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Volumn 156, Issue 2, 2011, Pages 313-318

The acidic sequence of the NS4A cofactor regulates ATP hydrolysis by the HCV NS3 helicase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CARRIER PROTEIN; HYBRID PROTEIN; NS3 PROTEIN, HEPATITIS C VIRUS; NS4A COFACTOR PEPTIDE, HEPATITIS C VIRUS; PRIMER DNA; RNA HELICASE; VIRUS PROTEIN;

EID: 79551542771     PISSN: 03048608     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00705-010-0838-2     Document Type: Article
Times cited : (8)

References (18)
  • 1
    • 34250681358 scopus 로고    scopus 로고
    • Hepatitis C virus proteins
    • Dubuisson J (2007) Hepatitis C virus proteins. World J Gastroenterol 13: 2406-2415.
    • (2007) World J Gastroenterol , vol.13 , pp. 2406-2415
    • Dubuisson, J.1
  • 2
    • 30144436268 scopus 로고    scopus 로고
    • RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP
    • Dumont S, Cheng W, Serebrov V, Beran RK, Tinoco I, Pyle AM, Bustamante C (2006) RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP. Nature 439: 105-108.
    • (2006) Nature , vol.439 , pp. 105-108
    • Dumont, S.1    Cheng, W.2    Serebrov, V.3    Beran, R.K.4    Tinoco, I.5    Pyle, A.M.6    Bustamante, C.7
  • 4
    • 34247625945 scopus 로고    scopus 로고
    • Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold
    • Aleshin AE, Shiryaev SA, Strongin AY, Liddington RC (2007) Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold. Protein Sci 16: 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
  • 6
    • 57149088067 scopus 로고    scopus 로고
    • Molecular targets for flavivirus drug discovery
    • Sampath A, Padmanabhan R (2009) Molecular targets for flavivirus drug discovery. Antiviral Res 81: 6-15.
    • (2009) Antiviral Res , vol.81 , pp. 6-15
    • Sampath, A.1    Padmanabhan, R.2
  • 8
    • 0033571623 scopus 로고    scopus 로고
    • Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase
    • Yao N, Reichert P, Taremi SS, Prosise WW, Weber PC (1999) Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase. Structure 7: 1353-1363.
    • (1999) Structure , vol.7 , pp. 1353-1363
    • Yao, N.1    Reichert, P.2    Taremi, S.S.3    Prosise, W.W.4    Weber, P.C.5
  • 9
    • 57649217269 scopus 로고    scopus 로고
    • Hepatitis C viral NS3-4A protease activity is enhanced by the NS3 helicase
    • Beran RK, Pyle AM (2008) Hepatitis C viral NS3-4A protease activity is enhanced by the NS3 helicase. J Biol Chem 283: 29929-29937.
    • (2008) J Biol Chem , vol.283 , pp. 29929-29937
    • Beran, R.K.1    Pyle, A.M.2
  • 10
    • 70349337005 scopus 로고    scopus 로고
    • NS4A regulates the ATPase activity of the NS3 helicase: a novel cofactor role of the non-structural protein NS4A from West Nile virus
    • Shiryaev SA, Chernov AV, Aleshin AE, Shiryaeva TN, Strongin AY (2009) NS4A regulates the ATPase activity of the NS3 helicase: a novel cofactor role of the non-structural protein NS4A from West Nile virus. J Gen Virol 90: 2081-2085.
    • (2009) J Gen Virol , vol.90 , pp. 2081-2085
    • Shiryaev, S.A.1    Chernov, A.V.2    Aleshin, A.E.3    Shiryaeva, T.N.4    Strongin, A.Y.5
  • 11
    • 63149134943 scopus 로고    scopus 로고
    • The NS4A protein of hepatitis C virus promotes RNA-coupled ATP hydrolysis by the NS3 helicase
    • Beran RK, Lindenbach BD, Pyle AM (2009) The NS4A protein of hepatitis C virus promotes RNA-coupled ATP hydrolysis by the NS3 helicase. J Virol 83: 3268-3275.
    • (2009) J Virol , vol.83 , pp. 3268-3275
