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Volumn 588, Issue 17, 2014, Pages 2794-2799

An inhibition model of BPTI to unlinked dengue virus NS2B-NS3 protease

Author keywords

Bovine pancreatic trypsin inhibitor; Closed active conformation; Dengue virus; NMR spectroscopy; NS2B NS3 protease

Indexed keywords

APROTININ; NONSTRUCTURAL PROTEIN 2; NONSTRUCTURAL PROTEIN 3; PROTEIN NS2B; PROTEINASE; UNCLASSIFIED DRUG;

EID: 84906246516     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2014.05.063     Document Type: Article
Times cited : (12)

References (22)
  • 2
    • 0034616194 scopus 로고    scopus 로고
    • Purified NS2B/NS3 serine protease of dengue virus type 2 exhibits cofactor NS2B dependence for cleavage of substrates with dibasic amino acids in vitro
    • R. Yusof, S. Clum, M. Wetzel, H.M. Murthy, and R. Padmanabhan Purified NS2B/NS3 serine protease of dengue virus type 2 exhibits cofactor NS2B dependence for cleavage of substrates with dibasic amino acids in vitro J. Biol. Chem. 275 2000 9963 9969
    • (2000) J. Biol. Chem. , vol.275 , pp. 9963-9969
    • Yusof, R.1    Clum, S.2    Wetzel, M.3    Murthy, H.M.4    Padmanabhan, R.5
  • 3
    • 0035824539 scopus 로고    scopus 로고
    • Activity of recombinant dengue 2 virus NS3 protease in the presence of a truncated NS2B co-factor, small peptide substrates, and inhibitors
    • D. Leung, K. Schroder, H. White, N.X. Fang, M.J. Stoermer, G. Abbenante, J.L. Martin, P.R. Young, and D.P. Fairlie Activity of recombinant dengue 2 virus NS3 protease in the presence of a truncated NS2B co-factor, small peptide substrates, and inhibitors J. Biol. Chem. 276 2001 45762 45771
    • (2001) J. Biol. Chem. , vol.276 , pp. 45762-45771
    • Leung, D.1    Schroder, K.2    White, H.3    Fang, N.X.4    Stoermer, M.J.5    Abbenante, G.6    Martin, J.L.7    Young, P.R.8    Fairlie, D.P.9
  • 5
    • 34247625945 scopus 로고    scopus 로고
    • Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold
    • A.E. Aleshin, S.A. Shiryaev, A.Y. Strongin, and R.C. Liddington Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold Protein Sci. 16 2007 795 806
    • (2007) Protein Sci. , vol.16 , pp. 795-806
    • Aleshin, A.E.1    Shiryaev, S.A.2    Strongin, A.Y.3    Liddington, R.C.4
  • 7
    • 84864957319 scopus 로고    scopus 로고
    • Critical effect of peptide cyclization on the potency of peptide inhibitors against dengue virus NS2B-NS3 protease
    • S. Xu, H. Li, X. Shao, C. Fan, B. Ericksen, J. Liu, C. Chi, and C. Wang Critical effect of peptide cyclization on the potency of peptide inhibitors against dengue virus NS2B-NS3 protease J. Med. Chem. 55 2012 6881 6887
    • (2012) J. Med. Chem. , vol.55 , pp. 6881-6887
    • Xu, S.1    Li, H.2    Shao, X.3    Fan, C.4    Ericksen, B.5    Liu, J.6    Chi, C.7    Wang, C.8
  • 8
    • 77954942481 scopus 로고    scopus 로고
    • Design, structure-based focusing and in silico screening of combinatorial library of peptidomimetic inhibitors of Dengue virus NS2B-NS3 protease
    • V. Frecer, and S. Miertus Design, structure-based focusing and in silico screening of combinatorial library of peptidomimetic inhibitors of Dengue virus NS2B-NS3 protease J. Comput. Aided Mol. Des. 24 2010 195 212
    • (2010) J. Comput. Aided Mol. Des. , vol.24 , pp. 195-212
    • Frecer, V.1    Miertus, S.2
  • 9
    • 84891560753 scopus 로고    scopus 로고
    • The flavivirus protease as a target for drug discovery
