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Volumn 3, Issue 3, 2009, Pages 334-342

NS3 helicases as drug targets

Author keywords

Dengue virus; Hepatitis C virus; NS3 helicase; West nile virus

Indexed keywords

ADENOSINE DIPHOSPHATE; APOLIPOPROTEIN; DEAD BOX PROTEIN; HELICASE; NONSTRUCTURAL PROTEIN 3; NUCLEIC ACID; RNA; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR ELF 4A; UNCLASSIFIED DRUG;

EID: 70449675063     PISSN: 18723136     EISSN: None     Source Type: Journal    
DOI: 10.2174/187231309789054850     Document Type: Review
Times cited : (1)

References (63)
  • 3
    • 38849209154 scopus 로고    scopus 로고
    • Pathogenic flaviviruses
    • Gould EA, Solomon T. Pathogenic flaviviruses. Lancet 2008; 371: 500-509
    • (2008) Lancet , vol.371 , pp. 500-509
    • Gould, E.A.1    Solomon, T.2
  • 4
    • 34547618419 scopus 로고    scopus 로고
    • Non-nucleoside inhibitors of the HCV NS5B polymerase: Progress in the discovery and development of novel agents for the treatment of HCV infections
    • Beaulieu PL. Non-nucleoside inhibitors of the HCV NS5B polymerase: progress in the discovery and development of novel agents for the treatment of HCV infections. Curr Opin Investig Drugs 2007; 8: 614-634
    • (2007) Curr Opin Investig Drugs , vol.8 , pp. 614-634
    • Beaulieu, P.L.1
  • 5
    • 42149130312 scopus 로고    scopus 로고
    • Future directions in therapy for chronic hepatitis C
    • Jensen DM, Ascione A. Future directions in therapy for chronic hepatitis C. Antiviral Ther 2008; 13: 31-36 (Pubitemid 351542496)
    • (2008) Antiviral Therapy , vol.13 , Issue.SUPPL. 1 , pp. 31-36
    • Jensen, D.M.1    Ascione, A.2
  • 6
    • 50249147367 scopus 로고    scopus 로고
    • The flavivirus polymerase as a target for drug discovery
    • Malet H, Massé N, Selisko B, et al. The flavivirus polymerase as a target for drug discovery. Antiviral Res 2008; 80: 23-35.
    • (2008) Antiviral Res , vol.80 , pp. 23-35
    • Malet, H.1    Massé, N.2    Selisko, B.3
  • 7
    • 57149088067 scopus 로고    scopus 로고
    • Molecular targets for flavivirus drug discovery
    • Sampath A, Padmanabhan R. Molecular targets for flavivirus drug discovery. Antiviral Res 2009; 81: 6-15.
    • (2009) Antiviral Res , vol.81 , pp. 6-15
    • Sampath, A.1    Padmanabhan, R.2
  • 8
    • 53249121029 scopus 로고    scopus 로고
    • Towards the design of antiviral inhibitors against flaviviruses: The case for the multifunctional NS3 protein from dengue virus as a target
    • Lescar J, Luo D, Xu T, et al. Towards the design of antiviral inhibitors against flaviviruses: the case for the multifunctional NS3 protein from dengue virus as a target. Antiviral Res 2008; 80: 94-101.
