메뉴 건너뛰기




Volumn 52, Issue 36, 2013, Pages 6151-6159

Aurintricarboxylic acid modulates the affinity of hepatitis C virus NS3 helicase for both nucleic acid and ATP

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SUBSTITUTION; ATP-BINDING SITE; AURINTRICARBOXYLIC ACIDS; DIRECT INTERACTIONS; HEPATITIS C VIRUS; MICRO-CALORIMETRY; THERMODYNAMIC PARAMETER; VIRUS REPLICATION;

EID: 84884253048     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi4006495     Document Type: Article
Times cited : (35)

References (47)
  • 1
    • 54949108677 scopus 로고    scopus 로고
    • PubChem: Integrated platform of small molecules and biological activities
    • Bolton, E. E., Wang, Y., Thiessen, P. A., and Bryant, S. H. (2008) PubChem: integrated platform of small molecules and biological activities Annu. Rep. Comput. Chem. 4, 217-241
    • (2008) Annu. Rep. Comput. Chem. , vol.4 , pp. 217-241
    • Bolton, E.E.1    Wang, Y.2    Thiessen, P.A.3    Bryant, S.H.4
  • 2
    • 0015896004 scopus 로고
    • The inhibition of nucleic acid-binding proteins by aurintricarboxylic acid
    • Blumenthal, T. and Landers, T. A. (1973) The inhibition of nucleic acid-binding proteins by aurintricarboxylic acid Biochem. Biophys. Res. Commun. 55, 680-688
    • (1973) Biochem. Biophys. Res. Commun. , vol.55 , pp. 680-688
    • Blumenthal, T.1    Landers, T.A.2
  • 3
    • 75549085930 scopus 로고    scopus 로고
    • Interaction of aurintricarboxylic acid (ATA) with four nucleic acid binding proteins DNase I, RNase A, reverse transcriptase and Taq polymerase
    • Ghosh, U., Giri, K., and Bhattacharyya, N. P. (2009) Interaction of aurintricarboxylic acid (ATA) with four nucleic acid binding proteins DNase I, RNase A, reverse transcriptase and Taq polymerase Spectrochim. Acta, Part A 74, 1145-1151
    • (2009) Spectrochim. Acta, Part A , vol.74 , pp. 1145-1151
    • Ghosh, U.1    Giri, K.2    Bhattacharyya, N.P.3
  • 4
    • 0018348757 scopus 로고
    • Fractionation and structural elucidation of the active components of aurintricarboxylic acid, a potent inhibitor of protein nucleic acid interactions
    • Gonzalez, R. G., Blackburn, B. J., and Schleich, T. (1979) Fractionation and structural elucidation of the active components of aurintricarboxylic acid, a potent inhibitor of protein nucleic acid interactions Biochim. Biophys. Acta 562, 534-545
    • (1979) Biochim. Biophys. Acta , vol.562 , pp. 534-545
    • Gonzalez, R.G.1    Blackburn, B.J.2    Schleich, T.3
  • 5
    • 0027102113 scopus 로고
    • Structure investigation and anti-HIV activities of high-molecular weight ATA polymers
    • Cushman, M., Wang, P., Schols, D., and De Clercq, E. (1992) Structure investigation and anti-HIV activities of high-molecular weight ATA polymers J. Org. Chem. 57, 7241-7248
    • (1992) J. Org. Chem. , vol.57 , pp. 7241-7248
    • Cushman, M.1    Wang, P.2    Schols, D.3    De Clercq, E.4
  • 6
    • 0024432753 scopus 로고
    • Characterization and use of the potent ribonuclease inhibitor aurintricarboxylic acid for the isolation of RNA from animal tissues
    • Skidmore, A. F. and Beebee, T. J. (1989) Characterization and use of the potent ribonuclease inhibitor aurintricarboxylic acid for the isolation of RNA from animal tissues Biochem. J. 263, 73-80
