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Antibody-Like Phosphorylation Sites in Focus of Statistically Based Bilingual Approach

DOI: 10.4236/cmb.2016.61001, PP. 1-22

Keywords: Ataxia Telangiectasia-Mutated-Protein (i.e. Kinase ATM, Whose Pathogenic Mutation Is Responsible for Early Death of People), Complementarity Determining Region 1 (of Immunoglobulins, i.e. CDR1 or Hypervariable Region 1), Database (of Functional Structures), Hypermutation (i.e. Mutation of DNA Sequences Mediated by Enzymes), Immunoglobulin (i.e. Ig or Antibody), Phosphorylation (Enzyme Mediated Modification Concerns Here Mostly Protein Sequences)

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Abstract:

In accordance with previous reports, the sequences related to phosporylated protein segments occur in conserved variable domains of immunoglobulins including first of all certain N-terminally located segments. Consequently, we look here for the sequences 1) composing human and mouse proteins different from antigen receptors, 2) identical with or highly similar to nucleotide sequence representatives of conserved variable immunoglobulin segments and 3) identical with or closely related to phosphorylation sites. More precisely, we searched for the corresponding actual pairs of DNA and protein sequence segments using five-step bilingual approach employing among others a) different types of BLAST searches, b) two in-principle-different machine-learning methods predicting phosphorylated sites and c) two large databases recording existing phosphorylation sites. The approach identified seven existing phosphorylation sites and thirty-seven related human and mouse segments achieving limits for several predictions or phylogenic parameters. Mostly serines phosporylated with ataxia-telangiectasia-related kinase (involved in regulation of DNA-double-strand-break repair) were indicated or predicted in this study. Hypermutation motifs, located in effective positions of the selected sequence segments, occurred significantly less frequently in transcribed than non-transcribed DNA strands suggesting thus the incidence of mutation events. In addition, marked differences between the numbers and proportions of human and mouse cancer-related sequence items were found in different steps of selection process. The possible role of hypermutation changes within the selected segments and the observed structural relationships are discussed here with respect to DNA damage, carcinogenesis, cancer vaccination, ageing and evolution. Taken together, our data represent additional and sometimes perhaps complementary information to the existing databases of empirically proven phosphorylation sites or pathogenically important spots.

 References

[1]  Kornev, A.P., Haste, N.M., Taylor, S.S. and Ten Eyck, L.F. (2006) Surface Comparison of Active and Inactive Protein Kinases Identifies a Conserved Activation Mechanism. Proceedings of National Academy of Sciences of the United States of America, 103, 17783-17788.
http://dx.doi.org/10.1073/pnas.0607656103
[2]  Kornev, A.P., Taylor, S.S. and Ten Eyck, L.F. (2008) A Helix Scaffold for the Assembly of Active Protein Kinases. Proceedings of National Academy of Sciences of the United States of America, 105, 14377-14382.
http://dx.doi.org/10.1073/pnas.0807988105
[3]  Joseph, R.E., Xie, Q. and Andreotti, A.H. (2010) Identification of an Allosteric Signaling Network within Tec Family Kinases. Journal of Molecular Biology, 403, 231-242.
http://dx.doi.org/10.1016/j.jmb.2010.08.035
[4]  Seco, J., Ferrer-Costa, C., Campanera, J.M., Soliva, R. and Barril, X. (2012) Allosteric Regulation of PKCq: Understanding Multistep Phosphorylation and Priming by Ligands in AGC Kinases. Proteins, 80, 269-280.
http://dx.doi.org/10.1002/prot.23205
[5]  Alberts, B., Johnson, A., Lewis, J., Raff, M., Roberts, K. and Walter, P. (2008) Molecular Biology of the Cell. 5th Edition, Garland Science, New York.
