메뉴 건너뛰기




Volumn 88, Issue 1, 2014, Pages 628-642

Hepatitis C virus RNA replication and virus particle assembly require specific dimerization of the NS4A protein transmembrane domain

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPHORIN A; NONSTRUCTURAL PROTEIN 4A; VIRUS DNA; VIRUS RNA;

EID: 84890873172     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02052-13     Document Type: Article
Times cited : (21)

References (115)
  • 1
    • 84973436381 scopus 로고    scopus 로고
    • Flaviviridae
    • In Knipe DM, Howley PM (ed),6th ed, vol . Lippincott Williams & Wilkins, Philadelphia, PA
    • Lindenbach BD, Murray CL, Thiel HJ, Rice CM. 2013. Flaviviridae, p 712-746. In Knipe DM, Howley PM (ed), Fields virology, 6th ed, vol 1. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2013) Fields virology , vol.1 , pp. 712-746
    • Lindenbach, B.D.1    Murray, C.L.2    Thiel, H.J.3    Rice, C.M.4
  • 3
    • 84855544169 scopus 로고    scopus 로고
    • An updated analysis of hepatitisCvirus genotypes and subtypes based on the complete coding region
    • Nakano T, Lau GM, Lau GM, Sugiyama M, Mizokami M. 2012. An updated analysis of hepatitisCvirus genotypes and subtypes based on the complete coding region. Liver Int. 32:339-345. http://dx.doi.org/10 .1111/j.1478-3231.2011.02684.x.
    • (2012) Liver Int. , vol.32 , pp. 339-345
    • Nakano, T.1    Lau, G.M.2    Lau, G.M.3    Sugiyama, M.4    Mizokami, M.5
  • 4
    • 11144246127 scopus 로고    scopus 로고
    • Novel insights into hepatitis C virus replication and persistence
    • Bartenschlager R, Frese M, Pietschmann T. 2004. Novel insights into hepatitis C virus replication and persistence. Adv. Virus Res. 63:71-180. http://dx.doi.org/10.1016/S0065-3527(04)63002-8.
    • (2004) Adv. Virus Res. , vol.63 , pp. 71-180
    • Bartenschlager, R.1    Frese, M.2    Pietschmann, T.3
  • 5
    • 0028831056 scopus 로고
    • Hepatitis C virus-encoded nonstructural protein NS4A has versatile functions in viral protein processing
    • Tanji Y, Hijikata M, Satoh S, Kaneko T, Shimotohno K. 1995. Hepatitis C virus-encoded nonstructural protein NS4A has versatile functions in viral protein processing. J. Virol. 69:1575-1581.
    • (1995) J. Virol. , vol.69 , pp. 1575-1581
    • Tanji, Y.1    Hijikata, M.2    Satoh, S.3    Kaneko, T.4    Shimotohno, K.5
  • 6
    • 0242456017 scopus 로고    scopus 로고
    • Subcellular localization, stability, and transcleavage competence of the hepatitis C virus NS3-NS4A complex expressed in tetracycline-regulated cell lines
    • Wölk B, Sansonno D, Kräusslich HG, Dammacco F, Rice CM, Blum HE, Moradpour D. 2000. Subcellular localization, stability, and transcleavage competence of the hepatitis C virus NS3-NS4A complex expressed in tetracycline-regulated cell lines. J. Virol. 74:2293-2304. http: //dx.doi.org/10.1128/JVI.74.5.2293-2304.2000.
    • (2000) J. Virol. , vol.74 , pp. 2293-2304
    • Wölk, B.1    Sansonno, D.2    Kräusslich, H.G.3    Dammacco, F.4    Rice, C.M.5    Blum, H.E.6    Moradpour, D.7
  • 7
    • 19944386940 scopus 로고    scopus 로고
    • Characterization of nonstructural protein membrane anchor deletion mutants expressed in the context of the hepatitis C virus polyprotein
    • Gosert R, Jendrsczok W, Berke JM, Brass V, Blum HE, Moradpour D. 2005. Characterization of nonstructural protein membrane anchor deletion mutants expressed in the context of the hepatitis C virus polyprotein. J. Virol. 79:7911-7917. http://dx.doi.org/10.1128/JVI.79.12.7911 -7917.2005.
    • (2005) J. Virol. , vol.79 , pp. 7911-7917
    • Gosert, R.1    Jendrsczok, W.2    Berke, J.M.3    Brass, V.4    Blum, H.E.5    Moradpour, D.6
  • 8
    • 55749102288 scopus 로고    scopus 로고
    • Structural determinants for membrane association and dynamic organization of the hepatitis C virus NS3-4A complex
    • Brass V, Berke JM, Montserret R, Blum HE, Penin F, Moradpour D. 2008. Structural determinants for membrane association and dynamic organization of the hepatitis C virus NS3-4A complex. Proc. Natl. Acad. Sci. U. S. A. 105:14545-14550. http://dx.doi.org/10.1073/pnas.0807298105.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 14545-14550
    • Brass, V.1    Berke, J.M.2    Montserret, R.3    Blum, H.E.4    Penin, F.5    Moradpour, D.6
  • 9
    • 0028290579 scopus 로고
    • Both NS3 and NS4A are required for proteolytic processing of hepatitis C virus nonstructural proteins
    • Failla C, Tomei L, De Francesco R. 1994. Both NS3 and NS4A are required for proteolytic processing of hepatitis C virus nonstructural proteins. J. Virol. 68:3753-3760.
    • (1994) J. Virol. , vol.68 , pp. 3753-3760
    • Failla, C.1    Tomei, L.2    De Francesco, R.3
  • 10
    • 0029074519 scopus 로고
    • A central region in the hepatitis C virus NS4A protein allows formation of an active NS3-NS4A serine proteinase complex in vivo and in vitro
    • Lin C, Thomson JA, Rice CM. 1995. A central region in the hepatitis C virus NS4A protein allows formation of an active NS3-NS4A serine proteinase complex in vivo and in vitro. J. Virol. 69:4373-4380.
