메뉴 건너뛰기




Volumn 83, Issue , 2011, Pages 1-42

Graphical representation and mathematical characterization of protein sequences and applications to viral proteins

Author keywords

avian and swine flu; conserved surface exposed peptides; coronavirus; Graphical representation of proteins; numerical characterisation of proteins; protein characteristics; protein phylogeny; viral proteins and disease

Indexed keywords


EID: 79956122631     PISSN: 18761623     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-381262-9.00001-X     Document Type: Chapter
Times cited : (25)

References (182)
  • 3
    • 31444455638 scopus 로고    scopus 로고
    • Novel 2D maps and coupling numbers for protein sequences. The first QSAR study of polygalacturonases; isolation and prediction of a novel sequence from Psidium guajava L
    • DOI 10.1016/j.febslet.2005.12.072, PII S0014579305015590
    • G. Aguero-Chapin, H. Gonzalez-Diaz, R. Molina, J. Varona-Santos, E. Uriarte, and Y. Gonzalez-Diaz Novel 2D maps and coupling numbers for protein sequences. The first QSAR study of polygalacturonases; isolation and prediction of a novel sequence from Psidium guajava L FEBS Lett. 580 2006 723 730 (Pubitemid 43152288)
    • (2006) FEBS Letters , vol.580 , Issue.3 , pp. 723-730
    • Aguero-Chapin, G.1    Gonzalez-Diaz, H.2    Molina, R.3    Varona-Santos, J.4    Uriarte, E.5    Gonzalez-Diaz, Y.6
  • 4
    • 65249098338 scopus 로고    scopus 로고
    • Alignment-free prediction of polygalacturonases with pseudofolding topological indices: Experimental isolation from Coffea arabica and prediction of a new sequence
    • G. Aguero-Chapin, J. Varona-Santos, G.A. de la Riva, A. Antunes, T. Gonzalez-Vlla, and E. Uriarte Alignment-free prediction of polygalacturonases with pseudofolding topological indices: experimental isolation from Coffea arabica and prediction of a new sequence J. Proteome Res. 8 2009 2122 2128
    • (2009) J. Proteome Res. , vol.8 , pp. 2122-2128
    • Aguero-Chapin, G.1    Varona-Santos, J.2    De La Riva, G.A.3    Antunes, A.4    Gonzalez-Vlla, T.5    Uriarte, E.6
  • 6
    • 0024964655 scopus 로고
    • Gap costs for multiple sequence alignment
    • S.F. Altschul Gap costs for multiple sequence alignment J. Theor. Biol. 138 1989 297 309
    • (1989) J. Theor. Biol. , vol.138 , pp. 297-309
    • Altschul, S.F.1
  • 7
    • 24644463186 scopus 로고    scopus 로고
    • A 2-D graphical representation of protein sequences based on nucleotide triplet codons
    • DOI 10.1016/j.cplett.2005.08.011, PII S0009261405011565
    • F. Bai, and T. Wang A 2-D graphical representation of protein sequences based on nucleotide triplet codons Chem. Phys. Lett. 413 2005 458 462 (Pubitemid 41285263)
    • (2005) Chemical Physics Letters , vol.413 , Issue.4-6 , pp. 458-462
    • Bai, F.1    Wang, T.2
  • 8
    • 33645325372 scopus 로고    scopus 로고
    • On graphical and numerical representation of protein sequences
    • F. Bai, and T. Wang On graphical and numerical representation of protein sequences J. Biomol. Struct. Dyn. 23 2006 537 546
    • (2006) J. Biomol. Struct. Dyn. , vol.23 , pp. 537-546
    • Bai, F.1    Wang, T.2
  • 9
    • 19744374010 scopus 로고    scopus 로고
    • Analysis of similarity between RNA secondary structures
    • DOI 10.1016/j.cplett.2005.04.052, PII S0009261405005828
    • F. Bai, W. Zhu, and T. Wang Analysis of similarity between RNA secondary structures Chem. Phys. Lett. 408 2005 258 263 (Pubitemid 40743888)
    • (2005) Chemical Physics Letters , vol.408 , Issue.4-6 , pp. 258-263
    • Bai, F.1    Zhu, W.2    Wang, T.3
  • 10
    • 0035812694 scopus 로고    scopus 로고
    • Protein structure prediction and structural genomics
    • DOI 10.1126/science.1065659
    • D. Baker, and A. Sali Protein structure prediction and structural genomics Science 294 2001 93 96 (Pubitemid 32952955)
    • (2001) Science , vol.294 , Issue.5540 , pp. 93-96
    • Baker, D.1    Sali, A.2
  • 11
    • 0018361151 scopus 로고
    • Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism
    • DOI 10.1016/0022-2836(79)90277-8
    • J. Baldwin, and C. Chothia Haemoglobin: the structural changes related to ligand binding and its allosteric mechanism J. Mol. Biol. 129 1979 175 220 (Pubitemid 9168805)
    • (1979) Journal of Molecular Biology , vol.129 , Issue.2 , pp. 175-220
    • Baldwin, J.1    Chothia, C.2
  • 12
    • 0031905560 scopus 로고    scopus 로고
    • Risky business: Challenges in vaccine risk communication
    • L.K. Ball, G. Evans, and A. Bostrom Risky business: challenges in vaccine risk communication Pediatrics 101 1998 453 458
    • (1998) Pediatrics , vol.101 , pp. 453-458
    • Ball, L.K.1    Evans, G.2    Bostrom, A.3
  • 13
    • 42449153333 scopus 로고    scopus 로고
    • Mathematical biodescriptors of proteomics maps: Background and applications
    • S.C. Basak, and B.D. Gute Mathematical biodescriptors of proteomics maps: background and applications Curr. Opin. Drug Discov. Devel. 11 2008 320 326 (Pubitemid 351572441)
    • (2008) Current Opinion in Drug Discovery and Development , vol.11 , Issue.3 , pp. 320-326
    • Basak, S.C.1    Gute, B.D.2
  • 14
    • 55249125163 scopus 로고    scopus 로고
    • Predicting pharmacological and toxicological activity of heterocyclic compounds using QSAR and molecular modeling
    • S.C. Basak, D. Mills, B.D. Gute, and R. Natarajan Predicting pharmacological and toxicological activity of heterocyclic compounds using QSAR and molecular modeling S.P. Gupta, QSAR and Molecular Modeling Studies of Heterocyclic Drugs I 2006 Springer-Verlag Berlin-Heidelberg-New York 39 80
    • (2006) QSAR and Molecular Modeling Studies of Heterocyclic Drugs i , pp. 39-80
    • Basak, S.C.1    Mills, D.2    Gute, B.D.3    Natarajan, R.4
  • 15
    • 79952715472 scopus 로고    scopus 로고
    • Characterization of dihydrofolate reductases from multiple strains of Plasmodium falciparum using mathematical descriptors of their inhibitors
    • S.C. Basak, D. Mills, and D.M. Hawkins Characterization of dihydrofolate reductases from multiple strains of Plasmodium falciparum using mathematical descriptors of their inhibitors Chem. Biodivers 8 2011 440 453
    • (2011) Chem. Biodivers , vol.8 , pp. 440-453
    • Basak, S.C.1    Mills, D.2    Hawkins, D.M.3
  • 16
    • 0033491334 scopus 로고    scopus 로고
    • Motif Trap: A rapid method to clone motifs that can target proteins to defined subcellular localisations