[6]  Blom, N., Gammeltoft, S. and Brunak, S. (1999) Sequence- and Structure-Based Prediction of Eukaryotic Protein Phosphorylation Sites. Journal of Molecular Biology, 294, 1351-1362.
http://dx.doi.org/10.1006/jmbi.1999.3310
[7]  Wong, Y.H., Lee, T.Y., Liang, H.K., Huang, C.M., Wang, T.Y., Yang, Y.H., Chu, C.H., Huang, H.D., Ko, M.T. and Hwang, J.K. (2007) KinasePhos 2.0: A Web Server for Identifying Protein Kinase-Specific Phosphorylation Sites Based on Sequences and Coupling Patterns. Nucleic Acids Research, 35, W588-W594.
http://dx.doi.org/10.1093/nar/gkm322
[8]  Kubrycht, J. and Sigler, K. (1997) Animal Membrane Receptors and Adhesive Molecules. Critical Reviews on Biotechnology, 17, 123-147.
http://dx.doi.org/10.3109/07388559709146610
[9]  Kubrycht, J., Borecky, J. and Sigler, K. (2002) Sequence Similarities of Protein Kinase Peptide Substrates and Inhibitors: Comparison of Their Primary Structures with Immunoglobulin Repeats. Folia Microbiologica, 47, 319-358.
http://dx.doi.org/10.1007/BF02818689
[10]  Kubrycht, J., Borecky, J., Soucek, P. and Jezek, P. (2004) Sequence Similarities of Protein Kinase Substrates and Inhibitors with Immunoglobulins and Model Immunoglobulin Homologue: Cell Adhesion Molecule from the Living Fossil Sponge Geodia Cydonium. Mapping of Coherent Database Similarities and Implications for Evolution of CDR1 and Hypermutation. Folia Microbiologica, 49, 219-246.
http://dx.doi.org/10.1007/BF02931038
[11]  Kubrycht, J., Sigler, K., Soucek, P. and Hudecek, J. (2013) Structures Composing Protein Domains. Biochimie, 95, 1511-1524.
http://dx.doi.org/10.1016/j.biochi.2013.04.001
[12]  James, L.C., Roversi, P. and Tawfik, D.S. (2003) Antibody Multispecificity Mediated by Conformational Diversity. Science, 299, 1362-1367.
http://dx.doi.org/10.1126/science.1079731
[13]  Kubrycht, J., Sigler, K., Ruzicka, M., Soucek, P., Borecky, J. and Jezek, J. (2006) Ancient Phylogenetic Beginnings of Immunoglobulin Hypermutation. Journal of Molecular Evolution, 63, 691-706.
http://dx.doi.org/10.1007/s00239-006-0051-9
[14]  Muramatsu, M., Kinoshita, K., Fagarasan, S., Yamada, S., Shinkai, Y. and Honjo, T. (2000) Class Switch Recombination and Hypermutation Require Activation-Induced Cytidine Deaminase (AID), a Potential RNA Editing Enzyme. Cell, 102, 553-563.
http://dx.doi.org/10.1016/S0092-8674(00)00078-7
[15]  Okazaki, I.M., Hiai, H., Kakazu, N., Yamada, S., Muramatsu, M., Kinoshita, K. and Honjo, T. (2003) Constitutive Expression of AID Leads to Tumorigenesis. The Journal of Experimental Medicine, 197, 1173-1181.
http://dx.doi.org/10.1084/jem.20030275
[16]  Kou, T., Marusawa, H., Kinoshita, K., Endo, Y., Okazaki, I., Ueda, Y., et al. (2006) Expression of Activation-Induced Cytidine Deaminase in Human Hepatocytes during Hepatocarcinogenesis. International Journal of Cancer, 120, 469-476.
http://dx.doi.org/10.1002/ijc.22292
[17]  Endo, Y., Marusawa, H., Kinoshita, K., Morisawa, T., Sakurai, T., Okazaki, I.M., Watashi, K., Shimotohno, K., Honjo, T. and Chiba, T. (2007) Expression of Activation-Induced Cytidine Deaminase in Human Hepatocytes via NF-kappaB Signaling. Oncogene, 26, 5587-5595.