    • (1989) Biochem. J. , vol.263 , pp. 73-80
    • Skidmore, A.F.1    Beebee, T.J.2
  • 7
    • 0019315381 scopus 로고
    • Mechanism of action of polymeric aurintricarboxylic acid, a potent inhibitor of protein - Nucleic acid interactions
    • Gonzalez, R. G., Haxo, R. S., and Schleich, T. (1980) Mechanism of action of polymeric aurintricarboxylic acid, a potent inhibitor of protein - nucleic acid interactions Biochemistry 19, 4299-4303
    • (1980) Biochemistry , vol.19 , pp. 4299-4303
    • Gonzalez, R.G.1    Haxo, R.S.2    Schleich, T.3
  • 9
    • 79551504928 scopus 로고    scopus 로고
    • Complementary non-radioactive assays for investigation of human flap endonuclease 1 activity
    • Dorjsuren, D., Kim, D., Maloney, D. J., Wilson, D. M., and Simeonov, A. (2011) Complementary non-radioactive assays for investigation of human flap endonuclease 1 activity Nucleic Acids Res. 39, e11
    • (2011) Nucleic Acids Res. , vol.39 , pp. 11
    • Dorjsuren, D.1    Kim, D.2    Maloney, D.J.3    Wilson, D.M.4    Simeonov, A.5
  • 13
    • 77949497846 scopus 로고    scopus 로고
    • Aurintricarboxylic acid is a potent inhibitor of influenza A and B virus neuraminidases
    • Hashem, A. M., Flaman, A. S., Farnsworth, A., Brown, E. G., Van Domselaar, G., He, R., and Li, X. (2009) Aurintricarboxylic acid is a potent inhibitor of influenza A and B virus neuraminidases PLoS One 4, e8350
    • (2009) PLoS One , vol.4 , pp. 8350
    • Hashem, A.M.1    Flaman, A.S.2    Farnsworth, A.3    Brown, E.G.4    Van Domselaar, G.5    He, R.6    Li, X.7
  • 14
    • 0028896030 scopus 로고
    • Aurintricarboxylic acid, a putative inhibitor of apoptosis, is a potent inhibitor of DNA topoisomerase II in vitro and in Chinese hamster fibrosarcoma cells
    • Benchokroun, Y., Couprie, J., and Larsen, A. K. (1995) Aurintricarboxylic acid, a putative inhibitor of apoptosis, is a potent inhibitor of DNA topoisomerase II in vitro and in Chinese hamster fibrosarcoma cells Biochem. Pharmacol. 49, 305-313
    • (1995) Biochem. Pharmacol. , vol.49 , pp. 305-313
    • Benchokroun, Y.1    Couprie, J.2    Larsen, A.K.3
  • 15
    • 0031982630 scopus 로고    scopus 로고
    • Activation of the Jak2-Stat5 signaling pathway in Nb2 lymphoma cells by an anti-apoptotic agent, aurintricarboxylic acid
    • Rui, H., Xu, J., Mehta, S., Fang, H., Williams, J., Dong, F., and Grimley, P. M. (1998) Activation of the Jak2-Stat5 signaling pathway in Nb2 lymphoma cells by an anti-apoptotic agent, aurintricarboxylic acid J. Biol. Chem. 273, 28-32
    • (1998) J. Biol. Chem. , vol.273 , pp. 28-32
    • Rui, H.1    Xu, J.2    Mehta, S.3    Fang, H.4    Williams, J.5    Dong, F.6    Grimley, P.M.7
  • 16
    • 0024514303 scopus 로고
    • Aurintricarboxylic acid is a potent inhibitor of phosphofructokinase
    • McCune, S. A., Foe, L. G., Kemp, R. G., and Jurin, R. R. (1989) Aurintricarboxylic acid is a potent inhibitor of phosphofructokinase Biochem. J. 259, 925-927
    • (1989) Biochem. J. , vol.259 , pp. 925-927
    • McCune, S.A.1    Foe, L.G.2    Kemp, R.G.3    Jurin, R.R.4
  • 17
    • 0036085386 scopus 로고    scopus 로고
    • Aurintricarboxylic acid protects against cell death caused by lipopolysaccharide in macrophages by decreasing inducible nitric-oxide synthase induction via IkappaB kinase, extracellular signal-regulated kinase, and p38 mitogen-activated protein kinase inhibition
