Computer Aided Multi Parameter Antigen Design: Impact of Synthetic Peptide Vaccines from Soybean Mosaic Virus
暂无分享,去创建一个
Karbhari V. Kale | S. Shankar | Virendra S. Gomase | K. Shyamkumar | K. Kale | V. Gomase | K. Shyamkumar | S. Shankar
[1] P Argos,et al. A conformational preference parameter to predict helices in integral membrane proteins. , 1986, Biochimica et biophysica acta.
[2] T. Steitz,et al. Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins. , 1986, Annual review of biophysics and biophysical chemistry.
[3] Barry Robson,et al. Protein structure prediction , 1993, Nature.
[4] Z. Cao,et al. MHC-BPS: MHC-binder prediction server for identifying peptides of flexible lengths from sequence-derived physicochemical properties , 2006, Immunogenetics.
[5] R D Appel,et al. Protein identification and analysis tools in the ExPASy server. , 1999, Methods in molecular biology.
[6] A. Giuliani,et al. A computational approach identifies two regions of Hepatitis C Virus E1 protein as interacting domains involved in viral fusion process , 2009, BMC Structural Biology.
[7] Ruurd van der Zee,et al. Prediction of sequential antigenic regions in proteins , 1985, FEBS letters.
[8] K. R. Woods,et al. Prediction of protein antigenic determinants from amino acid sequences. , 1981, Proceedings of the National Academy of Sciences of the United States of America.
[9] Gajendra P. S. Raghava,et al. MHCBN: a comprehensive database of MHC binding and non-binding peptides , 2003, Bioinform..
[10] R. Jernigan,et al. Estimation of effective interresidue contact energies from protein crystal structures: quasi-chemical approximation , 1985 .
[11] P M Cullis,et al. Affinities of amino acid side chains for solvent water. , 1981, Biochemistry.
[12] M. Levitt,et al. Conformation of amino acid side-chains in proteins. , 1978, Journal of molecular biology.
[13] K J Wilson,et al. The behaviour of peptides on reverse-phase supports during high-pressure liquid chromatography. , 1981, The Biochemical journal.
[14] P. Ponnuswamy,et al. Hydrophobic character of amino acid residues in globular proteins , 1978, Nature.
[15] H. Bull,et al. Surface tension of amino acid solutions: a hydrophobicity scale of the amino acid residues. , 1974, Archives of biochemistry and biophysics.
[16] J. Garnier,et al. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. , 1978, Journal of molecular biology.
[17] G. Rose,et al. Hydrophobicity of amino acid residues in globular proteins. , 1985, Science.
[18] Gajendra P. S. Raghava,et al. Identification of DNA-binding proteins using support vector machines and evolutionary profiles , 2007, BMC Bioinformatics.
[19] Tuija Kekarainen,et al. Mapping of viral genomic regions important in cross-protection between strains of a potyvirus. , 2002, Molecular plant-microbe interactions : MPMI.
[20] P. Tongaonkar,et al. A semi‐empirical method for prediction of antigenic determinants on protein antigens , 1990, FEBS letters.
[21] Gajendra P. S. Raghava,et al. Detection of Orientation of MHC Class II Binding Peptides Using Bioinformatics Tools , 2002 .
[22] R. Hodges,et al. New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: correlation of predicted surface residues with antigenicity and X-ray-derived accessible sites. , 1986, Biochemistry.
[23] Gunnar von Heijne,et al. On the Hydrophobic Nature of Signal Sequences , 1981 .
[24] A. Leo,et al. Extension of the fragment method to calculate amino acid zwitterion and side chain partition coefficients , 1987, Proteins.
[25] D. Eisenberg,et al. Correlation of sequence hydrophobicities measures similarity in three-dimensional protein structure. , 1983, Journal of molecular biology.
[26] R Cowan,et al. Hydrophobicity indices for amino acid residues as determined by high-performance liquid chromatography. , 1990, Peptide research.
[27] D. Eisenberg,et al. The hydrophobic moment detects periodicity in protein hydrophobicity. , 1984, Proceedings of the National Academy of Sciences of the United States of America.
[28] D. Mould,et al. Development of hydrophobicity parameters to analyze proteins which bear post- or cotranslational modifications. , 1991, Analytical biochemistry.
[29] Akintola A. Aboderin,et al. An empirical hydrophobicity scale for α-amino-acids and some of its applications , 1971 .
[30] C. Chothia. The nature of the accessible and buried surfaces in proteins. , 1976, Journal of molecular biology.
[31] M A Roseman,et al. Hydrophilicity of polar amino acid side-chains is markedly reduced by flanking peptide bonds. , 1988, Journal of molecular biology.
[32] Morten Nielsen,et al. Improved method for predicting linear B-cell epitopes , 2006, Immunome research.
[33] H. Guy. Amino acid side-chain partition energies and distribution of residues in soluble proteins. , 1985, Biophysical journal.
[34] R. Doolittle,et al. A simple method for displaying the hydropathic character of a protein. , 1982, Journal of molecular biology.