http://dx.doi.org/10.1038/sj.onc.1210344
[18]  Matsumoto, Y., Marusawa, H., Kinoshita, K., Endo, Y., Kou, T., Morisawa, T., Azuma, T., Okazaki, I.M., Honjo, T. and Chiba, T. (2007) Helicobacter Pylori Infection Triggers Aberrant Expression of Activation-Induced Cytidine Deaminase in Gastric Epithelium. Nature in Medicine, 13, 470-476.
http://dx.doi.org/10.1038/nm1566
[19]  Gordon, M.S., Kanegai, C.M., Doerr, J.R. and Wall, R. (2003) Somatic Hypermutation of the B Cell Receptor Genes B29 (Igbeta, CD79b) and mb1 (Igalpha, CD79a). Proceedings of National Academy of Sciences of the United States of America, 100, 4126-4131.
http://dx.doi.org/10.1073/pnas.0735266100
[20]  Duquette, M.L., Pham, P., Goodman, M.F. and Maizels, N. (2005) AID Binds to Transcription-Induced Structures in c-MYC that Map to Regions Associated with Translocation and Hypermutation. Oncogene, 24, 5791-5798.
http://dx.doi.org/10.1038/sj.onc.1208746
[21]  Rogozin, I.B. and Kolchanov, N.A. (1992) Somatic Hypermutagenesis in Immunoglobulin Genes. II. Influence of Neighbouring Base Sequences on Mutagenesis. Biochimica et Biophysica Acta, 1171, 11-18.
http://dx.doi.org/10.1016/0167-4781(92)90134-L
[22]  Wright, B.E., Schmidt, K.H., Davis, N., Hunt, A.T. and Minnick, M.F. (2008) II. Correlations between Secondary Structure Stability and Mutation Frequency during Somatic Hypermutation. Molecular Immunology, 45, 3600-3608.
http://dx.doi.org/10.1016/j.molimm.2008.05.012
[23]  Rogozin, I.B. and Diaz, M. (2004) Cutting Edge: DGYW/WRCH Is a Better Predictor of Mutability at G:C Bases in Ig Hypermutation than the Widely Accepted RGYW/WRCY Motif and Probably Reflects a Two-Step Activation-Induced Cytidine Deaminase-Triggered Process. The Journal of Immunology, 172, 3382-3384.
http://dx.doi.org/10.4049/jimmunol.172.6.3382
[24]  Dorner, T., Foster, S.J., Brezinschek, H.P. and Lipsky, P.E. (1998) Analysis of the Targeting of the Hypermutational Machinery and the Impact of Subsequent Selection on the Distribution of Nucleotide Changes in VHDJH Rearrangements. Immunology Reviews, 162, 161-171.
http://dx.doi.org/10.1111/j.1600-065X.1998.tb01439.x
[25]  Kubrycht, J. and Sigler, K. (2008) Length of the Hypermutation Motif DGYW/WRCH in the Focus of Statistical Limits. Implications for a Double-Motif or Extended Motif Recognition Models. Journal of Theoretical Biology, 255, 8-15.
http://dx.doi.org/10.1016/j.jtbi.2008.07.039
[26]  Beale, R.C.L., Petersen-Mahrt, S.K., Watt, I.N., Harris, R.S., Rada, C. and Neuberger, M.S. (2004) Comparison of the Differential Context-Dependence of DNA Deamination by APOBEC Enzymes: Correlation with Mutation Spectra in Vivo. Journal of Molecular Biology, 337, 585-596.
http://dx.doi.org/10.1016/j.jmb.2004.01.046
[27]  Bishop, K.N., Holmes, R.K., Sheehy, A.M., Davidson, N.O., Cho, S.J. and Malim, M.H. (2004) Cytidine Deamination of Retroviral DNA by Diverse APOBEC Proteins. Current Biology, 14, 1392-1396.
