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Volumn 59, Issue 4, 2015, Pages 1827-1836

Biochemical characterization of recombinant enterovirus 71 3c protease with fluorogenic model peptide substrates and development of a biochemical assay

Author keywords

[No Author keywords available]

Indexed keywords

ENTEROVIRUS 71 3C PROTEASE; FLUOROGENIC PEPTIDE; PEPTIDE DERIVATIVE; PROTEINASE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG; VIRUS PROTEIN; 3C PROTEASES; ANTIVIRUS AGENT; CYSTEINE PROTEINASE; FLUORESCENT DYE; PEPTIDE; PROTEINASE INHIBITOR;

EID: 84928910517     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.04698-14     Document Type: Article
Times cited : (19)

References (44)
  • 1
    • 0037240370 scopus 로고    scopus 로고
    • Epidemic hand, foot and mouth disease caused by human enterovirus 71, Singapore
    • Chan KP, Goh KT, Chong CY, Teo ES, Lau G, Ling AE. 2003. Epidemic hand, foot and mouth disease caused by human enterovirus 71, Singapore. Emerg Infect Dis 9:78-85. http://dx.doi.org/10.3201/eid1301.020112.
    • (2003) Emerg Infect Dis , vol.9 , pp. 78-85
    • Chan, K.P.1    Goh, K.T.2    Chong, C.Y.3    Teo, E.S.4    Lau, G.5    Ling, A.E.6
  • 2
    • 68349134833 scopus 로고    scopus 로고
    • Neuropathology in 2 cases of fatal enterovirus type 71 infection from a recent epidemic in the People's Republic of China: A histopathologic, immunohistochemical, and reverse transcription polymerase chain reaction study
    • Yang Y, Wang H, Gong E, Du J, Zhao X, McNutt MA, Wang S, Zhong Y, Gao Z, Zheng J. 2009. Neuropathology in 2 cases of fatal enterovirus type 71 infection from a recent epidemic in the People's Republic of China: a histopathologic, immunohistochemical, and reverse transcription polymerase chain reaction study. Hum Pathol 40:1288-1295. http://dx.doi.org/10.1016/j.humpath.2009.01.015.
    • (2009) Hum Pathol , vol.40 , pp. 1288-1295
    • Yang, Y.1    Wang, H.2    Gong, E.3    Du, J.4    Zhao, X.5    McNutt, M.A.6    Wang, S.7    Zhong, Y.8    Gao, Z.9    Zheng, J.10
  • 3
    • 34548756068 scopus 로고    scopus 로고
    • An eight-year study of epidemiologic features of enterovirus 71 infection in Taiwan
    • Chen S-C, Chang H-L, Yan T-R, Cheng Y-T, Chen K-T. 2007. An eight-year study of epidemiologic features of enterovirus 71 infection in Taiwan. Am J Trop Med Hyg 77:188-191.
    • (2007) Am J Trop Med Hyg , vol.77 , pp. 188-191
    • Chen, S.-C.1    Chang, H.-L.2    Yan, T.-R.3    Cheng, Y.-T.4    Chen, K.-T.5
  • 4
    • 59149091233 scopus 로고    scopus 로고
    • Genetic diversity of enterovirus 71 isolated from cases of hand, foot and mouth disease in the 1997, 2000 and 2005 outbreaks, Peninsular Malaysia
    • Chua K, Chua B, Lee C, Chem Y, Ismail N, Kiyu A, Kumarasamy V. 2007. Genetic diversity of enterovirus 71 isolated from cases of hand, foot and mouth disease in the 1997, 2000 and 2005 outbreaks, Peninsular Malaysia. Malays J Pathol 29:69-78.
