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Volumn 291, Issue 19, 2016, Pages 10078-10088

Hydrogen/Deuterium Exchange Kinetics Demonstrate Long Range 7 Effects of Thumb Site 2 Inhibitors of Hepatitis C Viral RNA-dependent RNA Polymerase

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; ELONGATION; ENZYMES; HYDROGEN; KINETICS;

EID: 84966340081     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.708370     Document Type: Article
Times cited : (23)

References (38)
  • 1
    • 84857144025 scopus 로고    scopus 로고
    • The increasing burden of mortality from viral hepatitis in the United States between 1999 and 2007
    • Ly, K. N., Xing, J., Klevens, R. M., Jiles, R. B., Ward, J. W., and Holmberg, S. D. (2012) The increasing burden of mortality from viral hepatitis in the United States between 1999 and 2007. Ann. Intern. Med. 156, 271-278
    • (2012) Ann. Intern. Med , vol.156 , pp. 271-278
    • Ly, K.N.1    Xing, J.2    Klevens, R.M.3    Jiles, R.B.4    Ward, J.W.5    Holmberg, S.D.6
  • 2
    • 84944390503 scopus 로고    scopus 로고
    • Hepatitis c virus treatment: Is it possible to cure all hepatitis c virus patients? Clin
    • Muir, A. J., and Naggie, S. (2015) Hepatitis C virus treatment: is it possible to cure all hepatitis C virus patients? Clin. Gastroenterol. Hepatol. 13, 2166-2172
    • (2015) Gastroenterol. Hepatol , vol.13 , pp. 2166-2172
    • Muir, A.J.1    Naggie, S.2
  • 3
    • 0032876683 scopus 로고    scopus 로고
    • Crystal structure of the RNA-dependent RNA polymerase from hepatitis c virus reveals a fully encircled active site
    • Lesburg, C. A., Cable, M. B., Ferrari, E., Hong, Z., Mannarino, A. F., and Weber, P. C. (1999) Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site. Nat. Struct. Biol. 6, 937-943
    • (1999) Nat. Struct. Biol , vol.6 , pp. 937-943
    • Lesburg, C.A.1    Cable, M.B.2    Ferrari, E.3    Hong, Z.4    Mannarino, A.F.5    Weber, P.C.6
  • 8
    • 84858973676 scopus 로고    scopus 로고
    • Assembly, purification, and pre-steady-state kinetic analysis of active RNA-dependent RNA polymerase elongation complex
    • Jin, Z., Leveque, V., Ma, H., Johnson, K. A., and Klumpp, K. (2012) Assembly, purification, and pre-steady-state kinetic analysis of active RNA-dependent RNA polymerase elongation complex. J. Biol. Chem. 287, 10674-10683
    • (2012) J. Biol. Chem. , vol.287 , pp. 10674-10683
    • Jin, Z.1    Leveque, V.2    Ma, H.3    Johnson, K.A.4    Klumpp, K.5
  • 9
    • 0028925773 scopus 로고
    • Mechanism of inhibition of HIV-1 reverse transcriptase by nonnucleoside inhibitors
    • Spence, R. A., Kati, W. M., Anderson, K. S., and Johnson, K. A. (1995) Mechanism of inhibition of HIV-1 reverse transcriptase by nonnucleoside inhibitors. Science 267, 988-993
    • (1995) Science , vol.267 , pp. 988-993
    • Spence, R.A.1    Kati, W.M.2    Anderson, K.S.3    Johnson, K.A.4
  • 10
    • 82555170294 scopus 로고    scopus 로고
    • An objective assessment of conformational variability in complexes of hepatitis c virus polymerase with non-nucleoside inhibitors
    • Caillet-Saguy, C., Simister, P. C., and Bressanelli, S. (2011) An objective assessment of conformational variability in complexes of hepatitis C virus polymerase with non-nucleoside inhibitors. J. Mol. Biol. 414, 370-384
    • (2011) J. Mol. Biol. , vol.414 , pp. 370-384
    • Caillet-Saguy, C.1    Simister, P.C.2    Bressanelli, S.3
  • 11
    • 84965165070 scopus 로고    scopus 로고
    • Thumb site 2 inhibitors of hepatitis c viral RNA-dependent RNA polymerase allosterically block the transition from initiation to elongation
    • Li, J., and Johnson, K. A. (2016) Thumb Site 2 Inhibitors of Hepatitis C viral RNA-dependent RNA polymerase allosterically block the transition from initiation to elongation. J. Biol. Chem. 291,
    • (2016) J. Biol. Chem , vol.291
    • Li, J.1    Johnson, K.A.2
  • 12
    • 77957770064 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange reveals distinct agonist/partial agonist receptor dynamics within Vitamin D receptor/retinoid x receptor heterodimer