http://dx.doi.org/10.1016/j.cub.2004.06.057
[28]  Henry, M., Guetard, D., Suspene, R., Rusniok, C., Wain-Hobson, S. and Vartanian, J.P. (2009) Genetic Editing of HBV DNA by Monodomain Human APOBEC3 Cytidine Deaminases and the Recombinant Nature of APOBEC3G. PLoS ONE, 4, e4277.
http://dx.doi.org/10.1371/journal.pone.0004277
[29]  Thielen, B.K., McNevin, J.P., McElrath, M.J., Hunt, B.V., Klein, K.C. and Lingappa, J.R. (2010) Innate Immune Signaling Induces High Levels of TC-Specific Deaminase Activity in Primary Monocyte-Derived Cells through Expression of APOBEC3A Isoforms. The Journal of Biological Chemistry, 285, 27753-27766.
http://dx.doi.org/10.1074/jbc.M110.102822
[30]  Roberts, S.A., Sterling, J., Thompson, C., Harris, S., Mav, D., Shah, R., et al. (2012) Clustered Mutations in Yeast and in Human Cancers Can Arise from Damaged Long Single-Strand DNA Regions. Molecular Cell, 46, 424-435.
http://dx.doi.org/10.1016/j.molcel.2012.03.030
[31]  Nakagawa, K., Taya, Y., Tamai, K. and Yamaizumi, M. (1999) Requirement of ATM in Phosphorylation of the Human p53 Protein at Serine 15 Following DNA Double-Strand Breaks. Molecular and Cellular Biology, 19, 2828-2834.
http://dx.doi.org/10.1128/MCB.19.4.2828
[32]  Lavin, M.F. (2007) ATM and the Mre11 Complex Combine to Recognize and Signal DNA Double-Strand Breaks. Oncogene, 26, 7749-7758.
http://dx.doi.org/10.1038/sj.onc.1210880
[33]  Di Domenico, E.G., Romano E., Del Porto, P. and Ascenzioni, F. (2014) Multifunctional Role of ATM/Tel1 Kinase in Genome Stability: From the DNA Damage Response to Telomere Maintenance. BioMed Research International, 2014, Article ID: 787404.
http://dx.doi.org/10.1155/2014/787404
[34]  Altschul, S.F., Madden, T.L., Schaffer, A.A., Zhang, J., Zhang, Z., Miller, W. and Lipman, D.J. (1997) Gapped BLAST and PSI-BLAST: A New Generation of Protein Database Search Programs. Nucleic Acids Research, 25, 3389-3402.
http://dx.doi.org/10.1093/nar/25.17.3389
[35]  Marchler-Bauer, A., Lu, S., Anderson, J.B., Chitsaz, F., Derbyshire, M.K., DeWeese-Scott, C., et al. (2011) CDD: A Conserved Domain Database for the Functional Annotation of Proteins. Nucleic Acids Research, 39, D225-D229.
http://dx.doi.org/10.1093/nar/gkq1189
[36]  Thompson, J.D., Higgins, D.G. and Gibson, T.J. (1994) CLUSTAL W: Improving the Sensitivity of Progressive Multiple Sequence Alignment through Sequence Weighting, Position-Specific Gap Penalties and Weight Matrix Choice. Nucleic Acids Research, 22, 4673-4680.
http://dx.doi.org/10.1093/nar/22.22.4673
[37]  Jaroszewski, L., Rychlewski, L., Li, Z., Li, W. and Godzik, A. (2005) FFAS03: A Server for Profile-Profile Sequence Alignments. Nucleic Acids Research, 33, W284-W288.
http://dx.doi.org/10.1093/nar/gki418
[38]  Jaroszewski, L., Li, Z., Cai, X.H., Weber, C. and Godzik, A. (2011) FFAS Server: Novel Features and Applications. Nucleic Acids Research, 39, W38-W44.
http://dx.doi.org/10.1093/nar/gkr441
[39]  Rice, P., Longden, I. and Bleasby, A. (2000) EMBOSS: The European Molecular Biology Open Software Suite. Trends in Genetics, 16, 276-277.