    • (2007) Malays J Pathol , vol.29 , pp. 69-78
    • Chua, K.1    Chua, B.2    Lee, C.3    Chem, Y.4    Ismail, N.5    Kiyu, A.6    Kumarasamy, V.7
  • 5
    • 84877616491 scopus 로고    scopus 로고
    • Crystal structure of enterovirus 71 RNA-dependent RNA polymerase complexed with its protein primer VPg: Implication for a trans mechanism of VPg uridylylation
    • Chen C, Wang Y, Shan C, Sun Y, Xu P, Zhou H, Yang C, Shi P-Y, Rao Z, Zhang B. 2013. Crystal structure of enterovirus 71 RNA-dependent RNA polymerase complexed with its protein primer VPg: implication for a trans mechanism of VPg uridylylation. J Virol 87:5755-5768. http://dx.doi.org/10.1128/JVI.02733-12.
    • (2013) J Virol , vol.87 , pp. 5755-5768
    • Chen, C.1    Wang, Y.2    Shan, C.3    Sun, Y.4    Xu, P.5    Zhou, H.6    Yang, C.7    Shi, P.-Y.8    Rao, Z.9    Zhang, B.10
  • 6
    • 84926174453 scopus 로고    scopus 로고
    • Crystal structure of the novel di-nucleotide cyclase from Vibrio cholerae (DncV) responsible for synthesizing a hybrid cyclic GMPAMP
    • Ming Z, Wang W, Xie Y, Ding P, Chen Y, Jin D, Sun Y, Xia B, Yan L, Lou Z. 2014. Crystal structure of the novel di-nucleotide cyclase from Vibrio cholerae (DncV) responsible for synthesizing a hybrid cyclic GMPAMP. Cell Res 24:1270-1273. http://dx.doi.org/10.1038/cr.2014.123.
    • (2014) Cell Res , vol.24 , pp. 1270-1273
    • Ming, Z.1    Wang, W.2    Xie, Y.3    Ding, P.4    Chen, Y.5    Jin, D.6    Sun, Y.7    Xia, B.8    Yan, L.9    Lou, Z.10
  • 7
    • 84907920692 scopus 로고    scopus 로고
    • Formation and working mechanism of the picornavirus VPg uridylylation complex
    • Sun Y, Guo Y, Lou Z. 2014. Formation and working mechanism of the picornavirus VPg uridylylation complex. Curr Opin Virol 9:24-30. http://dx.doi.org/10.1016/j.coviro.2014.09.003.
    • (2014) Curr Opin Virol , vol.9 , pp. 24-30
    • Sun, Y.1    Guo, Y.2    Lou, Z.3
  • 8
    • 84877307801 scopus 로고    scopus 로고
    • Structures of coxsackievirus, rhinovirus, and poliovirus polymerase elongation complexes solved by engineering RNA mediated crystal contacts
    • Gong P, Kortus MG, Nix JC, Davis RE, Peersen OB. 2013. Structures of coxsackievirus, rhinovirus, and poliovirus polymerase elongation complexes solved by engineering RNA mediated crystal contacts. PLoS One 8:e60272. http://dx.doi.org/10.1371/journal.pone.0060272.
    • (2013) PLoS One , vol.8 , pp. e60272
    • Gong, P.1    Kortus, M.G.2    Nix, J.C.3    Davis, R.E.4    Peersen, O.B.5
  • 9
    • 0036242282 scopus 로고    scopus 로고
    • An overview of the evolution of enterovirus 71 and its clinical and public health significance
    • McMinn PC. 2002. An overview of the evolution of enterovirus 71 and its clinical and public health significance. FEMS Microbiol Rev 26:91-107. http://dx.doi.org/10.1111/j.1574-6976.2002.tb00601.x.
    • (2002) FEMS Microbiol Rev , vol.26 , pp. 91-107
    • McMinn, P.C.1
  • 10
    • 79952537148 scopus 로고    scopus 로고
    • Structures of EV71 RNA-dependent RNA polymerase in complex with substrate and analogue provide a drug target against the hand-footand-mouth disease pandemic in China
    • Wu Y, Lou Z, Miao Y, Yu Y, Dong H, Peng W, Bartlam M, Li X, Rao Z. 2010. Structures of EV71 RNA-dependent RNA polymerase in complex with substrate and analogue provide a drug target against the hand-footand-mouth disease pandemic in China. Protein Cell 1:491-500. http://dx.doi.org/10.1007/s13238-010-0061-7.
