antigens. J Immunol Methods 2001, 257:1-16.
    • (2001) J Immunol Methods , vol.257 , pp. 1-16
    • Schirle, M.1    Weinschenk, T.2    Stevanović, S.3
  • 32
    • 2542477111 scopus 로고
    • T-cell antigenic sites tend to be amphipathic structures
    • DeLisi C, Berzofski JA: T-cell antigenic sites tend to be amphipathic structures. Proc Natl Acad Sci USA 1985, 82:7048-7052.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 7048-7052
    • DeLisi, C.1    Berzofski, J.A.2
  • 33
    • 0023779206 scopus 로고
    • A sequence pattern common to T cell epitopes
    • Rothbard JB, Taylor WR: A sequence pattern common to T cell epitopes. EMBO J 1988, 7:93-100.
    • (1988) EMBO J , vol.7 , pp. 93-100
    • Rothbard, J.B.1    Taylor, W.R.2
  • 34
    • 0029066338 scopus 로고
    • Two novel T cell epitope prediction algorithms based on MHC-binding motifs; comparison of predicted and published epitopes from Mycobacterium tuberculosis and HIV protein sequences
    • Meister GE, Roberts CG, Berzofsky JA, De Groot AS: Two novel T cell epitope prediction algorithms based on MHC-binding motifs; comparison of predicted and published epitopes from Mycobacterium tuberculosis and HIV protein sequences. Vaccine 1995, 13:581-591.
    • (1995) Vaccine , vol.13 , pp. 581-591
    • Meister, G.E.1    Roberts, C.G.2    Berzofsky, J.A.3    De Groot, A.S.4
  • 35
    • 0029939229 scopus 로고    scopus 로고
    • Statistical comparison of established T cell epitope predictors against a large database of human and murine antigens
    • Deavin AJ, Auton TR, Greaney PJ: Statistical comparison of established T cell epitope predictors against a large database of human and murine antigens. Mol Immunol 1996, 33:145-155.
    • (1996) Mol Immunol , vol.33 , pp. 145-155
    • Deavin, A.J.1    Auton, T.R.2    Greaney, P.J.3
  • 39
    • 0036727207 scopus 로고    scopus 로고
    • Prediction of MHC class I binding peptides using profile motifs
    • Reche PA, Glutting JP, Reinherz EL: Prediction of MHC class I binding peptides using profile motifs. Hum Immunol 2002, 63:701-709.
    • (2002) Hum Immunol , vol.63 , pp. 701-709
    • Reche, P.A.1    Glutting, J.P.2    Reinherz, E.L.3
  • 40
    • 5444249860 scopus 로고    scopus 로고
    • Enhancement to the RANK-PEP resource for the prediction of peptide binding to MHC molecules using profiles
    • Reche PA, Glutting JP, Reinherz EL: Enhancement to the RANK-PEP resource for the prediction of peptide binding to MHC molecules using profiles. Immunogenetics 2004, 56:405-419.
    • (2004) Immunogenetics , vol.56 , pp. 405-419
    • Reche, P.A.1    Glutting, J.P.2    Reinherz, E.L.3
  • 42
    • 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 2002, 1:263-272.
    • (2002) J Proteome Res , vol.1 , pp. 263-272
    • Doytchinova, I.A.1    Blythe, M.J.2    Flower, D.R.3
  • 43
    • 0344360732 scopus 로고    scopus 로고
    • Towards the in silico identification of class II restricted T cell epitopes: A partial least squares iterative self-consistent algorithm for affinity prediction
    • Doytchinova IA, Flower DR: Towards the in silico identification of class II restricted T cell epitopes: a partial least squares iterative self-consistent algorithm for affinity prediction. Bioinformatics 2003, 19:2263-2270.
    • (2003) Bioinformatics , vol.19 , pp. 2263-2270
    • Doytchinova, I.A.1    Flower, D.R.2
  • 44
    • 0027552389 scopus 로고
    • Using a neutral network to identify potential HLA-DRI binding sites within proteins
    • Bisset LR, Fierz W: Using a neutral network to identify potential HLA-DRI binding sites within proteins. J Mol Recognit 1993, 6:41-48.