    • L.A. Bejarano, and C. Gonzalez Motif trap: a rapid method to clone motifs that can target proteins to defined subcellular localisations J. Cell Sci. 112 Pt 23 1999 4207 4211 (Pubitemid 30122013)
    • (1999) Journal of Cell Science , vol.112 , Issue.23 , pp. 4207-4211
    • Bejarano, L.A.1    Gonzalez, C.2
  • 17
    • 33846036096 scopus 로고    scopus 로고
    • The worldwide Protein Data Bank (wwPDB): Ensuring a single, uniform archive of PDB data
    • H. Berman, K. Henrick, H. Nakamura, and J.L. Markley The worldwide Protein Data Bank (wwPDB): ensuring a single, uniform archive of PDB data Nucleic Acids Res. 35 2007 D301 D303
    • (2007) Nucleic Acids Res. , vol.35
    • Berman, H.1    Henrick, K.2    Nakamura, H.3    Markley, J.L.4
  • 18
    • 2942564430 scopus 로고    scopus 로고
    • Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence
    • DOI 10.1002/pmic.200300771
    • N. Blom, T. Sicheritz-Ponten, R. Gupta, S. Gammeltoft, and S. Brunak Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence Proteomics 4 2004 1633 1649 (Pubitemid 38738322)
    • (2004) Proteomics , vol.4 , Issue.6 , pp. 1633-1649
    • Blom, N.1    Sicheritz-Ponten, T.2    Gupta, R.3    Gammeltoft, S.4    Brunak, So.5
  • 19
    • 4143080522 scopus 로고    scopus 로고
    • Energetics of drug-DNA interactions
    • J.B. Chaires Energetics of drug-DNA interactions Biopolymers 44 1997 201 215
    • (1997) Biopolymers , vol.44 , pp. 201-215
    • Chaires, J.B.1
  • 21
    • 4744359693 scopus 로고    scopus 로고
    • Turning protein crystallisation from an art into a science
    • DOI 10.1016/j.sbi.2004.08.002, PII S0959440X04001368
    • N.E. Chayen Turning protein crystallisation from an art into a science Curr. Opin. Struct. Biol. 14 2004 577 583 (Pubitemid 39311821)
    • (2004) Current Opinion in Structural Biology , vol.14 , Issue.5 , pp. 577-583
    • Chayen, N.E.1
  • 23
    • 38749149916 scopus 로고    scopus 로고
    • Protein crystallization: From purified protein to diffraction-quality crystal
    • DOI 10.1038/nmeth.f.203, PII NMETH.F.203
    • N.E. Chayen, and E. Saridakis Protein crystallization: from purified protein to diffraction-quality crystal Nat Methods 5 2008 147 153 (Pubitemid 351181740)
    • (2008) Nature Methods , vol.5 , Issue.2 , pp. 147-153
    • Chayen, N.E.1    Saridakis, E.2
  • 24
    • 64249164773 scopus 로고    scopus 로고
    • Influenza virus antigenic variation, host antibody production and new approach to control epidemics
    • J. Chen, and Y.M. Deng Influenza virus antigenic variation, host antibody production and new approach to control epidemics Virol. J. 6 2009 30
    • (2009) Virol. J. , vol.6 , pp. 30
    • Chen, J.1    Deng, Y.M.2
  • 27
    • 0035178419 scopus 로고    scopus 로고
    • Prediction of protein signal sequences and their cleavage sites
    • K.C. Chou Prediction of protein signal sequences and their cleavage sites Proteins 42 2001 136 139
    • (2001) Proteins , vol.42 , pp. 136-139
    • Chou, K.C.1
  • 28
    • 0345305854 scopus 로고    scopus 로고
    • Prediction and classification of protein subcellular location-sequence- order effect and pseudo amino acid composition
    • K.C. Chou, and Y.D. Cai Prediction and classification of protein subcellular location-sequence-order effect and pseudo amino acid composition J. Cell. Biochem. 90 2003 1250 1260
    • (2003) J. Cell. Biochem. , vol.90 , pp. 1250-1260
    • Chou, K.C.1    Cai, Y.D.2
  • 29
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins
    • P.Y. Chou, and G.D. Fasman Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins Biochemistry 13 1974 211 222
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 30
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • P.Y. Chou, and G.D. Fasman Prediction of protein conformation Biochemistry 13 1974 222 245
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 31
    • 20044376908 scopus 로고    scopus 로고
    • Could it happen here? Vaccine risk controversies and the specter of derailment
    • J. Colgrove, and R. Bayer Could it happen here? Vaccine risk controversies and the specter of derailment Health Aff. (Millwood) 24 2005 729 739
    • (2005) Health Aff. (Millwood) , vol.24 , pp. 729-739
    • Colgrove, J.1    Bayer, R.2
  • 32
    • 41849087712 scopus 로고    scopus 로고
    • 3D-MEDNEs: An alternative "in silico" technique for chemical research in toxicology. 2. Quantitative proteome-toxicity relationships (QPTR) based on mass spectrum spiral entropy
    • DOI 10.1021/tx700296t
    • M. Cruz-Monteagudo, H. Gonzalez-Diaz, F. Borges, E.R. Dominguez, and M.N. Cordeiro 3D-MEDNEs: an alternative "in silico" technique for chemical research in toxicology. 2. quantitative proteome-toxicity relationships (QPTR) based on mass spectrum spiral entropy Chem. Res. Toxicol. 21 2008 619 632 (Pubitemid 351498038)
    • (2008) Chemical Research in Toxicology , vol.21 , Issue.3 , pp. 619-632
    • Cruz-Monteagudo, M.1    Gonzalez-Diaz, H.2    Borges, F.3    Dominguez, E.R.4    Cordeiro, M.N.D.S.5
  • 33
    • 49149091399 scopus 로고    scopus 로고
    • HP-Lattice QSAR for dynein proteins: Experimental proteomics (2D-electrophoresis, mass spectrometry) and theoretic study of a Leishmania infantum sequence
    • M.A. Dea-Ayuela, Y. Perez-Castillo, A. Meneses-Marcel, F.M. Ubeira, F. Bolas-Fernandez, and K.C. Chou HP-Lattice QSAR for dynein proteins: experimental proteomics (2D-electrophoresis, mass spectrometry) and theoretic study of a Leishmania infantum sequence Bioorg. Med. Chem. 16 2008 7770 7776
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 7770-7776
    • Dea-Ayuela, M.A.1    Perez-Castillo, Y.2    Meneses-Marcel, A.3    Ubeira, F.M.4    Bolas-Fernandez, F.5    Chou, K.C.6
  • 34
    • 0034755765 scopus 로고    scopus 로고
    • Multiple effects of codon usage optimization on expression and immunogenicity of DNA candidate vaccines encoding the human immunodeficiency virus type 1 Gag protein
    • DOI 10.1128/JVI.75.22.10991-11001.2001
    • L. Deml, A. Bojak, S. Steck, M. Graf, J. Wild, and R. Schirmbeck Multiple effects of codon usage optimization on expression and immunogenicity of DNA candidate vaccines encoding the human immunodeficiency virus type 1 Gag protein J. Virol. 75 2001 10991 11001 (Pubitemid 33031566)
    • (2001) Journal of Virology , vol.75 , Issue.22 , pp. 10991-11001
    • Deml, L.1    Bojak, A.2    Steck, S.3    Graf, M.4    Wild, J.5    Schirmbeck, R.6    Wolf, H.7    Wagner, R.8
  • 37
    • 34347375915 scopus 로고    scopus 로고
    • The protein folding problem: When will it be solved?