    • (1995) J. Virol. , vol.69 , pp. 4373-4380
    • Lin, C.1    Thomson, J.A.2    Rice, C.M.3
  • 13
    • 0031060172 scopus 로고    scopus 로고
    • The N-terminal region of hepatitis C virus-encoded NS5A is important for NS4A-dependent phosphorylation
    • Asabe SI, Tanji Y, Satoh S, Kaneko T, Kimura K, Shimotohno K. 1997. The N-terminal region of hepatitis C virus-encoded NS5A is important for NS4A-dependent phosphorylation. J. Virol. 71:790-796.
    • (1997) J. Virol. , vol.71 , pp. 790-796
    • Asabe, S.I.1    Tanji, Y.2    Satoh, S.3    Kaneko, T.4    Kimura, K.5    Shimotohno, K.6
  • 14
    • 34548188701 scopus 로고    scopus 로고
    • The C terminus of hepatitis C virus NS4A encodes an electrostatic switch that regulates NS5A hyperphosphorylation and viral replication
    • Lindenbach BD, Prágai BM, Montserret R, Beran RK, Pyle AM, Penin F, Rice CM. 2007. The C terminus of hepatitis C virus NS4A encodes an electrostatic switch that regulates NS5A hyperphosphorylation and viral replication. J. Virol. 81:8905-8918. http://dx.doi.org/10.1128/JVI.00937-07.
    • (2007) J. Virol. , vol.81 , pp. 8905-8918
    • Lindenbach, B.D.1    Prágai, B.M.2    Montserret, R.3    Beran, R.K.4    Pyle, A.M.5    Penin, F.6    Rice, C.M.7
  • 15
    • 78651399012 scopus 로고    scopus 로고
    • The acidic domain of hepatitis C virus NS4A contributes to RNA replication and virus particle assembly
    • Phan T, Kohlway A, Dimberu P, Pyle AM, Lindenbach BD. 2011. The acidic domain of hepatitis C virus NS4A contributes to RNA replication and virus particle assembly. J. Virol. 85:1193-1204. http://dx.doi.org/10 .1128/JVI.01889-10.
    • (2011) J. Virol. , vol.85 , pp. 1193-1204
    • Phan, T.1    Kohlway, A.2    Dimberu, P.3    Pyle, A.M.4    Lindenbach, B.D.5
  • 16
    • 0030860853 scopus 로고    scopus 로고
    • The hepatitis C virus NS4A protein: interactions with the NS4B and NS5A proteins
    • Lin C, Wu JW, Hsiao K, Su MS. 1997. The hepatitis C virus NS4A protein: interactions with the NS4B and NS5A proteins. J. Virol. 71: 6465-6471.
    • (1997) J. Virol. , vol.71 , pp. 6465-6471
    • Lin, C.1    Wu, J.W.2    Hsiao, K.3    Su, M.S.4
  • 18
    • 78951472458 scopus 로고    scopus 로고
    • Hepatitis C virus NS2 coordinates virus particle assembly through physical interactions with the E1-E2 glycoprotein and NS3-NS4A enzyme complexes
    • Stapleford KA, Lindenbach BD. 2011. Hepatitis C virus NS2 coordinates virus particle assembly through physical interactions with the E1-E2 glycoprotein and NS3-NS4A enzyme complexes. J. Virol. 85: 1706-1717. http://dx.doi.org/10.1128/JVI.02268-10.
    • (2011) J. Virol. , vol.85 , pp. 1706-1717
    • Stapleford, K.A.1    Lindenbach, B.D.2
  • 19
    • 0032489233 scopus 로고    scopus 로고
    • Complex formation of NS5B with NS3 and NS4A proteins of hepatitis C virus
    • Ishido S, Fujita T, Hotta H. 1998. Complex formation of NS5B with NS3 and NS4A proteins of hepatitis C virus. Biochem. Biophys. Res. Commun. 244:35-40. http://dx.doi.org/10.1006/bbrc.1998.8202.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 35-40
    • Ishido, S.1    Fujita, T.2    Hotta, H.3
  • 20
    • 0036891628 scopus 로고    scopus 로고
    • Inhibition of protein synthesis by the nonstructural proteins NS4A and NS4B of hepatitis C virus
    • Florese RH, Nagano-Fujii M, Iwanaga Y, Hidajat R, Hotta H. 2002. Inhibition of protein synthesis by the nonstructural proteins NS4A and NS4B of hepatitis C virus. Virus Res. 90:119-131. http://dx.doi.org/10 .1016/S0168-1702(02)00146-6.
    • (2002) Virus Res. , vol.90 , pp. 119-131
    • Florese, R.H.1    Nagano-Fujii, M.2    Iwanaga, Y.3    Hidajat, R.4    Hotta, H.5
  • 21
    • 0036139053 scopus 로고    scopus 로고
    • Hepatitis C virus NS4A and NS4B proteins suppress translation in vivo
    • Kato J, Kato N, Yoshida H, Ono-Nita SK, Shiratori Y, Omata M. 2002. Hepatitis C virus NS4A and NS4B proteins suppress translation in vivo. J. Med. Virol. 66:187-199. http://dx.doi.org/10.1002/jmv.2129.
    • (2002) J. Med. Virol. , vol.66 , pp. 187-199
    • Kato, J.1    Kato, N.2    Yoshida, H.3    Ono-Nita, S.K.4    Shiratori, Y.5    Omata, M.6
  • 22
    • 33845433207 scopus 로고    scopus 로고
    • Hepatitis C virus NS4A inhibits cap-dependent and the viral IRES-mediated translation through interacting with eukaryotic elongation factor 1A
    • Kou YH, Chou SM, Wang YM, Chang YT, Huang SY, Jung MY, Huang YH, Chen MR, Chang MF, Chang SC. 2006. Hepatitis C virus NS4A inhibits cap-dependent and the viral IRES-mediated translation through interacting with eukaryotic elongation factor 1A. J. Biomed. Sci. 13:861-874. http://dx.doi.org/10.1007/s11373-006-9104-8.