    • Beran, R.K.1    Lindenbach, B.D.2    Pyle, A.M.3
  • 13
    • 15444371665 scopus 로고    scopus 로고
    • Multiple full-length NS3 molecules are required for optimal unwinding of oligonucleotide DNA in vitro
    • Tackett AJ, Chen Y, Cameron CE, Raney KD (2005) Multiple full-length NS3 molecules are required for optimal unwinding of oligonucleotide DNA in vitro. J Biol Chem 280: 10797-10806.
    • (2005) J Biol Chem , vol.280 , pp. 10797-10806
    • Tackett, A.J.1    Chen, Y.2    Cameron, C.E.3    Raney, K.D.4
  • 14
    • 33645645084 scopus 로고    scopus 로고
    • Structural and biological identification of residues on the surface of NS3 helicase required for optimal replication of the hepatitis C virus
    • Mackintosh SG, Lu JZ, Jordan JB, Harrison MK, Sikora B, Sharma SD, Cameron CE, Raney KD, Sakon J (2006) Structural and biological identification of residues on the surface of NS3 helicase required for optimal replication of the hepatitis C virus. J Biol Chem 281: 3528-3535.
    • (2006) J Biol Chem , vol.281 , pp. 3528-3535
    • Mackintosh, S.G.1    Lu, J.Z.2    Jordan, J.B.3    Harrison, M.K.4    Sikora, B.5    Sharma, S.D.6    Cameron, C.E.7    Raney, K.D.8    Sakon, J.9
  • 15
    • 23244464646 scopus 로고    scopus 로고
    • Structure of the Dengue virus helicase/nucleoside triphosphatase catalytic domain at a resolution of 2.4 A
    • Xu T, Sampath A, Chao A, Wen D, Nanao M, Chene P, Vasudevan SG, Lescar J (2005) Structure of the Dengue virus helicase/nucleoside triphosphatase catalytic domain at a resolution of 2. 4 A. J Virol 79: 10278-10288.
    • (2005) J Virol , vol.79 , pp. 10278-10288
    • Xu, T.1    Sampath, A.2    Chao, A.3    Wen, D.4    Nanao, M.5    Chene, P.6    Vasudevan, S.G.7    Lescar, J.8
  • 16
    • 37349023165 scopus 로고    scopus 로고
    • Crystal structure of the NS3 protease-helicase from dengue virus
    • Luo D, Xu T, Hunke C, Gruber G, Vasudevan SG, Lescar J (2008) Crystal structure of the NS3 protease-helicase from dengue virus. J Virol 82: 173-183.
    • (2008) J Virol , vol.82 , pp. 173-183
    • Luo, D.1    Xu, T.2    Hunke, C.3    Gruber, G.4    Vasudevan, S.G.5    Lescar, J.6
  • 17
    • 72849147739 scopus 로고    scopus 로고
    • Crystal structure of a novel conformational state of the flavivirus NS3 protein: implications for polyprotein processing and viral replication
    • Assenberg R, Mastrangelo E, Walter TS, Verma A, Milani M, Owens RJ, Stuart DI, Grimes JM, Mancini EJ (2009) Crystal structure of a novel conformational state of the flavivirus NS3 protein: implications for polyprotein processing and viral replication. J Virol 83: 12895-12906.
    • (2009) J Virol , vol.83 , pp. 12895-12906
    • Assenberg, R.1    Mastrangelo, E.2    Walter, T.S.3    Verma, A.4    Milani, M.5    Owens, R.J.6    Stuart, D.I.7    Grimes, J.M.8    Mancini, E.J.9
  • 18
    • 33646167045 scopus 로고    scopus 로고
    • Regulated cleavages at the West Nile virus NS4A-2K-NS4B junctions play a major role in rearranging cytoplasmic membranes and Golgi trafficking of the NS4A protein
    • Roosendaal J, Westaway EG, Khromykh A, Mackenzie JM (2006) Regulated cleavages at the West Nile virus NS4A-2K-NS4B junctions play a major role in rearranging cytoplasmic membranes and Golgi trafficking of the NS4A protein. J Virol 80: 4623-4632.
    • (2006) J Virol , vol.80 , pp. 4623-4632
    • Roosendaal, J.1    Westaway, E.G.2    Khromykh, A.3    Mackenzie, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.