    • DOI 10.1016/j.sbi.2007.06.001, PII S0959440X07000772, Nucleic acids / Sequences and topology
    • K.A. Dill, S.B. Ozkan, T.R. Weikl, J.D. Chodera, and V.A. Voelz The protein folding problem: when will it be solved? Curr. Opin. Struct. Biol. 17 2007 342 346 (Pubitemid 47021366)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.3 , pp. 342-346
    • Dill, K.A.1    Ozkan, S.B.2    Weikl, T.R.3    Chodera, J.D.4    Voelz, V.A.5
  • 38
    • 38849126803 scopus 로고    scopus 로고
    • Recombinant therapeutic proteins: Production platforms and challenges
    • DOI 10.1002/biot.200700214
    • T. Dingermann Recombinant therapeutic proteins: production platforms and challenges Biotechnol. J. 3 2008 90 97 (Pubitemid 351200935)
    • (2008) Biotechnology Journal , vol.3 , Issue.1 , pp. 90-97
    • Dingermann, T.1
  • 39
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding and aggregation
    • DOI 10.1016/j.semcdb.2003.12.008
    • C.M. Dobson Principles of protein folding, misfolding and aggregation Semin. Cell Dev. Biol. 15 2004 3 16 (Pubitemid 38177363)
    • (2004) Seminars in Cell and Developmental Biology , vol.15 , Issue.1 , pp. 3-16
    • Dobson, C.M.1
  • 40
    • 48249134102 scopus 로고    scopus 로고
    • Mediation, modulation, and consequences of membrane-cytoskeleton interactions
    • G.J. Doherty, and H.T. McMahon Mediation, modulation, and consequences of membrane-cytoskeleton interactions Annu. Rev. Biophys. 37 2008 65 95
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 65-95
    • Doherty, G.J.1    McMahon, H.T.2
  • 41
    • 79956079283 scopus 로고    scopus 로고
    • Using the tools and resources of the RCSB protein data bank
    • S. Dutta, H.M. Berman, and W.F. Bluhm Using the tools and resources of the RCSB protein data bank Curr. Protoc. Bioinformatics 20 2007 1.9.1 1.9.24
    • (2007) Curr. Protoc. Bioinformatics , vol.20 , pp. 191-1924
    • Dutta, S.1    Berman, H.M.2    Bluhm, W.F.3
  • 42
    • 0029937428 scopus 로고    scopus 로고
    • Hidden Markov models
    • DOI 10.1016/S0959-440X(96)80056-X
    • S.R. Eddy Hidden Markov models Curr. Opin. Struct. Biol. 6 1996 361 365 (Pubitemid 26197437)
    • (1996) Current Opinion in Structural Biology , vol.6 , Issue.3 , pp. 361-365
    • Eddy, S.R.1
  • 43
    • 0022510143 scopus 로고
    • Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins
    • D.M. Engelman, T.A. Steitz, and A. Goldman Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins Annu. Rev. Biophys. Biophys. Chem. 15 1986 321 353
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 321-353
    • Engelman, D.M.1    Steitz, T.A.2    Goldman, A.3
  • 44
    • 0036083434 scopus 로고    scopus 로고
    • Characterization of the folding degree of proteins
    • E. Estrada Characterization of the folding degree of proteins Bioinformatics 18 2002 697 704 (Pubitemid 34679116)
    • (2002) Bioinformatics , vol.18 , Issue.5 , pp. 697-704
    • Estrada, E.1
  • 45
    • 0035159445 scopus 로고    scopus 로고
    • Recent advances on the role of topological indices in drug discovery research
    • E. Estrada, and E. Uriarte Recent advances on the role of topological indices in drug discovery research Curr. Med. Chem. 8 2001 1573 1588 (Pubitemid 33076803)
    • (2001) Current Medicinal Chemistry , vol.8 , Issue.13 , pp. 1573-1588
    • Estrada, E.1    Uriarte, E.2
  • 48
    • 0024348221 scopus 로고
    • Protein conformational prediction
    • G.D. Fasman Protein conformational prediction Trends Biochem. Sci. 14 1989 295 299 (Pubitemid 19187260)
    • (1989) Trends in Biochemical Sciences , vol.14 , Issue.7 , pp. 295-299
    • Fasman, G.D.1
  • 49
    • 0036139188 scopus 로고    scopus 로고
    • Probabilistic sampling of protein conformations: New hope for brute force?
    • DOI 10.1002/prot.1163
    • H.J. Feldman, and C.W. Hogue Probabilistic sampling of protein conformations: new hope for brute force? Proteins 46 2002 8 23 (Pubitemid 34033572)
    • (2002) Proteins: Structure, Function and Genetics , vol.46 , Issue.1 , pp. 8-23
    • Feldman, H.J.1    Hogue, C.W.V.2
  • 50
    • 37349058879 scopus 로고    scopus 로고
    • Classification of conformational stability of protein mutants from 3D pseudo-folding graph representation of protein sequences using support vector machines
    • DOI 10.1002/prot.21524
    • M. Fernandez, J. Caballero, L. Fernandez, J.I. Abreu, and G. Acosta Classification of conformational stability of protein mutants from 3D pseudo-folding graph representation of protein sequences using support vector machines Proteins 70 2008 167 175 (Pubitemid 350293458)
    • (2008) Proteins: Structure, Function and Genetics , vol.70 , Issue.1 , pp. 167-175
    • Fernandez, M.1    Caballero, J.2    Fernandez, L.3    Abreu, J.I.4    Acosta, G.5
  • 51
    • 0015184581 scopus 로고
    • Protein-protein interaction and enzymatic activity
    • C. Frieden Protein-protein interaction and enzymatic activity Annu. Rev. Biochem. 40 1971 653 696
    • (1971) Annu. Rev. Biochem. , vol.40 , pp. 653-696
    • Frieden, C.1
  • 52
    • 18244365849 scopus 로고    scopus 로고
    • Protein drug stability: A formulation challenge
    • DOI 10.1038/nrd1695
    • S. Frokjaer, and D.E. Otzen Protein drug stability: a formulation challenge Nat. Rev. Drug Discov. 4 2005 298 306 (Pubitemid 41130943)
    • (2005) Nature Reviews Drug Discovery , vol.4 , Issue.4 , pp. 298-306
    • Frokjaer, S.1    Otzen, D.E.2
  • 53
    • 0022592245 scopus 로고
    • A simple way to look at DNA
    • M.A. Gates A simple way to look at DNA J. Theor. Biol. 119 1986 319 328 (Pubitemid 16123352)
    • (1986) Journal of Theoretical Biology , vol.119 , Issue.3 , pp. 319-328
    • Gates, M.A.1
  • 54
    • 0024427560 scopus 로고
    • Overview of the stability and handling of recombinant protein drugs
    • J. Geigert Overview of the stability and handling of recombinant protein drugs J. Parenter. Sci. Technol. 43 1989 220 224 (Pubitemid 19248859)
    • (1989) Journal of Parenteral Science and Technology , vol.43 , Issue.5 , pp. 220-224
    • Geigert, J.1
  • 55
    • 77649331043 scopus 로고    scopus 로고
    • Computational analysis and determination of a highly conserved surface exposed segment in H5N1 avian flu and H1N1 swine flu neuraminidase
    • A. Ghosh, A. Nandy, and P. Nandy Computational analysis and determination of a highly conserved surface exposed segment in H5N1 avian flu and H1N1 swine flu neuraminidase BMC Struct. Biol. 10 2010 6
    • (2010) BMC Struct. Biol. , vol.10 , pp. 6
    • Ghosh, A.1    Nandy, A.2    Nandy, P.3
  • 56
    • 72949090425 scopus 로고    scopus 로고
    • Computational study of dispersion and extent of mutated and duplicated sequences of the H5N1 influenza neuraminidase over the period 19972008
    • A. Ghosh, A. Nandy, P. Nandy, B.D. Gute, and S.C. Basak Computational study of dispersion and extent of mutated and duplicated sequences of the H5N1 influenza neuraminidase over the period 19972008 J. Chem. Inf. Model. 49 2009 2627 2638
    • (2009) J. Chem. Inf. Model. , vol.49 , pp. 2627-2638
    • Ghosh, A.1    Nandy, A.2    Nandy, P.3    Gute, B.D.4    Basak, S.C.5
  • 57
    • 34948869804 scopus 로고    scopus 로고
    • The ultimate speed limit to protein folding is conformational searching
    • DOI 10.1021/ja066785b
    • K. Ghosh, S.B. Ozkan, and K.A. Dill The ultimate speed limit to protein folding is conformational searching J. Am. Chem. Soc. 129 2007 11920 11927 (Pubitemid 47515346)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.39 , pp. 11920-11927