    • (2006) J. Biomed. Sci. , vol.13 , pp. 861-874
    • Kou, Y.H.1    Chou, S.M.2    Wang, Y.M.3    Chang, Y.T.4    Huang, S.Y.5    Jung, M.Y.6    Huang, Y.H.7    Chen, M.R.8    Chang, M.F.9    Chang, S.C.10
  • 23
    • 14544280209 scopus 로고    scopus 로고
    • Immune evasion by hepatitis C virus NS3/4A protease-mediated cleavage of the Toll-like receptor 3 adaptor protein TRIF
    • Li K, Foy E, Ferreon JC, Nakamura M, Ferreon AC, Ikeda M, Ray SC, Gale M, Jr, Lemon SM. 2005. Immune evasion by hepatitis C virus NS3/4A protease-mediated cleavage of the Toll-like receptor 3 adaptor protein TRIF. Proc. Natl. Acad. Sci. U. S. A. 102:2992-2997. http://dx.doi .org/10.1073/pnas.0408824102.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 2992-2997
    • Li, K.1    Foy, E.2    Ferreon, J.C.3    Nakamura, M.4    Ferreon, A.C.5    Ikeda, M.6    Ray, S.C.7    Gale, M.8    Lemon, S.M.9
  • 24
    • 27144440476 scopus 로고    scopus 로고
    • Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
    • Meylan E, Curran J, Hofmann K, Moradpour D, Binder M, Bartenschlager R, Tschopp J. 2005. Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature 437:1167- 1172. http://dx.doi.org/10.1038/nature04193.
    • (2005) Nature , vol.437
    • Meylan, E.1    Curran, J.2    Hofmann, K.3    Moradpour, D.4    Binder, M.5    Bartenschlager, R.6    Tschopp, J.7
  • 25
    • 38049184252 scopus 로고    scopus 로고
    • Regulation of innate immunity against hepatitis C virus infection
    • Saito T, Gale M, Jr. 2008. Regulation of innate immunity against hepatitis C virus infection. Hepatol. Res. 38:115-122.
    • (2008) Hepatol. Res. , vol.38 , pp. 115-122
    • Saito, T.1    Gale, M.2
  • 27
    • 0037404536 scopus 로고    scopus 로고
    • Protein-protein interactions between hepatitis C virus nonstructural proteins
    • Dimitrova M, Imbert I, Kieny MP, Schuster C. 2003. Protein-protein interactions between hepatitis C virus nonstructural proteins. J. Virol. 77:5401-5414. http://dx.doi.org/10.1128/JVI.77.9.5401-5414.2003.
    • (2003) J. Virol. , vol.77 , pp. 5401-5414
    • Dimitrova, M.1    Imbert, I.2    Kieny, M.P.3    Schuster, C.4
  • 30
    • 0032876683 scopus 로고    scopus 로고
    • Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site
    • Lesburg CA, Cable MB, Ferrari E, Hong Z, Mannarino AF, Weber PC. 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. http://dx.doi.org/10.1038/13305.
    • (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
  • 31
    • 19644393931 scopus 로고    scopus 로고
    • Structure of the zinc-binding domain of an essential component of the hepatitis C virus replicase
    • Tellinghuisen TL, Marcotrigiano J, Rice CM. 2005. Structure of the zinc-binding domain of an essential component of the hepatitis C virus replicase. Nature 435:374-379. http://dx.doi.org/10.1038/nature03580.
    • (2005) Nature , vol.435 , pp. 374-379
    • Tellinghuisen, T.L.1    Marcotrigiano, J.2    Rice, C.M.3
  • 32
    • 66149115122 scopus 로고    scopus 로고
    • Crystal structure of a novel dimeric form of NS5A domain I protein from hepatitisCvirus
    • Love RA, Brodsky O, Hickey MJ, Wells PA, Cronin CN. 2009. Crystal structure of a novel dimeric form of NS5A domain I protein from hepatitisCvirus. J. Virol. 83:4395-4403. http://dx.doi.org/10.1128/JVI.02352 -08.
    • (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
  • 34
    • 0036100578 scopus 로고    scopus 로고
    • Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex
    • Egger D, Wölk B, Gosert R, Bianchi L, Blum HE, Moradpour D, Bienz K. 2002. Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex. J. Virol. 76: 5974-5984. http://dx.doi.org/10.1128/JVI.76.12.5974-5984.2002.
    • (2002) J. Virol. , vol.76 , pp. 5974-5984
    • Egger, D.1    Wölk, B.2    Gosert, R.3    Bianchi, L.4    Blum, H.E.5    Moradpour, D.6    Bienz, K.7
  • 35
    • 0345144016 scopus 로고    scopus 로고
    • Identification of the hepatitis C virus RNA replication complex in Huh-7 cells harboring subgenomic replicons
    • Gosert R, Egger D, Lohmann V, Bartenschlager R, Blum HE, Bienz K, Moradpour D. 2003. Identification of the hepatitis C virus RNA replication complex in Huh-7 cells harboring subgenomic replicons. J. Virol. 77:5487-5492. http://dx.doi.org/10.1128/JVI.77.9.5487-5492.2003.
    • (2003) J. Virol. , vol.77 , pp. 5487-5492
    • Gosert, R.1    Egger, D.2    Lohmann, V.3    Bartenschlager, R.4    Blum, H.E.5    Bienz, K.6    Moradpour, D.7
  • 36
    • 27144513392 scopus 로고    scopus 로고
    • Quantitative analysis of the hepatitis C virus replication complex
    • Quinkert D, Bartenschlager R, Lohmann V. 2005. Quantitative analysis of the hepatitis C virus replication complex. J. Virol. 79:13594-13605. http://dx.doi.org/10.1128/JVI.79.21.13594-13605.2005.
    • (2005) J. Virol. , vol.79 , pp. 13594-13605
    • Quinkert, D.1    Bartenschlager, R.2    Lohmann, V.3
  • 37
    • 77957957374 scopus 로고    scopus 로고
    • Hepatitis C virus RNA replication requires a conserved structural motif within the transmembrane domain of the NS5B RNAdependent RNA polymerase
    • Brass V, Gouttenoire J, Wahl A, Pal Z, Blum HE, Penin F, Moradpour D. 2010. Hepatitis C virus RNA replication requires a conserved structural motif within the transmembrane domain of the NS5B RNAdependent RNA polymerase. J. Virol. 84:11580-11584. http://dx.doi.org /10.1128/JVI.01519-10.
