메뉴 건너뛰기




Volumn 56, Issue , 2015, Pages 84-90

Using support vector machines to identify protein phosphorylation sites in viruses

Author keywords

Encoding scheme based on attribute grouping; Phosphorylation site; Position weight amino acid composition; Support vector machine; Virus proteins

Indexed keywords

AMINO ACIDS; ENCODING (SYMBOLS); PROTEINS; SUPPORT VECTOR MACHINES; VIRUSES;

EID: 84920265432     PISSN: 10933263     EISSN: 18734243     Source Type: Journal    
DOI: 10.1016/j.jmgm.2014.12.005     Document Type: Article
Times cited : (28)

References (48)
  • 1
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • P. Blume-Jensen, and T. Hunter Oncogenic kinase signalling Nature 411 2001 355 365
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 2
    • 0027310848 scopus 로고
    • The effects of phosphorylation on the structure and function of proteins
    • L.N. Johnson, and D. Barford The effects of phosphorylation on the structure and function of proteins Annu. Rev. Biophys. Biomol. Struct. 22 1993 199 232
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 199-232
    • Johnson, L.N.1    Barford, D.2
  • 3
    • 0037302253 scopus 로고    scopus 로고
    • Phosphorylation of rubella virus capsid regulates its RNA binding activity and virus replication
    • L.M.J. Law, J.C. Everitt, M.D. Beatch, C.F.B. Holmes, and T.C. Hobman Phosphorylation of rubella virus capsid regulates its RNA binding activity and virus replication J. Virol. 77 2003 1764 1771
    • (2003) J. Virol. , vol.77 , pp. 1764-1771
    • Law, L.M.J.1    Everitt, J.C.2    Beatch, M.D.3    Holmes, C.F.B.4    Hobman, T.C.5
  • 4
    • 2642563538 scopus 로고    scopus 로고
    • Phosphorylation of vesicular stomatitis virus phosphoprotein P is indispensable for virus growth
    • S.C. Das, and A.K. Pattnaik Phosphorylation of vesicular stomatitis virus phosphoprotein P is indispensable for virus growth J. Virol. 78 2004 6420 6430
    • (2004) J. Virol. , vol.78 , pp. 6420-6430
    • Das, S.C.1    Pattnaik, A.K.2
  • 5
    • 3543025697 scopus 로고    scopus 로고
    • The host cell MAP kinase ERK-2 regulates viral assembly and release by phosphorylating the p6gag protein of HIV-1
    • B. Hemonnot The host cell MAP kinase ERK-2 regulates viral assembly and release by phosphorylating the p6gag protein of HIV-1 J. Biol. Chem. 279 2004 32426 32434
    • (2004) J. Biol. Chem. , vol.279 , pp. 32426-32434
    • Hemonnot, B.1
  • 6
    • 84878202784 scopus 로고    scopus 로고
    • Tyrosine 132 phosphorylation of influenza a virus M1 protein is crucial for virus replication by controlling the nuclear import of M1
    • S. Wang, Z. Zhao, Y. Bi, L. Sun, X. Liu, and W. Liu Tyrosine 132 phosphorylation of influenza a virus M1 protein is crucial for virus replication by controlling the nuclear import of M1 J. Virol. 87 2013 6182 6191
    • (2013) J. Virol. , vol.87 , pp. 6182-6191
    • Wang, S.1    Zhao, Z.2    Bi, Y.3    Sun, L.4    Liu, X.5    Liu, W.6
  • 7
    • 67649470429 scopus 로고    scopus 로고
    • Three C-terminal phosphorylation sites in the Abutilon mosaic virus movement protein affect symptom development and viral DNA accumulation