    • (1993) J Mol Recognit , vol.6 , pp. 41-48
    • Bisset, L.R.1    Fierz, W.2
  • 45
    • 0035226804 scopus 로고    scopus 로고
    • Neural network method for predicting peptides that bind major histocompatibility complex molecules
    • Gulukota K, DeLisi C: Neural network method for predicting peptides that bind major histocompatibility complex molecules. Methods Mol Biol 2001, 156:201-209.
    • (2001) Methods Mol Biol , vol.156 , pp. 201-209
    • Gulukota, K.1    DeLisi, C.2
  • 47
    • 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 G, Hammer J, Harrison L: Prediction of MHC class II-binding peptides using an evolutionary algorithm and artificial neural network. Bioinformatics 1998, 14:121-130.
    • (1998) Bioinformatics , vol.14 , pp. 121-130
    • Brusic, V.1    Rudy, G.2    Honeyman, G.3    Hammer, J.4    Harrison, L.5
  • 48
    • 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 1999, 42:4650-4658.
    • (1999) J Med Chem , vol.42 , pp. 4650-4658
    • Rognan, D.1    Lauemoller, S.L.2    Holm, A.3    Buus, S.4    Tschinke, V.5
  • 49
    • 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 1995, 249:244-250.
    • (1995) J Mol Biol , vol.249 , pp. 244-250
    • Altuvia, Y.1    Schueler, O.2    Margalit, H.3
  • 50
    • 0035950043 scopus 로고    scopus 로고
    • Towards the quantitative prediction of T-cell epitopes: CoMFA and CoMSIA studies of peptides with affinity to class I MHC molecule HLA-A*0201
    • Doytchinova I, Flower DR: Towards the quantitative prediction of T-cell epitopes: CoMFA and CoMSIA studies of peptides with affinity to class I MHC molecule HLA-A*0201. J Med Chem 2001, 44:3572-3581.
    • (2001) J Med Chem , vol.44 , pp. 3572-3581
    • Doytchinova, I.1    Flower, D.R.2
  • 51
    • 0036706875 scopus 로고    scopus 로고
    • A Comparative Molecular Similarity Index Analysis (CoMSIA) study identifies an HLA-A2 binding supermotif
    • Doytchinova IA, Flower DR: A Comparative Molecular Similarity Index Analysis (CoMSIA) study identifies an HLA-A2 binding supermotif. J Comput-Aid Mol Des 2002, 16:535-544.
    • (2002) J Comput-Aid Mol Des , vol.16 , pp. 535-544
    • Doytchinova, I.A.1    Flower, D.R.2
  • 52
    • 0037245593 scopus 로고    scopus 로고
    • HLA-A3-supermotif defined by quantitative structure-activity relationship analysis
    • Guan P, Doytchinova IA, Flower DR: HLA-A3-supermotif defined by quantitative structure-activity relationship analysis. Protein Eng 2003, 16:11-18.
    • (2003) Protein Eng , vol.16 , pp. 11-18
    • Guan, P.1    Doytchinova, I.A.2    Flower, D.R.3
  • 53
    • 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 2002, 3:25.
    • (2002) BMC Bioinformatics , vol.3 , pp. 25
    • Dönnes, P.1    Elofsson, A.2
  • 54
    • 0142148183 scopus 로고    scopus 로고
    • Application of support vector machines for T-cell epitope predictions
    • Zhao Y, Pinilla C, Valmori D, Martin R, Simon R: Application of support vector machines for T-cell epitope predictions. Bioinformatics 2003, 19:1978-1984.
    • (2003) Bioinformatics , vol.19 , pp. 1978-1984
    • Zhao, Y.1    Pinilla, C.2    Valmori, D.3    Martin, R.4    Simon, R.5
  • 55
    • 0345291184 scopus 로고    scopus 로고
    • A theoretical approach towards the identification of cleavage-determining amino acid motifs of the 20S proteasome
    • Holzhutter HG, Frommel C, Kloetzel PM: A theoretical approach towards the identification of cleavage-determining amino acid motifs of the 20S proteasome. J Mol Biol 1999, 286:1251-1265.