http://dx.doi.org/10.1016/S0168-9525(00)02024-2
[40]  Diella, F., Cameron, S., Gemünd, C., Linding, R., Via, A., Kuster, B., Sicheritz-Pontén, T., Blom, N. and Gibson, T.J. (2004) Phospho.ELM: A Database of Experimentally Verified Phosphorylation Sites in Eukaryotic Proteins. BMC Bioinformatics, 5, 79.
http://dx.doi.org/10.1186/1471-2105-5-79
[41]  Dinkel, H., Chica, C., Via, A., Gould, C.M., Jensen, L.J., Gibson, T.J. and Diella, F. (2011) Phospho.ELM: A Database of Phosphorylation Sites-Update 2011. Nucleic Acids Research, 39, D261-D267.
http://dx.doi.org/10.1093/nar/gkq1104
[42]  Gnad, F., Gunawardena, J. and Mann, M. (2011) PHOSIDA 2011: The Posttranslational Modification Database. Nucleic Acids Research, 39, D253-D260.
http://dx.doi.org/10.1093/nar/gkq1159
[43]  Zvárová, J. (2001) Biomedical Statistics. I. The Fundamentals of Statistics for Biomedical Fields. Karolinum, Prague.
[44]  Mefford, J. (2012) Bayesian Statistics and Bias Analysis.
http://slideplayer.com/slide/8525698/
[45]  Lowry, R. (2001) 2x2 Contingency Table.
http://vassarstats.net/tab2x2.html
[46]  Dembo, A., Karlin, S. and Zeitouni, O. (1994) Limit Distribution of Maximal Non-Aligned Two-Sequence Segmental Score. The Annals of Probability, 22, 2022-2039.
http://dx.doi.org/10.1214/aop/1176988493
[47]  Karlin, S. and Altschul, S.F. (1990) Methods for Assessing the Statistical Significance of Molecular Sequence Features by Using General Scoring Schemes. Proceedings of National Academy of Sciences of the United States of America, 87, 2264-2268.
http://dx.doi.org/10.1073/pnas.87.6.2264
[48]  Potter, M., Padlan, E. and Rudikoff, S. (1976) Localized Deletion-Insertion Mutations: A Major Factor in the Evolution of Immunoglobulin Structural Variability. The Journal of Immunology, 117, 626-629.
[49]  Kabat, E.A., Wu, T.T., Perry, H.M., Gottesman, K.S. and Foeller, C. (1991) Sequences of Proteins of Immunological Interest. NIH publication No. 91-3242, Bethesda.
[50]  Schmid, F.X. (1993) Prolyl Isomerase: Enzymatic Catalysis of Slow Protein-Folding Reactions. Annual Review of Biophysics and Biomolecular Structure, 22, 123-142.
http://dx.doi.org/10.1146/annurev.bb.22.060193.001011
[51]  Snorek, M. (2002) Neural Networks and Neurocomputers. CVUT Publishing, Prague.
[52]  Waegeman, W., De Baets, B. and Boullart, L. (2008) Learning Layered Ranking Functions with Structured Support Vector Machines. Neural Networks, 21, 1511-1523.
http://dx.doi.org/10.1016/j.neunet.2008.07.008
[53]  Gao, S., Zhang, N., Duan, G.Y., Yang, Z., Ruan, J.S. and Zhang, T. (2009) Prediction of Function Changes Associated with Single-Point Protein Mutations Using Support Vector Machines (SVMs). Human Mutation, 30, 1161-1166.
http://dx.doi.org/10.1002/humu.21039
[54]  Rangwala, H., Kauffman, C. and Karypis, G. (2009) SvmPRAT: SVM-Based Protein Residue Annotation Toolkit. BMC Bioinformatics, 10, 439.
http://dx.doi.org/10.1186/1471-2105-10-439
[55]  Ansari, H.R. and Raghava, G.P. (2010) Identification of Conformational B-Cell Epitopes in an Antigen from Its Primary Sequence. Immunome Research, 6, 6.
