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Journal Abstract Search

385 related items for PubMed ID: 22007671

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  • 5. Homology modeling and molecular dynamics study of West Nile virus NS3 protease: a molecular basis for the catalytic activity increased by the NS2B cofactor.
    Zhou H, Singh NJ, Kim KS.
    Proteins; 2006 Nov 15; 65(3):692-701. PubMed ID: 16972281
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  • 6. The dengue virus NS2B-NS3 protease retains the closed conformation in the complex with BPTI.
    Chen WN, Loscha KV, Nitsche C, Graham B, Otting G.
    FEBS Lett; 2014 Jun 27; 588(14):2206-11. PubMed ID: 24859037
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  • 7. NMR analysis of the dynamic exchange of the NS2B cofactor between open and closed conformations of the West Nile virus NS2B-NS3 protease.
    Su XC, Ozawa K, Qi R, Vasudevan SG, Lim SP, Otting G.
    PLoS Negl Trop Dis; 2009 Dec 08; 3(12):e561. PubMed ID: 19997625
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  • 11. NMR analysis of a novel enzymatically active unlinked dengue NS2B-NS3 protease complex.
    Kim YM, Gayen S, Kang C, Joy J, Huang Q, Chen AS, Wee JL, Ang MJ, Lim HA, Hung AW, Li R, Noble CG, Lee le T, Yip A, Wang QY, Chia CS, Hill J, Shi PY, Keller TH.
    J Biol Chem; 2013 May 03; 288(18):12891-900. PubMed ID: 23511634
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  • 14. Identification of residues in the dengue virus type 2 NS2B cofactor that are critical for NS3 protease activation.
    Niyomrattanakit P, Winoyanuwattikun P, Chanprapaph S, Angsuthanasombat C, Panyim S, Katzenmeier G.
    J Virol; 2004 Dec 03; 78(24):13708-16. PubMed ID: 15564480
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  • 15. Crystal structure of Dengue virus NS3 protease in complex with a Bowman-Birk inhibitor: implications for flaviviral polyprotein processing and drug design.
    Murthy HM, Judge K, DeLucas L, Padmanabhan R.
    J Mol Biol; 2000 Aug 25; 301(4):759-67. PubMed ID: 10966782
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  • 16. Binding specificity of polypeptide substrates in NS2B/NS3pro serine protease of dengue virus type 2: A molecular dynamics Study.
    Yotmanee P, Rungrotmongkol T, Wichapong K, Choi SB, Wahab HA, Kungwan N, Hannongbua S.
    J Mol Graph Model; 2015 Jul 25; 60():24-33. PubMed ID: 26086900
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  • 17. Cysteine Disulfide Traps Reveal Distinct Conformational Ensembles in Dengue Virus NS2B-NS3 Protease.
    Hill ME, Yildiz M, Hardy JA.
    Biochemistry; 2019 Feb 12; 58(6):776-787. PubMed ID: 30472839
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  • 19. NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics.
    Gupta G, Lim L, Song J.
    PLoS One; 2015 Feb 12; 10(8):e0134823. PubMed ID: 26258523
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