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Volumn 34, Issue 1, 2008, Pages 81-90

Prediction of mutations engineered by randomness in H5N1 neuraminidases from influenza a virus

Author keywords

Influenza; Logistic regression; Mutation; Neuraminidase; Prediction

Indexed keywords

VIRUS HEMAGGLUTININ; VIRUS SIALIDASE;

EID: 38149089523     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00726-007-0579-z     Document Type: Article
Times cited : (19)

References (119)
  • 1
    • 0022416469 scopus 로고
    • Gene and protein sequence of an influenza neuraminidase with hemagglutinin activity
    • GM Air LR Ritchie WG Laver PM Colman 1985 Gene and protein sequence of an influenza neuraminidase with hemagglutinin activity Virology 145 117 122
    • (1985) Virology , vol.145 , pp. 117-122
    • Air, G.M.1    Ritchie, L.R.2    Laver, W.G.3    Colman, P.M.4
  • 8
    • 0027219970 scopus 로고
    • A vectorized sequence-coupling model for predicting HIV protease cleavage sites in proteins
    • KC Chou 1993 A vectorized sequence-coupling model for predicting HIV protease cleavage sites in proteins J Biol Chem 268 16938 16948
    • (1993) J Biol Chem , vol.268 , pp. 16938-16948
    • Chou, K.C.1
  • 9
    • 0027170793 scopus 로고
    • A formulation for correlating properties of peptides and its application to predicting human immunodeficiency virus protease-cleavable sites in proteins
    • JJ Chou 1993a A formulation for correlating properties of peptides and its application to predicting human immunodeficiency virus protease-cleavable sites in proteins Biopolymers 33 1405 1414
    • (1993) Biopolymers , vol.33 , pp. 1405-1414
    • Chou, J.J.1
  • 10
    • 0027325504 scopus 로고
    • Predicting cleavability of peptide sequences by HIV protease via correlation-angle approach
    • JJ Chou 1993b Predicting cleavability of peptide sequences by HIV protease via correlation-angle approach J Protein Chem 12 291 302
    • (1993) J Protein Chem , vol.12 , pp. 291-302
    • Chou, J.J.1
  • 11
    • 0030049315 scopus 로고    scopus 로고
    • Prediction of HIV protease cleavage sites in proteins
    • KC Chou 1996 Prediction of HIV protease cleavage sites in proteins Anal Biochem 233 1 14
    • (1996) Anal Biochem , vol.233 , pp. 1-14
    • Chou, K.C.1
  • 12
    • 2642517838 scopus 로고    scopus 로고
    • Insights from modelling the 3D structure of the extracellular domain of alpha7 nicotinic acetylcholine receptor
    • KC Chou 2004a Insights from modelling the 3D structure of the extracellular domain of alpha7 nicotinic acetylcholine receptor Biochem Biophys Res Commun 319 433 438
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 433-438
    • Chou, K.C.1
  • 13
    • 7044241339 scopus 로고    scopus 로고
    • Insights from modelling the tertiary structure of BACE2
    • KC Chou 2004b Insights from modelling the tertiary structure of BACE2 J Proteome Res 3 1069 1072
    • (2004) J Proteome Res , vol.3 , pp. 1069-1072
    • Chou, K.C.1
  • 14
    • 11144275172 scopus 로고    scopus 로고
    • Molecular therapeutic target for type-2 diabetes
    • KC Chou 2004c Molecular therapeutic target for type-2 diabetes J Proteome Res 3 1284 1288
    • (2004) J Proteome Res , vol.3 , pp. 1284-1288
    • Chou, K.C.1
  • 15
    • 3242792729 scopus 로고    scopus 로고
    • Structural bioinformatics and its impact to biomedical science
    • KC Chou 2004d Structural bioinformatics and its impact to biomedical science Curr Med Chem 11 2105 2134
    • (2004) Curr Med Chem , vol.11 , pp. 2105-2134
    • Chou, K.C.1
  • 16
    • 1642377868 scopus 로고    scopus 로고
    • Modelling extracellular domains of GABA-A receptors: Subtypes 1, 2, 3, and 5
    • KC Chou 2004e Modelling extracellular domains of GABA-A receptors: subtypes 1, 2, 3, and 5 Biochem Biophys Res Commun 316 636 642
    • (2004) Biochem Biophys Res Commun , vol.316 , pp. 636-642
    • Chou, K.C.1
  • 17
    • 17444427671 scopus 로고    scopus 로고
    • Modeling the tertiary structure of human cathepsin-E
    • KC Chou 2005 Modeling the tertiary structure of human cathepsin-E Biochem Biophys Res Commun 331 56 60
    • (2005) Biochem Biophys Res Commun , vol.331 , pp. 56-60
    • Chou, K.C.1
  • 18
    • 0031449933 scopus 로고    scopus 로고
    • Prediction of the tertiary structure and substrate binding site of caspase-8
    • KC Chou D Jones RL Heinrikson 1997 Prediction of the tertiary structure and substrate binding site of caspase-8 FEBS Lett 419 49 54
    • (1997) FEBS Lett , vol.419 , pp. 49-54
    • Chou, K.C.1    Jones, D.2    Heinrikson, R.L.3
  • 19
    • 0028071544 scopus 로고
    • Steady-state inhibition kinetics of processive nucleic acid polymerases and nucleases
    • KC Chou FJ Kezdy F Reusser 1994 Steady-state inhibition kinetics of processive nucleic acid polymerases and nucleases Anal Biochem 221 217 230
    • (1994) Anal Biochem , vol.221 , pp. 217-230
    • Chou, K.C.1    Kezdy, F.J.2    Reusser, F.3
  • 20
    • 0034737556 scopus 로고    scopus 로고
    • Prediction of the tertiary structure of a caspase-9/inhibitor complex
    • KC Chou AG Tomasselli RL Heinrikson 2000 Prediction of the tertiary structure of a caspase-9/inhibitor complex FEBS Lett 470 249 256
