메뉴 건너뛰기




Volumn 3, Issue , 2013, Pages

Structural basis for a class of nanomolar influenza A neuraminidase inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; ENZYME INHIBITOR; OSELTAMIVIR; SIALIDASE; VIRUS PROTEIN;

EID: 84893254796     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep02871     Document Type: Article
Times cited : (33)

References (29)
  • 1
    • 84945924302 scopus 로고    scopus 로고
    • Influenza fact sheet World Health Organization 211
    • Influenza fact sheet No. 211: World Health Organization; (2009)
    • (2009)
  • 2
    • 84862003840 scopus 로고    scopus 로고
    • Influenza neuraminidase
    • Air, G. M. Influenza neuraminidase. Influenza Other Respi Viruses. 6(4), 245-256 (2012)
    • (2012) Influenza Other Respi Viruses , vol.6 , Issue.4 , pp. 245-256
    • Air, G.M.1
  • 3
    • 84863230485 scopus 로고    scopus 로고
    • A distinct lineage of influenza A virus from bats
    • Tong, S. et al. A distinct lineage of influenza A virus from bats. Proc Natl Acad Sci U S A. 109(11), 4269-4274 (2012)
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.11 , pp. 4269-4274
    • Tong, S.1
  • 4
    • 33748437791 scopus 로고    scopus 로고
    • The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design
    • Russell, R. J. et al. The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design. Nature. 443(7107), 45-49 (2006)
    • (2006) Nature , vol.443 , Issue.7107 , pp. 45-49
    • Russell, R.J.1
  • 5
    • 84869233988 scopus 로고    scopus 로고
    • Crystal structures of two subtype N10 neuraminidase-like proteins from bat influenza A viruses reveal a diverged putative active site
    • Zhu, X. et al. Crystal structures of two subtype N10 neuraminidase-like proteins from bat influenza A viruses reveal a diverged putative active site. Proc Natl Acad Sci U S A. 109(46), 18903-18908 (2012)
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.46 , pp. 18903-18908
    • Zhu, X.1
  • 6
    • 84869222897 scopus 로고    scopus 로고
    • Structural and functional characterization of neuraminidase-like molecule N10 derived from bat influenza A virus
    • Li, Q. et al. Structural and functional characterization of neuraminidase-like molecule N10 derived from bat influenza A virus. Proc Natl Acad Sci U S A. 109(46), 18897-18902 (2012)
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.46 , pp. 18897-18902
    • Li, Q.1
  • 7
    • 84866902241 scopus 로고    scopus 로고
    • H1N1 2009 pandemic influenza virus: Resistance of the I223R neuraminidase mutant explained by kinetic and structural analysis
    • van der Vries, E. et al. H1N1 2009 pandemic influenza virus: resistance of the I223R neuraminidase mutant explained by kinetic and structural analysis. PLoS Pathog. 8(9), e1002914 (2012)
    • (2012) PLoS Pathog , vol.8 , Issue.9 , pp. e1002914
    • Van Der Vries, E.1
  • 8
    • 79960337244 scopus 로고    scopus 로고
    • Mechanism of 150-cavity formation in influenza neuraminidase
    • Amaro, R. E. et al. Mechanism of 150-cavity formation in influenza neuraminidase. Nat Commun. 2, 388 (2011)
    • (2011) Nat Commun , vol.2 , pp. 388
    • Amaro, R.E.1
  • 9
    • 77957767268 scopus 로고    scopus 로고
    • The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site
    • Li, Q. et al. The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site. Nat Struct Mol Biol. 17(10), 1266-1268 (2010)
    • (2011) Nat Struct Mol Biol , vol.17 , Issue.10 , pp. 1266-1268
    • Li, Q.1
  • 10
    • 84876041941 scopus 로고    scopus 로고
    • Plasticity of 150-loop in influenza neuraminidase explored by hamiltonian replica exchange molecular dynamics simulations
    • Han, N. &Mu, Y. Plasticity of 150-loop in influenza neuraminidase explored by hamiltonian replica exchange molecular dynamics simulations. PLoS One. 8(4), e60995 (2013)
    • (2013) PLoS One , vol.8 , Issue.4 , pp. e60995
    • Han, N.1    Mu, Y.2
  • 11
    • 84867566248 scopus 로고    scopus 로고
    • Synthesis and evaluation of novel 3-C-Alkylated-Neu5Ac2en derivatives as probes of influenza virus sialidase 150-loop flexibility