    • M. Brecher, J. Zhang, and H. Li The flavivirus protease as a target for drug discovery Virol. Sin. 28 2013 326 336
    • (2013) Virol. Sin. , vol.28 , pp. 326-336
    • Brecher, M.1    Zhang, J.2    Li, H.3
  • 11
    • 84890813052 scopus 로고    scopus 로고
    • Allosteric inhibition of the NS2B-NS3 protease from dengue virus
    • M. Yildiz, S. Ghosh, J.A. Bell, W. Sherman, and J.A. Hardy Allosteric inhibition of the NS2B-NS3 protease from dengue virus ACS Chem. Biol. 8 2013 2744 2752
    • (2013) ACS Chem. Biol. , vol.8 , pp. 2744-2752
    • Yildiz, M.1    Ghosh, S.2    Bell, J.A.3    Sherman, W.4    Hardy, J.A.5
  • 12
    • 84855921187 scopus 로고    scopus 로고
    • Ligand-bound structures of the dengue virus protease reveal the active conformation
    • C.G. Noble, C.C. Seh, A.T. Chao, and P.Y. Shi Ligand-bound structures of the dengue virus protease reveal the active conformation J. Virol. 86 2012 438 446
    • (2012) J. Virol. , vol.86 , pp. 438-446
    • Noble, C.G.1    Seh, C.C.2    Chao, A.T.3    Shi, P.Y.4
  • 14
    • 81855172065 scopus 로고    scopus 로고
    • Binding of low molecular weight inhibitors promotes large conformational changes in the dengue virus NS2B-NS3 protease: Fold analysis by pseudocontact shifts
    • L. de la Cruz, T.H. Nguyen, K. Ozawa, J. Shin, B. Graham, T. Huber, and G. Otting Binding of low molecular weight inhibitors promotes large conformational changes in the dengue virus NS2B-NS3 protease: fold analysis by pseudocontact shifts J. Am. Chem. Soc. 133 2011 19205 19215
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 19205-19215
    • De La Cruz, L.1    Nguyen, T.H.2    Ozawa, K.3    Shin, J.4    Graham, B.5    Huber, T.6    Otting, G.7
  • 15
    • 84899447129 scopus 로고    scopus 로고
    • Binding mode of the activity-modulating C-terminal segment of NS2B to NS3 in the dengue virus NS2B-NS3 protease
    • L. de la Cruz, W.N. Chen, B. Graham, and G. Otting Binding mode of the activity-modulating C-terminal segment of NS2B to NS3 in the dengue virus NS2B-NS3 protease FEBS J. 281 2014 1517 1533
    • (2014) FEBS J. , vol.281 , pp. 1517-1533
    • De La Cruz, L.1    Chen, W.N.2    Graham, B.3    Otting, G.4
  • 17
    • 84883490550 scopus 로고    scopus 로고
    • 15N resonance assignments of dengue virus NS2B-NS3p in complex with aprotinin
    • 15N resonance assignments of dengue virus NS2B-NS3p in complex with aprotinin Biomol. NMR Assign. 7 2013 137 139
    • (2013) Biomol. NMR Assign. , vol.7 , pp. 137-139
    • Bi, Y.1    Zhu, L.2    Li, H.3    Wu, B.4    Liu, J.5    Wang, J.6
  • 19
    • 77049143386 scopus 로고
    • The determination of enzyme inhibitor constants
    • M. Dixon The determination of enzyme inhibitor constants Biochem. J. 55 1953 170 171
    • (1953) Biochem. J. , vol.55 , pp. 170-171
    • Dixon, M.1
  • 21
    • 74549156902 scopus 로고    scopus 로고
    • NMR analysis of the dynamic exchange of the NS2B cofactor between open and closed conformations of the West Nile virus NS2B-NS3 protease
    • X.C. Su, K. Ozawa, R. Qi, S.G. Vasudevan, S.P. Lim, and G. Otting NMR analysis of the dynamic exchange of the NS2B cofactor between open and closed conformations of the West Nile virus NS2B-NS3 protease PLoS Negl. Trop. Dis. 3 2009 e561
    • (2009) PLoS Negl. Trop. Dis. , vol.3 , pp. 561
    • Su, X.C.1    Ozawa, K.2    Qi, R.3    Vasudevan, S.G.4    Lim, S.P.5    Otting, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.