    • Tsi, C. J., Chao, Y., Chen, C. W., and Lin, W. W. (2002) Aurintricarboxylic acid protects against cell death caused by lipopolysaccharide in macrophages by decreasing inducible nitric-oxide synthase induction via IkappaB kinase, extracellular signal-regulated kinase, and p38 mitogen-activated protein kinase inhibition Mol. Pharmacol. 62, 90-101
    • (2002) Mol. Pharmacol. , vol.62 , pp. 90-101
    • Tsi, C.J.1    Chao, Y.2    Chen, C.W.3    Lin, W.W.4
  • 18
    • 1842846611 scopus 로고    scopus 로고
    • Inhibition of cytokine-induced JAK-STAT signalling pathways by an endonuclease inhibitor aurintricarboxylic acid
    • Chen, C. W., Chao, Y., Chang, Y. H., Hsu, M. J., and Lin, W. W. (2002) Inhibition of cytokine-induced JAK-STAT signalling pathways by an endonuclease inhibitor aurintricarboxylic acid Br. J. Pharmacol. 137, 1011-1020
    • (2002) Br. J. Pharmacol. , vol.137 , pp. 1011-1020
    • Chen, C.W.1    Chao, Y.2    Chang, Y.H.3    Hsu, M.J.4    Lin, W.W.5
  • 19
    • 0029970903 scopus 로고    scopus 로고
    • The helicase activity associated with hepatitis C virus nonstructural protein 3 (NS3)
    • Tai, C. L., Chi, W. K., Chen, D. S., and Hwang, L. H. (1996) The helicase activity associated with hepatitis C virus nonstructural protein 3 (NS3) J. Virol. 70, 8477-8484
    • (1996) J. Virol. , vol.70 , pp. 8477-8484
    • Tai, C.L.1    Chi, W.K.2    Chen, D.S.3    Hwang, L.H.4
  • 23
    • 0346463036 scopus 로고    scopus 로고
    • The nonstructural protein 3 protease/helicase requires an intact protease domain to unwind duplex RNA efficiently
    • Frick, D. N., Rypma, R. S., Lam, A. M., and Gu, B. (2004) The nonstructural protein 3 protease/helicase requires an intact protease domain to unwind duplex RNA efficiently J. Biol. Chem. 279, 1269-1280
    • (2004) J. Biol. Chem. , vol.279 , pp. 1269-1280
    • Frick, D.N.1    Rypma, R.S.2    Lam, A.M.3    Gu, B.4
  • 24
    • 57649217269 scopus 로고    scopus 로고
    • Hepatitis C viral NS3-4A protease activity is enhanced by the NS3 helicase
    • Beran, R. K. and Pyle, A. M. (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
  • 26
    • 0032518490 scopus 로고    scopus 로고
    • Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: The crystal structure provides insights into the mode of unwinding
    • Kim, J. L., Morgenstern, K. A., Griffith, J. P., Dwyer, M. D., Thomson, J. A., Murcko, M. A., Lin, C., and Caron, P. R. (1998) Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding Structure 6, 89-100
    • (1998) Structure , vol.6 , pp. 89-100
    • Kim, J.L.1    Morgenstern, K.A.2    Griffith, J.P.3    Dwyer, M.D.4    Thomson, J.A.5    Murcko, M.A.6    Lin, C.7    Caron, P.R.8
  • 27
    • 20444440763 scopus 로고    scopus 로고
    • A Brownian motor mechanism of translocation and strand separation by hepatitis C virus helicase
    • Levin, M. K., Gurjar, M., and Patel, S. S. (2005) A Brownian motor mechanism of translocation and strand separation by hepatitis C virus helicase Nat. Struct. Mol. Biol. 12, 429-435
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 429-435
    • Levin, M.K.1    Gurjar, M.2    Patel, S.S.3
  • 28
    • 0038607629 scopus 로고    scopus 로고
