메뉴 건너뛰기




Volumn 250, Issue 1, 2013, Pages 197-207

In silico analysis of drug-resistant mutant of neuraminidase (N294S) against oseltamivir

Author keywords

Molecular docking; Molecular dynamic simulation; Neuraminidase; Normal mode analysis; Oseltamivir resistance

Indexed keywords


EID: 84873077420     PISSN: 0033183X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00709-012-0394-6     Document Type: Article
Times cited : (19)

References (46)
  • 1
    • 14144256567 scopus 로고    scopus 로고
    • Normal modes for predicting protein motions: a comprehensive database assessment and associated Web tool
    • Alexandrov V, Lehnert U, Echols N, Milburn D, Engelman D, Gerstein M (2005) Normal modes for predicting protein motions: a comprehensive database assessment and associated Web tool. Protein Sci 14(3): 633-643.
    • (2005) Protein Sci , vol.14 , Issue.3 , pp. 633-643
    • Alexandrov, V.1    Lehnert, U.2    Echols, N.3    Milburn, D.4    Engelman, D.5    Gerstein, M.6
  • 2
    • 80052451032 scopus 로고    scopus 로고
    • Relationships between membrane binding, affinity and cell internalization efficacy of a cell-penetrating peptide: penetratin as a case study
    • Alves ID, Bechara C, Walrant A, Zaltsman Y, Jiao CY, Sagan S (2011) Relationships between membrane binding, affinity and cell internalization efficacy of a cell-penetrating peptide: penetratin as a case study. PLoS One 6(9): e24096.
    • (2011) PLoS One , vol.6 , Issue.9
    • Alves, I.D.1    Bechara, C.2    Walrant, A.3    Zaltsman, Y.4    Jiao, C.Y.5    Sagan, S.6
  • 3
    • 72049097920 scopus 로고    scopus 로고
    • Oseltamivir resistance: what does it mean clinically?
    • Baum SG (2009) Oseltamivir resistance: what does it mean clinically? Clin Infect Dis 49(12): 1836-1837.
    • (2009) Clin Infect Dis , vol.49 , Issue.12 , pp. 1836-1837
    • Baum, S.G.1
  • 5
    • 0015371575 scopus 로고
    • A 2 (N2) neuraminidase of the X-7 influenza virus recombinant: determination of molecular size and subunit composition of the active unit
    • Bucher DJ, Kilbourne ED (1972) A 2 (N2) neuraminidase of the X-7 influenza virus recombinant: determination of molecular size and subunit composition of the active unit. J Virol 10(1): 60-66.
    • (1972) J Virol , vol.10 , Issue.1 , pp. 60-66
    • Bucher, D.J.1    Kilbourne, E.D.2
  • 6
    • 0033974667 scopus 로고    scopus 로고
    • Accommodating protein flexibility in computational drug design
    • Carlson HA, McCammon JA (2000) Accommodating protein flexibility in computational drug design. Mol Pharmacol 57(2): 213-218.
    • (2000) Mol Pharmacol , vol.57 , Issue.2 , pp. 213-218
    • Carlson, H.A.1    McCammon, J.A.2
  • 7
    • 21644473891 scopus 로고    scopus 로고
    • Representing receptor flexibility in ligand docking through relevant normal modes
    • Cavasotto CN, Kovacs JA, Abagyan RA (2005) Representing receptor flexibility in ligand docking through relevant normal modes. J Am Chem Soc 127(26): 9632-9640.
    • (2005) J Am Chem Soc , vol.127 , Issue.26 , pp. 9632-9640
    • Cavasotto, C.N.1    Kovacs, J.A.2    Abagyan, R.A.3
  • 8
    • 77954557128 scopus 로고    scopus 로고
    • Improving thermostability of papain through structure-based protein engineering
    • Choudhury D, Biswas S, Roy S, Dattagupta JK (2010) Improving thermostability of papain through structure-based protein engineering. Protein Eng Des Sel 23(6): 457-467.
    • (2010) Protein Eng Des Sel , vol.23 , Issue.6 , pp. 457-467
    • Choudhury, D.1    Biswas, S.2    Roy, S.3    Dattagupta, J.K.4
  • 10
    • 0020633096 scopus 로고
    • Structure of the catalytic and antigenic sites in influenza virus neuraminidase
    • Colman PM, Varghese JN, Laver WG (1983) Structure of the catalytic and antigenic sites in influenza virus neuraminidase. Nature 303(5912): 41-44.
    • (1983) Nature , vol.303 , Issue.5912 , pp. 41-44
    • Colman, P.M.1    Varghese, J.N.2    Laver, W.G.3
  • 11
    • 0033104039 scopus 로고    scopus 로고
