메뉴 건너뛰기




Volumn 475, Issue , 2015, Pages 46-55

Structural characterization of the HSP70 interaction domain of the hepatitis C viral protein NS5A

Author keywords

HCV; HSP70; IRES; NS5A; Peptide; Protein binding

Indexed keywords

HEAT SHOCK PROTEIN 70; NONSTRUCTURAL PROTEIN 5A; PHENYLALANINE; SYNTHETIC PEPTIDE; TYROSINE; VALINE; NS-5 PROTEIN, HEPATITIS C VIRUS; VIRUS PROTEIN;

EID: 84911881810     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2014.10.011     Document Type: Article
Times cited : (13)

References (36)
  • 2
    • 0009447935 scopus 로고    scopus 로고
    • University of Texas Medical Branch at Galveston, Galveston, TX
    • Baron S. Medical Microbiology 1996, University of Texas Medical Branch at Galveston, Galveston, TX. 4th ed.
    • (1996) Medical Microbiology
    • Baron, S.1
  • 3
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler D.M., Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 1986, 25:469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 4
    • 0037140752 scopus 로고    scopus 로고
    • Stacking and T-shape competition in aromatic-aromatic amino acid interactions
    • Chelli R., Gervasio F.L., Procacci P., Schettino V. Stacking and T-shape competition in aromatic-aromatic amino acid interactions. J. Am. Chem. Soc. 2002, 124:6133-6143.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 6133-6143
    • Chelli, R.1    Gervasio, F.L.2    Procacci, P.3    Schettino, V.4
  • 5
    • 79751513059 scopus 로고    scopus 로고
    • Hepatitis in 2010: the dawn of a new era in HCV therapy
    • Ciesek S., Manns M.P. Hepatitis in 2010: the dawn of a new era in HCV therapy. Nat. Rev. Gastroenterol. Hepatol. 2011, 8:69-71.
    • (2011) Nat. Rev. Gastroenterol. Hepatol. , vol.8 , pp. 69-71
    • Ciesek, S.1    Manns, M.P.2
  • 6
    • 0021430848 scopus 로고
    • Vibrational analysis of peptides, polypeptides, and proteins. XVIII. Conformational sensitivity of the alpha-helix spectrum: alpha I- and alpha II-poly(l-alanine)
    • Dwivedi A.M., Krimm S. Vibrational analysis of peptides, polypeptides, and proteins. XVIII. Conformational sensitivity of the alpha-helix spectrum: alpha I- and alpha II-poly(l-alanine). Biopolymers 1984, 23:923-943.
    • (1984) Biopolymers , vol.23 , pp. 923-943
    • Dwivedi, A.M.1    Krimm, S.2
  • 7
    • 0036841697 scopus 로고    scopus 로고
    • Hepatocellular carcinoma: an epidemiologic view
    • El-Serag H.B. Hepatocellular carcinoma: an epidemiologic view. J. Clin. Gastroenterol. 2002, 35:S72-S78.
    • (2002) J. Clin. Gastroenterol. , vol.35 , pp. S72-S78
    • El-Serag, H.B.1
  • 8
    • 0025232814 scopus 로고
    • Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids
    • Fields G.B., Noble R.L. Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int. J. Pept. Protein Res. 1990, 35:161-214.
    • (1990) Int. J. Pept. Protein Res. , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 10
    • 0037371766 scopus 로고    scopus 로고
    • The regulation of hepatitis C virus (HCV) internal ribosome-entry site-mediated translation by HCV replicons and nonstructural proteins
    • He Y., Yan W., Coito C., Li Y., Gale M., Katze M.G. The regulation of hepatitis C virus (HCV) internal ribosome-entry site-mediated translation by HCV replicons and nonstructural proteins. J. Gen. Virol. 2003, 84:535-543.
    • (2003) J. Gen. Virol. , vol.84 , pp. 535-543
    • He, Y.1    Yan, W.2    Coito, C.3    Li, Y.4    Gale, M.5    Katze, M.G.6
  • 11
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B., Kutzner C., van der Spoel D., Lindahl E. GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 2008, 4:435-447.
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 12
    • 67649197727 scopus 로고    scopus 로고