    • (2010) J. Virol. , vol.84 , pp. 11580-11584
    • Brass, V.1    Gouttenoire, J.2    Wahl, A.3    Pal, Z.4    Blum, H.E.5    Penin, F.6    Moradpour, D.7
  • 38
    • 0037474296 scopus 로고    scopus 로고
    • GALLEX, a measurement of heterologous association of transmembrane helices in a biological membrane
    • Schneider D, Engelman DM. 2003. GALLEX, a measurement of heterologous association of transmembrane helices in a biological membrane. J. Biol. Chem. 278:3105-3111. http://dx.doi.org/10.1074/jbc.M206287200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3105-3111
    • Schneider, D.1    Engelman, D.M.2
  • 39
    • 5144227144 scopus 로고    scopus 로고
    • Motifs of two small residues can assist but are not sufficient to mediate transmembrane helix interactions
    • Schneider D, Engelman DM. 2004. Motifs of two small residues can assist but are not sufficient to mediate transmembrane helix interactions. J. Mol. Biol. 343:799-804. http://dx.doi.org/10.1016/j.jmb.2004.08.083.
    • (2004) J. Mol. Biol. , vol.343 , pp. 799-804
    • Schneider, D.1    Engelman, D.M.2
  • 40
    • 33646078118 scopus 로고    scopus 로고
    • The stability of transmembrane helix interactions measured in a biological membrane
    • Finger C, Volkmer T, Prodohl A, Otzen DE, Engelman DM, Schneider D. 2006. The stability of transmembrane helix interactions measured in a biological membrane. J. Mol. Biol. 358:1221-1228. http://dx.doi.org /10.1016/j.jmb.2006.02.065.
    • (2006) J. Mol. Biol. , vol.358 , pp. 1221-1228
    • Finger, C.1    Volkmer, T.2    Prodohl, A.3    Otzen, D.E.4    Engelman, D.M.5    Schneider, D.6
  • 41
    • 0031908629 scopus 로고    scopus 로고
    • A new LexA-based genetic system for monitoring and analyzing protein heterodimerization in Escherichia coli
    • Dmitrova M, Younes-Cauet G, Oertel-Buchheit P, Porte D, Schnarr M, Granger-Schnarr M. 1998. A new LexA-based genetic system for monitoring and analyzing protein heterodimerization in Escherichia coli. Mol. Gen. Genet. 257:205-212. http://dx.doi.org/10.1007 /s004380050640.
    • (1998) Mol. Gen. Genet. , vol.257 , pp. 205-212
    • Dmitrova, M.1    Younes-Cauet, G.2    Oertel-Buchheit, P.3    Porte, D.4    Schnarr, M.5    Granger-Schnarr, M.6
  • 42
    • 0029143698 scopus 로고
    • Fos leucine zipper variants with increased association capacity
    • Porte D, Oertel-Buchheit P, Granger-Schnarr M, Schnarr M. 1995. Fos leucine zipper variants with increased association capacity. J. Biol. Chem. 270:22721-22730. http://dx.doi.org/10.1074/jbc.270.39.22721.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22721-22730
    • Porte, D.1    Oertel-Buchheit, P.2    Granger-Schnarr, M.3    Schnarr, M.4
  • 43
    • 0033514311 scopus 로고    scopus 로고
    • TOXCAT: a measure of transmembrane helix association in a biological membrane
    • Russ WP, Engelman DM. 1999. TOXCAT: a measure of transmembrane helix association in a biological membrane. Proc. Natl. Acad. Sci. U. S. A. 96:863-868. http://dx.doi.org/10.1073/pnas.96.3.863.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 863-868
    • Russ, W.P.1    Engelman, D.M.2
  • 44
    • 0029115282 scopus 로고
    • Membrane insertion of the bacterial signal transduction protein ToxR and requirements of transcription activation studied by modular replacement of different protein substructures
    • Kolmar H, Hennecke F, Gotze K, Janzer B, Vogt B, Mayer F, Fritz HJ. 1995. Membrane insertion of the bacterial signal transduction protein ToxR and requirements of transcription activation studied by modular replacement of different protein substructures. EMBO J. 14:3895-3904.
    • (1995) EMBO J. , vol.14 , pp. 3895-3904
    • Kolmar, H.1    Hennecke, F.2    Gotze, K.3    Janzer, B.4    Vogt, B.5    Mayer, F.6    Fritz, H.J.7
  • 45
    • 0028951388 scopus 로고
    • Analysis of Vibrio cholerae ToxR function by construction of novel fusion proteins
    • Ottemann KM, Mekalanos JJ. 1995. Analysis of Vibrio cholerae ToxR function by construction of novel fusion proteins. Mol. Microbiol. 15: 719-731.
    • (1995) Mol. Microbiol. , vol.15 , pp. 719-731
    • Ottemann, K.M.1    Mekalanos, J.J.2
  • 46
    • 0030575833 scopus 로고    scopus 로고
    • Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator
    • Langosch D, Brosig B, Kolmar H, Fritz HJ. 1996. Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator. J. Mol. Biol. 263:525-530. http://dx.doi .org/10.1006/jmbi.1996.0595.
    • (1996) J. Mol. Biol. , vol.263 , pp. 525-530
    • Langosch, D.1    Brosig, B.2    Kolmar, H.3    Fritz, H.J.4
  • 47
    • 0030059639 scopus 로고    scopus 로고
    • The ToxR protein of Vibrio cholerae forms homodimers and heterodimers
    • Ottemann KM, Mekalanos JJ. 1996. The ToxR protein of Vibrio cholerae forms homodimers and heterodimers. J. Bacteriol. 178:156-162.
    • (1996) J. Bacteriol. , vol.178 , pp. 156-162
    • Ottemann, K.M.1    Mekalanos, J.J.2
  • 48
    • 80054762434 scopus 로고    scopus 로고
    • Multi-Tox: application of the ToxRtranscriptional reporter assay to the study of multi-pass protein transmembrane domain oligomerization
    • Joce C, Wiener AA, Yin H. 2011. Multi-Tox: application of the ToxRtranscriptional reporter assay to the study of multi-pass protein transmembrane domain oligomerization. Biochim. Biophys. Acta 1808: 2948-2953. http://dx.doi.org/10.1016/j.bbamem.2011.07.008.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2948-2953
    • Joce, C.1    Wiener, A.A.2    Yin, H.3
  • 49
    • 0017251379 scopus 로고
    • Subunit structure of human erythrocyte glycophorin A
    • Furthmayr H, Marchesi VT. 1976. Subunit structure of human erythrocyte glycophorin A. Biochemistry 15:1137-1144. http://dx.doi.org/10 .1021/bi00650a028.