    • (2000) FEBS Lett , vol.470 , pp. 249-256
    • Chou, K.C.1    Tomasselli, A.G.2    Heinrikson, R.L.3
  • 21
    • 0033532596 scopus 로고    scopus 로고
    • A model of the complex between cyclin-dependent kinase 5(Cdk5) and the activation domain of neuronal Cdk5 activator
    • KC Chou KD Watenpaugh RL Heinrikson 1999 A model of the complex between cyclin-dependent kinase 5(Cdk5) and the activation domain of neuronal Cdk5 activator Biochem Biophys Res Commun 259 420 428
    • (1999) Biochem Biophys Res Commun , vol.259 , pp. 420-428
    • Chou, K.C.1    Watenpaugh, K.D.2    Heinrikson, R.L.3
  • 22
    • 33750554701 scopus 로고    scopus 로고
    • Progress in computational approach to drug development against SARS
    • KC Chou DQ Wei QS Du S Sirois WZ Zhong 2006 Progress in computational approach to drug development against SARS Curr Med Chem 13 3263 3270
    • (2006) Curr Med Chem , vol.13 , pp. 3263-3270
    • Chou, K.C.1    Wei, D.Q.2    Du, Q.S.3    Sirois, S.4    Zhong, W.Z.5
  • 23
    • 0041848237 scopus 로고    scopus 로고
    • Binding mechanism of coronavirus main proteinase with ligands and its implication to drug design against SARS
    • Erratum: ibid, 2003, 310, 675
    • KC Chou DQ Wei WZ Zhong 2003 Binding mechanism of coronavirus main proteinase with ligands and its implication to drug design against SARS Biochem Biophys Res Comm 308 148 151 Erratum: ibid, 2003, 310, 675
    • (2003) Biochem Biophys Res Comm , vol.308 , pp. 148-151
    • Chou, K.C.1    Wei, D.Q.2    Zhong, W.Z.3
  • 25
    • 0024504990 scopus 로고
    • Distinct lineages of influenza virus H4 hemagglutinin genes in different regions of the world
    • RO Donis WJ Bean Y Kawaoka RG Webster 1989 Distinct lineages of influenza virus H4 hemagglutinin genes in different regions of the world Virology 169 408 417
    • (1989) Virology , vol.169 , pp. 408-417
    • Donis, R.O.1    Bean, W.J.2    Kawaoka, Y.3    Webster, R.G.4
  • 27
    • 16244414853 scopus 로고    scopus 로고
    • Heuristic molecular lipophilicity potential (HMLP): A 2D-QSAR study to LADH of molecular family pyrazole and derivatives
    • QS Du PG Mezey KC Chou 2005 Heuristic molecular lipophilicity potential (HMLP): a 2D-QSAR study to LADH of molecular family pyrazole and derivatives J Comput Chem 26 461 470
    • (2005) J Comput Chem , vol.26 , pp. 461-470
    • Du, Q.S.1    Mezey, P.G.2    Chou, K.C.3
  • 28
    • 33846052414 scopus 로고    scopus 로고
    • Inhibitor design for SARS coronavirus main protease based on "distorted key theory"
    • QS Du H Sun KC Chou 2007 Inhibitor design for SARS coronavirus main protease based on "distorted key theory" Med Chem 3 1 6
    • (2007) Med Chem , vol.3 , pp. 1-6
    • Du, Q.S.1    Sun, H.2    Chou, K.C.3
  • 31
    • 0021712450 scopus 로고
    • Aligning amino acid sequences: Comparison of commonly used methods
    • DF Feng MS Johnson RF Doolittle 1985 Aligning amino acid sequences: comparison of commonly used methods J Mol Evol 21 112 125
    • (1985) J Mol Evol , vol.21 , pp. 112-125
    • Feng, D.F.1    Johnson, M.S.2    Doolittle, R.F.3
  • 32
    • 0030750055 scopus 로고    scopus 로고
    • Long term trends in the evolution of H(3) HA1 human influenza type a
    • WM Fitch RM Bush CA Bender NJ Cox 1997 Long term trends in the evolution of H(3) HA1 human influenza type A Proc Natl Acad Sci USA 94 7712 7718
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7712-7718
    • Fitch, W.M.1    Bush, R.M.2    Bender, C.A.3    Cox, N.J.4
  • 33
    • 1442351171 scopus 로고    scopus 로고
    • Controlling influenza by inhibiting the virus's neuraminidase
    • E Garman G Laver 2004 Controlling influenza by inhibiting the virus's neuraminidase Curr Drug Targ 5 119 136
    • (2004) Curr Drug Targ , vol.5 , pp. 119-136
    • Garman, E.1    Laver, G.2
  • 34
    • 33645750737 scopus 로고    scopus 로고
    • Pattern of positions sensitive to mutations in human haemoglobin α-chain
    • N Gao S Yan G Wu 2006 Pattern of positions sensitive to mutations in human haemoglobin α-chain Protein Pept Lett 13 101 107
    • (2006) Protein Pept Lett , vol.13 , pp. 101-107
    • Gao, N.1    Yan, S.2    Wu, G.3
  • 35
    • 34248679618 scopus 로고    scopus 로고
    • Agaritine and its derivatives are potential inhibitors against HIV proteases
    • WN Gao DQ Wei Y Li H Gao WR Xu AX Li KC Chou 2007 Agaritine and its derivatives are potential inhibitors against HIV proteases Med Chem 3 221 226
    • (2007) Med Chem , vol.3 , pp. 221-226
    • Gao, W.N.1    Wei, D.Q.2    Li, Y.3    Gao, H.4    Xu, W.R.5    Li, A.X.6    Chou, K.C.7
  • 36
    • 0342745990 scopus 로고
    • The specific enzyme of influenza virus and Vibrio cholerae
    • A Gottschalk 1957 The specific enzyme of influenza virus and Vibrio cholerae Biochim Biophys Acta 23 645 646
    • (1957) Biochim Biophys Acta , vol.23 , pp. 645-646
    • Gottschalk, A.1
  • 38
    • 0024477478 scopus 로고
    • Molecular cloning and analysis of the N5 neuraminidase subtype from an avian influenza virus
    • VR Harley CW Ward PJ Hudson 1989 Molecular cloning and analysis of the N5 neuraminidase subtype from an avian influenza virus Virology 169 239 243
    • (1989) Virology , vol.169 , pp. 239-243