    • Ghosh, K.1    Ozkan, S.B.2    Dill, K.A.3
  • 58
    • 0014854453 scopus 로고
    • The diagram, a method for comparing sequences. Its use with amino acid and nucleotide sequences
    • A.J. Gibbs, and G.A. McIntyre The diagram, a method for comparing sequences. Its use with amino acid and nucleotide sequences Eur. J. Biochem. 16 1970 1 11
    • (1970) Eur. J. Biochem. , vol.16 , pp. 1-11
    • Gibbs, A.J.1    McIntyre, G.A.2
  • 60
    • 25544474859 scopus 로고    scopus 로고
    • Overview of Immune System
    • W.H. Freeman and Company United State of America
    • R.A. Goldsby, T.J. Kindt, and B.A. Osborne Overview of Immune System Kuby Immunology 2000 W.H. Freeman and Company United State of America pp. 3
    • (2000) Kuby Immunology
    • Goldsby, R.A.1    Kindt, T.J.2    Osborne, B.A.3
  • 62
    • 23644443075 scopus 로고    scopus 로고
    • Recognition of stable protein mutants with 3D stochastic average electrostatic potentials
    • DOI 10.1016/j.febslet.2005.06.065, PII S001457930500815X
    • H. Gonzalez-Diaz, R. Molina, and E. Uriarte Recognition of stable protein mutants with 3D stochastic average electrostatic potentials FEBS Lett. 579 2005 4297 4301 (Pubitemid 41116355)
    • (2005) FEBS Letters , vol.579 , Issue.20 , pp. 4297-4301
    • Gonzalez-Diaz, H.1    Molina, R.2    Uriarte, E.3
  • 64
    • 59149084486 scopus 로고    scopus 로고
    • Predicting antimicrobial drugs and targets with the MARCH-INSIDE approach
    • H. Gonzalez-Diaz, F. Prado-Prado, and F.M. Ubeira Predicting antimicrobial drugs and targets with the MARCH-INSIDE approach Curr. Top. Med. Chem. 8 2008 1676 1690
    • (2008) Curr. Top. Med. Chem. , vol.8 , pp. 1676-1690
    • Gonzalez-Diaz, H.1    Prado-Prado, F.2    Ubeira, F.M.3
  • 65
    • 33947722304 scopus 로고    scopus 로고
    • Computational chemistry approach to protein kinase recognition using 3D stochastic van der Waals spectral moments
    • DOI 10.1002/jcc.20649
    • H. Gonzalez-Diaz, L. Saiz-Urra, R. Molina, Y. Gonzalez-Diaz, and A. Sanchez-Gonzalez Computational chemistry approach to protein kinase recognition using 3D stochastic van der Waals spectral moments J. Comput. Chem. 28 2007 1042 1048 (Pubitemid 46506707)
    • (2007) Journal of Computational Chemistry , vol.28 , Issue.6 , pp. 1042-1048
    • Gonzalez-Diaz, H.1    Saiz-Urra, L.2    Molina, R.3    Gonzalez-Diaz, Y.4    Sanchez-Gonzalez, A.5
  • 66
    • 34447254270 scopus 로고    scopus 로고
    • Medicinal chemistry and bioinformatics - Current trends in drugs discovery with networks topological indices
    • DOI 10.2174/156802607780906771
    • H. Gonzalez-Diaz, S. Vilar, L. Santana, and E. Uriarte Medicinal chemistry and bioinformaticscurrent trends in drugs discovery with networks topological indices Curr. Top. Med. Chem. 7 2007 1015 1029 (Pubitemid 47040529)
    • (2007) Current Topics in Medicinal Chemistry , vol.7 , Issue.10 , pp. 1015-1029
    • Gonzalez-Diaz, H.1    Vilar, S.2    Santana, L.3    Uriarte, E.4
  • 67
    • 3242695128 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus phylogeny: Toward consensus
    • DOI 10.1128/JVI.78.15.7863-7866.2004
    • A.E. Gorbalenya, E.J. Snijder, and W.J. Spaan Severe acute respiratory syndrome coronavirus phylogeny: toward consensus J. Virol. 78 2004 7863 7866 (Pubitemid 38944271)
    • (2004) Journal of Virology , vol.78 , Issue.15 , pp. 7863-7866
    • Gorbalenya, A.E.1    Snijder, E.J.2    Spaan, W.J.M.3
  • 68
    • 0027210418 scopus 로고
    • Optimal alignment between groups of sequences and its application to multiple sequence alignment
    • O. Gotoh Optimal alignment between groups of sequences and its application to multiple sequence alignment Comput. Appl. Biosci. 9 1993 361 370 (Pubitemid 23193511)
    • (1993) Computer Applications in the Biosciences , vol.9 , Issue.3 , pp. 361-370
    • Gotoh, O.1
  • 69
    • 0021849996 scopus 로고
    • Rotavirus neutralizing protein VP7: Antigenic determinants investigated by sequence analysis and peptide synthesis
    • P.R. Gunn, F. Sato, K.F. Powell, A.R. Bellamy, J.R. Napier, and D.R. Harding Rotavirus neutralizing protein VP7: antigenic determinants investigated by sequence analysis and peptide synthesis J. Virol. 54 1985 791 797 (Pubitemid 15014713)
    • (1985) Journal of Virology , vol.54 , Issue.3 , pp. 791-797
    • Gunn, P.R.1    Sato, F.2    Powell, K.F.H.3
  • 70
    • 0034046182 scopus 로고    scopus 로고
    • DNA vaccines: Immunology, application, and optimization
    • DOI 10.1146/annurev.immunol.18.1.927
    • S. Gurunathan, D.M. Klinman, and R.A. Seder DNA vaccines: immunology, application, and optimization Annu. Rev. Immunol. 18 2000 927 974 (Pubitemid 30365401)
    • (2000) Annual Review of Immunology , vol.18 , pp. 927-974
    • Gurunathan, S.1    Klinman, D.M.2    Seder, R.A.3
  • 71
    • 0020659327 scopus 로고
    • H curves, a novel method of representation of nucleotide series especially suited for long DNA sequences
    • E. Hamori, and J. Ruskin H curves, a novel method of representation of nucleotide series especially suited for long DNA sequences J. Biol. Chem. 258 1983 1318 1327 (Pubitemid 13139379)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.2 , pp. 1318-1327
    • Hamori, E.1    Ruskin, J.2
  • 72
    • 0035823083 scopus 로고    scopus 로고
    • Molecular basis for high virulence of Hong Kong H5N1 influenza a viruses
    • DOI 10.1126/science.1062882
    • M. Hatta, P. Gao, P. Halfmann, and Y. Kawaoka Molecular basis for high virulence of Hong Kong H5N1 influenza A viruses Science 293 2001 1840 1842 (Pubitemid 32845783)
    • (2001) Science , vol.293 , Issue.5536 , pp. 1840-1842
    • Hatta, H.1    Gao, P.2    Halfmann, P.3    Kawaoka, Y.4
  • 74
    • 0025340372 scopus 로고
    • Chaos game representation of gene structure
    • H.J. Jeffrey Chaos game representation of gene structure Nucleic Acids Res. 18 1990 2163 2170
    • (1990) Nucleic Acids Res. , vol.18 , pp. 2163-2170
    • Jeffrey, H.J.1
  • 75
    • 14544279925 scopus 로고    scopus 로고
    • Protein folding on the hexagonal lattice in the HP model
    • DOI 10.1142/S0219720005000850, PII S0219720005000850
    • M. Jiang, and B. Zhu Protein folding on the hexagonal lattice in the HP model J. Bioinform. Comput. Biol. 3 2005 19 34 (Pubitemid 40305482)
    • (2005) Journal of Bioinformatics and Computational Biology , vol.3 , Issue.1 , pp. 19-34
    • Jiang, M.1    Zhu, B.2
  • 76
    • 79956118733 scopus 로고    scopus 로고
    • Biological molecules
    • John Wiley & Sons (Asia) Pte Ltd Asia
    • G. Karp Biological molecules Cell and Molecular Biology 2008 John Wiley & Sons (Asia) Pte Ltd Asia p. 31
    • (2008) Cell and Molecular Biology
    • Karp, G.1
  • 77
    • 0008874240 scopus 로고
    • Structure and function in myoglobin and other proteins
    • J.C. Kendrew Structure and function in myoglobin and other proteins Fed. Proc. 18 1959 740 751
    • (1959) Fed. Proc. , vol.18 , pp. 740-751
    • Kendrew, J.C.1
  • 78
  • 80
    • 79956116665 scopus 로고    scopus 로고
    • PDBj Mine: Design and implementation of relational database interface for Protein Data Bank Japan
    • A.R. Kinjo, R. Yamashita, and H. Nakamura PDBj Mine: design and implementation of relational database interface for Protein Data Bank Japan Database (Oxford) Database published online August 25, 2010) 2010 2010 http://database.oxfordjournals.org/cgi/crossref-forward-links/2010/0/baq021 baq021.
