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Volumn 49, Issue 12, 2005, Pages 4834-4842

Biphenylsulfonacetic acid inhibitors of the human papillomavirus type 6 E1 helicase inhibit ATP hydrolysis by an allosteric mechanism involving tyrosine 486

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ANTIVIRUS AGENT; BIPHENYLSULFONACETIC ACID INHIBITOR; CYSTEINE; GLYCOPROTEIN E1; HELICASE; TYROSINE; UNCLASSIFIED DRUG; VIRUS ENZYME;

EID: 28844467115     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.49.12.4834-4842.2005     Document Type: Article
Times cited : (37)

References (42)
  • 1
    • 4043175756 scopus 로고    scopus 로고
    • The X-ray structure of the papillomavirus helicase in complex with its molecular matchmaker E2
    • Abbate, E. A., J. M. Berger, and M. R. Botchan. 2004. The X-ray structure of the papillomavirus helicase in complex with its molecular matchmaker E2. Genes Dev. 18:1981-1996.
    • (2004) Genes Dev. , vol.18 , pp. 1981-1996
    • Abbate, E.A.1    Berger, J.M.2    Botchan, M.R.3
  • 2
    • 14744293594 scopus 로고    scopus 로고
    • The epidemiology of human papillomavirus infections
    • Baseman, J. G., and L. A. Koutsky. 2005. The epidemiology of human papillomavirus infections. J. Clin. Virol. 32(Suppl. 1):S16-S24.
    • (2005) J. Clin. Virol. , vol.32 , Issue.SUPPL. 1
    • Baseman, J.G.1    Koutsky, L.A.2
  • 3
    • 0029073168 scopus 로고
    • Amino-terminal domains of the bovine papillomavirus type 1 E1 and E2 proteins participate in complex formation
    • Benson, J. D., and P. M. Howley. 1995. Amino-terminal domains of the bovine papillomavirus type 1 E1 and E2 proteins participate in complex formation. J. Virol. 69:4364-4372.
    • (1995) J. Virol. , vol.69 , pp. 4364-4372
    • Benson, J.D.1    Howley, P.M.2
  • 4
    • 0030971469 scopus 로고    scopus 로고
    • Functional interactions between papillomavirus E1 and E2 proteins
    • Berg, M., and A. Stenlund. 1997. Functional interactions between papillomavirus E1 and E2 proteins. J. Virol. 71:3853-3863.
    • (1997) J. Virol. , vol.71 , pp. 3853-3863
    • Berg, M.1    Stenlund, A.2
  • 5
    • 0021213168 scopus 로고
    • A common function for polyoma virus large-T and papillomavirus E1 proteins?
    • Clertant, P., and I. Seif. 1984. A common function for polyoma virus large-T and papillomavirus E1 proteins? Nature 311:276-279.
    • (1984) Nature , vol.311 , pp. 276-279
    • Clertant, P.1    Seif, I.2
  • 7
    • 0035859911 scopus 로고    scopus 로고
    • Selection and characterization of a new class of peptide exosite inhibitors of coagulation factor VIIa
    • Dennis, M. S., M. Roberge, C. Quan, and R. A. Lazarus. 2001. Selection and characterization of a new class of peptide exosite inhibitors of coagulation factor VIIa. Biochemistry 40:9513-9521.
    • (2001) Biochemistry , vol.40 , pp. 9513-9521
    • Dennis, M.S.1    Roberge, M.2    Quan, C.3    Lazarus, R.A.4
  • 9
    • 0028998313 scopus 로고
    • Identification of the primase active site of the herpes simplex virus type 1 helicase-primase
    • Dracheva, S., E. V. Koonin, and J. J. Crute. 1995. Identification of the primase active site of the herpes simplex virus type 1 helicase-primase. J. Biol. Chem. 270:14148-14153.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14148-14153
    • Dracheva, S.1    Koonin, E.V.2    Crute, J.J.3
  • 10
    • 0346731236 scopus 로고    scopus 로고
    • Discovery of small-molecule inhibitors of the ATPase activity of human papillomavirus E1 helicase
    • Faucher, A. M., P. W. White, C. Brochu, C. Grand-Maitre, J. Rancourt, and G. Fazal. 2004. Discovery of small-molecule inhibitors of the ATPase activity of human papillomavirus E1 helicase. J. Med. Chem. 47:18-21.