    • Zhang, J., Chalmers, M. J., Stayrook, K. R., Burris, L. L., Garcia-Ordonez, R. D., Pascal, B. D., Burris, T. P., Dodge, J. A., and Griffin, P. R. (2010) Hydrogen/deuterium exchange reveals distinct agonist/partial agonist receptor dynamics within vitamin D receptor/retinoid X receptor heterodimer. Structure 18, 1332-1341
    • (2010) Structure , vol.18 , pp. 1332-1341
    • Zhang, J.1    Chalmers, M.J.2    Stayrook, K.R.3    Burris, L.L.4    Garcia-Ordonez, R.D.5    Pascal, B.D.6    Burris, T.P.7    Dodge, J.A.8    Griffin, P.R.9
  • 13
    • 80054081804 scopus 로고    scopus 로고
    • Ligand-dependent perturbation of the conformational ensemble for the gpcr β2 adrenergic receptor revealed by hdx
    • West, G. M., Chien, E. Y., Katritch, V., Gatchalian, J., Chalmers, M. J., Stevens, R. C., and Griffin, P. R. (2011) Ligand-dependent perturbation of the conformational ensemble for the GPCR β2 adrenergic receptor revealed by HDX. Structure 19, 1424-1432
    • (2011) Structure , vol.19 , pp. 1424-1432
    • West, G.M.1    Chien, E.Y.2    Katritch, V.3    Gatchalian, J.4    Chalmers, M.J.5    Stevens, R.C.6    Griffin, P.R.7
  • 14
    • 78651233149 scopus 로고    scopus 로고
    • Allosteric suppression of HIV-1 reverse transcriptase structural dynamics upon inhibitor binding
    • Seckler, J. M., Barkley, M. D., and Wintrode, P. L. (2011) Allosteric suppression of HIV-1 reverse transcriptase structural dynamics upon inhibitor binding. Biophys. J. 100, 144-153
    • (2011) Biophys J. , vol.100 , pp. 144-153
    • Seckler, J.M.1    Barkley, M.D.2    Wintrode, P.L.3
  • 16
    • 33847061197 scopus 로고    scopus 로고
    • Networks for the allosteric control of protein kinases
    • Shi, Z., Resing, K. A., and Ahn, N. G. (2006) Networks for the allosteric control of protein kinases. Curr. Opin. Struct. Biol. 16, 686-692
    • (2006) Curr. Opin. Struct. Biol , vol.16 , pp. 686-692
    • Shi, Z.1    Resing, K.A.2    Ahn, N.G.3
  • 18
    • 84945393213 scopus 로고    scopus 로고
    • Subtle dynamic changes accompany hck activation by HIV-1 Nef and are reversed by an antiretroviral kinase inhibitor
    • Wales, T. E., Hochrein, J. M., Morgan, C. R., Emert-Sedlak, L. A., Smith-gall, T. E., and Engen, J. R. (2015) Subtle dynamic changes accompany hck activation by HIV-1 Nef and are reversed by an antiretroviral kinase inhibitor. Biochemistry 54, 6382-6391
    • (2015) Biochemistry , vol.54 , pp. 6382-6391
    • Wales, T.E.1    Hochrein, J.M.2    Morgan, C.R.3    Emert-Sedlak, L.A.4    Smith-Gall, T.E.5    Engen, J.R.6
  • 20
    • 79954547968 scopus 로고    scopus 로고
    • The utility of hydrogen/deuterium exchange mass spectrometry in biopharmaceutical comparability studies
    • Houde, D., Berkowitz, S. A., and Engen, J. R. (2011) The utility of hydrogen/deuterium exchange mass spectrometry in biopharmaceutical comparability studies. J. Pharm. Sci. 100, 2071-2086
    • (2011) J. Pharm. Sci. , vol.100 , pp. 2071-2086
    • Houde, D.1    Berkowitz, S.A.2    Engen, J.R.3
  • 21
    • 84890532160 scopus 로고    scopus 로고
    • Analysis of overlapped and noisy hydrogen/deuterium exchange mass spectra
    • Guttman, M., Weis, D. D., Engen, J. R., and Lee, K. K. (2013) Analysis of overlapped and noisy hydrogen/deuterium exchange mass spectra. J. Am. Soc. Mass Spectrom. 24, 1906-1912
    • (2013) J. Am. Soc. Mass Spectrom. , vol.24 , pp. 1906-1912
    • Guttman, M.1    Weis, D.D.2    Engen, J.R.3    Lee, K.K.4
  • 22
    • 68849132703 scopus 로고    scopus 로고
    • Solution structural dynamics of HIV-1 reverse transcriptase heterodimer
    • Seckler, J. M., Howard, K. J., Barkley, M. D., and Wintrode, P. L. (2009) Solution structural dynamics of HIV-1 reverse transcriptase heterodimer. Biochemistry 48, 7646-7655
    • (2009) Biochemistry , vol.48 , pp. 7646-7655
    • Seckler, J.M.1    Howard, K.J.2    Barkley, M.D.3    Wintrode, P.L.4
  • 23
  • 26
    • 84893922355 scopus 로고    scopus 로고