    • (2010) Database (Oxford) Database Published Online August 25, 2010) , vol.2010
    • Kinjo, A.R.1    Yamashita, R.2    Nakamura, H.3
  • 81
    • 0017229891 scopus 로고
    • Binding of drugs to serum albumin (first of two parts)
    • J. Koch-Weser, and E.M. Sellers Binding of drugs to serum albumin (first of two parts) N. Engl. J. Med. 294 1976 311 316
    • (1976) N. Engl. J. Med. , vol.294 , pp. 311-316
    • Koch-Weser, J.1    Sellers, E.M.2
  • 84
    • 33846220327 scopus 로고    scopus 로고
    • West Nile virus
    • DOI 10.1016/S1474-4422(07)70030-3, PII S1474442207700303
    • L.D. Kramer, J. Li, and P.Y. Shi West Nile virus Lancet Neurol. 6 2007 171 181 (Pubitemid 46099081)
    • (2007) Lancet Neurology , vol.6 , Issue.2 , pp. 171-181
    • Kramer, L.D.1    Li, J.2    Shi, P.-Y.3
  • 86
    • 45949109669 scopus 로고    scopus 로고
    • MEGA: A biologist-centric software for evolutionary analysis of DNA and protein sequences
    • DOI 10.1093/bib/bbn017, Special Issue: Critical Technologies for Bioinformatics
    • S. Kumar, M. Nei, J. Dudley, and K. Tamura MEGA: a biologist-centric software for evolutionary analysis of DNA and protein sequences Brief Bioinform. 9 2008 299 306 (Pubitemid 351890826)
    • (2008) Briefings in Bioinformatics , vol.9 , Issue.4 , pp. 299-306
    • Kumar, S.1    Nei, M.2    Dudley, J.3    Tamura, K.4
  • 87
    • 0025081218 scopus 로고
    • Coronavirus: Organization, replication and expression of genome
    • M.M. Lai Coronavirus: organization, replication and expression of genome Annu. Rev. Microbiol. 44 1990 303 333
    • (1990) Annu. Rev. Microbiol. , vol.44 , pp. 303-333
    • Lai, M.M.1
  • 88
    • 50849143158 scopus 로고    scopus 로고
    • Evolutionary and transmission dynamics of reassortant H5N1 influenza virus in Indonesia
    • T.T. Lam, C.C. Hon, O.G. Pybus, S.L. Kosakovsky Pond, R.T. Wong, and C.W. Yip Evolutionary and transmission dynamics of reassortant H5N1 influenza virus in Indonesia PLoS Pathog. 4 2008 e1000130
    • (2008) PLoS Pathog. , vol.4 , pp. 1000130
    • Lam, T.T.1    Hon, C.C.2    Pybus, O.G.3    Kosakovsky Pond, S.L.4    Wong, R.T.5    Yip, C.W.6
  • 89
    • 41549106212 scopus 로고    scopus 로고
    • Chromosome evolution with naked eye: Palindromic context of the life origin
    • S. Larionov, A. Loskutov, and E. Ryadchenko Chromosome evolution with naked eye: palindromic context of the life origin Chaos 18 2008 013105
    • (2008) Chaos , vol.18 , pp. 013105
    • Larionov, S.1    Loskutov, A.2    Ryadchenko, E.3
  • 90
    • 0036293431 scopus 로고    scopus 로고
    • Design of novel peptide analogs with potent fungicidal activity, based on PMAP-23 antimicrobial peptide isolated from porcine myeloid
    • DOI 10.1016/S0006-291X(02)00222-X, PII S0006291X0200222X
    • D.G. Lee, P.I. Kim, Y. Park, E.R. Woo, J.S. Choi, and C.H. Choi Design of novel peptide analogs with potent fungicidal activity, based on PMAP-23 antimicrobial peptide isolated from porcine myeloid Biochem. Biophys. Res. Commun. 293 2002 231 238 (Pubitemid 34694196)
    • (2002) Biochemical and Biophysical Research Communications , vol.293 , Issue.1 , pp. 231-238
    • Lee, D.G.1    Kim, P.I.2    Park, Y.3    Woo, E.-R.4    Choi, J.S.5    Choi, C.-H.6    Hahm, K.-S.7
  • 91
    • 0034280320 scopus 로고    scopus 로고
    • Protein structure prediction methods for drug design
    • T. Lengauer, and R. Zimmer Protein structure prediction methods for drug design Brief. Bioinform. 1 2000 275 288
    • (2000) Brief. Bioinform. , vol.1 , pp. 275-288
    • Lengauer, T.1    Zimmer, R.2
  • 92
    • 0028889673 scopus 로고
    • Random walk and gap plots of DNA sequences
    • P.M. Leong, and S. Morgenthaler Random walk and gap plots of DNA sequences Comput. Appl. Biosci. 11 1995 503 507
    • (1995) Comput. Appl. Biosci. , vol.11 , pp. 503-507
    • Leong, P.M.1    Morgenthaler, S.2
  • 93
    • 59649112357 scopus 로고    scopus 로고
    • Rotavirus architecture at subnanometer resolution
    • Z. Li, M.L. Baker, W. Jiang, M.K. Estes, and B.V. Prasad Rotavirus architecture at subnanometer resolution J. Virol. 83 2009 1754 1766
    • (2009) J. Virol. , vol.83 , pp. 1754-1766
    • Li, Z.1    Baker, M.L.2    Jiang, W.3    Estes, M.K.4    Prasad, B.V.5
  • 95
    • 42049104155 scopus 로고    scopus 로고
    • 2-D graphical representation of protein sequences and its application to coronavirus phylogeny
    • C. Li, L. Xing, and X. Wang 2-D graphical representation of protein sequences and its application to coronavirus phylogeny BMB Rep. 41 2008 217 222 (Pubitemid 351518994)
    • (2008) Journal of Biochemistry and Molecular Biology , vol.41 , Issue.3 , pp. 217-222
    • Li, C.1    Xing, L.2    Wang, X.3
  • 96
    • 60349115403 scopus 로고    scopus 로고
    • 3-D maps and coupling numbers for protein sequences
    • C. Li, X. Yu, L. Yang, X. Zheng, and Z. Wang 3-D maps and coupling numbers for protein sequences Physica A 388 2009 1967 1972
    • (2009) Physica A , vol.388 , pp. 1967-1972
    • Li, C.1    Yu, X.2    Yang, L.3    Zheng, X.4    Wang, Z.5
  • 97
    • 33645883236 scopus 로고    scopus 로고
    • Coronavirus phylogeny based on triplets of nucleic acids bases
    • B. Liao, Y. Liu, R. Li, and W. Zhu Coronavirus phylogeny based on triplets of nucleic acids bases Chem. Phys. Lett. 421 2006 313 318
    • (2006) Chem. Phys. Lett. , vol.421 , pp. 313-318
    • Liao, B.1    Liu, Y.2    Li, R.3    Zhu, W.4
  • 98
    • 77956159324 scopus 로고    scopus 로고
    • Vector representations and related matrices of DNA primary sequence based on L-tuple
    • Y.Z. Liu, and T.M. Wang Vector representations and related matrices of DNA primary sequence based on L-tuple Math. Biosci. 227 2010 147 152
    • (2010) Math. Biosci. , vol.227 , pp. 147-152
    • Liu, Y.Z.1    Wang, T.M.2
  • 101
    • 0030580057 scopus 로고    scopus 로고
    • Antibody-antigen interactions: Contact analysis and binding site topography
    • DOI 10.1006/jmbi.1996.0548
    • R.M. MacCallum, A.C. Martin, and J.M. Thornton Antibody-antigen interactions: contact analysis and binding site topography J. Mol. Biol. 262 1996 732 745 (Pubitemid 26343518)
    • (1996) Journal of Molecular Biology , vol.262 , Issue.5 , pp. 732-745
    • MacCallum, R.M.1    Martin, A.C.R.2    Thornton, J.M.3
  • 103
    • 41149116500 scopus 로고    scopus 로고
    • BioMagResBank (BMRB) as a partner in the Worldwide Protein Data Bank (wwPDB): New policies affecting biomolecular NMR depositions
    • J.L. Markley, E.L. Ulrich, H.M. Berman, K. Henrick, H. Nakamura, and H. Akutsu BioMagResBank (BMRB) as a partner in the Worldwide Protein Data Bank (wwPDB): new policies affecting biomolecular NMR depositions J. Biomol. NMR 40 2008 153 155
    • (2008) J. Biomol. NMR , vol.40 , pp. 153-155
    • Markley, J.L.1    Ulrich, E.L.2    Berman, H.M.3    Henrick, K.4    Nakamura, H.5    Akutsu, H.6
  • 104
    • 0033738137 scopus 로고    scopus 로고
    • A comparison of signal sequence prediction methods using a test set of signal peptides
    • K.M. Menne, H. Hermjakob, and R. Apweiler A comparison of signal sequence prediction methods using a test set of signal peptides Bioinformatics 16 2000 741 742
    • (2000) Bioinformatics , vol.16 , pp. 741-742
    • Menne, K.M.1    Hermjakob, H.2    Apweiler, R.3
  • 105
    • 0014296306 scopus 로고
    • The binding of drugs by plasma proteins
    • M.C. Meyer, and D.E. Guttman The binding of drugs by plasma proteins J. Pharm. Sci. 57 1968 895 918
    • (1968) J. Pharm. Sci. , vol.57 , pp. 895-918
    • Meyer, M.C.1    Guttman, D.E.2
  • 106
    • 77954606302 scopus 로고    scopus 로고
    • DNA drugs come of age
    • M.P. Morrow, and D.B. Weiner DNA drugs come of age Sci. Am. 303 2010 49 53
    • (2010) Sci. Am. , vol.303 , pp. 49-53
    • Morrow, M.P.1    Weiner, D.B.2
  • 107
    • 4444250331 scopus 로고    scopus 로고
    • Oseltamivir-resistant influenza?