    • (2010) Protein Cell , vol.1 , pp. 491-500
    • Wu, Y.1    Lou, Z.2    Miao, Y.3    Yu, Y.4    Dong, H.5    Peng, W.6    Bartlam, M.7    Li, X.8    Rao, Z.9
  • 11
    • 84908339254 scopus 로고    scopus 로고
    • Cyclophilin a associates with enterovirus-71 virus capsid and plays an essential role in viral infection as an uncoating regulator
    • Qing J, Wang Y, Sun Y, Huang J, Yan W, Wang J, Su D, Ni C, Li J, Rao Z. 2014. Cyclophilin a associates with enterovirus-71 virus capsid and plays an essential role in viral infection as an uncoating regulator. PLoS Pathol 10:e1004422. http://dx.doi.org/10.1371/journal.ppat.1004422.
    • (2014) PLoS Pathol , vol.10 , pp. e1004422
    • Qing, J.1    Wang, Y.2    Sun, Y.3    Huang, J.4    Yan, W.5    Wang, J.6    Su, D.7    Ni, C.8    Li, J.9    Rao, Z.10
  • 12
    • 33646549883 scopus 로고    scopus 로고
    • Use of fluorescence resonance energy transfer for rapid detection of enteroviral infection in vivo
    • Hwang Y-C, Chen W, Yates MV. 2006. Use of fluorescence resonance energy transfer for rapid detection of enteroviral infection in vivo. Appl Environ Microbiol 72:3710-3715. http://dx.doi.org/10.1128/AEM.72.5.3710-3715.2006.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 3710-3715
    • Hwang, Y.-C.1    Chen, W.2    Yates, M.V.3
  • 13
    • 0027451701 scopus 로고
    • RNA-dependent cleavage of VP0 capsid protein in provirions of hepatitis Avirus
    • Bishop NE, Anderson DA. 1993. RNA-dependent cleavage of VP0 capsid protein in provirions of hepatitis Avirus. Virology 197:616-623. http://dx.doi.org/10.1006/viro.1993.1636.
    • (1993) Virology , vol.197 , pp. 616-623
    • Bishop, N.E.1    Anderson, D.A.2
  • 14
    • 33947386595 scopus 로고    scopus 로고
    • Crystal structure of poliovirus 3CD protein: Virally encoded protease and precursor to the RNA-dependent RNApolymerase
    • Marcotte LL, Wass AB, Gohara DW, Pathak HB, Arnold JJ, Filman DJ, Cameron CE, Hogle JM. 2007. Crystal structure of poliovirus 3CD protein: virally encoded protease and precursor to the RNA-dependent RNApolymerase. J Virol 81:3583-3596. http://dx.doi.org/10.1128/JVI.02306-06.
    • (2007) J Virol , vol.81 , pp. 3583-3596
    • Marcotte, L.L.1    Wass, A.B.2    Gohara, D.W.3    Pathak, H.B.4    Arnold, J.J.5    Filman, D.J.6    Cameron, C.E.7    Hogle, J.M.8
  • 15
    • 0028235532 scopus 로고
    • Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein
    • Matthews DA, Smith WW, Ferre RA, Condon B, Budahazi G, Slsson W, Villafranca J, Janson CA, McElroy H, Gribskov C. 1994. Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein. Cell 77:761-771. http://dx.doi.org/10.1016/0092-8674(94)90059-0.