    • Rudrawar, S. et al. Synthesis and evaluation of novel 3-C-Alkylated-Neu5Ac2en derivatives as probes of influenza virus sialidase 150-loop flexibility. Org Biomol Chem. 10(43), 8628-8639 (2012)
    • (2012) Org Biomol Chem , vol.10 , Issue.43 , pp. 8628-8639
    • Rudrawar, S.1
  • 12
    • 78650045655 scopus 로고    scopus 로고
    • Novel sialic acid derivatives lock open the 150-loop of an influenza A virus group-1 sialidase
    • Rudrawar, S. et al. Novel sialic acid derivatives lock open the 150-loop of an influenza A virus group-1 sialidase. Nat Commun. 1, 113 (2010)
    • (2011) Nat Commun , vol.1 , pp. 113
    • Rudrawar, S.1
  • 13
    • 77958509160 scopus 로고    scopus 로고
    • Carbocycles related to oseltamivir as influenza virus group-1-specific neuraminidase inhibitors. Binding to N1 enzymes in the context of virus-like particles
    • Mohan, S., McAtamney, S., Haselhorst, T., von Itzstein, M. &Pinto, B. M. Carbocycles related to oseltamivir as influenza virus group-1-specific neuraminidase inhibitors. Binding to N1 enzymes in the context of virus-like particles. J Med Chem. 53(20), 7377-7391 (2010)
    • (2011) J Med Chem , vol.53 , Issue.20 , pp. 7377-7391
    • Mohan, S.1    McAtamney, S.2    Haselhorst, T.3    Von Itzstein, M.4    Pinto, B.M.5
  • 14
    • 77953138513 scopus 로고    scopus 로고
    • Analogs of zanamivir with modified C4-substituents as the inhibitors against the group-1 neuraminidases of influenza viruses
    • Wen, W. H. et al. Analogs of zanamivir with modified C4-substituents as the inhibitors against the group-1 neuraminidases of influenza viruses. Bioorg Med Chem. 18(11), 4074-4084 (2010)
    • (2011) Bioorg Med Chem , vol.18 , Issue.11 , pp. 4074-4084
    • Wen, W.H.1
  • 15
    • 84875440351 scopus 로고    scopus 로고
    • The influence of 150-cavity binders on the dynamics of influenza A neuraminidases as revealed by molecular dynamics simulations and combined clustering
    • Greenway, K. T., LeGresley, E. B. &Pinto, B. M. The influence of 150-cavity binders on the dynamics of influenza A neuraminidases as revealed by molecular dynamics simulations and combined clustering. PLoS One. 8(3), e59873 (2013)
    • (2013) PLoS One , vol.8 , Issue.3 , pp. e59873
    • Greenway, K.T.1    LeGresley, E.B.2    Pinto, B.M.3
  • 16
    • 67949124553 scopus 로고    scopus 로고
    • Characterizing loop dynamics and ligand recognition in human-And avian-type influenza neuraminidases via generalized born molecular dynamics and end-point free energy calculations
    • Amaro, R. E., Cheng, X., Ivanov, I., Xu, D. &McCammon, J. A. Characterizing loop dynamics and ligand recognition in human-And avian-type influenza neuraminidases via generalized born molecular dynamics and end-point free energy calculations. J Am Chem Soc. 131(13), 4702-4709 (2009)
    • (2009) J Am Chem Soc , vol.131 , Issue.13 , pp. 4702-4709
    • Amaro, R.E.1    Cheng, X.2    Ivanov, I.3    Xu, D.4    McCammon, J.A.5
  • 17
    • 84875763136 scopus 로고    scopus 로고
    • Induced opening of influenza virus neuraminidase N2 150-loop suggests an important role in inhibitor binding
    • Wu, Y. et al. Induced opening of influenza virus neuraminidase N2 150-loop suggests an important role in inhibitor binding. Sci Rep. 3, 1551 (2013)
    • (2013) Sci Rep , vol.3 , pp. 1551
    • Wu, Y.1
  • 18
    • 79953856447 scopus 로고    scopus 로고
    • Replication inhibition activity of carbocycles related to oseltamivir on influenza A virus in vitro
    • Niikura, M., Bance, N., Mohan, S. &Pinto, B. M. Replication inhibition activity of carbocycles related to oseltamivir on influenza A virus in vitro. Antiviral Res. 90(3), 160-163 (2011)
    • (2011) Antiviral Res , vol.90 , Issue.3 , pp. 160-163
    • Niikura, M.1    Bance, N.2    Mohan, S.3    Pinto, B.M.4
  • 19
    • 79955471904 scopus 로고    scopus 로고
    • Inhibitor selectivity of a new class of oseltamivir analogs against viral neuraminidase over human neuraminidase enzymes
    • Albohy, A., Mohan, S., Zheng, R. B., Pinto, B. M. &Cairo, C. W. Inhibitor selectivity of a new class of oseltamivir analogs against viral neuraminidase over human neuraminidase enzymes. Bioorg Med Chem. 19(9), 2817-2822 (2011)