    • (2004) J. Med. Chem. , vol.47 , pp. 18-21
    • Faucher, A.M.1    White, P.W.2    Brochu, C.3    Grand-Maitre, C.4    Rancourt, J.5    Fazal, G.6
  • 11
    • 0033548196 scopus 로고    scopus 로고
    • Biochemical and electron microscopic image analysis of the hexameric E1 helicase
    • Fouts, E. T., X. Yu, E. H. Egelman, and M. R. Botchan. 1999. Biochemical and electron microscopic image analysis of the hexameric E1 helicase. J. Biol. Chem. 274:4447-4458.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4447-4458
    • Fouts, E.T.1    Yu, X.2    Egelman, E.H.3    Botchan, M.R.4
  • 12
    • 0028598275 scopus 로고
    • Binding of the human papillomavirus E1 origin-recognition protein is regulated through complex formation with the E2 enhancer-binding protein
    • Frattini, M. G., and L. A. Laimins. 1994. Binding of the human papillomavirus E1 origin-recognition protein is regulated through complex formation with the E2 enhancer-binding protein. Proc. Natl. Acad. Sci. USA 91:12398-12402.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12398-12402
    • Frattini, M.G.1    Laimins, L.A.2
  • 13
    • 0141758201 scopus 로고    scopus 로고
    • Helicases as antiviral drug targets
    • Frick, D. N. 2003. Helicases as antiviral drug targets. Drug News Perspect. 16:355-362.
    • (2003) Drug News Perspect. , vol.16 , pp. 355-362
    • Frick, D.N.1
  • 14
    • 4444226952 scopus 로고    scopus 로고
    • Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen
    • Gai, D., R. Zhao, D. Li, C. V. Finkielstein, and X. S. Chen. 2004. Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen. Cell 119:47-60.
    • (2004) Cell , vol.119 , pp. 47-60
    • Gai, D.1    Zhao, R.2    Li, D.3    Finkielstein, C.V.4    Chen, X.S.5
  • 15
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure-function relationships
    • Gorbalenya, A. E., and E. V. Koonin. 1993. Helicases: amino acid sequence comparisons and structure-function relationships. Curr. Opin. Struct. Biol. 3:419-429.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 16
    • 0000557446 scopus 로고    scopus 로고
    • Papillomaviridae: The viruses and their replication
    • B. N. Fields, D. M. Knipe, and P. M. Howley (ed.). Lippincott-Raven Press, Philadelphia, Pa.
    • Howley, P. M. 1996. Papillomaviridae: the viruses and their replication, p. 2045-2076. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fields virology, 3rd ed. Lippincott-Raven Press, Philadelphia, Pa.
    • (1996) Fields Virology, 3rd Ed. , pp. 2045-2076
    • Howley, P.M.1
  • 17
    • 0025885626 scopus 로고
    • Kinetic analysis of the inhibition of the epidermal growth factor receptor tyrosine kinase by Lavendustin-A and its analogue
    • Hsu, C. Y., P. E. Persons, A. P. Spada, R. A. Bednar, A. Levitzki, and A. Zilberstein. 1991. Kinetic analysis of the inhibition of the epidermal growth factor receptor tyrosine kinase by Lavendustin-A and its analogue. J. Biol. Chem. 266:21105-21112.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21105-21112
    • Hsu, C.Y.1    Persons, P.E.2    Spada, A.P.3    Bednar, R.A.4    Levitzki, A.5    Zilberstein, A.6
  • 18
    • 0013946834 scopus 로고
    • A new micromethod for the colorimetric determination of inorganic phosphate
    • Itaya, K., and M. Ui. 1966. A new micromethod for the colorimetric determination of inorganic phosphate. Clin. Chim. Acta 14:361-366.
    • (1966) Clin. Chim. Acta , vol.14 , pp. 361-366
    • Itaya, K.1    Ui, M.2
  • 19
    • 0036571335 scopus 로고    scopus 로고
    • An ATPase assay using scintillation proximity beads for high-throughput screening or kinetic analysis
    • Jeffery, J. A., J. R. Sharom, M. Fazekas, P. Rudd, E. Weichner, L. Thauvette, and P. W. White. 2002. An ATPase assay using scintillation proximity beads for high-throughput screening or kinetic analysis. Anal. Biochem. 304:55-62.