    • (1994) Cell , vol.77 , pp. 761-771
    • Matthews, D.A.1    Smith, W.W.2    Ferre, R.A.3    Condon, B.4    Budahazi, G.5    Slsson, W.6    Villafranca, J.7    Janson, C.A.8    McElroy, H.9    Gribskov, C.10
  • 16
    • 84870666504 scopus 로고    scopus 로고
    • Enterovirus 71 VPg uridylation uses a two-molecular mechanism of 3D polymerase
    • Sun Y, Wang Y, Shan C, Chen C, Xu P, Song M, Zhou H, Yang C, Xu W, Shi P-Y. 2012. Enterovirus 71 VPg uridylation uses a two-molecular mechanism of 3D polymerase. J Virol 86:13662-13671. http://dx.doi.org/10.1128/JVI.01712-12.
    • (2012) J Virol , vol.86 , pp. 13662-13671
    • Sun, Y.1    Wang, Y.2    Shan, C.3    Chen, C.4    Xu, P.5    Song, M.6    Zhou, H.7    Yang, C.8    Xu, W.9    Shi, P.-Y.10
  • 17
    • 70349659010 scopus 로고    scopus 로고
    • Enterovirus 71 3C protease cleaves a novel target CstF-64 and inhibits cellular polyadenylation
    • Weng K-F, Li M-L, Hung C-T, Shih S-R. 2009. Enterovirus 71 3C protease cleaves a novel target CstF-64 and inhibits cellular polyadenylation. PLoS Pathol 5:e1000593. http://dx.doi.org/10.1371/journal.ppat.1000593.
    • (2009) PLoS Pathol , vol.5 , pp. e1000593
    • Weng, K.-F.1    Li, M.-L.2    Hung, C.-T.3    Shih, S.-R.4
  • 18
    • 0025885346 scopus 로고
    • Poliovirus proteinase 3C converts an active form of transcription factor IIIC to an inactive form: A mechanism for inhibition of host cell polymerase III transcription by poliovirus
    • Clark ME, Hämmerle T, Wimmer E, Dasgupta A. 1991. Poliovirus proteinase 3C converts an active form of transcription factor IIIC to an inactive form: a mechanism for inhibition of host cell polymerase III transcription by poliovirus. EMBO J 10:2941.
    • (1991) EMBO J , vol.10 , pp. 2941
    • Clark, M.E.1    Hämmerle, T.2    Wimmer, E.3    Dasgupta, A.4
  • 19
    • 0025190848 scopus 로고
    • Foot-and-mouth disease virus protease 3C induces specific proteolytic cleavage of host cell histone H3
    • Falk M, Grigera P, Bergmann I, Zibert A, Multhaup G, Beck E. 1990. Foot-and-mouth disease virus protease 3C induces specific proteolytic cleavage of host cell histone H3. J Virol 64:748-756.
    • (1990) J Virol , vol.64 , pp. 748-756
    • Falk, M.1    Grigera, P.2    Bergmann, I.3    Zibert, A.4    Multhaup, G.5    Beck, E.6
  • 20
    • 0035695178 scopus 로고    scopus 로고
    • Poliovirus 3C protease-mediated degradation of transcriptional activator p53 requires a cellular activity
    • Weidman MK, Yalamanchili P, Ng B, Tsai W, Dasgupta A. 2001. Poliovirus 3C protease-mediated degradation of transcriptional activator p53 requires a cellular activity. Virology 291:260-271. http://dx.doi.org/10.1006/viro.2001.1215.
    • (2001) Virology , vol.291 , pp. 260-271
    • Weidman, M.K.1    Yalamanchili, P.2    Ng, B.3    Tsai, W.4    Dasgupta, A.5
  • 21
    • 0031016644 scopus 로고    scopus 로고
    • Inhibition of host cell transcription by poliovirus: Cleavage of transcription factor CREB by poliovirus-encoded protease 3Cpro
    • Yalamanchili P, Datta U, Dasgupta A. 1997. Inhibition of host cell transcription by poliovirus: cleavage of transcription factor CREB by poliovirus-encoded protease 3Cpro. J Virol 71:1220-1226.