    • New tricks for modelers from the crystallography toolkit: the particle mesh Ewald algorithm and its use in nucleic acid simulations
    • Darden T, Perera L, Li L, Pedersen L (1999) New tricks for modelers from the crystallography toolkit: the particle mesh Ewald algorithm and its use in nucleic acid simulations. Structure 7(3): 55-60.
    • (1999) Structure , vol.7 , Issue.3 , pp. 55-60
    • Darden, T.1    Perera, L.2    Li, L.3    Pedersen, L.4
  • 12
    • 2342518038 scopus 로고    scopus 로고
    • On the use of low-frequency normal modes to enforce collective movements in refining macromolecular structural models
    • Delarue M, Dumas P (2004) On the use of low-frequency normal modes to enforce collective movements in refining macromolecular structural models. Proc Natl Acad Sci U S A 101(18): 6957-62.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.18 , pp. 6957-6962
    • Delarue, M.1    Dumas, P.2
  • 13
    • 33846617350 scopus 로고    scopus 로고
    • Study of drug resistance of chicken influenza A virus (H5N1) from homology-modeled 3D structures of neuraminidases
    • Du QS, Wang SQ, Chou KC (2007) Study of drug resistance of chicken influenza A virus (H5N1) from homology-modeled 3D structures of neuraminidases. Biochem Biophys Res Commun 354(3): 634-640.
    • (2007) Biochem Biophys Res Commun , vol.354 , Issue.3 , pp. 634-640
    • Du, Q.S.1    Wang, S.Q.2    Chou, K.C.3
  • 14
    • 33344474627 scopus 로고    scopus 로고
    • A complete small molecule dataset from the protein data bank
    • Feldman J, Snyder KA, Ticoll A, Pintilie G, Hogue CW (2006) A complete small molecule dataset from the protein data bank. FEBS Lett 580(6): 1649-1653.
    • (2006) FEBS Lett , vol.580 , Issue.6 , pp. 1649-1653
    • Feldman, J.1    Snyder, K.A.2    Ticoll, A.3    Pintilie, G.4    Hogue, C.W.5
  • 15
    • 31444452744 scopus 로고
    • Automatic generation of 3D-atomic coordinates for organic molecules
    • Gasteiger J, Rudolph C, Sadowski J (1990) Automatic generation of 3D-atomic coordinates for organic molecules. Tetrahedron Comput Meth 3: 537-547.
    • (1990) Tetrahedron Comput Meth , vol.3 , pp. 537-547
    • Gasteiger, J.1    Rudolph, C.2    Sadowski, J.3
  • 16
    • 0034603350 scopus 로고    scopus 로고
    • Influenza virus neuraminidase inhibitors
    • Gubareva LV, Kaiser L, Hayden FG (2000) Influenza virus neuraminidase inhibitors. Lancet 355(9206): 827-835.
    • (2000) Lancet , vol.355 , Issue.9206 , pp. 827-835
    • Gubareva, L.V.1    Kaiser, L.2    Hayden, F.G.3
  • 17
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B, Kutzner C, Spoel D, Lindahl E (2008) GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4(3): 435-447.
    • (2008) J Chem Theory Comput , vol.4 , Issue.3 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Spoel, D.3    Lindahl, E.4
  • 18
    • 0037414799 scopus 로고    scopus 로고
    • Folding and function of the troponin tail domain. Effects of cardiomyopathic troponin T mutations
    • Hinkle A, Tobacman LS (2003) Folding and function of the troponin tail domain. Effects of cardiomyopathic troponin T mutations. J Biol Chem 278(1): 506-513.
    • (2003) J Biol Chem , vol.278 , Issue.1 , pp. 506-513
    • Hinkle, A.1    Tobacman, L.S.2
  • 20
    • 0031048319 scopus 로고    scopus 로고
    • Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity
    • Kim CU, Lew W, Williams MA, Liu H, Zhang L, Swaminathan S, Bischofberger N, Chen MS, Mendel DB, Tai CY (1997) Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity. J Am Chem Soc 119(4): 681-690.
    • (1997) J Am Chem Soc , vol.119 , Issue.4 , pp. 681-690
    • Kim, C.U.1    Lew, W.2    Williams, M.A.3    Liu, H.4    Zhang, L.5    Swaminathan, S.6    Bischofberger, N.7    Chen, M.S.8    Mendel, D.B.9    Tai, C.Y.10
  • 21
    • 50849118817 scopus 로고    scopus 로고
    • Bacteriophage lambda stabilization by auxiliary protein gpD: timing, location, and mechanism of attachment determined by cryo-EM