    • (2008) Antiviral Res , vol.80 , pp. 94-101
    • Lescar, J.1    Luo, D.2    Xu, T.3
  • 10
    • 34548271074 scopus 로고    scopus 로고
    • Novel protease and polymerase inhibitors for the treatment of hepatitis C virus infection
    • DOI 10.1517/13543784.16.8.1171
    • Sheldon J, Barreiro P, Vincent V. Novel protease and polymerase inhibitors for the treatment of hepatitis C infections. Expert Opin Investig Drugs 2007; 16: 1171-1181 (Pubitemid 47317010)
    • (2007) Expert Opinion on Investigational Drugs , vol.16 , Issue.8 , pp. 1171-1181
    • Sheldon, J.1    Barreiro, P.2    Soriano, V.3
  • 13
    • 28844451513 scopus 로고    scopus 로고
    • Helicase-catalysed translocation and strand separation
    • Eoff RL, Raney KD. Helicase-catalysed translocation and strand separation. Biochem Soc Transac 2005; 33: 1474-1478
    • (2005) Biochem Soc Transac , vol.33 , pp. 1474-1478
    • Eoff, R.L.1    Raney, K.D.2
  • 14
    • 0035692794 scopus 로고    scopus 로고
    • WaterLOGSY as a method for primary NMR screening: Practical aspects and range of applicability
    • DOI 10.1023/A:1013302231549
    • Dalvit C, Fogliatto GP, Stewart A, Veronesi M, Stockman B. WaterLOGSY as a method for primary NMR screening: practical aspects and range of applicability. J Biomol NMR 2001; 21: 349-359 (Pubitemid 34071389)
    • (2001) Journal of Biomolecular NMR , vol.21 , Issue.4 , pp. 349-359
    • Dalvit, C.1    Fogliatto, G.2    Stewart, A.3    Veronesi, M.4    Stockman, B.5
  • 15
    • 30144436268 scopus 로고    scopus 로고
    • RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP
    • DOI 10.1038/nature04331
    • Dumont S, Cheng W, Serebrov V, et al. RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP. Nature 2006; 439: 105-108 (Pubitemid 43053637)
    • (2006) Nature , vol.439 , Issue.7072 , pp. 105-108
    • Dumont, S.1    Cheng, W.2    Serebrov, V.3    Beran, R.K.4    Tinoco Jr., I.5    Pyle, A.M.6    Bustamante, C.7
  • 16
    • 20444440763 scopus 로고    scopus 로고
    • A Brownian motor mechanism of translocation and strand separation by hepatitis C virus helicase
    • DOI 10.1038/nsmb920
    • Levin MK, Gurjar M, Patel SS. A brownian motor mechanism of translocation and strand separation by hepatitis C virus helicase. Nat Struct Mol Biol 2005; 12: 429-435 (Pubitemid 43085903)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.5 , pp. 429-435
    • Levin, M.K.1    Gurjar, M.2    Patel, S.S.3
  • 17
    • 33745823112 scopus 로고    scopus 로고
    • Mechanisms of helicases
    • Patel SS, Donmez I. Mechanisms of helicases. J Biol Chem 2006; 281: 18265-18268
    • (2006) J Biol Chem , vol.281 , pp. 18265-18268
    • Patel, S.S.1    Donmez, I.2
  • 18
    • 3342896727 scopus 로고    scopus 로고
    • Periodic cycles of RNA unwinding and pausing by hepatitis C virus NS3 helicase
    • DOI 10.1038/nature02704
    • Serebrov V, Pyle AM. Periodic cycles of RNA unwinding and pausing by hepatitis C virus NS3 helicase. Nature 2004; 430: 476-480 (Pubitemid 38987912)
    • (2004) Nature , vol.430 , Issue.6998 , pp. 476-480
    • Serebrov, V.1    Pyle, A.M.2
  • 19
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton MR, Dillingham MS, Wigley DB. Structure and mechanism of helicases and nucleic acid translocases. Ann Rev Biochem 2007; 76: 23-50.