    • (1997) J Virol , vol.71 , pp. 1220-1226
    • Yalamanchili, P.1    Datta, U.2    Dasgupta, A.3
  • 22
    • 84871975653 scopus 로고    scopus 로고
    • Antiviral drug discovery for the treatment of enterovirus 71 infections
    • Shang L, Xu M, Yin Z. 2013. Antiviral drug discovery for the treatment of enterovirus 71 infections. Antiviral Res 97:183-194. http://dx.doi.org/10.1016/j.antiviral.2012.12.005.
    • (2013) Antiviral Res , vol.97 , pp. 183-194
    • Shang, L.1    Xu, M.2    Yin, Z.3
  • 23
    • 79953902499 scopus 로고    scopus 로고
    • Crystal structure of human enterovirus 71 3C protease
    • Cui S, Wang J, Fan T, Qin B, Guo L, Lei X, Wang J, Wang M, Jin Q. 2011. Crystal structure of human enterovirus 71 3C protease. J Mol Biol 408:449-461. http://dx.doi.org/10.1016/j.jmb.2011.03.007.
    • (2011) J Mol Biol , vol.408 , pp. 449-461
    • Cui, S.1    Wang, J.2    Fan, T.3    Qin, B.4    Guo, L.5    Lei, X.6    Wang, J.7    Wang, M.8    Jin, Q.9
  • 24
    • 80054007220 scopus 로고    scopus 로고
    • Crystal structures of enterovirus 71 3C protease complexed with rupintrivir reveal the roles of catalytically important residues
    • Wang J, Fan T, Yao X, Wu Z, Guo L, Lei X, Wang J, Wang M, Jin Q, Cui S. 2011. Crystal structures of enterovirus 71 3C protease complexed with rupintrivir reveal the roles of catalytically important residues. J Virol 85:10021-10030. http://dx.doi.org/10.1128/JVI.05107-11.
    • (2011) J Virol , vol.85 , pp. 10021-10030
    • Wang, J.1    Fan, T.2    Yao, X.3    Wu, Z.4    Guo, L.5    Lei, X.6    Wang, J.7    Wang, M.8    Jin, Q.9    Cui, S.10
  • 25
    • 80054000375 scopus 로고    scopus 로고
    • Enterovirus 71 and coxsackievirus A16 3C proteases: Binding to rupintrivir and their substrates and anti-hand, foot, and mouth disease virus drug design
    • Lu G, Qi J, Chen Z, Xu X, Gao F, Lin D, Qian W, Liu H, Jiang H, Yan J. 2011. Enterovirus 71 and coxsackievirus A16 3C proteases: binding to rupintrivir and their substrates and anti-hand, foot, and mouth disease virus drug design. J Virol 85:10319-10331. http://dx.doi.org/10.1128/JVI.00787-11.
    • (2011) J Virol , vol.85 , pp. 10319-10331
    • Lu, G.1    Qi, J.2    Chen, Z.3    Xu, X.4    Gao, F.5    Lin, D.6    Qian, W.7    Liu, H.8    Jiang, H.9    Yan, J.10
  • 27
    • 0002807032 scopus 로고
    • Dependence of the kinetics of singlet-singlet energy transfer on spectral overlap
    • Haugland RP, Yguerabide J, Stryer L. 1969. Dependence of the kinetics of singlet-singlet energy transfer on spectral overlap. Proc Natl Acad Sci U S A 63:23-30. http://dx.doi.org/10.1073/pnas.63.1.23.