    • Harley, V.R.1    Ward, C.W.2    Hudson, P.J.3
  • 39
    • 0018398739 scopus 로고
    • Outliers in clinical chemistry quality-control schemes
    • MJR Healy 1979 Outliers in clinical chemistry quality-control schemes Clin Chem 25 675 677
    • (1979) Clin Chem , vol.25 , pp. 675-677
    • Healy, M.J.R.1
  • 40
    • 0037135669 scopus 로고    scopus 로고
    • Realities and enigmas of human viral influenza: Pathogenesis, epidemiology and control
    • MR Hilleman 2002 Realities and enigmas of human viral influenza: pathogenesis, epidemiology and control Vaccine 20 3068 3087
    • (2002) Vaccine , vol.20 , pp. 3068-3087
    • Hilleman, M.R.1
  • 44
    • 38149028366 scopus 로고    scopus 로고
    • Influenza virus resources (2006) http://www.ncbi.nlm.nih.gov/genomes/FLU/ Database/multiple.cgi
    • (2006) Influenza Virus Resources
  • 45
    • 0005544155 scopus 로고
    • Multiple-alphabet amino acid sequence comparisons of the immunoglobulin kappa-chain constant domain
    • S Karlin G Ghandour 1985 Multiple-alphabet amino acid sequence comparisons of the immunoglobulin kappa-chain constant domain Proc Natl Acad Sci USA 82 8597 8601
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 8597-8601
    • Karlin, S.1    Ghandour, G.2
  • 48
    • 34249743013 scopus 로고    scopus 로고
    • Computational studies of the binding mechanism of calmodulin with chrysin
    • L Li DQ Wei JF Wang KC Chou 2007 Computational studies of the binding mechanism of calmodulin with chrysin Biochem Biophys Res Commun 358 1102 1107
    • (2007) Biochem Biophys Res Commun , vol.358 , pp. 1102-1107
    • Li, L.1    Wei, D.Q.2    Wang, J.F.3    Chou, K.C.4
  • 50
    • 0036134748 scopus 로고    scopus 로고
    • Estimating amino acid substitution models: A comparison of Dayhoff's estimator, the resolvent approach and a maximum likelihood method
    • T Müller R Spang M Vingron 2002 Estimating amino acid substitution models: a comparison of Dayhoff's estimator, the resolvent approach and a maximum likelihood method Mol Biol Evol 19 8 13
    • (2002) Mol Biol Evol , vol.19 , pp. 8-13
    • Müller, T.1    Spang, R.2    Vingron, M.3
  • 51
    • 1242285459 scopus 로고    scopus 로고
    • A new millennium conundrum: How to use a powerful class of influenza anti-neuraminidase drugs (NAIs) in the community
    • J Oxford S Balasingam R Lambkin 2004 A new millennium conundrum: how to use a powerful class of influenza anti-neuraminidase drugs (NAIs) in the community J Antimicrob Chemother 53 133 136
    • (2004) J Antimicrob Chemother , vol.53 , pp. 133-136
    • Oxford, J.1    Balasingam, S.2    Lambkin, R.3
  • 52
    • 0000545033 scopus 로고
    • Interactions of animal viruses with cell surface receptors
    • Academic Press Orlando
    • JC Paulson 1985 Interactions of animal viruses with cell surface receptors M Connor The receptors Academic Press Orlando 131 219
    • (1985) The Receptors , pp. 131-219
    • Paulson, J.C.1    Connor, M.2
  • 53
    • 0029044113 scopus 로고
    • Do hemagglutinin genes of highly pathogenic avian influenza viruses constitute unique phylogenetic lineages?
    • C Rohm T Horimoto Y Kawaoka J Suss RG Webster 1995 Do hemagglutinin genes of highly pathogenic avian influenza viruses constitute unique phylogenetic lineages? Virology 209 664 670
    • (1995) Virology , vol.209 , pp. 664-670
    • Rohm, C.1    Horimoto, T.2    Kawaoka, Y.3    Suss, J.4    Webster, R.G.5
  • 55
    • 1642491743 scopus 로고    scopus 로고
    • Evolutional analysis of human influenza a virus N2 neuraminidase genes based on the transition of the low-pH stability of sialidase activity
    • T Suzuki T Takahashi T Saito CT Guo KI Hidari D Miyamoto Y Suzuki 2004 Evolutional analysis of human influenza A virus N2 neuraminidase genes based on the transition of the low-pH stability of sialidase activity FEBS Lett 557 228 232
    • (2004) FEBS Lett , vol.557 , pp. 228-232
    • Suzuki, T.1    Takahashi, T.2    Saito, T.3    Guo, C.T.4    Hidari, K.I.5    Miyamoto, D.6    Suzuki, Y.7
  • 56
    • 0029595415 scopus 로고
    • Neural network prediction of the HIV-1 protease cleavage sites
    • TB Thompson KC Chou C Zheng 1995 Neural network prediction of the HIV-1 protease cleavage sites J Theor Biol 177 369 379
    • (1995) J Theor Biol , vol.177 , pp. 369-379
    • Thompson, T.B.1    Chou, K.C.2    Zheng, C.3
  • 57
    • 33847129220 scopus 로고    scopus 로고
    • 3D structure modeling of cytochrome P450 2C19 and its implication for personalized drug design
    • Corrigendum: ibid, 2007, 357, 330
    • JF Wang DQ Wei L Li SY Zheng YX Li KC Chou 2007a 3D structure modeling of cytochrome P450 2C19 and its implication for personalized drug design Biochem Biophys Res Commun 355 513 519 Corrigendum: ibid, 2007, 357, 330
    • (2007) Biochem Biophys Res Commun , vol.355 , pp. 513-519
    • Wang, J.F.1    Wei, D.Q.2    Li, L.3    Zheng, S.Y.4    Li, Y.X.5    Chou, K.C.6
  • 58
    • 34249993539 scopus 로고    scopus 로고
    • Insights from modeling the 3D structure of NAD(P)H-dependent D-xylose reductase of Pichia stipitis and its binding interactions with NAD and NADP