    • T. Kleinow, M. Nischang, A. Beck, U. Kratzer, F. Tanwir, W. Preiss, G. Kepp, and H. Jeske Three C-terminal phosphorylation sites in the Abutilon mosaic virus movement protein affect symptom development and viral DNA accumulation Virology 390 2009 89 101
    • (2009) Virology , vol.390 , pp. 89-101
    • Kleinow, T.1    Nischang, M.2    Beck, A.3    Kratzer, U.4    Tanwir, F.5    Preiss, W.6    Kepp, G.7    Jeske, H.8
  • 8
    • 84881604077 scopus 로고    scopus 로고
    • Polo-like kinase 1 inhibits the activity of positive transcription elongation factor of RNA pol II b (P-TEFb)
    • Y. Wang, L. Jiang, Y. Huang, M. Deng, T. Liu, W. Lai, and X. Ye Polo-like kinase 1 inhibits the activity of positive transcription elongation factor of RNA pol II b (P-TEFb) PLOS ONE 8 2013 e72289
    • (2013) PLOS ONE , vol.8 , pp. 72289
    • Wang, Y.1    Jiang, L.2    Huang, Y.3    Deng, M.4    Liu, T.5    Lai, W.6    Ye, X.7
  • 9
    • 84869053077 scopus 로고    scopus 로고
    • Roles of the phosphorylation of specific serines and threonines in the NS1 protein of human influenza A viruses
    • T.Y. Hsiang, L. Zhou, and R.M. Krug Roles of the phosphorylation of specific serines and threonines in the NS1 protein of human influenza A viruses J. Virol. 86 2012 10370 10376
    • (2012) J. Virol. , vol.86 , pp. 10370-10376
    • Hsiang, T.Y.1    Zhou, L.2    Krug, R.M.3
  • 10
    • 84877002649 scopus 로고    scopus 로고
    • Ser/Thr kinase-like protein of Nicotiana benthamiana is involved in the cell-to-cell movement of Bamboo mosaic virus
    • S.F. Cheng, M.S. Tsai, C.L. Huang, Y.P. Huang, I.H. Chen, N.S. Lin, Y.H. Hsu, C.H. Tsai, and C.P. Cheng Ser/Thr kinase-like protein of Nicotiana benthamiana is involved in the cell-to-cell movement of Bamboo mosaic virus PLOS ONE 8 2013 e62907
    • (2013) PLOS ONE , vol.8 , pp. 62907
    • Cheng, S.F.1    Tsai, M.S.2    Huang, C.L.3    Huang, Y.P.4    Chen, I.H.5    Lin, N.S.6    Hsu, Y.H.7    Tsai, C.H.8    Cheng, C.P.9
  • 11
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • R. Aebersold, and M. Mann Mass spectrometry-based proteomics Nature 422 2003 198 207
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 12
    • 2942562627 scopus 로고    scopus 로고
    • The phosphorylation site database: A guide to the serine-, threonine-, and/or tyrosine-phosphorylated proteins in prokaryotic organisms
    • S.M. Wurgler-Murphy, D.M. King, and P.J. Kennelly The phosphorylation site database: a guide to the serine-, threonine-, and/or tyrosine-phosphorylated proteins in prokaryotic organisms Proteomics 4 2004 1562 1570
    • (2004) Proteomics , vol.4 , pp. 1562-1570
    • Wurgler-Murphy, S.M.1    King, D.M.2    Kennelly, P.J.3
  • 14
    • 2942598149 scopus 로고    scopus 로고
    • PhosphoSite: A bioinformatics resource dedicated to physiological protein phosphorylation
    • P.V. Hornbeck, I. Chabra, J.M. Kornhauser, E. Skrzypek, and B. Zhang PhosphoSite: a bioinformatics resource dedicated to physiological protein phosphorylation Proteomics 4 2004 1551 1561
    • (2004) Proteomics , vol.4 , pp. 1551-1561
    • Hornbeck, P.V.1    Chabra, I.2    Kornhauser, J.M.3    Skrzypek, E.4    Zhang, B.5
  • 16
    • 67649213067 scopus 로고    scopus 로고
    • Phosphopeptide fragmentation and analysis by mass spectrometry
    • P.J. Boersema, S. Mohammed, and A.J. Heck Phosphopeptide fragmentation and analysis by mass spectrometry J. Mass Spectrom. 44 2009 861 878