    • (1969) Proc Natl Acad Sci U S A , vol.63 , pp. 23-30
    • Haugland, R.P.1    Yguerabide, J.2    Stryer, L.3
  • 30
    • 84859452102 scopus 로고    scopus 로고
    • Crimean-Congo hemorrhagic fever virus nucleoprotein reveals endonuclease activity in bunyaviruses
    • Guo Y, Wang W, Ji W, Deng M, Sun Y, Zhou H, Yang C, Deng F, Wang H, Hu Z. 2012. Crimean-Congo hemorrhagic fever virus nucleoprotein reveals endonuclease activity in bunyaviruses. Proc Natl Acad Sci U S A 109:5046-5051. http://dx.doi.org/10.1073/pnas.1200808109.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 5046-5051
    • Guo, Y.1    Wang, W.2    Ji, W.3    Deng, M.4    Sun, Y.5    Zhou, H.6    Yang, C.7    Deng, F.8    Wang, H.9    Hu, Z.10
  • 31
    • 34249758919 scopus 로고
    • Internally quenched fluorogenic protease substrates: Solid-phase synthesis and fluorescence spectroscopy of peptides containing ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs
    • Hirata IY, Cezari MHS, Nakaie CR, Boschcov P, Ito AS, Juliano MA, Juliano L. 1995. Internally quenched fluorogenic protease substrates: solid-phase synthesis and fluorescence spectroscopy of peptides containing ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs. Lett Pept Sci 1:299-308. http://dx.doi.org/10.1007/BF00119771.
    • (1995) Lett Pept Sci , vol.1 , pp. 299-308
    • Hirata, I.Y.1    Cezari, M.H.S.2    Nakaie, C.R.3    Boschcov, P.4    Ito, A.S.5    Juliano, M.A.6    Juliano, L.7
  • 32
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • Zhang J-H, Chung TD, Oldenburg KR. 1999. A simple statistical parameter for use in evaluation and validation of high throughput screening assays. J Biomol Screen 4:67-73. http://dx.doi.org/10.1177/108705719900400206.
    • (1999) J Biomol Screen , vol.4 , pp. 67-73
    • Zhang, J.-H.1    Chung, T.D.2    Oldenburg, K.R.3
  • 33
    • 38849206403 scopus 로고    scopus 로고
    • CHARMM force field parameters for nitroalkanes and nitroarenes
    • Klauda JB, Brooks BR. 2008. CHARMM force field parameters for nitroalkanes and nitroarenes. J Chem Theor Comput 4:107-115. http://dx.doi.org/10.1021/ct700191v.
    • (2008) J Chem Theor Comput , vol.4 , pp. 107-115
    • Klauda, J.B.1    Brooks, B.R.2
  • 34
    • 0035950051 scopus 로고    scopus 로고
    • Ligand-protein database: Linking protein-ligand complex structures to binding data
    • Roche O, Kiyama R, Brooks CL. 2001. Ligand-protein database: linking protein-ligand complex structures to binding data. J Med Chem 44:3592-3598. http://dx.doi.org/10.1021/jm000467k.
    • (2001) J Med Chem , vol.44 , pp. 3592-3598
    • Roche, O.1    Kiyama, R.2    Brooks, C.L.3
  • 35
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • Jorgensen WL, Chandrasekhar J, Madura JD, Impey RW, Klein ML. 1983. Comparison of simple potential functions for simulating liquid water. J Chem Phys 79:926-935. http://dx.doi.org/10.1063/1.445869.
    • (1983) J Chem Phys , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Madura, J.D.3    Impey, R.W.4    Klein, M.L.5
  • 36
    • 84952104504 scopus 로고
    • An analysis of the accuracy of Langevin and molecular dynamics algorithms
    • Pastor RW, Brooks BR, Szabo A. 1988. An analysis of the accuracy of Langevin and molecular dynamics algorithms. Mol Phys 65:1409-1419. http://dx.doi.org/10.1080/00268978800101881.
    • (1988) Mol Phys , vol.65 , pp. 1409-1419
    • Pastor, R.W.1    Brooks, B.R.2    Szabo, A.3
  • 37
    • 84908598870 scopus 로고    scopus 로고
    • An adenosine nucleoside analogue NITD008 inhibits EV71 proliferation
    • Shang L, Wang Y, Qing J, Shu B, Cao L, Lou Z, Gong P, Sun Y, Yin Z. 2014. An adenosine nucleoside analogue NITD008 inhibits EV71 proliferation. Antiviral Res 112:47-58. http://dx.doi.org/10.1016/j.antiviral.2014.10.009.