    • JF Wang DQ Wei Y Lin YH Wang HL Du KC Chou 2007c Insights from modeling the 3D structure of NAD(P)H-dependent D-xylose reductase of Pichia stipitis and its binding interactions with NAD and NADP Biochem Biophys Res Commun 359 323 329
    • (2007) Biochem Biophys Res Commun , vol.359 , pp. 323-329
    • Wang, J.F.1    Wei, D.Q.2    Lin, Y.3    Wang, Y.H.4    Du, H.L.5    Chou, K.C.6
  • 59
    • 33846617350 scopus 로고    scopus 로고
    • Study of drug resistance of chicken influenza a virus (H5N1) from homology-modeled 3D structures of neuraminidases
    • SQ Wang QS Du KC Chou 2007b Study of drug resistance of chicken influenza A virus (H5N1) from homology-modeled 3D structures of neuraminidases Biochem Biophys Res Commun 354 634 640
    • (2007) Biochem Biophys Res Commun , vol.354 , pp. 634-640
    • Wang, S.Q.1    Du, Q.S.2    Chou, K.C.3
  • 60
    • 33646160618 scopus 로고    scopus 로고
    • Insights from modeling the 3D structure of H5N1 influenza virus neuraminidase and its binding interactions with ligands
    • DQ Wei QS Du H Sun KC Chou 2006 Insights from modeling the 3D structure of H5N1 influenza virus neuraminidase and its binding interactions with ligands Biochem Biophys Res Commun 344 1048 1055
    • (2006) Biochem Biophys Res Commun , vol.344 , pp. 1048-1055
    • Wei, D.Q.1    Du, Q.S.2    Sun, H.3    Chou, K.C.4
  • 61
    • 33846449105 scopus 로고    scopus 로고
    • Molecular insights of SAH enzyme catalysis and their implication for inhibitor design
    • H Wei R Zhang C Wang H Zheng KC Chou DQ Wei 2007 Molecular insights of SAH enzyme catalysis and their implication for inhibitor design J Theor Biol 244 692 702
    • (2007) J Theor Biol , vol.244 , pp. 692-702
    • Wei, H.1    Zhang, R.2    Wang, C.3    Zheng, H.4    Chou, K.C.5    Wei, D.Q.6
  • 62
    • 0031172024 scopus 로고    scopus 로고
    • An explanation for failure to predict cyclosporine area under the curve using a limited sampling strategy: A beginner's second note
    • G Wu 1997 An explanation for failure to predict cyclosporine area under the curve using a limited sampling strategy: a beginner's second note Pharmacol Res 35 547 552
    • (1997) Pharmacol Res , vol.35 , pp. 547-552
    • Wu, G.1
  • 64
    • 0034708151 scopus 로고    scopus 로고
    • Frequency and Markov chain analysis of amino-acid sequence of human glutathione reductase
    • G Wu 2000a Frequency and Markov chain analysis of amino-acid sequence of human glutathione reductase Biochem Biophys Res Commun 268 823 826
    • (2000) Biochem Biophys Res Commun , vol.268 , pp. 823-826
    • Wu, G.1
  • 65
    • 0034729355 scopus 로고    scopus 로고
    • Frequency and Markov chain analysis of amino-acid sequence of human tumor necrosis factor
    • G Wu 2000b Frequency and Markov chain analysis of amino-acid sequence of human tumor necrosis factor Cancer Lett 153 145 150
    • (2000) Cancer Lett , vol.153 , pp. 145-150
    • Wu, G.1
  • 66
    • 0034492525 scopus 로고    scopus 로고
    • Frequency and Markov chain analysis of amino-acid sequences of mouse p53
    • G Wu 2000c Frequency and Markov chain analysis of amino-acid sequences of mouse p53 Human Exper Toxicol 19 535 539
    • (2000) Human Exper Toxicol , vol.19 , pp. 535-539
    • Wu, G.1
  • 67
    • 0033933698 scopus 로고    scopus 로고
    • Frequency and Markov chain analysis of the amino acid sequence of human alcohol dehydrogenase α-chain
    • G Wu 2000d Frequency and Markov chain analysis of the amino acid sequence of human alcohol dehydrogenase α-chain Alcohol Alcohol 35 302 306
    • (2000) Alcohol Alcohol , vol.35 , pp. 302-306
    • Wu, G.1
  • 68
    • 0034045072 scopus 로고    scopus 로고
    • Frequency and Markov chain analysis of the amino- acid sequence of sheep p53 protein
    • G Wu 2000e Frequency and Markov chain analysis of the amino- acid sequence of sheep p53 protein J Biochem Mol Biol Biophys 4 179 185
    • (2000) J Biochem Mol Biol Biophys , vol.4 , pp. 179-185
    • Wu, G.1
  • 69
    • 0041027162 scopus 로고    scopus 로고
    • The first, second and third order Markov chain analysis on amino acids sequence of human tyrosine aminotransferase and its variant causing tyrosinemia type II
    • G Wu 2000f The first, second and third order Markov chain analysis on amino acids sequence of human tyrosine aminotransferase and its variant causing tyrosinemia type II Pediatr Relat Top 39 37 47
    • (2000) Pediatr Relat Top , vol.39 , pp. 37-47
    • Wu, G.1
  • 70
    • 0033949146 scopus 로고    scopus 로고
    • The first, second, third and fourth order Markov chain analysis on amino acids sequence of human dopamine β-hydroxylase
    • G Wu 2000g The first, second, third and fourth order Markov chain analysis on amino acids sequence of human dopamine β-hydroxylase Mol Psychiatry 5 448 451
    • (2000) Mol Psychiatry , vol.5 , pp. 448-451
    • Wu, G.1
  • 71
    • 0029555741 scopus 로고
    • Effects of different sampling strategies on predictions of blood cyclosporine concentrations in haematological patients with multidrug resistance by Bayesian and non-linear least squares methods
    • G Wu M Baraldo F Pea P Cossettini M Furlanut 1995 Effects of different sampling strategies on predictions of blood cyclosporine concentrations in haematological patients with multidrug resistance by Bayesian and non-linear least squares methods Pharmacol Res 32 355 362