    • ATP binding modulates the nucleic acid affinity of hepatitis C virus helicase
    • Levin, M. K., Gurjar, M. M., and Patel, S. S. (2003) ATP binding modulates the nucleic acid affinity of hepatitis C virus helicase J. Biol. Chem. 278, 23311-23316
    • (2003) J. Biol. Chem. , vol.278 , pp. 23311-23316
    • Levin, M.K.1    Gurjar, M.M.2    Patel, S.S.3
  • 29
    • 76249111702 scopus 로고    scopus 로고
    • Three conformational snapshots of the hepatitis C virus NS3 helicase reveal a ratchet translocation mechanism
    • Gu, M. and Rice, C. M. (2010) Three conformational snapshots of the hepatitis C virus NS3 helicase reveal a ratchet translocation mechanism Proc. Natl. Acad. Sci. U. S. A. 107, 521-528
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 521-528
    • Gu, M.1    Rice, C.M.2
  • 31
    • 77749289804 scopus 로고    scopus 로고
    • Mechanism and specificity of a symmetrical benzimidazolephenylcarboxamide helicase inhibitor
    • Belon, C. A., High, Y. D., Lin, T. I., Pauwels, F., and Frick, D. N. (2010) Mechanism and specificity of a symmetrical benzimidazolephenylcarboxamide helicase inhibitor Biochemistry 49, 1822-1832
    • (2010) Biochemistry , vol.49 , pp. 1822-1832
    • Belon, C.A.1    High, Y.D.2    Lin, T.I.3    Pauwels, F.4    Frick, D.N.5
  • 32
    • 33845771358 scopus 로고    scopus 로고
    • Role of divalent metal cations in ATP hydrolysis catalyzed by the hepatitis C virus NS3 helicase: Magnesium provides a bridge for ATP to fuel unwinding
    • Frick, D. N., Banik, S., and Rypma, R. S. (2007) Role of divalent metal cations in ATP hydrolysis catalyzed by the hepatitis C virus NS3 helicase: magnesium provides a bridge for ATP to fuel unwinding J. Mol. Biol. 365, 1017-1032
    • (2007) J. Mol. Biol. , vol.365 , pp. 1017-1032
    • Frick, D.N.1    Banik, S.2    Rypma, R.S.3
  • 33
    • 6044262451 scopus 로고    scopus 로고
    • Electrostatic analysis of the hepatitis C virus NS3 helicase reveals both active and allosteric site locations
    • Frick, D. N., Rypma, R. S., Lam, A. M., and Frenz, C. M. (2004) Electrostatic analysis of the hepatitis C virus NS3 helicase reveals both active and allosteric site locations Nucleic Acids Res. 32, 5519-5528
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5519-5528
    • Frick, D.N.1    Rypma, R.S.2    Lam, A.M.3    Frenz, C.M.4
  • 34
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50% inhibition (I50) of an enzymatic reaction
    • Cheng, Y. and Prusoff, W. H. (1973) Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50% inhibition (I50) of an enzymatic reaction Biochem. Pharmacol. 22, 3099-3108
    • (1973) Biochem. Pharmacol. , vol.22 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2
  • 37
    • 84895070518 scopus 로고    scopus 로고
    • Modulation of the hepatitis C virus NS3 helicase activity by divalent metal cations
    • Frick, D. N., Banik, S., and Rypma, R. S. (2006) Modulation of the hepatitis C virus NS3 helicase activity by divalent metal cations Hepatology 44, 342A-342A
    • (2006) Hepatology , vol.44
    • Frick, D.N.1    Banik, S.2    Rypma, R.S.3
  • 38
    • 0027199917 scopus 로고
    • Hepatitis C virus NS3 protein polynucleotide-stimulated nucleoside triphosphatase and comparison with the related pestivirus and flavivirus enzymes