    • (2014) Antiviral Res , vol.112 , pp. 47-58
    • Shang, L.1    Wang, Y.2    Qing, J.3    Shu, B.4    Cao, L.5    Lou, Z.6    Gong, P.7    Sun, Y.8    Yin, Z.9
  • 38
    • 33750000959 scopus 로고    scopus 로고
    • Creation of a recombinant peptide substrate for fluorescence resonance energy transfer-based protease assays
    • Zhang L, Lawson HL, Harish VC, Huff JD, Knovich MA, Owen J. 2006. Creation of a recombinant peptide substrate for fluorescence resonance energy transfer-based protease assays. Anal Biochem 358:298-300. http://dx.doi.org/10.1016/j.ab.2006.06.022.
    • (2006) Anal Biochem , vol.358 , pp. 298-300
    • Zhang, L.1    Lawson, H.L.2    Harish, V.C.3    Huff, J.D.4    Knovich, M.A.5    Owen, J.6
  • 39
    • 33846106926 scopus 로고    scopus 로고
    • Substrate specificity of recombinant dengue 2 virus NS2B-NS3 protease: Influence of natural and unnatural basic amino acids on hydrolysis of synthetic fluorescent substrates
    • Gouvea I, Izidoro M, Judice W, Cezari M, Caliendo G, Santagada V, Dos Santos C, Queiroz M, Juliano M, Young P. 2007. Substrate specificity of recombinant dengue 2 virus NS2B-NS3 protease: influence of natural and unnatural basic amino acids on hydrolysis of synthetic fluorescent substrates. Arch Biochem Biophys 457:187-196. http://dx.doi.org/10.1016/j.abb.2006.11.005.
    • (2007) Arch Biochem Biophys , vol.457 , pp. 187-196
    • Gouvea, I.1    Izidoro, M.2    Judice, W.3    Cezari, M.4    Caliendo, G.5    Santagada, V.6    Dos Santos, C.7    Queiroz, M.8    Juliano, M.9    Young, P.10
  • 40
    • 84895076942 scopus 로고    scopus 로고
    • Current progress in antiviral strategies
    • Lou Z, Sun Y, Rao Z. 2014. Current progress in antiviral strategies. Trends Pharmacol Sci 35:86-102. http://dx.doi.org/10.1016/j.tips.2013.11.006.
    • (2014) Trends Pharmacol Sci , vol.35 , pp. 86-102
    • Lou, Z.1    Sun, Y.2    Rao, Z.3
  • 42
    • 59749091428 scopus 로고    scopus 로고
    • Real-time monitoring of human enterovirus (HEV)-infected cells and anti-HEV 3C protease potency by fluorescence resonance energy transfer
    • Tsai M-T, Cheng Y-H, Liu Y-N, Liao N-C, Lu W-W, Kung S-H. 2009. Real-time monitoring of human enterovirus (HEV)-infected cells and anti-HEV 3C protease potency by fluorescence resonance energy transfer. Antimicrob Agents Chemother 53:748-755. http://dx.doi.org/10.1128/AAC.00841-08.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 748-755
    • Tsai, M.-T.1    Cheng, Y.-H.2    Liu, Y.-N.3    Liao, N.-C.4    Lu, W.-W.5    Kung, S.-H.6
  • 43
    • 84883795344 scopus 로고    scopus 로고
    • Structural perspective on the formation of ribonucleoprotein complex in negative-sense singlestranded RNA viruses
    • Zhou H, Sun Y, Guo Y, Lou Z. 2013. Structural perspective on the formation of ribonucleoprotein complex in negative-sense singlestranded RNA viruses. Trends Microbiol 21:475-484. http://dx.doi.org/10.1016/j.tim.2013.07.006.
    • (2013) Trends Microbiol , vol.21 , pp. 475-484
    • Zhou, H.1    Sun, Y.2    Guo, Y.3    Lou, Z.4
  • 44
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert J-P, Ciccotti G, Berendsen HJC. 1977. Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J Comput Phys 23:327-341. http://dx.doi.org/10.1016/0021-9991(77)90098-5.
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.