    • (2009) J. Mass Spectrom. , vol.44 , pp. 861-878
    • Boersema, P.J.1    Mohammed, S.2    Heck, A.J.3
  • 17
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
    • N. Blom, S. Gammeltoft, and S. Brunak Sequence and structure-based prediction of eukaryotic protein phosphorylation sites J. Mol. Biol. 294 1999 1351 1362
    • (1999) J. Mol. Biol. , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 18
    • 34248576306 scopus 로고    scopus 로고
    • NetPhosYeast: Prediction of protein phosphorylation sites in yeast
    • C.R. Ingrell, M.L. Miller, O.N. Jensen, and N. Blom NetPhosYeast: prediction of protein phosphorylation sites in yeast Bioinformatics 23 2007 895 897
    • (2007) Bioinformatics , vol.23 , pp. 895-897
    • Ingrell, C.R.1    Miller, M.L.2    Jensen, O.N.3    Blom, N.4
  • 19
    • 22344445559 scopus 로고    scopus 로고
    • Incorporating hidden Markov models for identifying protein kinase-specific phosphorylation sites
    • H.D. Huang, T.Y. Lee, S.W. Tzeng, L.C. Wu, J.T. Horng, A.P. Tsou, and K.T. Huang Incorporating hidden Markov models for identifying protein kinase-specific phosphorylation sites J. Comput. Chem. 26 2005 1032 1041
    • (2005) J. Comput. Chem. , vol.26 , pp. 1032-1041
    • Huang, H.D.1    Lee, T.Y.2    Tzeng, S.W.3    Wu, L.C.4    Horng, J.T.5    Tsou, A.P.6    Huang, K.T.7
  • 20
    • 44849086809 scopus 로고    scopus 로고
    • Predikin and PredikinDB: A computational framework for the prediction of protein kinase peptide specificity and an associated database of phosphorylation sites
    • N.F. Saunders, R.I. Brinkworth, T. Huber, B.E. Kemp, and B. Kobe Predikin and PredikinDB: a computational framework for the prediction of protein kinase peptide specificity and an associated database of phosphorylation sites BMC Bioinform. 9 2008 245
    • (2008) BMC Bioinform. , vol.9 , pp. 245
    • Saunders, N.F.1    Brinkworth, R.I.2    Huber, T.3    Kemp, B.E.4    Kobe, B.5
  • 21
    • 0035072833 scopus 로고    scopus 로고
    • A motif-based profile scanning approach for genome-wide prediction of signaling pathways
    • M.B. Yaffe, G.G. Leparc, J. Lai, T. Obata, S. Volinia, and L.C. Cantley A motif-based profile scanning approach for genome-wide prediction of signaling pathways Nat. Biotechnol. 19 2001 348 353
    • (2001) Nat. Biotechnol. , vol.19 , pp. 348-353
    • Yaffe, M.B.1    Leparc, G.G.2    Lai, J.3    Obata, T.4    Volinia, S.5    Cantley, L.C.6
  • 22
    • 45549090122 scopus 로고    scopus 로고
    • Prediction of phosphotyrosine signaling networks using a scoring matrix-assisted ligand identification approach
    • L. Li, C. Wu, H. Huang, K. Zhang, J. Gan, and S.S. Li Prediction of phosphotyrosine signaling networks using a scoring matrix-assisted ligand identification approach Nucleic Acids Res. 36 2008 3263 3273
    • (2008) Nucleic Acids Res. , vol.36 , pp. 3263-3273
    • Li, L.1    Wu, C.2    Huang, H.3    Zhang, K.4    Gan, J.5    Li, S.S.6
  • 23
    • 77953252823 scopus 로고    scopus 로고
    • Functional classification of proteins based on projection of amino acid sequences: Application for prediction of protein kinase substrates
    • B. Sobolev, D. Filimonov, A. Lagunin, A. Zakharov, O. Koborova, A. Kel, and V. Poroikov Functional classification of proteins based on projection of amino acid sequences: application for prediction of protein kinase substrates BMC Bioinform. 11 2010 313