    • DOI 10.1016/S0140-6736(04)16947-X, PII S014067360416947X
    • A. Moscona Oseltamivir-resistant influenza? Lancet 364 2004 733 734 (Pubitemid 39165079)
    • (2004) Lancet , vol.364 , Issue.9436 , pp. 733-734
    • Moscona, A.1
  • 108
    • 29144433925 scopus 로고    scopus 로고
    • Oseltamivir resistance - Disabling our influenza defenses
    • DOI 10.1056/NEJMp058291
    • A. Moscona Oseltamivir resistancedisabling our influenza defenses N. Engl. J. Med. 353 2005 2633 2636 (Pubitemid 41817709)
    • (2005) New England Journal of Medicine , vol.353 , Issue.25 , pp. 2633-2636
    • Moscona, A.1
  • 109
    • 61849118968 scopus 로고    scopus 로고
    • Global transmission of oseltamivir-resistant influenza
    • A. Moscona Global transmission of oseltamivir-resistant influenza N. Engl. J. Med. 360 2009 953 956
    • (2009) N. Engl. J. Med. , vol.360 , pp. 953-956
    • Moscona, A.1
  • 111
    • 60749111710 scopus 로고    scopus 로고
    • Multi-target QPDR classification model for human breast and colon cancer-related proteins using star graph topological indices
    • C.R. Munteanu, A.L. Magalhaes, E. Uriarte, and H. Gonzalez-Diaz Multi-target QPDR classification model for human breast and colon cancer-related proteins using star graph topological indices J. Theor. Biol. 257 2009 303 311
    • (2009) J. Theor. Biol. , vol.257 , pp. 303-311
    • Munteanu, C.R.1    Magalhaes, A.L.2    Uriarte, E.3    Gonzalez-Diaz, H.4
  • 112
    • 0036596254 scopus 로고    scopus 로고
    • Development of PDBj: Advanced database for protein structures
    • H. Nakamura, N. Ito, and M. Kusunoki Development of PDBj: Advanced database for protein structures Tanpakushitsu Kakusan Koso 47 2002 1097 1101
    • (2002) Tanpakushitsu Kakusan Koso , vol.47 , pp. 1097-1101
    • Nakamura, H.1    Ito, N.2    Kusunoki, M.3
  • 113
    • 0000347441 scopus 로고
    • A new graphical representation and analysis of DNA sequence structure: I. methodology and application to globin genes
    • A. Nandy A new graphical representation and analysis of DNA sequence structure: I. methodology and application to globin genes Curr. Sci. 66 1994 309 314
    • (1994) Curr. Sci. , vol.66 , pp. 309-314
    • Nandy, A.1
  • 114
    • 69949109749 scopus 로고    scopus 로고
    • Empirical relationship between intra-purine and intra-pyrimidine differences in conserved gene sequences
    • A. Nandy Empirical relationship between intra-purine and intra-pyrimidine differences in conserved gene sequences PLoS ONE 4 2009 e6829
    • (2009) PLoS ONE , vol.4 , pp. 6829
    • Nandy, A.1
  • 116
    • 79952202492 scopus 로고    scopus 로고
    • New approaches to drug-DNA interactions based on graphical representation and numerical characterization of DNA sequences
    • A. Nandy, and S.C. Basak New approaches to drug-DNA interactions based on graphical representation and numerical characterization of DNA sequences Curr. Comput. Aided Drug Des. 6 2010 283 289
    • (2010) Curr. Comput. Aided Drug Des. , vol.6 , pp. 283-289
    • Nandy, A.1    Basak, S.C.2
  • 117
    • 34250884662 scopus 로고    scopus 로고
    • Graphical representation and numerical characterization of H5N1 avian flu neuraminidase gene sequence
    • DOI 10.1021/ci600558w
    • A. Nandy, S.C. Basak, and B.D. Gute Graphical representation and numerical characterization of H5N1 avian flu neuraminidase gene sequence J. Chem. Inf. Model. 47 2007 945 951 (Pubitemid 46973709)
    • (2007) Journal of Chemical Information and Modeling , vol.47 , Issue.3 , pp. 945-951
    • Nandy, A.1    Basak, S.C.2    Gute, B.D.3
  • 118
    • 67649850616 scopus 로고    scopus 로고
    • Numerical characterization of protein sequences and application to voltage-gated sodium channel alpha subunit phylogeny
    • A. Nandy, A. Ghosh, and P. Nandy Numerical characterization of protein sequences and application to voltage-gated sodium channel alpha subunit phylogeny In Silico Biol. 9 2009 77 87
    • (2009) Silico Biol. , vol.9 , pp. 77-87
    • Nandy, A.1    Ghosh, A.2    Nandy, P.3
  • 119
    • 33749518282 scopus 로고    scopus 로고
    • Mathematical descriptors of DNA sequences: Development and applications
    • A. Nandy, M. Harle, and S.C. Basak Mathematical descriptors of DNA sequences: development and applications ARKIVOC 9 2006 211 238 (Pubitemid 44527394)
    • (2006) Arkivoc , vol.2006 , Issue.9 , pp. 211-238
    • Nandy, A.1    Harle, M.2    Basak, S.C.3
  • 120
    • 0011479281 scopus 로고
    • Graphical analysis of DNA sequence structure: II. Relative abundances of nucleotides in DNAs, gene evolution and duplication
    • A. Nandy, and P. Nandy Graphical analysis of DNA sequence structure: II. Relative abundances of nucleotides in DNAs, gene evolution and duplication Curr. Sci. 68 1995 75 85
    • (1995) Curr. Sci. , vol.68 , pp. 75-85
    • Nandy, A.1    Nandy, P.2
  • 121
    • 0037435480 scopus 로고    scopus 로고
    • On the uniqueness of quantitative DNA difference descriptions in 2D graphical representation models
    • DOI 10.1016/S0009-2614(02)01830-4, PII S0009261402018304
    • A. Nandy, and P. Nandy On the uniqueness of quantitative DNA difference descriptors in 2D graphical representation models Chem. Phys. Lett. 368 2003 102 107 (Pubitemid 36002836)
    • (2003) Chemical Physics Letters , vol.368 , Issue.1-2 , pp. 102-107
    • Nandy, A.1    Nandy, P.2
  • 122
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • S.B. Needleman, and C.D. Wunsch A general method applicable to the search for similarities in the amino acid sequence of two proteins J. Mol. Biol. 48 1970 443 453
    • (1970) J. Mol. Biol. , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 123
    • 47349096545 scopus 로고    scopus 로고
    • Representation of proteins as walks in 20-D space
    • DOI 10.1080/10629360802085066, PII 793153943
    • M. Novic, and M. Randic Representation of proteins as walks in 20-D space SAR QSAR Environ. Res. 19 2008 317 337 (Pubitemid 351998858)
    • (2008) SAR and QSAR in Environmental Research , vol.19 , Issue.3-4 , pp. 317-337
    • Novic, M.1    Randic, M.2
  • 125
    • 84934444542 scopus 로고    scopus 로고
    • Peptide-based drug design: Here and now
    • L. Otvos Jr. Peptide-based drug design: here and now Methods Mol. Biol. 494 2008 1 8
    • (2008) Methods Mol. Biol. , vol.494 , pp. 1-8
    • Otvos Jr., L.1
  • 126
    • 3042694679 scopus 로고    scopus 로고
    • Building blocks for peptide drugs
    • J. Owens Building blocks for peptide drugs Nat. Rev. Drug Discov. 3 2004 476 (Pubitemid 38807527)
    • (2004) Nature Reviews Drug Discovery , vol.3 , Issue.6 , pp. 476