    • (1995) Pharmacol Res , vol.32 , pp. 355-362
    • Wu, G.1    Baraldo, M.2    Pea, F.3    Cossettini, P.4    Furlanut, M.5
  • 72
    • 0030184843 scopus 로고    scopus 로고
    • Prediction of blood cyclosporine concentrations in haematological patients with multidrug resistance by one-, two- and three-compartment models using Bayesian and non-linear least squares methods
    • G Wu P Cossettini M Furlanut 1996 Prediction of blood cyclosporine concentrations in haematological patients with multidrug resistance by one-, two- and three-compartment models using Bayesian and non-linear least squares methods Pharmacol Res 34 47 57
    • (1996) Pharmacol Res , vol.34 , pp. 47-57
    • Wu, G.1    Cossettini, P.2    Furlanut, M.3
  • 73
    • 0011316732 scopus 로고    scopus 로고
    • Frequency and Markov chain analysis of amino-acids sequence of human platelet-activating factor acetylhydrolase α-subunit and its variant causing the lissencephaly syndrome
    • G Wu S Yan 2000a Frequency and Markov chain analysis of amino-acids sequence of human platelet-activating factor acetylhydrolase α-subunit and its variant causing the lissencephaly syndrome Pediatr Relat Top 39 513 526
    • (2000) Pediatr Relat Top , vol.39 , pp. 513-526
    • Wu, G.1    Yan, S.2
  • 74
    • 0034489063 scopus 로고    scopus 로고
    • Prediction of two- and three-amino acid sequence of human acute myeloid leukemia 1 protein from its amino acid composition
    • G Wu S Yan 2000b Prediction of two- and three-amino acid sequence of human acute myeloid leukemia 1 protein from its amino acid composition Comp Haematol Int 10 85 89
    • (2000) Comp Haematol Int , vol.10 , pp. 85-89
    • Wu, G.1    Yan, S.2
  • 75
    • 0034081862 scopus 로고    scopus 로고
    • Prediction of two- and three-amino-acid sequences of Citrobacter Freundii β-lactamase from its amino acid composition
    • G Wu S Yan 2000c Prediction of two- and three-amino-acid sequences of Citrobacter Freundii β-lactamase from its amino acid composition J Mol Microbiol Biotechnol 2 277 281
    • (2000) J Mol Microbiol Biotechnol , vol.2 , pp. 277-281
    • Wu, G.1    Yan, S.2
  • 76
    • 0034489671 scopus 로고    scopus 로고
    • Prediction of distributions of amino acids and amino acid pairs in human haemoglobin α-chain and its seven variants causing α-thalassemia from their occurrences according to the random mechanism
    • G Wu S Yan 2000d Prediction of distributions of amino acids and amino acid pairs in human haemoglobin α-chain and its seven variants causing α-thalassemia from their occurrences according to the random mechanism Comp Haematol Int 10 80 84
    • (2000) Comp Haematol Int , vol.10 , pp. 80-84
    • Wu, G.1    Yan, S.2
  • 77
    • 0035789798 scopus 로고    scopus 로고
    • Frequency and Markov chain analysis of amino-acid sequences of human connective tissue growth factor
    • G Wu S Yan 2001a Frequency and Markov chain analysis of amino-acid sequences of human connective tissue growth factor J Mol Model 5 120 124
    • (2001) J Mol Model , vol.5 , pp. 120-124
    • Wu, G.1    Yan, S.2
  • 78
    • 0034956435 scopus 로고    scopus 로고
    • Prediction of presence and absence of two- and three-amino-acid sequence of human monoamine oxidase B from its amino acid composition according to the random mechanism
    • G Wu S Yan 2001b Prediction of presence and absence of two- and three-amino-acid sequence of human monoamine oxidase B from its amino acid composition according to the random mechanism Biomol Eng 18 23 27
    • (2001) Biomol Eng , vol.18 , pp. 23-27
    • Wu, G.1    Yan, S.2
  • 79
    • 0346510430 scopus 로고    scopus 로고
    • Prediction of presence and absence of two- and three-amino-acid sequence of human tyrosinase from their amino acid composition and related changes in human tyrosinase variant causing oculocutaneous albinism
    • G Wu S Yan 2001c Prediction of presence and absence of two- and three-amino-acid sequence of human tyrosinase from their amino acid composition and related changes in human tyrosinase variant causing oculocutaneous albinism Pediatr Relat Top 40 153 166
    • (2001) Pediatr Relat Top , vol.40 , pp. 153-166
    • Wu, G.1    Yan, S.2
  • 80
    • 0035761651 scopus 로고    scopus 로고
    • Analysis of distributions of amino acids, amino acid pairs and triplets in human insulin precursor and four variants from their occurrences according to the random mechanism
    • G Wu S Yan 2001d Analysis of distributions of amino acids, amino acid pairs and triplets in human insulin precursor and four variants from their occurrences according to the random mechanism J Biochem Mol Biol Biophys 5 293 300
    • (2001) J Biochem Mol Biol Biophys , vol.5 , pp. 293-300
    • Wu, G.1    Yan, S.2
  • 81
    • 0035789132 scopus 로고    scopus 로고
    • Analysis of distributions of amino acids and amino acid pairs in human tumor necrosis factor precursor and its eight variants according to random mechanism
    • G Wu S Yan 2001e Analysis of distributions of amino acids and amino acid pairs in human tumor necrosis factor precursor and its eight variants according to random mechanism J Mol Model 7 318 323