    • (2007) Ann Rev Biochem , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 20
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • DOI 10.1016/j.gene.2005.10.019, PII S0378111905006359
    • Cordin O, Banroques J, Tanner NK, Linder P. The DEAD-box protein family of RNA helicases. Gene 2006; 367: 17-37. (Pubitemid 43286737)
    • (2006) Gene , vol.367 , Issue.1-2 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 21
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker JE, Saraste M, Runswick MJ, Gay NJ. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1982; 1: 945-951
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 23
    • 34347385000 scopus 로고    scopus 로고
    • RNA helicases - One fold for many functions
    • DOI 10.1016/j.sbi.2007.05.007, PII S0959440X07000723, Nucleic acids / Sequences and topology
    • Jankowsky E, Fairman ME. RNA helicases - one fold many functions. Curr Opin Struct Biol 2007; 17: 316-324 (Pubitemid 47021361)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.3 , pp. 316-324
    • Jankowsky, E.1    Fairman, M.E.2
  • 24
    • 40849130890 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of the Japanese encephalitis virus NS3 helicase/ nucleoside triphosphatase at a resolution of 1.8 Å
    • Yamashita T, Unno H, Mori Y, et al. Crystal structure of the catalytic domain of the Japanese encephalitis virus NS3 helicase/ nucleoside triphosphatase at a resolution of 1.8 Å. Virology 2008; 373: 426-436
    • (2008) Virology , vol.373 , pp. 426-436
    • Yamashita, T.1    Unno, H.2    Mori, Y.3
  • 25
    • 57149091105 scopus 로고    scopus 로고
    • Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein
    • Luo D, Xu T, Watson RP, et al. Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein. EMBO J 2008; 27: 3209-3219
    • (2008) EMBO J , vol.27 , pp. 3209-3219
    • Luo, D.1    Xu, T.2    Watson, R.P.3
  • 26
    • 6044262451 scopus 로고    scopus 로고
    • Electrostatic analysis of hepatitis C virus NS3 helicase reveals both active and allosteric site locations
    • Frick DN, Rypma RS, Lam AMI, Frenz CM. Electrostatic analysis of hepatitis C virus NS3 helicase reveals both active and allosteric site locations. Nucleic Acids Res 2004; 32: 5519-5528
    • (2004) Nucleic Acids Res , vol.32 , pp. 5519-5528
    • Frick, D.N.1    Rypma, R.S.2    Lam, A.M.I.3    Frenz, C.M.4
  • 27
    • 23244464646 scopus 로고    scopus 로고
    • Structure of the Dengue virus helicase/nucleoside triphosphatase catalytic domain at a resolution of 2.4 Å
    • Xu T, Sampath A, Chao A, et al. Structure of the Dengue virus helicase/nucleoside triphosphatase catalytic domain at a resolution of 2.4 Å. J Virol 2005; 79: 10278-10288
    • (2005) J Virol , vol.79 , pp. 10278-10288
    • Xu, T.1    Sampath, A.2    Chao, A.3
  • 29
    • 38549142580 scopus 로고    scopus 로고
    • RNA unwinding activity of the hepatitis C virus NS3 helicase is modulated by the NS5B polymerase
    • Jennings TA, Chen Y, Sikora D, et al. RNA unwinding activity of the hepatitis C virus NS3 helicase is modulated by the NS5B polymerase. Biochemistry 2008; 47: 1126-1135
    • (2008) Biochemistry , vol.47 , pp. 1126-1135
    • Jennings, T.A.1    Chen, Y.2    Sikora, D.3
  • 30
    • 21644463166 scopus 로고    scopus 로고
    • Stimulation of hepatitis C virus (HCV) nonstructural protein 3 (NS3) helicase activity by the NS3 protease domain and by HCV RNA-dependent RNA polymerase
    • DOI 10.1128/JVI.79.14.8687-8697.2005
    • Zhang C, Cai Z, Kim YC, et al. Stimulation of hepatitis C virus (HCV) nonstructural protein 3 (NS3) helicase activity by the NS3 protease domain and by HCV RNA-dependent polymerase. J Virol 2005; 79: 8687-8697 (Pubitemid 40934779)