    • (1976) Biochemistry , vol.15 , pp. 1137-1144
    • Furthmayr, H.1    Marchesi, V.T.2
  • 50
    • 0027050182 scopus 로고
    • Sequence specificity in the dimerization of transmembrane alpha-helices
    • Lemmon MA, Flanagan JM, Treutlein HR, Zhang J, Engelman DM. 1992. Sequence specificity in the dimerization of transmembrane alpha-helices. Biochemistry 31:12719-12725. http://dx.doi.org/10.1021/bi00166a002.
    • (1992) Biochemistry , vol.31 , pp. 12719-12725
    • Lemmon, M.A.1    Flanagan, J.M.2    Treutlein, H.R.3    Zhang, J.4    Engelman, D.M.5
  • 51
    • 0030777759 scopus 로고    scopus 로고
    • The effect of point mutations on the free energy of transmembrane alpha-helix dimerization
    • Fleming KG, Ackerman AL, Engelman DM. 1997. The effect of point mutations on the free energy of transmembrane alpha-helix dimerization. J. Mol. Biol. 272:266-275. http://dx.doi.org/10.1006/jmbi.1997 .1236.
    • (1997) J. Mol. Biol. , vol.272 , pp. 266-275
    • Fleming, K.G.1    Ackerman, A.L.2    Engelman, D.M.3
  • 52
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: structure and implications
    • MacKenzie KR, Prestegard JH, Engelman DM. 1997. A transmembrane helix dimer: structure and implications. Science 276:131-133. http://dx .doi.org/10.1126/science.276.5309.131.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 53
    • 77955656071 scopus 로고    scopus 로고
    • The membrane environment modulates self-association of the human GpA TM domain-implications for membrane protein folding and transmembrane signaling
    • Anbazhagan V, Schneider D. 2010. The membrane environment modulates self-association of the human GpA TM domain-implications for membrane protein folding and transmembrane signaling. Biochim. Biophys. Acta 1798:1899-1907. http://dx.doi.org/10.1016/j.bbamem.2010 .06.027.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1899-1907
    • Anbazhagan, V.1    Schneider, D.2
  • 54
    • 0031956790 scopus 로고    scopus 로고
    • The dimerization motif of the glycophorin A transmembrane segment in membranes: importance of glycine residues
    • Brosig B, Langosch D. 1998. The dimerization motif of the glycophorin A transmembrane segment in membranes: importance of glycine residues. Protein Sci. 7:1052-1056.
    • (1998) Protein Sci. , vol.7 , pp. 1052-1056
    • Brosig, B.1    Langosch, D.2
  • 55
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: a framework for transmembrane helix-helix association
    • Russ WP, Engelman DM. 2000. The GxxxG motif: a framework for transmembrane helix-helix association. J. Mol. Biol. 296:911-919. http: //dx.doi.org/10.1006/jmbi.1999.3489.
    • (2000) J. Mol. Biol. , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 56
    • 0037076540 scopus 로고    scopus 로고
    • GXXXG and AXXXA: common alpha-helical interaction motifs in proteins, particularly in extremophiles
    • Kleiger G, Grothe R, Mallick P, Eisenberg D. 2002. GXXXG and AXXXA: common alpha-helical interaction motifs in proteins, particularly in extremophiles. Biochemistry 41:5990-5997. http://dx.doi.org/10 .1021/bi0200763.
    • (2002) Biochemistry , vol.41 , pp. 5990-5997
    • Kleiger, G.1    Grothe, R.2    Mallick, P.3    Eisenberg, D.4
  • 57
    • 1942469334 scopus 로고    scopus 로고
    • The affinity of GXXXG motifs in transmembrane helix-helix interactions is modulated by long-range communication
    • Melnyk RA, Kim S, Curran AR, Engelman DM, Bowie JU, Deber CM. 2004. The affinity of GXXXG motifs in transmembrane helix-helix interactions is modulated by long-range communication. J. Biol. Chem. 279: 16591-16597. http://dx.doi.org/10.1074/jbc.M313936200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 16591-16597
    • Melnyk, R.A.1    Kim, S.2    Curran, A.R.3    Engelman, D.M.4    Bowie, J.U.5    Deber, C.M.6
  • 58
    • 0034711958 scopus 로고    scopus 로고
    • Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions
    • Senes A, Gerstein M, Engelman DM. 2000. Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions. J. Mol. Biol. 296:921-936. http://dx.doi.org/10.1006/jmbi .1999.3488.
    • (2000) J. Mol. Biol. , vol.296 , pp. 921-936
    • Senes, A.1    Gerstein, M.2    Engelman, D.M.3
  • 59
    • 0037085373 scopus 로고    scopus 로고
    • The single transmembrane domains of ErbB receptors self-associate in cell membranes
    • Mendrola JM, Berger MB, King MC, Lemmon MA. 2002. The single transmembrane domains of ErbB receptors self-associate in cell membranes. J. Biol. Chem. 277:4704-4712. http://dx.doi.org/10.1074/jbc .M108681200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4704-4712
    • Mendrola, J.M.1    Berger, M.B.2    King, M.C.3    Lemmon, M.A.4
  • 60
    • 0035979146 scopus 로고    scopus 로고
    • The Calpha- H...O hydrogen bond: a determinant of stability and specificity in transmembrane helix interactions
    • Senes A, Ubarretxena-Belandia I, Engelman DM. 2001. The Calpha- H...O hydrogen bond: a determinant of stability and specificity in transmembrane helix interactions. Proc. Natl. Acad. Sci. U. S. A. 98:9056- 9061. http://dx.doi.org/10.1073/pnas.161280798.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98
    • Senes, A.1    Ubarretxena-Belandia, I.2    Engelman, D.M.3
  • 61
    • 84859742466 scopus 로고    scopus 로고
    • Unipro UGENE: a unified bioinformatics toolkit
    • UGENE team.