    • (1999) J Mol Biol , vol.286 , pp. 1251-1265
    • Holzhutter, H.G.1    Frommel, C.2    Kloetzel, P.M.3
  • 58
    • 0029148985 scopus 로고
    • Requirements for peptide binding to the human transporter associated with antigen processing revealed by peptide scans and complex peptide libraries
    • Uebel S, Meyer TH, Kraas W, Kienle S, Jung G, Wiesmüller KH, Tampé R: Requirements for peptide binding to the human transporter associated with antigen processing revealed by peptide scans and complex peptide libraries. J Biol Chem 1995, 270:18512-18516.
    • (1995) J Biol Chem , vol.270 , pp. 18512-18516
    • Uebel, S.1    Meyer, T.H.2    Kraas, W.3    Kienle, S.4    Jung, G.5    Wiesmüller, K.H.6    Tampé, R.7
  • 60
    • 0041589474 scopus 로고    scopus 로고
    • Identifying MHC class I epitopes by predicting the TAP transport efficiency of epitope precursors
    • Peters B, Bulik S, Tampé R, van Endert PM, Holzhütter HG: Identifying MHC class I epitopes by predicting the TAP transport efficiency of epitope precursors. J Immunol 2003, 171:1741-1749.
    • (2003) J Immunol , vol.171 , pp. 1741-1749
    • Peters, B.1    Bulik, S.2    Tampé, R.3    van Endert, P.M.4    Holzhütter, H.G.5
  • 61
    • 1342268087 scopus 로고    scopus 로고
    • Analysis and prediction of affinity of TAP binding peptides using cascade SVM
    • Bhasin M, Raghava GPS: Analysis and prediction of affinity of TAP binding peptides using cascade SVM. Protein Sci 2004, 13:596-607.
    • (2004) Protein Sci , vol.13 , pp. 596-607
    • Bhasin, M.1    Raghava, G.P.S.2
  • 64
    • 25444476693 scopus 로고    scopus 로고
    • Generating quantitative models describing the sequence specificity of biological process with the stabilized matrix method
    • Peters B, Sette A: Generating quantitative models describing the sequence specificity of biological process with the stabilized matrix method. BMC Bioinformatics 2005, 6:132 [http://www.mhc-pathway.net].
    • (2005) BMC Bioinformatics , vol.6 , pp. 132
    • Peters, B.1    Sette, A.2
  • 65
    • 23844528191 scopus 로고    scopus 로고
    • An integrative approach to CTL epitope prediction: A combined algorithm integrating MHC class I binding, TAP transport efficiency, and proteasomal cleavage predictions
    • Larsen MV, Lundegaard C, Lamberth K, Buus S, Brunak S, Lund O, Nielsen M: An integrative approach to CTL epitope prediction: A combined algorithm integrating MHC class I binding, TAP transport efficiency, and proteasomal cleavage predictions. Eur J Immunol 2005, 35:2295-2303 [http://www.cbs.dtu.dk/services/NetCTL].
    • (2005) Eur J Immunol , vol.35 , pp. 2295-2303
    • Larsen, M.V.1    Lundegaard, C.2    Lamberth, K.3    Buus, S.4    Brunak, S.5    Lund, O.6    Nielsen, M.7
  • 66
    • 23644443226 scopus 로고    scopus 로고
    • Integrated modeling of the major events in the MHC class I antigen processing pathway
    • Dönnes P, Kohlbacher O: Integrated modeling of the major events in the MHC class I antigen processing pathway. Protein Sci 2005, 14:2132-2140 [http://www-bs.informatik.uni-tuebingen.de/WAPP].