http://dx.doi.org/10.1186/1745-7580-6-6
[56]  Oprea, M., Cowell, L.G. and Kepler, T.B. (2001) The Targeting of Somatic Hypermutation Closely Resembles That of Meiotic Mutation. The Journal of Immunology, 166, 892-899.
http://dx.doi.org/10.4049/jimmunol.166.2.892
[57]  Yoder, J.A., Turner, P.M., Wright, P.D., Wittamer, V., Bertrand, J.Y., Traver, D. and Litman, G.W. (2010) Developmental and Tissue-Specific Expression of NITRs. Immuno-genetics, 62, 117-122.
http://dx.doi.org/10.1007/s00251-009-0416-5
[58]  Wilson, P., Liu, Y.J., Banchereau, J., Capra, J.D. and Pascual, V. (1998) Amino Acid Insertions and Deletions Contribute to Diversify the Human Ig Repertoire. Immunological Reviews, 162, 143-151.
http://dx.doi.org/10.1111/j.1600-065X.1998.tb01437.x
[59]  Papavasiliou, F.N. and Schatz, D.G. (2000) Cell-Cycle-Regulated DNA Double-Stranded Breaks in Somatic Hypermutation of Immunoglobulin Genes. Nature, 408, 216-221.
http://dx.doi.org/10.1038/35041599
[60]  Shen, H.M. (2007) Activation-Induced Cytidine Deaminase Acts on Double-Strand Breaks in Vitro. Molecular Immunology, 44, 974-983.
http://dx.doi.org/10.1016/j.molimm.2006.03.015
[61]  Holliday, R. (1995) Understanding Ageing. Cambridge University Press, New York.
http://dx.doi.org/10.1017/CBO9780511623233
[62]  Crawford, T.O., Skolasky, R.L., Fernandez, R., Rosquist, K.J. and Lederman, H.M. (2006) Survival Probability in Ataxia Telangiectasia. Archives of Disease in Childhood, 91, 610-611.
http://dx.doi.org/10.1136/adc.2006.094268
[63]  Boohaker, R.J. and Xu, B. (2014) The Versatile Functions of ATM Kinase. Biomedical Journal, 37, 3-9.
http://dx.doi.org/10.4103/2319-4170.125655
[64]  Ohlin, M. and Borrebaeck, C.A.K. (1998) Insertions and Deletions in Hypervariable Loops of Antibody Heavy Chains Contribute to Molecular Diversity. Molecular Immunology, 35, 233-238.
http://dx.doi.org/10.1016/S0161-5890(98)00030-3
[65]  Jeng, Y.M., Wu, M.Z., Mao, T.L., Chang, M.H. and Hsu, H.C. (2000) Somatic Mutations of Beta-Catenin Play a Crucial Role in the Tumorigenesis of Sporadic Hepatoblastoma. Cancer Letters, 152, 45-51.
http://dx.doi.org/10.1016/S0304-3835(99)00433-4
[66]  Radivojac, P., Baenziger, P.H., Kann, M.G., Mort, M.E., Hahn, M.W. and Mooney, S.D. (2008) Gain and Loss of Phosphorylation Sites in Human Cancer. Bioinformatics, 24, i241-i247.
http://dx.doi.org/10.1093/bioinformatics/btn267
[67]  Hu, Z., Wan, X., Hao, R., Zhang, H., Li, L., Li, L., et al. (2015) Phosphorylation of Mutationally Introduced Tyrosine in the Activation Loop of HER2 Confers Gain-of-Function Activity. PLoS ONE, 10, e0123623.
http://dx.doi.org/10.1371/journal.pone.0123623
[68]  Ndegwa, N., Côté, R.G., Ovelleiro, D., D’Eustachio, P., Hermjakob, H., Vizcaíno, J.A. and Croft, D. (2011) Critical Amino Acid Residues in Proteins: A BioMart Integration of Reactome Protein Annotations with PRIDE Mass Spectrometry Data and COSMIC Somatic Mutations. Database, 2011, bar047.