    • Okonechnikov K, Golosova O, Fursov M; UGENE team. 2012. Unipro UGENE: a unified bioinformatics toolkit. Bioinformatics 28:1166-1167. http://dx.doi.org/10.1093/bioinformatics/bts091.
    • (2012) Bioinformatics , vol.28 , pp. 1166-1167
    • Okonechnikov, K.1    Golosova, O.2    Fursov, M.3
  • 62
    • 0029019484 scopus 로고
    • Control of the Escherichia coli rrnB P1 promoter strength by ppGpp
    • Zhang X, Bremer H. 1995. Control of the Escherichia coli rrnB P1 promoter strength by ppGpp. J. Biol. Chem. 270:11181-11189. http://dx .doi.org/10.1074/jbc.270.19.11181.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11181-11189
    • Zhang, X.1    Bremer, H.2
  • 63
    • 0020042649 scopus 로고
    • Filamentous phage pre-coat is an integral membrane protein: analysis by a new method of membrane preparation
    • Russel M, Model P. 1982. Filamentous phage pre-coat is an integral membrane protein: analysis by a new method of membrane preparation. Cell 28:177-184. http://dx.doi.org/10.1016/0092-8674(82)90387-7.
    • (1982) Cell , vol.28 , pp. 177-184
    • Russel, M.1    Model, P.2
  • 64
    • 73349087177 scopus 로고    scopus 로고
    • The single transmembrane domains of human receptor tyrosine kinases encode self-interactions
    • Finger C, Escher C, Schneider D. 2009. The single transmembrane domains of human receptor tyrosine kinases encode self-interactions. Sci. Signal. 2:ra56. http://dx.doi.org/10.1126/scisignal.2000547.
    • (2009) Sci. Signal. , vol.2
    • Finger, C.1    Escher, C.2    Schneider, D.3
  • 65
    • 0029557910 scopus 로고
    • Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban
    • Adams PD, Arkin IT, Engelman DM, Brunger AT. 1995. Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban. Nat. Struct. Biol. 2:154- 162. http://dx.doi.org/10.1038/nsb0295-154.
    • (1995) Nat. Struct. Biol. , vol.2
    • Adams, P.D.1    Arkin, I.T.2    Engelman, D.M.3    Brunger, A.T.4
  • 66
    • 0029847652 scopus 로고    scopus 로고
    • Improved prediction for the structure of the dimeric transmembrane domain of glycophorin A obtained through global searching
    • Adams PD, Engelman DM, Brunger AT. 1996. Improved prediction for the structure of the dimeric transmembrane domain of glycophorin A obtained through global searching. Proteins 26:257-261. http: //dx.doi.org/10.1002/(SICI)1097-0134(199611)26:3257::AID-PROT23 .0.CO;2-B.
    • (1996) Proteins , vol.26 , pp. 257-261
    • Adams, P.D.1    Engelman, D.M.2    Brunger, A.T.3
  • 68
    • 74249090260 scopus 로고    scopus 로고
    • Improving physical realism, stereochemistry, and side-chain accuracy in homology modeling: four approaches that performed well in CASP8
    • Krieger E, Joo K, Lee J, Lee J, Raman S, Thompson J, Tyka M, Baker D, Karplus K. 2009. Improving physical realism, stereochemistry, and side-chain accuracy in homology modeling: four approaches that performed well in CASP8. Proteins 77(Suppl 9):114-122. http://dx.doi.org /10.1002/prot.22570.
    • (2009) Proteins , vol.77 , Issue.SUPPL. 9 , pp. 114-122
    • Krieger, E.1    Joo, K.2    Lee, J.3    Lee, J.4    Raman, S.5    Thompson, J.6    Tyka, M.7    Baker, D.8    Karplus, K.9
  • 69
    • 33847233683 scopus 로고    scopus 로고
    • How important are transmembrane helices of bitopic membrane proteins? Biochim
    • Zviling M, Kochva U, Arkin IT. 2007. How important are transmembrane helices of bitopic membrane proteins? Biochim. Biophys. Acta 1768:387-392. http://dx.doi.org/10.1016/j.bbamem.2006.11.019.
    • (2007) Biophys. Acta , vol.1768 , pp. 387-392
    • Zviling, M.1    Kochva, U.2    Arkin, I.T.3
  • 70
    • 3843102625 scopus 로고    scopus 로고
    • Sequence context modulates the stability of a GxxxG-mediated transmembrane helix-helix dimer
    • Doura AK, Kobus FJ, Dubrovsky L, Hibbard E, Fleming KG. 2004. Sequence context modulates the stability of a GxxxG-mediated transmembrane helix-helix dimer. J. Mol. Biol. 341:991-998. http://dx.doi .org/10.1016/j.jmb.2004.06.042.
    • (2004) J. Mol. Biol. , vol.341 , pp. 991-998
    • Doura, A.K.1    Kobus, F.J.2    Dubrovsky, L.3    Hibbard, E.4    Fleming, K.G.5
  • 71
    • 0344687314 scopus 로고    scopus 로고
    • Side-chain contributions to membrane protein structure and stability
    • Faham S, Yang D, Bare E, Yohannan S, Whitelegge JP, Bowie JU. 2004. Side-chain contributions to membrane protein structure and stability. J. Mol. Biol. 335:297-305. http://dx.doi.org/10.1016/j.jmb.2003.10.041.
    • (2004) J. Mol. Biol. , vol.335 , pp. 297-305
    • Faham, S.1    Yang, D.2    Bare, E.3    Yohannan, S.4    Whitelegge, J.P.5    Bowie, J.U.6
  • 72
    • 0031740601 scopus 로고    scopus 로고
    • Hydrophobic interactions of peptides with membrane interfaces
    • White SH, Wimley WC. 1998. Hydrophobic interactions of peptides with membrane interfaces. Biochim. Biophys. Acta 1376:339-352. http: //dx.doi.org/10.1016/S0304-4157(98)00021-5.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 339-352
    • White, S.H.1    Wimley, W.C.2
  • 73
    • 0033609498 scopus 로고    scopus 로고
    • The aromatic residues Trp and Phe have different effects on the positioning of a transmembrane helix in the microsomal membrane
    • Braun P, von Heijne G. 1999. The aromatic residues Trp and Phe have different effects on the positioning of a transmembrane helix in the microsomal membrane. Biochemistry 38:9778-9782. http://dx.doi.org/10 .1021/bi990923a.