    • (2010) BMC Bioinform. , vol.11 , pp. 313
    • Sobolev, B.1    Filimonov, D.2    Lagunin, A.3    Zakharov, A.4    Koborova, O.5    Kel, A.6    Poroikov, V.7
  • 24
    • 37049020959 scopus 로고    scopus 로고
    • AutoMotif Server for prediction of phosphorylation sites in proteins using support vector machine: 2007 update
    • D. Plewczynski, A. Tkacz, L.S. Wyrwicz, L. Rychlewski, and K. Ginalski AutoMotif Server for prediction of phosphorylation sites in proteins using support vector machine: 2007 update J. Mol. Model. 14 2008 69 76
    • (2008) J. Mol. Model. , vol.14 , pp. 69-76
    • Plewczynski, D.1    Tkacz, A.2    Wyrwicz, L.S.3    Rychlewski, L.4    Ginalski, K.5
  • 25
    • 65849416300 scopus 로고    scopus 로고
    • Detection and characterization of 3D-signature phosphorylation site motifs and their contribution towards improved phosphorylation site prediction in proteins
    • P. Durek, C. Schudoma, W. Weckwerth, J. Selbig, and D. Walther Detection and characterization of 3D-signature phosphorylation site motifs and their contribution towards improved phosphorylation site prediction in proteins BMC Bioinform. 10 2009 1 17
    • (2009) BMC Bioinform. , vol.10 , pp. 1-17
    • Durek, P.1    Schudoma, C.2    Weckwerth, W.3    Selbig, J.4    Walther, D.5
  • 26
    • 78650806643 scopus 로고    scopus 로고
    • The Musite open-source framework for phosphorylation-site prediction
    • J. Gao, and D. Xu The Musite open-source framework for phosphorylation-site prediction BMC Bioinform. 11 Suppl. 12 2010 S9
    • (2010) BMC Bioinform. , vol.11 , pp. 9
    • Gao, J.1    Xu, D.2
  • 27
    • 79952198810 scopus 로고    scopus 로고
    • Enhanced prediction of conformational flexibility and phosphorylation in proteins
    • K. Swaminathan, R. Adamczak, A. Porollo, and J. Meller Enhanced prediction of conformational flexibility and phosphorylation in proteins Adv. Exp. Med. Biol. 680 2010 307 319
    • (2010) Adv. Exp. Med. Biol. , vol.680 , pp. 307-319
    • Swaminathan, K.1    Adamczak, R.2    Porollo, A.3    Meller, J.4
  • 28
    • 80054937592 scopus 로고    scopus 로고
    • Computational prediction of eukaryotic phosphorylation sites
    • B. Trost, and A. Kusalik Computational prediction of eukaryotic phosphorylation sites Bioinformatics 27 2011 2927 2935
    • (2011) Bioinformatics , vol.27 , pp. 2927-2935
    • Trost, B.1    Kusalik, A.2
  • 29
    • 78651272733 scopus 로고    scopus 로고
    • From sequence to structural analysis in protein phosphorylation motifs
    • A. Via, F. Diella, T.J. Gibson, and M. Helmer-Citterich From sequence to structural analysis in protein phosphorylation motifs Front. Biosci. 16 2011 1261 1275
    • (2011) Front. Biosci. , vol.16 , pp. 1261-1275
    • Via, A.1    Diella, F.2    Gibson, T.J.3    Helmer-Citterich, M.4
  • 30
    • 77956620738 scopus 로고    scopus 로고
    • Collection and motif-based prediction of phosphorylation sites in human viruses
    • D. Schwartz, and G.M. Church Collection and motif-based prediction of phosphorylation sites in human viruses Sci. Signal. 3 2010 rs2
    • (2010) Sci. Signal. , vol.3 , pp. 2
    • Schwartz, D.1    Church, G.M.2
  • 31