    • Lander GC, Evilevitch A, Jeembaeva M, Potter CS, Carragher B, Johnson J (2008) Bacteriophage lambda stabilization by auxiliary protein gpD: timing, location, and mechanism of attachment determined by cryo-EM. Structure 16(9): 1399-406.
    • (2008) Structure , vol.16 , Issue.9 , pp. 1399-1406
    • Lander, G.C.1    Evilevitch, A.2    Jeembaeva, M.3    Potter, C.S.4    Carragher, B.5    Johnson, J.6
  • 22
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: a package for molecular simulation and trajectory analysis
    • Lindahl E, Hess B, van der Spoel D (2001) GROMACS 3. 0: a package for molecular simulation and trajectory analysis. J Mol Mod 7(8): 306-317.
    • (2001) J Mol Mod , vol.7 , Issue.8 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 23
    • 34547575992 scopus 로고    scopus 로고
    • firestar-prediction of functionally important residues using structural templates and alignment reliability
    • Lopez G, Valencia A, Tress ML (2007) firestar-prediction of functionally important residues using structural templates and alignment reliability. Nucleic Acids Res 35: 573-577.
    • (2007) Nucleic Acids Res , vol.35 , pp. 573-577
    • Lopez, G.1    Valencia, A.2    Tress, M.L.3
  • 24
    • 7644241814 scopus 로고    scopus 로고
    • Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium
    • Matrosovich MN, Matrosovich TY, Gray T, Roberts NA, Klenk H (2004) Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium. J Virol 78(22): 12665-12667.
    • (2004) J Virol , vol.78 , Issue.22 , pp. 12665-12667
    • Matrosovich, M.N.1    Matrosovich, T.Y.2    Gray, T.3    Roberts, N.A.4    Klenk, H.5
  • 25
    • 0033897803 scopus 로고    scopus 로고
    • Resistance of influenza viruses to neuraminidase inhibitors-a review
    • McKimm-Breschkin JL (2000) Resistance of influenza viruses to neuraminidase inhibitors-a review. Antiviral Res 47(1): 1-17.
    • (2000) Antiviral Res , vol.47 , Issue.1 , pp. 1-17
    • McKimm-Breschkin, J.L.1
  • 26
    • 10844257486 scopus 로고    scopus 로고
    • Solvation influences flap collapse in HIV-1 protease
    • Meagher KL, Carlson HA (2005) Solvation influences flap collapse in HIV-1 protease. Proteins: Struct Func Bioinf 58(1): 119-125.
    • (2005) Proteins: Struct Func Bioinf , vol.58 , Issue.1 , pp. 119-125
    • Meagher, K.L.1    Carlson, H.A.2
  • 27
    • 29144433925 scopus 로고    scopus 로고
    • Oseltamivir resistance-disabling our influenza defenses
    • Moscona A (2005) Oseltamivir resistance-disabling our influenza defenses. N Engl J Med 353(25): 2633-2636.
    • (2005) N Engl J Med , vol.353 , Issue.25 , pp. 2633-2636
    • Moscona, A.1
  • 28
    • 36249003887 scopus 로고    scopus 로고
    • Origin of highly pathogenic H5N1 avian influenza virus in China and genetic characterization of donor and recipient viruses
    • Mukhtar MM, Rasool ST, Song D, Zhu C, Hao Q, Zhu Y, Wu J (2007) Origin of highly pathogenic H5N1 avian influenza virus in China and genetic characterization of donor and recipient viruses. J Gen Virol 88(11): 3094-3099.
    • (2007) J Gen Virol , vol.88 , Issue.11 , pp. 3094-3099
    • Mukhtar, M.M.1    Rasool, S.T.2    Song, D.3    Zhu, C.4    Hao, Q.5    Zhu, Y.6    Wu, J.7
  • 29
    • 10944240992 scopus 로고    scopus 로고
    • Influenza: old and new threats
    • Pales PS (2004) Influenza: old and new threats. Nat Med 10: 82-87.
    • (2004) Nat Med , vol.10 , pp. 82-87
    • Pales, P.S.1
  • 30
    • 0033955909 scopus 로고    scopus 로고
    • Protein thermal stability: insights from atomic displacement parameters (B values)
    • Parthasarathy S, Murthy MR (2000) Protein thermal stability: insights from atomic displacement parameters (B values). Protein Eng 13(1): 9-13.
    • (2000) Protein Eng , vol.13 , Issue.1 , pp. 9-13
    • Parthasarathy, S.1    Murthy, M.R.2
  • 31
    • 44149083268 scopus 로고    scopus 로고
    • Effect of deleterious nsSNP on the HER2 receptor based on stability and binding affinity with herceptin: a computational approach