    • (1999) Biochemistry , vol.38 , pp. 9778-9782
    • Braun, P.1    von Heijne, G.2
  • 74
    • 6344236852 scopus 로고    scopus 로고
    • Complex interactions at the helix-helix interface stabilize the glycophorin A transmembrane dimer
    • Doura AK, Fleming KG. 2004. Complex interactions at the helix-helix interface stabilize the glycophorin A transmembrane dimer. J. Mol. Biol. 343:1487-1497. http://dx.doi.org/10.1016/j.jmb.2004.09.011.
    • (2004) J. Mol. Biol. , vol.343 , pp. 1487-1497
    • Doura, A.K.1    Fleming, K.G.2
  • 75
    • 46049088691 scopus 로고    scopus 로고
    • Protein-protein interactions in the membrane: sequence, structural, and biological motifs
    • Moore DT, Berger BW, DeGrado WF. 2008. Protein-protein interactions in the membrane: sequence, structural, and biological motifs. Structure 16:991-1001. http://dx.doi.org/10.1016/j.str.2008.05.007.
    • (2008) Structure , vol.16 , pp. 991-1001
    • Moore, D.T.1    Berger, B.W.2    DeGrado, W.F.3
  • 77
    • 84860817692 scopus 로고    scopus 로고
    • Robust full-length hepatitis C virus genotype 2a and 2b infectious cultures using mutations identified by a systematic approach applicable to patient strains
    • Li YP, Ramirez S, Gottwein JM, Scheel TK, Mikkelsen L, Purcell RH, Bukh J. 2012. Robust full-length hepatitis C virus genotype 2a and 2b infectious cultures using mutations identified by a systematic approach applicable to patient strains. Proc. Natl. Acad. Sci. U. S. A. 109:E1101- 1110. http://dx.doi.org/10.1073/pnas.1203829109.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109
    • Li, Y.P.1    Ramirez, S.2    Gottwein, J.M.3    Scheel, T.K.4    Mikkelsen, L.5    Purcell, R.H.6    Bukh, J.7
  • 78
    • 84870372937 scopus 로고    scopus 로고
    • Highly efficient full-length hepatitis C virus genotype 1 (strain TN) infectious culture system
    • Li YP, Ramirez S, Jensen SB, Purcell RH, Gottwein JM, Bukh J. 2012. Highly efficient full-length hepatitis C virus genotype 1 (strain TN) infectious culture system. Proc. Natl. Acad. Sci. U. S. A. 109:19757-19762. http://dx.doi.org/10.1073/pnas.1218260109.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 19757-19762
    • Li, Y.P.1    Ramirez, S.2    Jensen, S.B.3    Purcell, R.H.4    Gottwein, J.M.5    Bukh, J.6
  • 79
    • 0032732426 scopus 로고    scopus 로고
    • Detergents modulate dimerization, but not helicity, of the glycophorin A transmembrane domain
    • Fisher LE, Engelman DM, Sturgis JN. 1999. Detergents modulate dimerization, but not helicity, of the glycophorin A transmembrane domain. J. Mol. Biol. 293:639-651. http://dx.doi.org/10.1006/jmbi.1999 .3126.
    • (1999) J. Mol. Biol. , vol.293 , pp. 639-651
    • Fisher, L.E.1    Engelman, D.M.2    Sturgis, J.N.3
  • 80
    • 0242353821 scopus 로고    scopus 로고
    • Effect of detergents on the association of the glycophorin a transmembrane helix
    • Fisher LE, Engelman DM, Sturgis JN. 2003. Effect of detergents on the association of the glycophorin a transmembrane helix. Biophys. J. 85: 3097-3105. http://dx.doi.org/10.1016/S0006-3495(03)74728-6.
    • (2003) Biophys. J. , vol.85 , pp. 3097-3105
    • Fisher, L.E.1    Engelman, D.M.2    Sturgis, J.N.3
  • 81
    • 33646902110 scopus 로고    scopus 로고
    • Folding and stability of alpha-helical integral membrane proteins
    • Mackenzie KR. 2006. Folding and stability of alpha-helical integral membrane proteins. Chem. Rev. 106:1931-1977. http://dx.doi.org/10 .1021/cr0404388.
    • (2006) Chem. Rev. , vol.106 , pp. 1931-1977
    • Mackenzie, K.R.1
  • 82
    • 84857529575 scopus 로고    scopus 로고
    • Transmembrane helix-helix interactions are modulated by the sequence context and by lipid bilayer properties
    • Cymer F, Veerappan A, Schneider D. 2012. Transmembrane helix-helix interactions are modulated by the sequence context and by lipid bilayer properties. Biochim. Biophys. Acta 1818:963-973. http://dx.doi.org/10 .1016/j.bbamem.2011.07.035.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 963-973
    • Cymer, F.1    Veerappan, A.2    Schneider, D.3
  • 83
    • 84879022013 scopus 로고    scopus 로고
    • ACH-806, an NS4A antagonist, inhibits hepatitis C virus replication through altering the composition of viral replication complexes
    • 29 April Antimicrob. Agents Chemother
    • Yang W, Sun Y, Hou X, Zhao Y, Fabrycki J, Chen D, Wang X, Agarwal A, Phadke A, Deshpande M, Huang M. 29 April 2013. ACH-806, an NS4A antagonist, inhibits hepatitis C virus replication through altering the composition of viral replication complexes. Antimicrob. Agents Chemother. http://dx.doi.org/10.1128/AAC.02630-12.