    • (2001) J Mol Model , vol.7 , pp. 318-323
    • Wu, G.1    Yan, S.2
  • 82
    • 0036905929 scopus 로고    scopus 로고
    • Determination of amino acid pairs sensitive to variants in human low-density lipoprotein receptor precursor by means of a random approach
    • G Wu S Yan 2002a Determination of amino acid pairs sensitive to variants in human low-density lipoprotein receptor precursor by means of a random approach J Biochem Mol Biol Biophys 6 401 406
    • (2002) J Biochem Mol Biol Biophys , vol.6 , pp. 401-406
    • Wu, G.1    Yan, S.2
  • 83
    • 0036957716 scopus 로고    scopus 로고
    • Estimation of amino acid pairs sensitive to variants in human phenylalanine hydroxylase protein by means of a random approach
    • G Wu S Yan 2002b Estimation of amino acid pairs sensitive to variants in human phenylalanine hydroxylase protein by means of a random approach Peptides 23 2085 2090
    • (2002) Peptides , vol.23 , pp. 2085-2090
    • Wu, G.1    Yan, S.2
  • 84
    • 0036208782 scopus 로고    scopus 로고
    • Random analysis of presence and absence of two- and three-amino-acid sequences and distributions of amino acids, two- and three-amino-acid sequences in bovine p53 protein
    • G Wu S Yan 2002c Random analysis of presence and absence of two- and three-amino-acid sequences and distributions of amino acids, two- and three-amino-acid sequences in bovine p53 protein Mol Biol Today 3 31 37
    • (2002) Mol Biol Today , vol.3 , pp. 31-37
    • Wu, G.1    Yan, S.2
  • 85
    • 0036902739 scopus 로고    scopus 로고
    • Analysis of distributions of amino acids in the primary structure of apoptosis regulator Bcl-2 family according to the random mechanism
    • G Wu S Yan 2002d Analysis of distributions of amino acids in the primary structure of apoptosis regulator Bcl-2 family according to the random mechanism J Biochem Mol Biol Biophys 6 407 414
    • (2002) J Biochem Mol Biol Biophys , vol.6 , pp. 407-414
    • Wu, G.1    Yan, S.2
  • 86
    • 0036979848 scopus 로고    scopus 로고
    • Analysis of distributions of amino acids in the primary structure of tumor suppressor p53 family according to the random mechanism
    • G Wu S Yan 2002e Analysis of distributions of amino acids in the primary structure of tumor suppressor p53 family according to the random mechanism J Mol Model 8 191 198
    • (2002) J Mol Model , vol.8 , pp. 191-198
    • Wu, G.1    Yan, S.2
  • 87
    • 0036756031 scopus 로고    scopus 로고
    • Randomness in the primary structure of protein: Methods and implications
    • G Wu S Yan 2002f Randomness in the primary structure of protein: methods and implications Mol Biol Today 3 55 69
    • (2002) Mol Biol Today , vol.3 , pp. 55-69
    • Wu, G.1    Yan, S.2
  • 88
    • 0038066458 scopus 로고    scopus 로고
    • Analysis of amino acid pairs sensitive to variants in human collagen α5(IV) chain precursor by means of a random approach
    • G Wu S Yan 2003a Analysis of amino acid pairs sensitive to variants in human collagen α5(IV) chain precursor by means of a random approach Peptides 24 347 352
    • (2003) Peptides , vol.24 , pp. 347-352
    • Wu, G.1    Yan, S.2
  • 89
    • 0038805166 scopus 로고    scopus 로고
    • Determination of amino acid pairs in human haemoglobulin α-chain sensitive to variants by means of a random approach
    • G Wu S Yan 2003b Determination of amino acid pairs in human haemoglobulin α-chain sensitive to variants by means of a random approach Comp Clin Pathol 12 21 25
    • (2003) Comp Clin Pathol , vol.12 , pp. 21-25
    • Wu, G.1    Yan, S.2
  • 90
    • 0347300717 scopus 로고    scopus 로고
    • Determination of amino acid pairs in human p53 protein sensitive to mutations/variants by means of a random approach
    • G Wu S Yan 2003c Determination of amino acid pairs in human p53 protein sensitive to mutations/variants by means of a random approach J Mol Model 9 337 341
    • (2003) J Mol Model , vol.9 , pp. 337-341
    • Wu, G.1    Yan, S.2
  • 91
    • 2342608968 scopus 로고    scopus 로고
    • Determination of amino acid pairs in Von Hippel-Lindau disease tumour suppressor (G7 protein) sensitive to variants by means of a random approach
    • G Wu S Yan 2003d Determination of amino acid pairs in Von Hippel-Lindau disease tumour suppressor (G7 protein) sensitive to variants by means of a random approach J Appl Res 3 512 520
    • (2003) J Appl Res , vol.3 , pp. 512-520
    • Wu, G.1    Yan, S.2
  • 92
    • 0038218136 scopus 로고    scopus 로고
    • Determination of amino acid pairs sensitive to variants in human β-glucocerebrosidase by means of a random approach
    • G Wu S Yan 2003e Determination of amino acid pairs sensitive to variants in human β-glucocerebrosidase by means of a random approach Protein Eng 16 195 199
    • (2003) Protein Eng , vol.16 , pp. 195-199
    • Wu, G.1    Yan, S.2
  • 93
    • 0842276870 scopus 로고    scopus 로고
    • Determination of amino acid pairs sensitive to variants in human Bruton's tyrosine kinase by means of a random approach
    • G Wu S Yan 2003f Determination of amino acid pairs sensitive to variants in human Bruton's tyrosine kinase by means of a random approach Mol Simul 29 249 254
    • (2003) Mol Simul , vol.29 , pp. 249-254