    • (2005) Journal of Virology , vol.79 , Issue.14 , pp. 8687-8697
    • Zhang, C.1    Cai, Z.2    Kim, Y.-C.3    Kumar, R.4    Yuan, F.5    Shi, P.-Y.6    Kao, C.7    Luo, G.8
  • 31
    • 37349023165 scopus 로고    scopus 로고
    • Crystal structure of the NS3 protease-helicase from dengue virus
    • DOI 10.1128/JVI.01788-07
    • Luo D, Xu T, Hunke C, Grüber G, Vasudevan SG, Lescar J. Crystal structure of the NS3 protease-helicase from Dengue virus. J Virol 2008; 82: 173-183 (Pubitemid 350309134)
    • (2008) Journal of Virology , vol.82 , Issue.1 , pp. 173-183
    • Luo, D.1    Xu, T.2    Hunke, C.3    Gruber, G.4    Vasudevan, S.G.5    Lescar, J.6
  • 32
    • 0033571623 scopus 로고    scopus 로고
    • Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase
    • DOI 10.1016/S0969-2126(00)80025-8
    • Yao N, Reichert P, Taremi SS, Prosise WW, Weber PC. Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase. Structure 1999; 7: 1353-1363 (Pubitemid 29529876)
    • (1999) Structure , vol.7 , Issue.11 , pp. 1353-1363
    • Yao, N.1    Reichert, P.2    Taremi, S.S.3    Prosise, W.W.4    Weber, P.C.5
  • 33
    • 34250346935 scopus 로고    scopus 로고
    • Functional characterization of cis and trans activity of the flavivirus NS2B-NS3 protease
    • Bera AK, Kuhn RJ, Smith JL. Functional characterization of cis and trans activity of the flavivirus NS2B-NS3 protease. J Biol Chem 2007; 282: 12883-12892
    • (2007) J Biol Chem , vol.282 , pp. 12883-12892
    • Bera, A.K.1    Kuhn, R.J.2    Smith, J.L.3
  • 34
    • 0346463036 scopus 로고    scopus 로고
    • The Nonstructural Protein 3 Protease/Helicase Requires an Intact Protease Domain to Unwind Duplex RNA Efficiently
    • DOI 10.1074/jbc.M310630200
    • Frick DN, Rypma RS, Lam AMI, Gu B. The nonstructural protein 3 protease/helicase requires an intact protease domain to unwind duplex RNA efficiently. J Biol Chem 2004; 279: 1269-1280 (Pubitemid 38082651)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.2 , pp. 1269-1280
    • Frick, D.N.1    Rypma, R.S.2    Lam, A.M.I.3    Gu, B.4
  • 35
    • 19544394438 scopus 로고    scopus 로고
    • The RNA-unwinding activity of hepatitis C virus non-structural protein 3 (NS3) is positively modulated by its protease domain
    • DOI 10.2174/0929866053765716
    • Gu B, Pruss CM, Gates AT, Khandekar SS. The RNA-unwinding activity of hepatitis C virus non-structural protein 3 (NS3) is positively modulated by its protease domain. Protein Pept Lett 2005; 12: 315-321 (Pubitemid 40727850)
    • (2005) Protein and Peptide Letters , vol.12 , Issue.4 , pp. 315-321
    • Gu, B.1    Pruss, C.M.2    Gates, A.T.3    Khandekar, S.S.4
  • 36
    • 22844443626 scopus 로고    scopus 로고
    • Modulation of the nucleoside triphosphatase/RNA helicase and 5′-RNA triphosphatase activities of Dengue virus type 2 nonstructural protein 3 (NS3) by interaction with NS5, the RNA-dependent RNA polymerase
    • Yon C, Teramoto T, Mueller N, et al. Modulation of the nucleoside triphosphatase/RNA helicase and 5′-RNA triphosphatase activities of Dengue virus type 2 nonstructural protein 3 (NS3) by interaction with NS5, the RNA-dependent RNA polymerase. J Biol Chem 2005; 280: 27412-27419
    • (2005) J Biol Chem , vol.280 , pp. 27412-27419
    • Yon, C.1    Teramoto, T.2    Mueller, N.3
  • 37
    • 2542468381 scopus 로고    scopus 로고
    • The functional interaction of the hepatitis C virus helicase molecules is responsible for unwinding processivity