    • (2002) Anal. Biochem. , vol.304 , pp. 55-62
    • Jeffery, J.A.1    Sharom, J.R.2    Fazekas, M.3    Rudd, P.4    Weichner, E.5    Thauvette, L.6    White, P.W.7
  • 21
    • 2942618208 scopus 로고    scopus 로고
    • Pathogenesis of human papillomaviruses in differentiating epithelia
    • Longworth, M. S., and L. A. Laimins. 2004. Pathogenesis of human papillomaviruses in differentiating epithelia. Microbiol. Mol. Biol. Rev. 68:362-372.
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 362-372
    • Longworth, M.S.1    Laimins, L.A.2
  • 22
    • 0025613266 scopus 로고
    • Targeting the E1 replication protein to the papillomavirus origin of replication by complex formation with the E2 transactivator
    • Mohr, I. J., R. Clark, S. Sun, E. J. Androphy, P. MacPherson, and M. R. Botchan. 1990. Targeting the E1 replication protein to the papillomavirus origin of replication by complex formation with the E2 transactivator. Science 250:1694-1699.
    • (1990) Science , vol.250 , pp. 1694-1699
    • Mohr, I.J.1    Clark, R.2    Sun, S.3    Androphy, E.J.4    MacPherson, P.5    Botchan, M.R.6
  • 24
    • 0031716454 scopus 로고    scopus 로고
    • Molecular targets for human papillomaviruses: Prospects for antiviral therapy
    • Phelps, W. C., J. A. Barnes, and D. C. Lobe. 1998. Molecular targets for human papillomaviruses: prospects for antiviral therapy. Antivir. Chem. Chemother. 9:359-377.
    • (1998) Antivir. Chem. Chemother. , vol.9 , pp. 359-377
    • Phelps, W.C.1    Barnes, J.A.2    Lobe, D.C.3
  • 25
    • 0035859944 scopus 로고    scopus 로고
    • A novel exosite on coagulation factor VIIa and its molecular interactions with a new class of peptide inhibitors
    • Roberge, M., L. Santell, M. S. Dennis, C. Eigenbrot, M. A. Dwyer, and R. A. Lazarus. 2001. A novel exosite on coagulation factor VIIa and its molecular interactions with a new class of peptide inhibitors. Biochemistry 40:9522-9531.
    • (2001) Biochemistry , vol.40 , pp. 9522-9531
    • Roberge, M.1    Santell, L.2    Dennis, M.S.3    Eigenbrot, C.4    Dwyer, M.A.5    Lazarus, R.A.6
  • 26
    • 0032401759 scopus 로고    scopus 로고
    • Recruitment and loading of the E1 initiator protein: An ATP-dependent process catalysed by a transcription factor
    • Sanders, C. M., and A. Stenlund. 1998. Recruitment and loading of the E1 initiator protein: an ATP-dependent process catalysed by a transcription factor. EMBO J. 17:7044-7055.
    • (1998) EMBO J. , vol.17 , pp. 7044-7055
    • Sanders, C.M.1    Stenlund, A.2
  • 27
    • 0029617680 scopus 로고
    • Co-operative interaction between the initiator E1 and the transcriptional activator E2 is required for replicator specific DNA replication of bovine papillomavirus in vivo and in vitro
    • Sedman, J., and A. Stenlund. 1995. Co-operative interaction between the initiator E1 and the transcriptional activator E2 is required for replicator specific DNA replication of bovine papillomavirus in vivo and in vitro. EMBO J. 14:6218-6228.
    • (1995) EMBO J. , vol.14 , pp. 6218-6228
    • Sedman, J.1    Stenlund, A.2
  • 28
    • 0031926580 scopus 로고    scopus 로고
    • The papillomavirus E1 protein forms a DNA-dependent hexameric complex with ATPase and DNA helicase activities
    • Sedman, J., and A. Stenlund. 1998. The papillomavirus E1 protein forms a DNA-dependent hexameric complex with ATPase and DNA helicase activities. J. Virol. 72:6893-6897.
    • (1998) J. Virol. , vol.72 , pp. 6893-6897
    • Sedman, J.1    Stenlund, A.2
  • 30
    • 0027400464 scopus 로고
    • Bovine papilloma virus (BPV)-encoded E2 protein enhances binding of E1 protein to the BPV replication origin
    • Seo, Y. S., F. Muller, M. Lusky, E. Gibbs, H. Y. Kim, B. Phillips, and J. Hurwitz. 1993. Bovine papilloma virus (BPV)-encoded E2 protein enhances binding of E1 protein to the BPV replication origin. Proc. Natl. Acad. Sci. USA 90:2865-2869.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2865-2869
    • Seo, Y.S.1    Muller, F.2    Lusky, M.3    Gibbs, E.4    Kim, H.Y.5    Phillips, B.6    Hurwitz, J.7
  • 31
    • 0000882988 scopus 로고    scopus 로고
    • Papillomaviruses
    • B. N. Fields, D. M. Knipe, and P. M. Howley (ed.). Lippincott-Raven, Philadelphia, Pa.