    • (2011) Bioorg Med Chem , vol.19 , Issue.9 , pp. 2817-2822
    • Albohy, A.1    Mohan, S.2    Zheng, R.B.3    Pinto, B.M.4    Cairo, C.W.5
  • 20
    • 54049124684 scopus 로고    scopus 로고
    • Limited inhibitory effects of oseltamivir and zanamivir on human sialidases
    • Hata, K. et al. Limited inhibitory effects of oseltamivir and zanamivir on human sialidases. Antimicrob Agents Chemother. 52(10), 3484-3491 (2008)
    • (2008) Antimicrob Agents Chemother , vol.52 , Issue.10 , pp. 3484-3491
    • Hata, K.1
  • 21
    • 0035190544 scopus 로고    scopus 로고
    • Comparison of the activities of zanamivir, oseltamivir, and RWJ-270201 against clinical isolates of influenza virus and neuraminidase inhibitor-resistant variants
    • Gubareva, L. V., Webster, R. G. &Hayden, F. G. Comparison of the activities of zanamivir, oseltamivir, and RWJ-270201 against clinical isolates of influenza virus and neuraminidase inhibitor-resistant variants. Antimicrob Agents Chemother. 45(12), 3403-3408 (2001)
    • (2001) Antimicrob Agents Chemother , vol.45 , Issue.12 , pp. 3403-3408
    • Gubareva, L.V.1    Webster, R.G.2    Hayden, F.G.3
  • 22
    • 46249111790 scopus 로고    scopus 로고
    • Crystal structures of oseltamivir-resistant influenza virus neuraminidase mutants
    • Collins, P. J. et al. Crystal structures of oseltamivir-resistant influenza virus neuraminidase mutants. Nature. 453(7199), 1258-1261 (2008)
    • (2008) Nature , vol.453 , Issue.7199 , pp. 1258-1261
    • Collins, P.J.1
  • 23
    • 0027287506 scopus 로고
    • Rational design of potent sialidase-based inhibitors of influenza virus replication
    • von Itzstein, M. et al. Rational design of potent sialidase-based inhibitors of influenza virus replication. Nature. 363(6428), 418-423 (1993)
    • (1993) Nature , vol.363 , Issue.6428 , pp. 418-423
    • Von Itzstein, M.1
  • 24
    • 34848839869 scopus 로고    scopus 로고
    • Synthesis of tamiflu and its phosphonate congeners possessing potent anti-influenza activity
    • Shie, J. J. et al. Synthesis of tamiflu and its phosphonate congeners possessing potent anti-influenza activity. J Am Chem Soc. 129(39), 11892-11893 (2007)
    • (2007) J Am Chem Soc , vol.129 , Issue.39 , pp. 11892-11893
    • Shie, J.J.1
  • 25
    • 0036805385 scopus 로고    scopus 로고
    • Comparison of colorimetric, fluorometric, and visual methods for determining anti-influenza (H1N1 and H3N2) virus activities and toxicities of compounds
    • Smee, D. F., Morrison, A. C., Barnard, D. L. &Sidwell, R. W. Comparison of colorimetric, fluorometric, and visual methods for determining anti-influenza (H1N1 and H3N2) virus activities and toxicities of compounds. J Virol Methods. 106(1), 71-79 (2002)
    • (2002) J Virol Methods , vol.106 , Issue.1 , pp. 71-79
    • Smee, D.F.1    Morrison, A.C.2    Barnard, D.L.3    Sidwell, R.W.4
  • 26
    • 0035115174 scopus 로고    scopus 로고
    • Cyclopentane neuraminidase inhibitors with potent in vitro anti-influenza virus activities
    • Smee, D. F., Huffman, J. H., Morrison, A. C., Barnard, D. L. &Sidwell, R. W. Cyclopentane neuraminidase inhibitors with potent in vitro anti-influenza virus activities. Antimicrob Agents Chemother. 45(3), 743-748 (2001)
    • (2001) Antimicrob Agents Chemother , vol.45 , Issue.3 , pp. 743-748
    • Smee, D.F.1    Huffman, J.H.2    Morrison, A.C.3    Barnard, D.L.4    Sidwell, R.W.5
  • 27
    • 84945945175 scopus 로고
    • Sawyer, L., Isaacs, N., Bailey, S. (eds Data Collection and Processing. 556-562 (SERC Daresbury Laboratory: Warrington
    • Otwinowski, Z. &Minor, W. In: Sawyer, L., Isaacs, N., Bailey, S. (eds). Data Collection and Processing. 556-562 (SERC Daresbury Laboratory: Warrington, 1993)
    • (1993)
    • Otwinowski, Z.1    Minor, W.2
  • 28
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr. 66(Pt 2), 213-221 (2010)
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.2 , pp. 213-221
    • Adams, P.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.