    • Wu, G.1    Yan, S.2
  • 94
    • 0038307305 scopus 로고    scopus 로고
    • Determination of amino acid pairs sensitive to variants in human coagulation factor IX precursor by means of a random approach
    • G Wu S Yan 2003g Determination of amino acid pairs sensitive to variants in human coagulation factor IX precursor by means of a random approach J Biomed Sci 10 451 454
    • (2003) J Biomed Sci , vol.10 , pp. 451-454
    • Wu, G.1    Yan, S.2
  • 95
    • 0842287567 scopus 로고    scopus 로고
    • Prediction of amino acid pairs sensitive to mutations in the spike protein from SARS related coronavirus
    • G Wu S Yan 2003h Prediction of amino acid pairs sensitive to mutations in the spike protein from SARS related coronavirus Peptides 24 1837 1845
    • (2003) Peptides , vol.24 , pp. 1837-1845
    • Wu, G.1    Yan, S.2
  • 96
    • 33646245388 scopus 로고    scopus 로고
    • Amino acid pairs sensitive to variants in human collagen α1(I) chain precursor
    • G Wu S Yan 2004a Amino acid pairs sensitive to variants in human collagen α1(I) chain precursor EXCLI J 3 10 19
    • (2004) EXCLI J , vol.3 , pp. 10-19
    • Wu, G.1    Yan, S.2
  • 97
    • 2442707531 scopus 로고    scopus 로고
    • Determination of amino acid pairs sensitive to variants in human copper-transporting ATPase 2
    • G Wu S Yan 2004b Determination of amino acid pairs sensitive to variants in human copper-transporting ATPase 2 Biochem Biophys Res Commun 319 27 31
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 27-31
    • Wu, G.1    Yan, S.2
  • 98
    • 1842790539 scopus 로고    scopus 로고
    • Fate of 130 hemagglutinins from different influenza a viruses
    • G Wu S Yan 2004c Fate of 130 hemagglutinins from different influenza A viruses Biochem Biophys Res Commun 317 917 924
    • (2004) Biochem Biophys Res Commun , vol.317 , pp. 917-924
    • Wu, G.1    Yan, S.2
  • 99
    • 2942528833 scopus 로고    scopus 로고
    • Potential targets for anti-SARS drugs in the structural proteins from SARS related coronavirus
    • G Wu S Yan 2004d Potential targets for anti-SARS drugs in the structural proteins from SARS related coronavirus Peptides 25 901 908
    • (2004) Peptides , vol.25 , pp. 901-908
    • Wu, G.1    Yan, S.2
  • 100
    • 33646235586 scopus 로고    scopus 로고
    • Susceptible amino acid pairs in variants of human collagen α1(III) chain precursor
    • G Wu S Yan 2004e Susceptible amino acid pairs in variants of human collagen α1(III) chain precursor EXCLI J 3 20 28
    • (2004) EXCLI J , vol.3 , pp. 20-28
    • Wu, G.1    Yan, S.2
  • 101
    • 3242747499 scopus 로고    scopus 로고
    • Determination of sensitive positions to mutations in human p53 protein
    • G Wu S Yan 2004f Determination of sensitive positions to mutations in human p53 protein Biochem Biophys Res Commun 321 313 319
    • (2004) Biochem Biophys Res Commun , vol.321 , pp. 313-319
    • Wu, G.1    Yan, S.2
  • 102
    • 21444440227 scopus 로고    scopus 로고
    • Amino acid pairs susceptible to variants in human protein C precursor
    • G Wu S Yan 2005a Amino acid pairs susceptible to variants in human protein C precursor Protein Pept Lett 10 491 494
    • (2005) Protein Pept Lett , vol.10 , pp. 491-494
    • Wu, G.1    Yan, S.2
  • 103
    • 26944481544 scopus 로고    scopus 로고
    • Mutation features of 215 polymerase proteins from different influenza a viruses
    • G Wu S Yan 2005b Mutation features of 215 polymerase proteins from different influenza A viruses Med Sci Monit 11 BR367 BR372
    • (2005) Med Sci Monit , vol.11
    • Wu, G.1    Yan, S.2
  • 104
    • 14844293839 scopus 로고    scopus 로고
    • Reasoning of spike glycoproteins being more vulnerable to mutations among 158 coronavirus proteins from different species
    • G Wu S Yan 2005c Reasoning of spike glycoproteins being more vulnerable to mutations among 158 coronavirus proteins from different species J Mol Model 11 8 16
    • (2005) J Mol Model , vol.11 , pp. 8-16
    • Wu, G.1    Yan, S.2
  • 105
    • 20444492748 scopus 로고    scopus 로고
    • Timing of mutation in hemagglutinins from influenza a virus by means of unpredictable portion of amino-acid pair and fast Fourier transform
    • G Wu S Yan 2005d Timing of mutation in hemagglutinins from influenza A virus by means of unpredictable portion of amino-acid pair and fast Fourier transform Biochem Biophys Res Commun 333 70 78
    • (2005) Biochem Biophys Res Commun , vol.333 , pp. 70-78
    • Wu, G.1    Yan, S.2
  • 106
    • 33750621120 scopus 로고    scopus 로고
    • Searching of main cause leading to severe influenza a virus mutations and consequently to influenza pandemics/epidemics
    • G Wu S Yan 2005e Searching of main cause leading to severe influenza A virus mutations and consequently to influenza pandemics/epidemics Am J Infect Dis 1 116 123
    • (2005) Am J Infect Dis , vol.1 , pp. 116-123
    • Wu, G.1    Yan, S.2
  • 107
    • 9944247042 scopus 로고    scopus 로고
    • Prediction of mutation trend in hemagglutinins and neuraminidases from influenza a viruses by means of cross-impact analysis
    • G Wu S Yan 2005f Prediction of mutation trend in hemagglutinins and neuraminidases from influenza A viruses by means of cross-impact analysis Biochem Biophys Res Commun 326 475 482