http://dx.doi.org/10.1093/database/bar047
[69]  Reimand, J., Wagih, O. and Bader, G.D. (2013) The Mutational Landscape of Phosphorylation Signaling in Cancer. Scientific Reports, 3, 2651.
http://dx.doi.org/10.1038/srep02651
[70]  Soucek, P., Gut, I., Trneny, M., Skovlund, E., Kristensen, T., Børresen-Dale, A.-L. and Kristensen, V.N. (2003) Multiplex Single-Tube Screening for Mutations in the Nijmegen Breakage Syndrome (NBS1) Gene in Hodgkin’s and Non-Hodgkin’s Lymphoma Patients of Slavic Origin. European Journal of Human Genetics, 11, 416-419.
http://dx.doi.org/10.1038/sj.ejhg.5200972
[71]  Soucek, P., Borovanova, T., Pohlreich, P., Kleibl, Z. and Novotny, J. (2007) Role of Single Nucleotide Polymorphisms and Haplotypes in BRCA1 in Breast Cancer: Czech Case-Control Study. Breast Cancer Research and Treatment, 103, 219-224.
http://dx.doi.org/10.1007/s10549-006-9367-9
[72]  Mohelnikova-Duchonova, B., Havranek, O., Hlavata, I., Foretova, L., Kleibl, Z., Pohlreich, P. and Soucek, P. (2010) CHEK2 Gene Alterations in the Forkhead-Associated Domain, 1100delC and del5395 Do Not Modify the Risk of Sporadic Pancreatic Cancer. Cancer Epidemiology, 34, 656-658.
http://dx.doi.org/10.1016/j.canep.2010.06.008
[73]  Smith, G.P. (1985) Filamentous Fusion Phage: Novel Expression Vectors That Display Cloned Antigens on the Virion Surface. Science, 228, 1315-1317.
http://dx.doi.org/10.1126/science.4001944
[74]  Schmitz, R., Baumann, G. and Gram, H. (1996) Catalytic Specificity of Phosphotyrosine Kinases Blk, Lyn, c-Src and Syk as Assessed by Phage Display. Journal of Molecular Biology, 260, 664-677.
http://dx.doi.org/10.1006/jmbi.1996.0429
[75]  Fack, F., Hugle-Dorr, B., Song, D., Queitsch, I., Petersen, G. and Bautz, E.K.F. (1997) Epitope Mapping by Phage Display: Random Versus Gene-Fragment Libraries. Journal of Immunological Methods, 206, 43-52.
http://dx.doi.org/10.1016/S0022-1759(97)00083-5
[76]  Reche, P.A. and Reinherz, E.L. (2005) PEPVAC: A Web Server for Multi-Epitope Vaccine Development Based on the Prediction of Supertypic MHC ligands. Nucleic Acids Research, 33, W138-W141.
http://dx.doi.org/10.1093/nar/gki357
[77]  Shehzadi, A., Rehman, S. and Indrees, M. (2011) Promiscuous Prediction and Conservancy Analysis of CTL Binding Epitopes of HCV 3a Viral Proteome from Punjab Pakistan: An in Silico Approach. Virology Journal, 8, 55.
http://dx.doi.org/10.1186/1743-422X-8-55
[78]  Kubrycht, J., Sigler, K. and Soucek, P. (2012) Virtual Interactomics of Proteins from Biochemical Standpoint. Molecular Biology International, 2012, Article ID: 976385.
http://dx.doi.org/10.1155/2012/976385
[79]  Jing, H., Takagi, J., Liu, J.H., Lindgren, S., Zhang, R.G., Joachimiak, A., Wang, J.H. and Springer, T.A. (2002) Archaeal Surface Layer Proteins Contain Beta Propeller, PKD, and Beta Helix Domains and Are Related to Metazoan Cell Surface Proteins. Structure, 10, 1453-1464.
http://dx.doi.org/10.1016/S0969-2126(02)00840-7

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