    • Owens, J.1
  • 130
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • D.N. Perkins, D.J. Pappin, D.M. Creasy, and J.S. Cottrell Probability-based protein identification by searching sequence databases using mass spectrometry data Electrophoresis 20 1999 3551 3567 (Pubitemid 30007252)
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 131
  • 132
    • 36949066642 scopus 로고
    • Structure of haemoglobin: A three-dimensional Fourier synthesis at 5.5-A. resolution, obtained by X-ray analysis
    • M.F. Perutz, M.G. Rossmann, A.F. Cullis, H. Muirhead, G. Will, and A.C. North Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5-A. resolution, obtained by X-ray analysis Nature 185 1960 416 422
    • (1960) Nature , vol.185 , pp. 416-422
    • Perutz, M.F.1    Rossmann, M.G.2    Cullis, A.F.3    Muirhead, H.4    Will, G.5    North, A.C.6
  • 133
    • 15744385737 scopus 로고
    • Crystal structure of human carboxyhaemoglobin
    • M.F. Perutz, and O. Weisz Crystal structure of human carboxyhaemoglobin Nature 160 1947 786
    • (1947) Nature , vol.160 , pp. 786
    • Perutz, M.F.1    Weisz, O.2
  • 136
    • 38349011533 scopus 로고    scopus 로고
    • Mechanisms of protein fibril formation: Nucleated polymerization with competing off-pathway aggregation
    • E.T. Powers, and D.L. Powers Mechanisms of protein fibril formation: nucleated polymerization with competing off-pathway aggregation Biophys. J. 94 2008 379 391
    • (2008) Biophys. J. , vol.94 , pp. 379-391
    • Powers, E.T.1    Powers, D.L.2
  • 139
    • 1442336331 scopus 로고    scopus 로고
    • Graphical representations of DNA as 2-D map
    • M. Randic Graphical representations of DNA as 2-D map Chem. Phys. Lett. 386 2004 468
    • (2004) Chem. Phys. Lett. , vol.386 , pp. 468
    • Randic, M.1
  • 140
    • 33846325883 scopus 로고    scopus 로고
    • Spectrum-like graphical representation of DNA based on codons
    • M. Randic Spectrum-like graphical representation of DNA based on codons Acta Chim. Slov. 53 2006 477 485
    • (2006) Acta Chim. Slov. , vol.53 , pp. 477-485
    • Randic, M.1
  • 141
    • 32344433839 scopus 로고    scopus 로고
    • Novel 2-D graphical representation of proteins
    • DOI 10.1016/j.cplett.2005.11.091, PII S000926140501835X
    • M. Randic, D. Butina, and J. Zupan Novel 2-D graphical representation of proteins Chem. Phys. Lett. 419 2006 528 532 (Pubitemid 43220524)
    • (2006) Chemical Physics Letters , vol.419 , Issue.4-6 , pp. 528-532
    • Randic, M.1    Butina, D.2    Zupan, J.3
  • 142
    • 17844389846 scopus 로고    scopus 로고
    • Four-color map representation of DNA or RNA sequences and their numerical characterization
    • DOI 10.1016/j.cplett.2005.03.086, PII S0009261405003957
    • M. Randic, N. Lers, D. Plavsic, S.C. Basak, and A.T. Balaban Four-color map representation of DNA or RNA sequences and their numerical characterization Chem. Phys. Lett. 407 2005 205 208 (Pubitemid 40584111)
    • (2005) Chemical Physics Letters , vol.407 , Issue.1-3 , pp. 205-208
    • Randic, M.1    Lers, N.2    Plavsic, D.3    Basak, S.C.4    Balaban, A.T.5
  • 143
    • 47349126419 scopus 로고    scopus 로고
    • On novel representation of proteins based on amino acid adjacency matrix
    • DOI 10.1080/10629360802085082, PII 793152530
    • M. Randic, M. Novic, and M. Vracko On novel representation of proteins based on amino acid adjacency matrix SAR QSAR Environ. Res. 19 2008 339 349 (Pubitemid 351998857)
    • (2008) SAR and QSAR in Environmental Research , vol.19 , Issue.3-4 , pp. 339-349
    • Randic, M.1    Novic, M.2    Vracko, M.3
  • 144
    • 0037470662 scopus 로고    scopus 로고
    • Analysis of similarity/dissimilarity of DNA sequences based on novel 2-D graphical representation
    • M. Randic, M. Vracko, N. Lers, and D. Plavsic Analysis of similarity/dissimilarity of DNA sequences based on novel 2-D graphical representation Chem. Phys. Lett. 371 2003 202
    • (2003) Chem. Phys. Lett. , vol.371 , pp. 202
    • Randic, M.1    Vracko, M.2    Lers, N.3    Plavsic, D.4
  • 145
    • 0037435485 scopus 로고    scopus 로고
    • Novel 2-D graphical representation of DNA sequences and their numerical characterization
    • M. Randic, M. Vracko, N. Lers, and D. Plavsic Novel 2-D graphical representation of DNA sequences and their numerical characterization Chem. Phys. Lett. 368 2003 1
    • (2003) Chem. Phys. Lett. , vol.368 , pp. 1
    • Randic, M.1    Vracko, M.2    Lers, N.3    Plavsic, D.4
  • 146
    • 0034266159 scopus 로고    scopus 로고
    • On 3-D graphical representation of DNA primary sequences and their numerical characterization
    • M. Randic, M. Vracko, A. Nandy, and S.C. Basak On 3-D graphical representation of DNA primary sequences and their numerical characterization J. Chem. Inf. Comput. Sci. 40 2000 1235 1244
    • (2000) J. Chem. Inf. Comput. Sci. , vol.40 , pp. 1235-1244
    • Randic, M.1    Vracko, M.2    Nandy, A.3    Basak, S.C.4
  • 148
    • 7444235858 scopus 로고    scopus 로고
    • Unique graphical representation of protein sequences based on nucleotide triplet codons
    • M. Randic, J. Zupan, and A.T. Balaban Unique graphical representation of protein sequences based on nucleotide triplet codons Chem. Phys. Lett. 397 2004 247 252
    • (2004) Chem. Phys. Lett. , vol.397 , pp. 247-252
    • Randic, M.1    Zupan, J.2    Balaban, A.T.3
  • 150
    • 0030585164 scopus 로고    scopus 로고
    • Kinesin and myosin: Molecular motors with similar engines
    • I. Rayment Kinesin and myosin: molecular motors with similar engines Structure 4 1996 501 504 (Pubitemid 126657543)
    • (1996) Structure , vol.4 , Issue.5 , pp. 501-504
    • Rayment, I.1
  • 152
    • 0033990046 scopus 로고    scopus 로고
    • Phylogenetic analysis using PHYLIP
    • J.D. Retief Phylogenetic analysis using PHYLIP Methods Mol. Biol. 132 2000 243 258
    • (2000) Methods Mol. Biol. , vol.132 , pp. 243-258
    • Retief, J.D.1
  • 153
    • 20444421544 scopus 로고    scopus 로고
    • Interpretation of protein adsorption: Surface-induced conformational changes
    • DOI 10.1021/ja042898o
    • P. Roach, D. Farrar, and C.C. Perry Interpretation of protein adsorption: surface-induced conformational changes J. Am. Chem. Soc. 127 2005 8168 8173 (Pubitemid 40799673)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.22 , pp. 8168-8173
    • Roach, P.1    Farrar, D.2    Perry, C.C.3
  • 154
    • 33645459798 scopus 로고    scopus 로고
    • Surface tailoring for controlled protein adsorption: Effect of topography at the nanometer scale and chemistry