    • Shah, K. V., and P. M. Howley. 1996. Papillomaviruses, p. 2045-2076. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fields virology. Lippincott-Raven, Philadelphia, Pa.
    • (1996) Fields Virology , pp. 2045-2076
    • Shah, K.V.1    Howley, P.M.2
  • 32
    • 0021970530 scopus 로고
    • An immunoaffinity purification procedure for SV40 large T antigen
    • Simanis, V., and D. P. Lane. 1985. An immunoaffinity purification procedure for SV40 large T antigen. Virology 144:88-100.
    • (1985) Virology , vol.144 , pp. 88-100
    • Simanis, V.1    Lane, D.P.2
  • 33
    • 0141891451 scopus 로고    scopus 로고
    • Initiation of DNA replication: Lessons from viral initiator proteins
    • Stenlund, A. 2003. Initiation of DNA replication: lessons from viral initiator proteins. Nat. Rev. Mol. Cell Biol. 4:777-785.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 777-785
    • Stenlund, A.1
  • 34
    • 7244245847 scopus 로고    scopus 로고
    • HPV proteins as targets for therapeutic intervention
    • Sterlinko, G. H., and L. Banks. 2004. HPV proteins as targets for therapeutic intervention. Antivir. Ther. 9:665-678.
    • (2004) Antivir. Ther. , vol.9 , pp. 665-678
    • Sterlinko, G.H.1    Banks, L.2
  • 35
    • 0033852428 scopus 로고    scopus 로고
    • Identification of domains of the human papillomavirus type 11 E1 helicase involved in oligomerization and binding to the viral origin
    • Titolo, S., A. Pelletier, A.-M. Pulichino, K. Brault, E. Wardrop, P. W. White, M. G. Cordingley, and J. Archambault. 2000. Identification of domains of the human papillomavirus type 11 E1 helicase involved in oligomerization and binding to the viral origin. J. Virol. 74:7349-7361.
    • (2000) J. Virol. , vol.74 , pp. 7349-7361
    • Titolo, S.1    Pelletier, A.2    Pulichino, A.-M.3    Brault, K.4    Wardrop, E.5    White, P.W.6    Cordingley, M.G.7    Archambault, J.8
  • 38
    • 0035933838 scopus 로고    scopus 로고
    • Characterization of recombinant HPV6 and 11 E1 helicases: Effect of ATP on the interaction of E1 with E2 and mapping of a minimal helicase domain
    • White, P. W., A. Pelletier, K. Brault, S. Titolo, E. Weichner, L. Thauvette, M. Fazekas, M. G. Cordingley, and J. Archambault. 2001. Characterization of recombinant HPV6 and 11 E1 helicases: effect of ATP on the interaction of E1 with E2 and mapping of a minimal helicase domain. J. Biol. Chem. 276:22426-22438.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22426-22438
    • White, P.W.1    Pelletier, A.2    Brault, K.3    Titolo, S.4    Weichner, E.5    Thauvette, L.6    Fazekas, M.7    Cordingley, M.G.8    Archambault, J.9
  • 40
    • 0035988870 scopus 로고    scopus 로고
    • Papillomavirus E1 proteins: Form, function, and features
    • Wilson, V. G., M. West, K. Woytek, and D. Rangasamy. 2002. Papillomavirus E1 proteins: form, function, and features. Virus Genes 24:275-290.
    • (2002) Virus Genes , vol.24 , pp. 275-290
    • Wilson, V.G.1    West, M.2    Woytek, K.3    Rangasamy, D.4
  • 41
    • 0028145879 scopus 로고
    • Papilloma formation by cotton-tail rabbit papillomavirus requires E1 and E2 regulatory genes in addition to E6 and E7 transforming genes
    • Wu, X., W. Xiao, and J. L. Brandsma. 1994. Papilloma formation by cotton-tail rabbit papillomavirus requires E1 and E2 regulatory genes in addition to E6 and E7 transforming genes. J. Virol. 68:6097-6102.
    • (1994) J. Virol. , vol.68 , pp. 6097-6102
    • Wu, X.1    Xiao, W.2    Brandsma, J.L.3


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