    • Domain III of NS5A contributes to both RNA replication and assembly of hepatitis C virus particles
    • Hughes M., Griffin S., Harris M. Domain III of NS5A contributes to both RNA replication and assembly of hepatitis C virus particles. J. Gen. Virol. 2009, 90:1329-1334.
    • (2009) J. Gen. Virol. , vol.90 , pp. 1329-1334
    • Hughes, M.1    Griffin, S.2    Harris, M.3
  • 13
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983, 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 17
    • 0033550299 scopus 로고    scopus 로고
    • Salt bridge stability in monomeric proteins
    • Kumar S., Nussinov R. Salt bridge stability in monomeric proteins. J. Mol. Biol. 1999, 293:1241-1255.
    • (1999) J. Mol. Biol. , vol.293 , pp. 1241-1255
    • Kumar, S.1    Nussinov, R.2
  • 19
    • 84859817677 scopus 로고    scopus 로고
    • Nonstructural 5A protein of hepatitis C virus regulates heat shock protein 72 for its own propagation
    • Lim Y.S., Shin K.S., Oh S.H., Kang S.M., Won S.J., Hwang S.B. Nonstructural 5A protein of hepatitis C virus regulates heat shock protein 72 for its own propagation. J. Viral Hepat. 2012, 19:353-363.
    • (2012) J. Viral Hepat. , vol.19 , pp. 353-363
    • Lim, Y.S.1    Shin, K.S.2    Oh, S.H.3    Kang, S.M.4    Won, S.J.5    Hwang, S.B.6
  • 20
    • 23944476834 scopus 로고    scopus 로고
    • Unravelling hepatitis C virus replication from genome to function
    • Lindenbach B.D., Rice C.M. Unravelling hepatitis C virus replication from genome to function. Nature 2005, 436:933-938.
    • (2005) Nature , vol.436 , pp. 933-938
    • Lindenbach, B.D.1    Rice, C.M.2
  • 21
    • 66149115122 scopus 로고    scopus 로고
    • Crystal structure of a novel dimeric form of NS5A domain I protein from hepatitis C virus
    • Love R.A., Brodsky O., Hickey M.J., Wells P.A., Cronin C.N. Crystal structure of a novel dimeric form of NS5A domain I protein from hepatitis C virus. J. Virol. 2009, 83:4395-4403.
    • (2009) J. Virol. , vol.83 , pp. 4395-4403
    • Love, R.A.1    Brodsky, O.2    Hickey, M.J.3    Wells, P.A.4    Cronin, C.N.5
  • 22
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: cellular functions and molecular mechanism
    • Mayer M.P., Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci. 2005, 62:670-684.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 23
    • 0032546782 scopus 로고    scopus 로고
    • Pi-Stacking interactions. Alive and well in proteins
    • McGaughey G.B., Gagne M., Rappe A.K. pi-Stacking interactions. Alive and well in proteins. J. Biol. Chem. 1998, 273:15458-15463.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15458-15463
    • McGaughey, G.B.1    Gagne, M.2    Rappe, A.K.3
  • 25
    • 77951901108 scopus 로고    scopus 로고
    • Insights into the biology of IRES elements through riboproteomic approaches
    • Pacheco A., Martinez-Salas E. Insights into the biology of IRES elements through riboproteomic approaches. J. Biomed. Biotechnol. 2010, 2010:458927.
    • (2010) J. Biomed. Biotechnol. , vol.2010 , pp. 458927
    • Pacheco, A.1    Martinez-Salas, E.2
  • 26
    • 68949117729 scopus 로고    scopus 로고
    • The heat shock cognate protein 70 is associated with hepatitis C virus particles and modulates virus infectivity
    • Parent R., Qu X., Petit M.A., Beretta L. The heat shock cognate protein 70 is associated with hepatitis C virus particles and modulates virus infectivity. Hepatology 2009, 49:1798-1809.
    • (2009) Hepatology , vol.49 , pp. 1798-1809
    • Parent, R.1    Qu, X.2    Petit, M.A.3    Beretta, L.4
  • 27
    • 23944506014 scopus 로고    scopus 로고
    • Global epidemiology of hepatitis C virus infection