    • Rajasekaran R, George Priya Doss C, Sudandiradoss C, Ramanathan K, Purohit R, Sethumadhavan R (2008) Effect of deleterious nsSNP on the HER2 receptor based on stability and binding affinity with herceptin: a computational approach. C R Biol 331(6): 409-417.
    • (2008) C R Biol , vol.331 , Issue.6 , pp. 409-417
    • Rajasekaran, R.1    George Priya Doss, C.2    Sudandiradoss, C.3    Ramanathan, K.4    Purohit, R.5    Sethumadhavan, R.6
  • 32
    • 0022555901 scopus 로고
    • Study of protein dynamics by X-ray diffraction
    • Ringe D, Petsko GA (1986) Study of protein dynamics by X-ray diffraction. Methods Enzymol 131: 389-433.
    • (1986) Methods Enzymol , vol.131 , pp. 389-433
    • Ringe, D.1    Petsko, G.A.2
  • 35
    • 34948823863 scopus 로고    scopus 로고
    • Preparation of neuraminidase-specific antiserum from the H9N2 subtype of avian influenza virus Turk
    • Shirvan AN, Moradi M, Aminian M, Madani R (2007) Preparation of neuraminidase-specific antiserum from the H9N2 subtype of avian influenza virus Turk. J Vet Anim 31(4): 219-223.
    • (2007) J. Vet. Anim. , vol.31 , Issue.4 , pp. 219-223
    • Shirvan, A.N.1    Moradi, M.2    Aminian, M.3    Madani, R.4
  • 37
    • 58149302838 scopus 로고    scopus 로고
    • Analysis of a point mutation in H5N1 avian influenza virus hemagglutinin in relation to virus entry into live mammalian cells
    • Su Y, Yang HY, Zhang BJ, Jia HL, Tien P (2008) Analysis of a point mutation in H5N1 avian influenza virus hemagglutinin in relation to virus entry into live mammalian cells. Arch Virol 153(12): 2253-2261.
    • (2008) Arch Virol , vol.153 , Issue.12 , pp. 2253-2261
    • Su, Y.1    Yang, H.Y.2    Zhang, B.J.3    Jia, H.L.4    Tien, P.5
  • 38
    • 3242875210 scopus 로고    scopus 로고
    • ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement
    • Suhre K, Sanejouand YH (2004) ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids 32: 610-614.
    • (2004) Nucleic Acids , vol.32 , pp. 610-614
    • Suhre, K.1    Sanejouand, Y.H.2
  • 39
    • 0347482478 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion
    • Takeda M, Leser GP, Russell CJ, Lamb RA (2003) Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion. Proc Natl Acad Sci 100(25): 14610-14617.
    • (2003) Proc Natl Acad Sci , vol.100 , Issue.25 , pp. 14610-14617
    • Takeda, M.1    Leser, G.P.2    Russell, C.J.3    Lamb, R.A.4
  • 40
    • 0037666888 scopus 로고    scopus 로고
    • Implications of protein flexibility for drug discovery
    • Teague SJ (2003) Implications of protein flexibility for drug discovery. Nat Rev Drug Discov 2(7): 527-541.
    • (2003) Nat Rev Drug Discov , vol.2 , Issue.7 , pp. 527-541
    • Teague, S.J.1
  • 41
    • 10644254613 scopus 로고    scopus 로고
    • Planaria Software, Seattle
    • Thompson MA (2004) ArgusLab 4. 0. 1. Planaria Software, Seattle. http://www. ArgusLab. com.
    • (2004) ArgusLab 4. 0. 1
    • Thompson, M.A.1
  • 43
    • 0032526697 scopus 로고    scopus 로고
    • Drug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase
    • Varghese JN, Smith PW, Sollis SL, Blick SJ, Sahasrabudhe A, Mckimm-Breschkin JL, Colman PM (1998) Drug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase. Structure 6(6): 735-746.
    • (1998) Structure , vol.6 , Issue.6 , pp. 735-746
    • Varghese, J.N.1    Smith, P.W.2    Sollis, S.L.3    Blick, S.J.4    Sahasrabudhe, A.5    Mckimm-Breschkin, J.L.6    Colman, P.M.7
  • 45
    • 0028922586 scopus 로고
    • LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions
    • Wallace AC, Laskowski RA, Thornton JM (1995) LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng 8(2): 127-134.
    • (1995) Protein Eng , vol.8 , Issue.2 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 46
    • 13944277320 scopus 로고    scopus 로고
    • Prediction of protein B-factor profiles
    • Yuan Z, Bailey TL, Teasdale RD (2005) Prediction of protein B-factor profiles. Proteins 58(4): 905-912.
    • (2005) Proteins , vol.58 , Issue.4 , pp. 905-912
    • Yuan, Z.1    Bailey, T.L.2    Teasdale, R.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.