    • Molecular modeling and residue interaction network studies on the mechanism of binding and resistance of the HCV NS5B polymerase mutants to VX-222 and ANA598
    • Xue, W., Jiao, P., Liu, H., and Yao, X. (2014) Molecular modeling and residue interaction network studies on the mechanism of binding and resistance of the HCV NS5B polymerase mutants to VX-222 and ANA598. Antiviral Res. 104, 40-51
    • (2014) Antiviral Res , vol.104 , pp. 40-51
    • Xue, W.1    Jiao, P.2    Liu, H.3    Yao, X.4
  • 28
    • 84921657223 scopus 로고    scopus 로고
    • Hydrophobic and charged residues in the c-terminal arm of hepatitis c virus RNA-dependent RNA polymerase regulate initiation and elongation
    • Cherry, A. L., Dennis, C. A., Baron, A., Eisele, L. E., Thommes, P. A., and Jaeger, J. (2015) Hydrophobic and charged residues in the C-terminal arm of hepatitis C virus RNA-dependent RNA polymerase regulate initiation and elongation. J. Virol. 89, 2052-2063
    • (2015) J. Virol. , vol.89 , pp. 2052-2063
    • Cherry, A.L.1    Dennis, C.A.2    Baron, A.3    Eisele, L.E.4    Thommes, P.A.5    Jaeger, J.6
  • 29
    • 0030696119 scopus 로고    scopus 로고
    • Identification and localization of slow, natural, cooperative unfolding in the hematopoietic cell kinase SH3 domain by amide hydrogen exchange and mass spectrometry
    • Engen, J. R., Smithgall, T. E., Gmeiner, W. H., and Smith, D. L. (1997) Identification and localization of slow, natural, cooperative unfolding in the hematopoietic cell kinase SH3 domain by amide hydrogen exchange and mass spectrometry. Biochemistry 36, 14384-14391
    • (1997) Biochemistry , vol.36 , pp. 14384-14391
    • Engen, J.R.1    Smithgall, T.E.2    Gmeiner, W.H.3    Smith, D.L.4
  • 30
    • 84873050231 scopus 로고    scopus 로고
    • Resolution of the interaction mechanisms and characteristics of non-nucleoside inhibitors of hepatitis C virus polymerase
    • Winquist, J., Abdurakhmanov, E., Baraznenok, V., Henderson, I., Vrang, L., and Danielson, U. H. (2013) Resolution of the interaction mechanisms and characteristics of non-nucleoside inhibitors of hepatitis C virus polymerase. Antiviral Res. 97, 356-368
    • (2013) Antiviral Res , vol.97 , pp. 356-368
    • Winquist, J.1    Abdurakhmanov, E.2    Baraznenok, V.3    Henderson, I.4    Vrang, L.5    Danielson, U.H.6
  • 31
    • 75749148378 scopus 로고    scopus 로고
    • Investigating solution-phase protein structure and dynamics by hydrogen exchange mass spectrometry
    • ps1706s58
    • Morgan, C. R., and Engen, J. R. (2009) Investigating solution-phase protein structure and dynamics by hydrogen exchange mass spectrometry. Curr. Protoc. Protein Sci. 10.1002/0471140864.ps1706s58
    • (2009) Curr. Protoc. Protein Sci.
    • Morgan, C.R.1    Engen, J.R.2
  • 32
    • 84939817161 scopus 로고    scopus 로고
    • How amide hydrogens exchange in native proteins
    • Persson, F., and Halle, B. (2015) How amide hydrogens exchange in native proteins. Proc. Natl. Acad. Sci. U.S.A. 112, 10383-10388
    • (2015) Proc. Natl. Acad. Sci. U. S. A , vol.112 , pp. 10383-10388
    • Persson, F.1    Halle, B.2
  • 35
    • 0035919073 scopus 로고    scopus 로고
    • A novel mechanism to ensure terminal initiation by hepatitis C virus NS5B polymerase
    • Hong, Z., Cameron, C. E., Walker, M. P., Castro, C., Yao, N., Lau, J. Y., and Zhong, W. (2001) A novel mechanism to ensure terminal initiation by hepatitis C virus NS5B polymerase. Virology 285, 6-11
    • (2001) Virology , vol.285 , pp. 6-11
    • Hong, Z.1    Cameron, C.E.2    Walker, M.P.3    Castro, C.4    Yao, N.5    Lau, J.Y.6    Zhong, W.7
  • 37
    • 84871094298 scopus 로고    scopus 로고
    • Thumb inhibitor binding eliminates functionally important dynamics in the hepatitis C virus RNA polymerase
    • Davis, B. C., and Thorpe, I. F. (2013) Thumb inhibitor binding eliminates functionally important dynamics in the hepatitis C virus RNA polymerase. Proteins 81, 40-52
    • (2013) Proteins , vol.81 , pp. 40-52
    • Davis, B.C.1    Thorpe, I.F.2


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