    • Levin MK, Wang YH, Patel SS. The functional interaction of the hepatitis C virus helicase molecules is responsible for unwinding processivity. J Biol Chem 2004; 279: 26005-26012
    • (2004) J Biol Chem , vol.279 , pp. 26005-26012
    • Levin, M.K.1    Wang, Y.H.2    Patel, S.S.3
  • 38
    • 36849075152 scopus 로고    scopus 로고
    • The serine protease domain of hepatitis C viral NS3 activates RNA helicase activity by promoting the binding of RNA substrate
    • DOI 10.1074/jbc.M707165200
    • Beran RKF, Serebrov V, Pyle AM. The serine protease domain of hepatitis C viral NS3 activates RNA helicase activity by promoting the binding of RNA substrate. J Biol Chem 2007; 282: 34913-34920 (Pubitemid 350232430)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.48 , pp. 34913-34920
    • Beran, R.K.F.1    Serebrov, V.2    Pyle, A.M.3
  • 39
    • 0033609061 scopus 로고    scopus 로고
    • Modulation of hepatitis C virus NS3 protease and helicase activities through the interaction with NS4A
    • Gallinari P, Paolini C, Brennan D, Nardi C, Steinkühler C, De Francesco R. Modulation of hepatitis C virus NS3 protease and helicase activities through the interaction with NS4A. Biochemistry 1999; 38: 5620-5632 (Pubitemid 129514870)
    • (1999) Biochemistry , vol.38 , Issue.17 , pp. 5620-5632
    • Gallinari, P.1    Paolini, C.2    Brennan, D.3    Nardi, C.4    Steinkuhler, C.5    De Francesco, R.6
  • 41
    • 0036500976 scopus 로고    scopus 로고
    • The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding activity
    • Pang PS, Jankowsky E, Planet PJ, Pyle AM. The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding activity. EMBO J 2002; 21: 1168-1176
    • (2002) EMBO J , vol.21 , pp. 1168-1176
    • Pang, P.S.1    Jankowsky, E.2    Planet, P.J.3    Pyle, A.M.4
  • 42
    • 47749152947 scopus 로고    scopus 로고
    • The two-component NS2B-NS3 proteinase represses DNA unwinding activity of the West Nile virus NS3 helicase
    • Chernov AV, Shiryaev SA, Aleshin AE, et al. The two-component NS2B-NS3 proteinase represses DNA unwinding activity of the West Nile virus NS3 helicase. J Biol Chem 2008; 283: 17270-17278
    • (2008) J Biol Chem , vol.283 , pp. 17270-17278
    • Chernov, A.V.1    Shiryaev, S.A.2    Aleshin, A.E.3
  • 43
    • 23244450531 scopus 로고    scopus 로고
    • Structure of the flavivirus helicase: Implications for catalytic activity, protein interactions, and proteolytic processing
    • DOI 10.1128/JVI.79.16.10268-10277.2005
    • Wu J, Bera AK, Kuhn RJ, Smith JL. Structure of the flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing. J Virol 2005; 79: 10268-10277 (Pubitemid 41098568)
    • (2005) Journal of Virology , vol.79 , Issue.16 , pp. 10268-10277
    • Wu, J.1    Bera, A.K.2    Kuhn, R.J.3    Smith, J.L.4
  • 44
    • 0033559918 scopus 로고    scopus 로고
    • Hydrogen bonding, hydrophobic interactions, and failure of the rigid receptor hypothesis
    • DOI 10.1002/(SICI)1521-3773(19990315)38:6<736::AID-ANIE736>3.0. CO;2-R
    • Davis AM, Teague SJ. Hydrogen bonding, hydrophobic interactions, and failure of the rigid receptor hypothesis. Angew Chem Int Ed 1999; 38: 736-749 (Pubitemid 29146588)
    • (1999) Angewandte Chemie - International Edition , vol.38 , Issue.6 , pp. 736-749
    • Davis, A.M.1    Teague, S.J.2
  • 45
    • 56549131177 scopus 로고    scopus 로고
    • The thermodynamics of protein-ligand interaction and solvation: Insights for ligand design
    • Olsson TSG, Williams MA, Pitt WR, Ladbury JE. The thermodynamics of protein-ligand interaction and solvation: insights for ligand design. J Mol Biol 2008; 384: 1002-1017
    • (2008) J Mol Biol , vol.384 , pp. 1002-1017