    • (2005) Protein Sci , vol.14 , pp. 2132-2140
    • Dönnes, P.1    Kohlbacher, O.2
  • 68
    • 2942627444 scopus 로고    scopus 로고
    • Coupling in silico and in vitro analysis of peptide-MHC binding: A Bioinformatic approach enabling prediction of superbinding peptides and anchorless epitopes
    • Doytchinova IA, Walshe VA, Jones NA, Gloster SE, Borrow P, Flower DR: Coupling in silico and in vitro analysis of peptide-MHC binding: A Bioinformatic approach enabling prediction of superbinding peptides and anchorless epitopes. J Immunol 2004, 172:7495-7502.
    • (2004) J Immunol , vol.172 , pp. 7495-7502
    • Doytchinova, I.A.1    Walshe, V.A.2    Jones, N.A.3    Gloster, S.E.4    Borrow, P.5    Flower, D.R.6
  • 69
    • 9144231300 scopus 로고    scopus 로고
    • Transporter associated with antigen processing preselection of peptides binding to the MHC: A Bioinformatic evaluation
    • Doytchinova IA, Hemsley S, Flower DR: Transporter associated with antigen processing preselection of peptides binding to the MHC: A Bioinformatic evaluation. J Immunol 2004, 173:6813-6819.
    • (2004) J Immunol , vol.173 , pp. 6813-6819
    • Doytchinova, I.A.1    Hemsley, S.2    Flower, D.R.3
  • 70
    • 33645636041 scopus 로고    scopus 로고
    • Class I T cell epitope prediction: Improvements using a combination of Proteasome cleavage, TAP affinity, and MHC binding
    • in press
    • Doytchinova IA, Flower DR: Class I T cell epitope prediction: improvements using a combination of Proteasome cleavage, TAP affinity, and MHC binding. Mol Immun 2006 in press.
    • (2006) Mol Immun
    • Doytchinova, I.A.1    Flower, D.R.2
  • 71
    • 84886765482 scopus 로고    scopus 로고
    • EpiJen server for T cell epitope prediction
    • EpiJen server for T cell epitope prediction [http;//www.jenner.ac.uk/ EpiJen].
  • 72
    • 0141507084 scopus 로고    scopus 로고
    • The HLA-A2-supermotif: A QSAR definition
    • Doytchinova IA, Flower DR: The HLA-A2-supermotif: A QSAR definition. Org & Biomol Chem 2003, 1:2648-2654.
    • (2003) Org & Biomol Chem , vol.1 , pp. 2648-2654
    • Doytchinova, I.A.1    Flower, D.R.2
  • 74
    • 33947485697 scopus 로고
    • A mathematical contribution to structure - Activity studies
    • Free SM Jr, Wilson JW: A mathematical contribution to structure - activity studies. J Med Chem 1964, 53:395-399.
    • (1964) J Med Chem , vol.53 , pp. 395-399
    • Free Jr., S.M.1    Wilson, J.W.2
  • 76
    • 0031570893 scopus 로고    scopus 로고
    • The generation of MHC class I-associated peptides is only partially inhibited by proteasome inhibitors: Involvement of nonproteasomal cytosolic proteases in antigen processing
    • Vinitsky A, Anton LC, Snyder HL, Orlowski M, Bennink JR, Yewdell JW: The generation of MHC class I-associated peptides is only partially inhibited by proteasome inhibitors: involvement of nonproteasomal cytosolic proteases in antigen processing. J Immunol 1997, 159:554-564.
    • (1997) J Immunol , vol.159 , pp. 554-564
    • Vinitsky, A.1    Anton, L.C.2    Snyder, H.L.3    Orlowski, M.4    Bennink, J.R.5    Yewdell, J.W.6
  • 80
    • 0032563221 scopus 로고    scopus 로고
    • Interferon-gamma can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase
    • Beninga J, Rock KL, Goldberg AL: Interferon-gamma can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase. J Biol Chem 1998, 273:18734-18742.
    • (1998) J Biol Chem , vol.273 , pp. 18734-18742
    • Beninga, J.1    Rock, K.L.2    Goldberg, A.L.3
  • 82
    • 0037015624 scopus 로고    scopus 로고
    • ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum
    • Serwold T, Gonzalez F, Kim J, Jacob R, Shastri N: ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum. Nature 2002, 419:480-483.