    • (2005) Biochem Biophys Res Commun , vol.326 , pp. 475-482
    • Wu, G.1    Yan, S.2
  • 108
    • 26444529845 scopus 로고    scopus 로고
    • Determination of mutation trend in proteins by means of translation probability between RNA codes and mutated amino acids
    • G Wu S Yan 2005g Determination of mutation trend in proteins by means of translation probability between RNA codes and mutated amino acids Biochem Biophys Res Commun 337 692 700
    • (2005) Biochem Biophys Res Commun , vol.337 , pp. 692-700
    • Wu, G.1    Yan, S.2
  • 109
    • 33646424787 scopus 로고    scopus 로고
    • Fate of influenza a virus proteins
    • G Wu S Yan 2006a Fate of influenza A virus proteins Protein Pept Lett 13 377 384
    • (2006) Protein Pept Lett , vol.13 , pp. 377-384
    • Wu, G.1    Yan, S.2
  • 110
    • 33646242537 scopus 로고    scopus 로고
    • Mutation trend of hemagglutinin of influenza a virus: A review from computational mutation viewpoint
    • G Wu S Yan 2006b Mutation trend of hemagglutinin of influenza A virus: a review from computational mutation viewpoint Acta Pharmacol Sin 27 513 526
    • (2006) Acta Pharmacol Sin , vol.27 , pp. 513-526
    • Wu, G.1    Yan, S.2
  • 111
    • 33646233147 scopus 로고    scopus 로고
    • Timing of mutation in hemagglutinins from influenza a virus by means of amino-acid distribution rank and fast Fourier transform
    • G Wu S Yan 2006c Timing of mutation in hemagglutinins from influenza A virus by means of amino-acid distribution rank and fast Fourier transform Protein Pept Lett 13 143 148
    • (2006) Protein Pept Lett , vol.13 , pp. 143-148
    • Wu, G.1    Yan, S.2
  • 112
    • 33646760257 scopus 로고    scopus 로고
    • Determination of mutation trend in hemagglutinins by means of translation probability between RNA codons and mutated amino acids
    • G Wu S Yan 2006d Determination of mutation trend in hemagglutinins by means of translation probability between RNA codons and mutated amino acids Protein Pept Lett 13 601 609
    • (2006) Protein Pept Lett , vol.13 , pp. 601-609
    • Wu, G.1    Yan, S.2
  • 113
    • 33751086728 scopus 로고    scopus 로고
    • Prediction of possible mutations in H5N1 hemagglutinins of influenza a virus by means of logistic regression
    • G Wu S Yan 2006e Prediction of possible mutations in H5N1 hemagglutinins of influenza A virus by means of logistic regression Comp Clin Pathol 15 255 261
    • (2006) Comp Clin Pathol , vol.15 , pp. 255-261
    • Wu, G.1    Yan, S.2
  • 114
    • 33750615509 scopus 로고    scopus 로고
    • Prediction of mutations in H5N1 hemagglutinins from influenza a virus
    • G Wu S Yan 2006f Prediction of mutations in H5N1 hemagglutinins from influenza A virus Protein Pept Lett 13 971 976
    • (2006) Protein Pept Lett , vol.13 , pp. 971-976
    • Wu, G.1    Yan, S.2
  • 115
    • 33846970590 scopus 로고    scopus 로고
    • Improvement of model for prediction of hemagglutinin mutations in H5N1 influenza viruses with distinguishing of arginine, leucine and serine
    • G Wu S Yan 2007a Improvement of model for prediction of hemagglutinin mutations in H5N1 influenza viruses with distinguishing of arginine, leucine and serine Protein Pept Lett 14 191 196
    • (2007) Protein Pept Lett , vol.14 , pp. 191-196
    • Wu, G.1    Yan, S.2
  • 116
    • 40449101244 scopus 로고    scopus 로고
    • Translation probability between RNA codons and translated amino acids, and its applications to protein mutations
    • Nova Science Publishers New York
    • G Wu S Yan 2007b Translation probability between RNA codons and translated amino acids, and its applications to protein mutations MH Ostrovskiy Leading-edge messenger RNA research communications Nova Science Publishers New York
    • (2007) Leading-edge Messenger RNA Research Communications
    • Wu, G.1    Yan, S.2    Ostrovskiy, M.H.3
  • 117
    • 34249655224 scopus 로고    scopus 로고
    • Improvement of prediction of mutation positions in H5N1 hemagglutinins of influenza a virus using neural network with distinguishing of arginine, leucine and serine
    • G Wu S Yan 2007c Improvement of prediction of mutation positions in H5N1 hemagglutinins of influenza A virus using neural network with distinguishing of arginine, leucine and serine Protein Pept Lett 14 465 470
    • (2007) Protein Pept Lett , vol.14 , pp. 465-470
    • Wu, G.1    Yan, S.2
  • 118
    • 40049092267 scopus 로고    scopus 로고
    • Prediction of mutations initiated by internal power in H3N2 hemagglutinins of influenza A virus from North America
    • Wu G, Yan S (2007d) Prediction of mutations initiated by internal power in H3N2 hemagglutinins of influenza A virus from North America. Int J Pept Res Ther ( http://dx.doi.org/10.1007/s10989-007-9104-1 )
    • (2007) Int J Pept Res Ther
    • Wu, G.1    Yan, S.2
  • 119
    • 0032712272 scopus 로고    scopus 로고
    • Epidemiology and pathogenesis of influenza
    • Suppl B
    • MC Zambon 1999 Epidemiology and pathogenesis of influenza J Antimicrob Chemother 44 Suppl B 3 9
    • (1999) J Antimicrob Chemother , vol.44 , pp. 3-9
    • Zambon, M.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.