    • Suzich, J. A., Tamura, J. K., Palmer-Hill, F., Warrener, P., Grakoui, A., Rice, C. M., Feinstone, S. M., and Collett, M. S. (1993) Hepatitis C virus NS3 protein polynucleotide-stimulated nucleoside triphosphatase and comparison with the related pestivirus and flavivirus enzymes J. Virol. 67, 6152-6158
    • (1993) J. Virol. , vol.67 , pp. 6152-6158
    • Suzich, J.A.1    Tamura, J.K.2    Palmer-Hill, F.3    Warrener, P.4    Grakoui, A.5    Rice, C.M.6    Feinstone, S.M.7    Collett, M.S.8
  • 39
    • 0037377763 scopus 로고    scopus 로고
    • Hepatitis C virus NS3 ATPases/helicases from different genotypes exhibit variations in enzymatic properties
    • Lam, A. M., Keeney, D., Eckert, P. Q., and Frick, D. N. (2003) Hepatitis C virus NS3 ATPases/helicases from different genotypes exhibit variations in enzymatic properties J. Virol. 77, 3950-3961
    • (2003) J. Virol. , vol.77 , pp. 3950-3961
    • Lam, A.M.1    Keeney, D.2    Eckert, P.Q.3    Frick, D.N.4
  • 40
    • 0345293146 scopus 로고    scopus 로고
    • On the value of c: Can low affinity systems be studied by isothermal titration calorimetry?
    • Turnbull, W. B. and Daranas, A. H. (2003) On the value of c: can low affinity systems be studied by isothermal titration calorimetry? J. Am. Chem. Soc. 125, 14859-14866
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14859-14866
    • Turnbull, W.B.1    Daranas, A.H.2
  • 41
    • 0029784485 scopus 로고    scopus 로고
    • A steady-state and pre-steady-state kinetic analysis of the NTPase activity associated with the hepatitis C virus NS3 helicase domain
    • Preugschat, F., Averett, D. R., Clarke, B. E., and Porter, D. J. (1996) A steady-state and pre-steady-state kinetic analysis of the NTPase activity associated with the hepatitis C virus NS3 helicase domain J. Biol. Chem. 271, 24449-24457
    • (1996) J. Biol. Chem. , vol.271 , pp. 24449-24457
    • Preugschat, F.1    Averett, D.R.2    Clarke, B.E.3    Porter, D.J.4
  • 43
    • 0032510963 scopus 로고    scopus 로고
    • Crystal structure of RNA helicase from genotype 1b hepatitis C virus. A feasible mechanism of unwinding duplex RNA
    • Cho, H. S., Ha, N. C., Kang, L. W., Chung, K. M., Back, S. H., Jang, S. K., and Oh, B. H. (1998) Crystal structure of RNA helicase from genotype 1b hepatitis C virus. A feasible mechanism of unwinding duplex RNA J. Biol. Chem. 273, 15045-15052
    • (1998) J. Biol. Chem. , vol.273 , pp. 15045-15052
    • Cho, H.S.1    Ha, N.C.2    Kang, L.W.3    Chung, K.M.4    Back, S.H.5    Jang, S.K.6    Oh, B.H.7
  • 47
    • 0026063679 scopus 로고
    • Preparation and anti-HIV activities of aurintricarboxylic acid fractions and analogues: Direct correlation of antiviral potency with molecular weight
    • Cushman, M., Wang, P. L., Chang, S. H., Wild, C., De Clercq, E., Schols, D., Goldman, M. E., and Bowen, J. A. (1991) Preparation and anti-HIV activities of aurintricarboxylic acid fractions and analogues: direct correlation of antiviral potency with molecular weight J. Med. Chem. 34, 329-337
    • (1991) J. Med. Chem. , vol.34 , pp. 329-337
    • Cushman, M.1    Wang, P.L.2    Chang, S.H.3    Wild, C.4    De Clercq, E.5    Schols, D.6    Goldman, M.E.7    Bowen, J.A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.