    • Olsson, T.S.G.1    Williams, M.A.2    Pitt, W.R.3    Ladbury, J.E.4
  • 46
    • 0013627747 scopus 로고    scopus 로고
    • Mutational analysis of the hepatitis C virus RNA helicase
    • Kim DW, Kim J, Gwack Y, Han JH, Choe J. Mutational analysis of the hepatitis C virus RNA helicase. J Virol 1997; 71: 9400-9409 (Pubitemid 27492383)
    • (1997) Journal of Virology , vol.71 , Issue.12 , pp. 9400-9409
    • Kim, D.W.1    Kim, J.2    Gwack, Y.3    Han, J.H.4    Choe, J.5
  • 47
    • 0034802008 scopus 로고    scopus 로고
    • Mutagenesis of the Dengue virus type 2 NS3 protein within and outside helicases motifs: Effects on enzyme activity and virus replication
    • Matusan AE, Pryor MJ, Davidson AD, Wright PJ. Mutagenesis of the Dengue virus type 2 NS3 protein within and outside helicases motifs: effects on enzyme activity and virus replication. J Virol 2001; 75: 9633-9643
    • (2001) J Virol , vol.75 , pp. 9633-9643
    • Matusan, A.E.1    Pryor, M.J.2    Davidson, A.D.3    Wright, P.J.4
  • 48
    • 0034870450 scopus 로고    scopus 로고
    • Structure- based mutational analysis of the hepatitis C virus NS3 helicase
    • Tai CL, Pan WC, Liaw SH, Yang UC, Hwang LH, Chen DS. Structure- based mutational analysis of the hepatitis C virus NS3 helicase. J Virol 2001; 75: 8289-8297
    • (2001) J Virol , vol.75 , pp. 8289-8297
    • Tai, C.L.1    Pan, W.C.2    Liaw, S.H.3    Yang, U.C.4    Hwang, L.H.5    Chen, D.S.6
  • 49
    • 33745273034 scopus 로고    scopus 로고
    • Structure- based mutational analysis of the NS3 helicase from Dengue virus
    • Sampath A, Xu T, Chao A, Luo D, Lescar J, Vasudevan SG. Structure- based mutational analysis of the NS3 helicase from Dengue virus. J Virol 2006; 80: 6686-6690
    • (2006) J Virol , vol.80 , pp. 6686-6690
    • Sampath, A.1    Xu, T.2    Chao, A.3    Luo, D.4    Lescar, J.5    Vasudevan, S.G.6
  • 50
    • 0034595282 scopus 로고    scopus 로고
    • Strand-separating activity of hepatitis C virus helicase in the absence of ATP
    • Porter DJT, Preugschat F. Strand-separating activity of hepatitis C virus helicase in the absence of ATP. Biochemistry 2000; 39: 5166-5173
    • (2000) Biochemistry , vol.39 , pp. 5166-5173
    • Porter, D.J.T.1    Preugschat, F.2
  • 51
    • 0032518490 scopus 로고    scopus 로고
    • Hepatitis C virus RNA helicase domain with a bound oligonucleotide: The crystal structure provides insights into the mode of unwinding
    • Kim JL, Morgenstern KA, Griffith JP, et al. Hepatitis C virus RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding. Structure 1998; 6: 89-100.
    • (1998) Structure , vol.6 , pp. 89-100
    • Kim, J.L.1    Morgenstern, K.A.2    Griffith, J.P.3
  • 52
    • 22244485047 scopus 로고    scopus 로고
    • Specific targeting of hepatitis C virus NS3 RNA helicase. Discovery of the potent and selective competitive nucleotide-mimicking inhibitor QU663
    • Maga G, Gemma S, Fattorusso C, et al. Specific targeting of hepatitis C virus NS3 RNA helicase. Discovery of the potent and selective competitive nucleotide-mimicking inhibitor QU663. Biochemistry 2005; 44: 9637-9644
    • (2005) Biochemistry , vol.44 , pp. 9637-9644
    • Maga, G.1    Gemma, S.2    Fattorusso, C.3
  • 53
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • Velankar SS, Soultanas P, Dillingham MS, Subramanya HS, Wigley DB. Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate and inchworm mechanism. Cell 1999; 97: 75-84. (Pubitemid 29165891)
    • (1999) Cell , vol.97 , Issue.1 , pp. 75-84
    • Velankar, S.S.1    Soultanas, P.2    Dillingham, M.S.3    Subramanya, H.S.4    Wigley, D.B.5