    • 84864270584 scopus 로고    scopus 로고
    • Identifying protein phosphorylation sites with kinase substrate specificity on human viruses
    • N.A. Bretaña, C.T. Lu, C.Y. Chiang, M.G. Su, K.i. Huang, T.Y. Lee, and S.L. Weng Identifying protein phosphorylation sites with kinase substrate specificity on human viruses PLOS ONE 7 2012 e40694
    • (2012) PLOS ONE , vol.7 , pp. 40694
    • Bretaña, N.A.1    Lu, C.T.2    Chiang, C.Y.3    Su, M.G.4    Huang, K.I.5    Lee, T.Y.6    Weng, S.L.7
  • 33
    • 79959469922 scopus 로고    scopus 로고
    • PlantPhos: Using maximal dependence decomposition to identify plant phosphorylation sites with substrate site specificity
    • T.-Y. Lee, N. Bretaña, and C.-T. Lu PlantPhos: using maximal dependence decomposition to identify plant phosphorylation sites with substrate site specificity BMC Bioinform. 12 2011 261
    • (2011) BMC Bioinform. , vol.12 , pp. 261
    • Lee, T.-Y.1    Bretaña, N.2    Lu, C.-T.3
  • 35
    • 78650153738 scopus 로고    scopus 로고
    • Musite, a tool for global prediction of general and kinase-specific phosphorylation sites
    • J. Gao, J.J. Thelen, A.K. Dunker, and X. Dong Musite, a tool for global prediction of general and kinase-specific phosphorylation sites Mol. Cell Proteomics 9 2010 2586 2600
    • (2010) Mol. Cell Proteomics , vol.9 , pp. 2586-2600
    • Gao, J.1    Thelen, J.J.2    Dunker, A.K.3    Dong, X.4
  • 36
    • 33744968432 scopus 로고    scopus 로고
    • Characterizing the microenvironment surrounding phosphorylated protein sites
    • S.C. Fan, and X.G. Zhang Characterizing the microenvironment surrounding phosphorylated protein sites Genomics Proteomics Bioinform. 3 2005 213 217
    • (2005) Genomics Proteomics Bioinform. , vol.3 , pp. 213-217
    • Fan, S.C.1    Zhang, X.G.2
  • 37
    • 33750528233 scopus 로고    scopus 로고
    • A novel method for apoptosis protein subcellular localization prediction combining encoding based on grouped weight and support vector machine
    • Z.H. Zhang, Z.H. Wang, Z.R. Zhang, and Y.X. Wang A novel method for apoptosis protein subcellular localization prediction combining encoding based on grouped weight and support vector machine FEBS Lett. 580 2006 6169 6174
    • (2006) FEBS Lett. , vol.580 , pp. 6169-6174
    • Zhang, Z.H.1    Wang, Z.H.2    Zhang, Z.R.3    Wang, Y.X.4
  • 38
    • 59449107736 scopus 로고    scopus 로고
    • An ensemble of reduced alphabets with protein encoding based on grouped weight for predicting DNA-binding proteins
    • L. Nanni, and A. Lumini An ensemble of reduced alphabets with protein encoding based on grouped weight for predicting DNA-binding proteins Amino Acids 36 2009 167 175
    • (2009) Amino Acids , vol.36 , pp. 167-175
    • Nanni, L.1    Lumini, A.2
  • 39
    • 34249753618 scopus 로고
    • Support-vector networks
    • C. Cortes, and V. Vapnik Support-vector networks Mach. Learn. 20 1995 273 297
    • (1995) Mach. Learn. , vol.20 , pp. 273-297
    • Cortes, C.1    Vapnik, V.2
  • 40
    • 79955702502 scopus 로고    scopus 로고
    • LIBSVM: A library for support vector machines
    • Software available at
    • C.C. Chang, and C.J. Lin LIBSVM: a library for support vector machines ACM Trans. Intell. Syst. Technol. 2 2011 1 27 Software available at http://www.csie.ntu.edu.tw/∼cjlin/libsvm