    • P. Roach, D. Farrar, and C.C. Perry Surface tailoring for controlled protein adsorption: effect of topography at the nanometer scale and chemistry J. Am. Chem. Soc. 128 2006 3939 3945
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 3939-3945
    • Roach, P.1    Farrar, D.2    Perry, C.C.3
  • 156
    • 0019365279 scopus 로고
    • A general method for site-directed mutagenesis in prokaryotes
    • DOI 10.1038/289085a0
    • G.B. Ruvkun, and F.M. Ausubel A general method for site-directed mutagenesis in prokaryotes Nature 289 1981 85 88 (Pubitemid 11178462)
    • (1981) Nature , vol.289 , Issue.5793 , pp. 85-88
    • Ruvkun, G.B.1    Ausubel, F.M.2
  • 157
    • 12444308929 scopus 로고
    • The arrangement of amino acids in proteins
    • F. Sanger The arrangement of amino acids in proteins Adv. Protein Chem. 7 1952 1 67
    • (1952) Adv. Protein Chem. , vol.7 , pp. 1-67
    • Sanger, F.1
  • 158
    • 77049132676 scopus 로고
    • The amino-acid sequence in the glycyl chain of insulin. I. The identification of lower peptides from partial hydrolysates
    • F. Sanger, and E.O. Thompson The amino-acid sequence in the glycyl chain of insulin. I. The identification of lower peptides from partial hydrolysates Biochem. J. 53 1953 353 366
    • (1953) Biochem. J. , vol.53 , pp. 353-366
    • Sanger, F.1    Thompson, E.O.2
  • 159
    • 76949111135 scopus 로고
    • The amino-acid sequence in the phenylalanyl chain of insulin. I. The identification of lower peptides from partial hydrolysates
    • F. Sanger, and H. Tuppy The amino-acid sequence in the phenylalanyl chain of insulin. I. The identification of lower peptides from partial hydrolysates Biochem. J. 49 1951 463 481
    • (1951) Biochem. J. , vol.49 , pp. 463-481
    • Sanger, F.1    Tuppy, H.2
  • 160
    • 0036598634 scopus 로고    scopus 로고
    • Bioequivalence and the immunogenicity of biopharmaceuticals
    • H. Schellekens Bioequivalence and the immunogenicity of biopharmaceuticals Nat. Rev. Drug Discov. 1 2002 457 462 (Pubitemid 37361488)
    • (2002) Nature Reviews Drug Discovery , vol.1 , Issue.6 , pp. 457-462
    • Schellekens, H.1
  • 161
    • 58149114611 scopus 로고    scopus 로고
    • Predicting protein fold pattern with functional domain and sequential evolution information
    • H.B. Shen, and K.C. Chou Predicting protein fold pattern with functional domain and sequential evolution information J. Theor. Biol. 256 2009 441 446
    • (2009) J. Theor. Biol. , vol.256 , pp. 441-446
    • Shen, H.B.1    Chou, K.C.2
  • 162
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • T.F. Smith, and M.S. Waterman Identification of common molecular subsequences J. Mol. Biol. 147 1981 195 197
    • (1981) J. Mol. Biol. , vol.147 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 163
    • 0022431785 scopus 로고
    • The statistical distribution of nucleic acid similarities
    • T.F. Smith, M.S. Waterman, and C. Burks The statistical distribution of nucleic acid similarities Nucleic Acids Res. 13 1985 645 656
    • (1985) Nucleic Acids Res. , vol.13 , pp. 645-656
    • Smith, T.F.1    Waterman, M.S.2    Burks, C.3
  • 164
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • DOI 10.1093/molbev/msm092
    • K. Tamura, J. Dudley, M. Nei, and S. Kumar MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0 Mol. Biol. Evol. 24 2007 1596 1599 (Pubitemid 47236692)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.8 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 166
    • 0037666888 scopus 로고    scopus 로고
    • Implications of protein flexibility for drug discovery
    • S.J. Teague Implications of protein flexibility for drug discovery Nat. Rev. Drug Discov. 2 2003 527 541 (Pubitemid 37361745)
    • (2003) Nature Reviews Drug Discovery , vol.2 , Issue.7 , pp. 527-541
    • Teague, S.J.1
  • 167
    • 60649108435 scopus 로고    scopus 로고
    • A new similarity/diversity measure for the characterization of DNA sequences
    • R. Todeschini, D. Ballabio, V. Consonni, and A. Mauri A new similarity/diversity measure for the characterization of DNA sequences Croat. Chem. Acta 81 2008 657 664
    • (2008) Croat. Chem. Acta , vol.81 , pp. 657-664
    • Todeschini, R.1    Ballabio, D.2    Consonni, V.3    Mauri, A.4
  • 168
    • 33750321979 scopus 로고    scopus 로고
    • Characterization of DNA primary sequences by a new similarity/diversity measure based on the partial ordering
    • DOI 10.1021/ci060099e
    • R. Todeschini, V. Consonni, A. Mauri, and D. Ballabio Characterization of DNA primary sequences by a new similarity/diversity measure based on the partial ordering J. Chem. Inf. Model. 46 2006 1905 1911 (Pubitemid 44625961)
    • (2006) Journal of Chemical Information and Modeling , vol.46 , Issue.5 , pp. 1905-1911
    • Todeschini, R.1    Consonni, V.2    Mauri, A.3    Ballabio, D.4
  • 176
    • 57049145806 scopus 로고    scopus 로고
    • QSAR model for alignment-free prediction of human breast cancer biomarkers based on electrostatic potentials of protein pseudofolding HP-lattice networks
    • S. Vilar, H. Gonzalez-Diaz, L. Santana, and E. Uriarte QSAR model for alignment-free prediction of human breast cancer biomarkers based on electrostatic potentials of protein pseudofolding HP-lattice networks J. Comput. Chem. 29 2008 2613 2622
    • (2008) J. Comput. Chem. , vol.29 , pp. 2613-2622
    • Vilar, S.1    Gonzalez-Diaz, H.2    Santana, L.3    Uriarte, E.4
  • 178
    • 0032726679 scopus 로고    scopus 로고
    • A computational approach to simplifying the protein folding alphabet
    • DOI 10.1038/14918
    • J. Wang, and W. Wang A computational approach to simplifying the protein folding alphabet Nat. Struct. Biol. 6 1999 1033 1038 (Pubitemid 29519597)
    • (1999) Nature Structural Biology , vol.6 , Issue.11 , pp. 1033-1038
    • Wang, J.1    Wang, W.2
  • 179
    • 77958563968 scopus 로고    scopus 로고
    • 2D random walk representation of Begonia × tuberhybrida multiallelic loci used for germplasm identification
    • I. Wiesner, and D. Wiesnerova 2D random walk representation of Begonia × tuberhybrida multiallelic loci used for germplasm identification Biologia Plantarum 54 2010 353 356
    • (2010) Biologia Plantarum , vol.54 , pp. 353-356
    • Wiesner, I.1    Wiesnerova, D.2
  • 181
    • 64049090391 scopus 로고    scopus 로고
    • An introduction to epitope prediction methods and software
    • X. Yang, and X. Yu An introduction to epitope prediction methods and software Rev. Med. Virol. 19 2009 77 96
    • (2009) Rev. Med. Virol. , vol.19 , pp. 77-96
    • Yang, X.1    Yu, X.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.