    • (2002) Nature , vol.419 , pp. 480-483
    • Serwold, T.1    Gonzalez, F.2    Kim, J.3    Jacob, R.4    Shastri, N.5
  • 84
    • 0036884090 scopus 로고    scopus 로고
    • The ER aminopeptidase ERAPI enhances or limits antigen presentation by trimming epitopes to 8-9 residues
    • York IA, Chang S-C, Saric T, Keys JA, Favreau JM, Goldberg AL, Rock KL: The ER aminopeptidase ERAPI enhances or limits antigen presentation by trimming epitopes to 8-9 residues. Nat Immunol 2002, 3:1177-1184.
    • (2002) Nat Immunol , vol.3 , pp. 1177-1184
    • York, I.A.1    Chang, S.-C.2    Saric, T.3    Keys, J.A.4    Favreau, J.M.5    Goldberg, A.L.6    Rock, K.L.7
  • 85
    • 1142269466 scopus 로고    scopus 로고
    • Immune recognition of a human renal cancer antigen through post-translational protein splicing
    • Hanada K, Yewdell JW, Yang JC: Immune recognition of a human renal cancer antigen through post-translational protein splicing. Nature 2004, 427:252-256.
    • (2004) Nature , vol.427 , pp. 252-256
    • Hanada, K.1    Yewdell, J.W.2    Yang, J.C.3
  • 88
    • 33645473696 scopus 로고    scopus 로고
    • SYBYL 6.9. Tripos Inc., St. Louis
    • SYBYL 6.9. Tripos Inc., St. Louis; 2004.
    • (2004)
  • 89
    • 0031191630 scopus 로고    scopus 로고
    • The use of the area under the ROC curve in the evaluation of machine learning algorithms
    • Bradley AP: The use of the area under the ROC curve in the evaluation of machine learning algorithms. Pattern Recognition 1997, 30:1145-1159.
    • (1997) Pattern Recognition , vol.30 , pp. 1145-1159
    • Bradley, A.P.1
  • 90
    • 33751392117 scopus 로고
    • Clustering of chemical structures on the basis of two-dimensional similarity measures
    • Barnard JM, Downs GM: Clustering of chemical structures on the basis of two-dimensional similarity measures. J Chem Inf Comput Sci 1992, 32:644-649.
    • (1992) J Chem Inf Comput Sci , vol.32 , pp. 644-649
    • Barnard, J.M.1    Downs, G.M.2
  • 91
    • 0342645323 scopus 로고    scopus 로고
    • Use of structure-activity data to compare structure-based clustering methods and descriptors for use in compound selection
    • Brown RD, Martin YC: Use of structure-activity data to compare structure-based clustering methods and descriptors for use in compound selection. J Chem Inf Comput Sci 1996, 36:572-584.
    • (1996) J Chem Inf Comput Sci , vol.36 , pp. 572-584
    • Brown, R.D.1    Martin, Y.C.2
  • 92
    • 84872274276 scopus 로고    scopus 로고
    • HIV Molecular Immunology Database
    • HIV Molecular Immunology Database [http://www.hiv.lanl.gov]
  • 93
    • 17044440337 scopus 로고    scopus 로고
    • Translation from cryptic reading frames of DNA vaccines generates an extended repertoire of immunogenic, MHC class I-restricted epitopes
    • Schirmbeck R, Riedl P, Fissolo N, Lemonnier FA, Bertoletti A, Reimann J: Translation from cryptic reading frames of DNA vaccines generates an extended repertoire of immunogenic, MHC class I-restricted epitopes. J Immunol 2005, 174:4647-4656.
    • (2005) J Immunol , vol.174 , pp. 4647-4656
    • Schirmbeck, R.1    Riedl, P.2    Fissolo, N.3    Lemonnier, F.A.4    Bertoletti, A.5    Reimann, J.6


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