    • (2011) ACM Trans. Intell. Syst. Technol. , vol.2 , pp. 1-27
    • Chang, C.C.1    Lin, C.J.2
  • 41
    • 33745622868 scopus 로고    scopus 로고
    • Two Sample Logo: A graphical representation of the differences between two sets of sequence alignments
    • V. Vacic, L.M. Iakoucheva, and P. Radivojac Two Sample Logo: a graphical representation of the differences between two sets of sequence alignments Bioinformatics 22 2006 1536 1537
    • (2006) Bioinformatics , vol.22 , pp. 1536-1537
    • Vacic, V.1    Iakoucheva, L.M.2    Radivojac, P.3
  • 43
    • 79952177511 scopus 로고    scopus 로고
    • Identification of novel phosphorylation motifs through an integrative computational and experimental analysis of the human phosphoproteome
    • R. Amanchy, K. Kandasamy, S. Mathivanan, B. Periaswamy, and R. Reddy Identification of novel phosphorylation motifs through an integrative computational and experimental analysis of the human phosphoproteome J. Proteomics Bioinform. 04 2011 022 035
    • (2011) J. Proteomics Bioinform. , vol.4 , pp. 022-035
    • Amanchy, R.1    Kandasamy, K.2    Mathivanan, S.3    Periaswamy, B.4    Reddy, R.5
  • 44
    • 0025158107 scopus 로고
    • Protein kinase recognition sequence motifs
    • B.E. Kemp, and R.B. Pearson Protein kinase recognition sequence motifs Trends Biochem. Sci. 15 1990 342 346
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 342-346
    • Kemp, B.E.1    Pearson, R.B.2
  • 45
    • 61649126270 scopus 로고    scopus 로고
    • Predicting protein post-translational modifications using meta-analysis of proteome scale data sets
    • D. Schwartz, M.F. Chou, and G.M. Church Predicting protein post-translational modifications using meta-analysis of proteome scale data sets Mol. Cell Proteomics 8 2009 365 379
    • (2009) Mol. Cell Proteomics , vol.8 , pp. 365-379
    • Schwartz, D.1    Chou, M.F.2    Church, G.M.3
  • 46
    • 34248213042 scopus 로고    scopus 로고
    • PkaPS: Prediction of protein kinase A phosphorylation sites with the simplified kinase-substrate binding model
    • G. Neuberger, G. Schneider, and F. Eisenhaber pkaPS: prediction of protein kinase A phosphorylation sites with the simplified kinase-substrate binding model Biol. Direct 2 2007 1
    • (2007) Biol. Direct , vol.2 , pp. 1
    • Neuberger, G.1    Schneider, G.2    Eisenhaber, F.3
  • 47
    • 75149118340 scopus 로고    scopus 로고
    • PostMod: Sequence based prediction of kinase-specific phosphorylation sites with indirect relationship
    • I. Jung, A. Matsuyama, M. Yoshida, and D. Kim PostMod: sequence based prediction of kinase-specific phosphorylation sites with indirect relationship BMC Bioinform. 11 Suppl. 1 2010 S10
    • (2010) BMC Bioinform. , vol.11 , pp. 10
    • Jung, I.1    Matsuyama, A.2    Yoshida, M.3    Kim, D.4
  • 48
    • 77952464216 scopus 로고    scopus 로고
    • Machine learning approach to predict protein phosphorylation sites by incorporating evolutionary information
    • A. Biswas, N. Noman, and S. Abdur Machine learning approach to predict protein phosphorylation sites by incorporating evolutionary information BMC Bioinform. 11 2010 273
    • (2010) BMC Bioinform. , vol.11 , pp. 273
    • Biswas, A.1    Noman, N.2    Abdur, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.