  • 55
    • 4143121255 scopus 로고    scopus 로고
    • Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery
    • DOI 10.1016/j.ab.2004.04.031, PII S0003269704003756
    • Lo MC, Aulabaugh A, Jin G, et al. Evaluation of fluorescencebased thermal shift assays for hit identification in drug discovery. Anal Biochem 2004; 332: 153-159 (Pubitemid 39099482)
    • (2004) Analytical Biochemistry , vol.332 , Issue.1 , pp. 153-159
    • Lo, M.-C.1    Aulabaugh, A.2    Jin, G.3    Cowling, R.4    Bard, J.5    Malamas, M.6    Ellestad, G.7
  • 56
    • 34748876762 scopus 로고    scopus 로고
    • Structure of the Murray Valley encephalitis virus RNA helicase at 1.9 Å resolution
    • Mancini EJ, Assenberg R, Verma A, et al. Structure of the Murray Valley encephalitis virus RNA helicase at 1.9 Å resolution. Protein Sci 2007; 16: 2294-2300
    • (2007) Protein Sci , vol.16 , pp. 2294-2300
    • Mancini, E.J.1    Assenberg, R.2    Verma, A.3
  • 57
    • 34547949535 scopus 로고    scopus 로고
    • Crystal structure and activity of Kunjin virus NS3 helicase; protease and helicase domain assembly in the full-length NS3 protein
    • Mastrangelo E, Milani M, Bollati M, et al. Crystal structure and activity of Kunjin virus NS3 helicase; protease and helicase domain assembly in the full-length NS3 protein. J Mol Biol 2007; 372: 444-455
    • (2007) J Mol Biol , vol.372 , pp. 444-455
    • Mastrangelo, E.1    Milani, M.2    Bollati, M.3
  • 58
    • 38549123983 scopus 로고    scopus 로고
    • Structure and biochemical analysis of Kokobera virus helicase
    • Speroni S, De Colibus L, Mastrangelo E, et al. Structure and biochemical analysis of Kokobera virus helicase. Proteins 2007; 70: 1120-1123
    • (2007) Proteins , vol.70 , pp. 1120-1123
    • Speroni, S.1    De Colibus, L.2    Mastrangelo, E.3
  • 59
    • 0029662220 scopus 로고    scopus 로고
    • 2+-ATPase produces pumps defective in ATP binding
    • DOI 10.1074/jbc.271.42.25778
    • McIntosh DB, Wooley DG, Vilsen B, Andersen JP. Mutagenesis of segment 487Phe-Ser-Arg-Asp-Arg-Lys492 of sarcoplasmic reticulum Ca2+-ATPase produces pumps defective in ATP binding. J Biol Chem 1996; 271: 25778-25789 (Pubitemid 26347405)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.42 , pp. 25778-25789
    • McIntosh, D.B.1    Woolley, D.G.2    Vilsen, B.3    Andersen, J.P.4
  • 60
    • 0032510963 scopus 로고    scopus 로고
    • Crystal structure of RNA helicase from genotype 1b hepatitis C virus
    • Cho HS, Ha NC, Kang LW, et al. Crystal structure of RNA helicase from genotype 1b hepatitis C virus. J Biol Chem 1998; 273: 15045-15052
    • (1998) J Biol Chem , vol.273 , pp. 15045-15052
    • Cho, H.S.1    Ha, N.C.2    Kang, L.W.3
  • 62
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for multiple sequence alignments
    • Notredame C, Higgins D, Heringa J. T-Coffee: A novel method for multiple sequence alignments. J Mol Biol 2000; 302: 205-217
    • (2000) J Mol Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.2    Heringa, J.3
  • 63
    • 0031370977 scopus 로고    scopus 로고
    • LIGSITE: Automatic and efficient detection of potential small molecule-binding sites in proteins
    • DOI 10.1016/S1093-3263(98)00002-3, PII S1093326398000023
    • Hendlich M, Rippman F, Barnickel G. LIGSITE: automatic and efficient detection of potential small molecule-binding sites in proteins. J Mol Graph Model 1997; 15: 359-363 (Pubitemid 28409807)
    • (1997) Journal of Molecular Graphics and Modelling , vol.15 , Issue.6 , pp. 359-363
    • Hendlich, M.1    Rippmann, F.2    Barnickel, G.3


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