    • Shepard C.W., Finelli L., Alter M.J. Global epidemiology of hepatitis C virus infection. Lancet Infect. Dis. 2005, 5:558-567.
    • (2005) Lancet Infect. Dis. , vol.5 , pp. 558-567
    • Shepard, C.W.1    Finelli, L.2    Alter, M.J.3
  • 29
    • 0001345210 scopus 로고
    • Isotopically enhanced infrared spectroscopy: a novel method for examining secondary structure at specific sites in conformationally heterogeneous peptides
    • Tadesse L., Nazarbaghi R., Walters L. Isotopically enhanced infrared spectroscopy: a novel method for examining secondary structure at specific sites in conformationally heterogeneous peptides. J. Am. Chem. Soc. 1991, 113:7036-7037.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 7036-7037
    • Tadesse, L.1    Nazarbaghi, R.2    Walters, L.3
  • 30
    • 38349162328 scopus 로고    scopus 로고
    • Identification of residues required for RNA replication in domains II and III of the hepatitis C virus NS5A protein
    • Tellinghuisen T.L., Foss K.L., Treadaway J.C., Rice C.M. Identification of residues required for RNA replication in domains II and III of the hepatitis C virus NS5A protein. J. Virol. 2008, 82:1073-1083.
    • (2008) J. Virol. , vol.82 , pp. 1073-1083
    • Tellinghuisen, T.L.1    Foss, K.L.2    Treadaway, J.C.3    Rice, C.M.4
  • 31
    • 19644393931 scopus 로고    scopus 로고
    • Structure of the zinc-binding domain of an essential component of the hepatitis C virus replicase
    • Tellinghuisen T.L., Marcotrigiano J., Rice C.M. Structure of the zinc-binding domain of an essential component of the hepatitis C virus replicase. Nature 2005, 435:374-379.
    • (2005) Nature , vol.435 , pp. 374-379
    • Tellinghuisen, T.L.1    Marcotrigiano, J.2    Rice, C.M.3
  • 32
    • 0031719703 scopus 로고    scopus 로고
    • Constitutive overexpression of the major inducible 70kDa heat shock protein mediates large plaque formation by measles virus
    • Vasconcelos D.Y., Cai X.H., Oglesbee M.J. Constitutive overexpression of the major inducible 70kDa heat shock protein mediates large plaque formation by measles virus. J. Gen. Virol. 1998, 79(Pt 9):2239-2247.
    • (1998) J. Gen. Virol. , vol.79 , pp. 2239-2247
    • Vasconcelos, D.Y.1    Cai, X.H.2    Oglesbee, M.J.3
  • 33
    • 0027153210 scopus 로고
    • Translation of human hepatitis C virus RNA in cultured cells is mediated by an internal ribosome-binding mechanism
    • Wang C., Sarnow P., Siddiqui A. Translation of human hepatitis C virus RNA in cultured cells is mediated by an internal ribosome-binding mechanism. J. Virol. 1993, 67:3338-3344.
    • (1993) J. Virol. , vol.67 , pp. 3338-3344
    • Wang, C.1    Sarnow, P.2    Siddiqui, A.3
  • 34
    • 38849105568 scopus 로고    scopus 로고
    • The heat shock protein 70 cochaperone YDJ1 is required for efficient membrane-specific flock house virus RNA replication complex assembly and function in Saccharomyces cerevisiae
    • Weeks S.A., Miller D.J. The heat shock protein 70 cochaperone YDJ1 is required for efficient membrane-specific flock house virus RNA replication complex assembly and function in Saccharomyces cerevisiae. J. Virol. 2008, 82:2004-2012.
    • (2008) J. Virol. , vol.82 , pp. 2004-2012
    • Weeks, S.A.1    Miller, D.J.2
  • 35
    • 84878307910 scopus 로고    scopus 로고
    • Bacterial microcompartment shells of diverse functional types possess pentameric vertex proteins
    • Wheatley N.M., Gidaniyan S.D., Liu Y., Cascio D., Yeates T.O. Bacterial microcompartment shells of diverse functional types possess pentameric vertex proteins. Protein Sci. 2013, 22:660-665.
    • (2013) Protein Sci. , vol.22 , pp. 660-665
    • Wheatley, N.M.1    Gidaniyan, S.D.2    Liu, Y.3    Cascio, D.4    Yeates, T.O.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.