    • (2013)
    • Yang, W.1    Sun, Y.2    Hou, X.3    Zhao, Y.4    Fabrycki, J.5    Chen, D.6    Wang, X.7    Agarwal, A.8    Phadke, A.9    Deshpande, M.10    Huang, M.11
  • 84
    • 44449099603 scopus 로고    scopus 로고
    • Selection of replicon variants resistant to ACH-806, a novel hepatitis C virus inhibitor with no cross-resistance to NS3 protease and NS5B polymerase inhibitors
    • Yang W, Zhao Y, Fabrycki J, Hou X, Nie X, Sanchez A, Phadke A, Deshpande M, Agarwal A, Huang M. 2008. Selection of replicon variants resistant to ACH-806, a novel hepatitis C virus inhibitor with no cross-resistance to NS3 protease and NS5B polymerase inhibitors. Antimicrob. Agents Chemother. 52:2043-2052. http://dx.doi.org/10.1128 /AAC.01548-07.
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 2043-2052
    • Yang, W.1    Zhao, Y.2    Fabrycki, J.3    Hou, X.4    Nie, X.5    Sanchez, A.6    Phadke, A.7    Deshpande, M.8    Agarwal, A.9    Huang, M.10
  • 85
    • 0001041988 scopus 로고    scopus 로고
    • Probing the folding and unfolding of wildtype and mutant forms of bacteriorhodopsin in micellar solutions: evaluation of reversible unfolding conditions
    • Chen GQ, Gouaux E. 1999. Probing the folding and unfolding of wildtype and mutant forms of bacteriorhodopsin in micellar solutions: evaluation of reversible unfolding conditions. Biochemistry 38:15380 - 15387. http://dx.doi.org/10.1021/bi9909039.
    • (1999) Biochemistry , vol.38
    • Chen, G.Q.1    Gouaux, E.2
  • 86
    • 23644460494 scopus 로고    scopus 로고
    • Oligomerization of the fifth transmembrane domain from the adenosine A2A receptor
    • Thévenin D, Lazarova T, Roberts MF, Robinson CR. 2005. Oligomerization of the fifth transmembrane domain from the adenosine A2A receptor. Protein Sci. 14:2177-2186. http://dx.doi.org/10.1110/ps.051409205.
    • (2005) Protein Sci. , vol.14 , pp. 2177-2186
    • Thévenin, D.1    Lazarova, T.2    Roberts, M.F.3    Robinson, C.R.4
  • 87
    • 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. http://dx.doi.org/10.1074/jbc.M512100200.
    • (2006) J. Biol. Chem. , vol.281
    • 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
  • 88
    • 2542468381 scopus 로고    scopus 로고
    • The functional interaction of the hepatitis C virus helicase molecules is responsible for unwinding processivity
    • Levin MK, Wang YH, Patel SS. 2004. The functional interaction of the hepatitis C virus helicase molecules is responsible for unwinding processivity. J. Biol. Chem. 279:26005-26012. http://dx.doi.org/10.1074/jbc .M403257200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26005-26012
    • Levin, M.K.1    Wang, Y.H.2    Patel, S.S.3
  • 89
    • 64149127878 scopus 로고    scopus 로고
    • NS3 helicase from the hepatitis C virus can function as a monomer or oligomer depending on enzyme and substrate concentrations
    • Jennings TA, Mackintosh SG, Harrison MK, Sikora D, Sikora B, Dave B, Tackett AJ, Cameron CE, Raney KD. 2009. NS3 helicase from the hepatitis C virus can function as a monomer or oligomer depending on enzyme and substrate concentrations. J. Biol. Chem. 284:4806-4814. http://dx.doi.org/10.1074/jbc.M805540200.
    • (2009) J. Biol. Chem. , vol.284 , pp. 4806-4814
    • Jennings, T.A.1    Mackintosh, S.G.2    Harrison, M.K.3    Sikora, D.4    Sikora, B.5    Dave, B.6    Tackett, A.J.7    Cameron, C.E.8    Raney, K.D.9
  • 90
    • 59049088498 scopus 로고    scopus 로고
    • Establishing a mechanistic basis for the large kinetic steps of the NS3 helicase
    • Serebrov V, Beran RK, Pyle AM. 2009. Establishing a mechanistic basis for the large kinetic steps of the NS3 helicase. J. Biol. Chem. http://dx.doi .org/10.1074/jbc.M805460200. 284:2512-2521.
    • (2009) J. Biol. Chem.
    • Serebrov, V.1    Beran, R.K.2    Pyle, A.M.3
  • 91
    • 33745823112 scopus 로고    scopus 로고
    • Mechanisms of helicases
    • Patel SS, Donmez I. 2006. Mechanisms of helicases. J. Biol. Chem. 281:18265-18268. http://dx.doi.org/10.1074/jbc.R600008200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 18265-18268
    • Patel, S.S.1    Donmez, I.2
  • 92
    • 0036500976 scopus 로고    scopus 로고
    • The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding
    • Pang PS, Jankowsky E, Planet PJ, Pyle AM. 2002. The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding. EMBO J. 21:1168-1176. http://dx.doi.org/10.1093/emboj /21.5.1168.
    • (2002) EMBO J. , vol.21 , pp. 1168-1176
    • Pang, P.S.1    Jankowsky, E.2    Planet, P.J.3    Pyle, A.M.4
  • 93
    • 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. http: //dx.doi.org/10.1128/JVI.00942-09.
    • (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
  • 94
    • 79955383686 scopus 로고    scopus 로고
    • Unmasking the active helicase conformation of nonstructural protein 3 from hepatitis C virus
    • Ding SC, Kohlway AS, Pyle AM. 2011. Unmasking the active helicase conformation of nonstructural protein 3 from hepatitis C virus. J. Virol. 85:4343-4353. http://dx.doi.org/10.1128/JVI.02130-10.
    • (2011) J. Virol. , vol.85 , pp. 4343-4353
    • Ding, S.C.1    Kohlway, A.S.2    Pyle, A.M.3
  • 95
    • 77953306294 scopus 로고    scopus 로고
    • Flexibility between the protease and helicase domains of the dengue virus NS3 protein conferred by the linker region and its functional implications
    • Luo D, Wei N, Doan DN, Paradkar PN, Chong Y, Davidson AD, Kotaka M, Lescar J, Vasudevan SG. 2010. Flexibility between the protease and helicase domains of the dengue virus NS3 protein conferred by the linker region and its functional implications. J. Biol. Chem. 285: 18817-18827. http://dx.doi.org/10.1074/jbc.M109.090936.
    • (2010) J. Biol. Chem. , vol.285 , pp. 18817-18827
    • Luo, D.1    Wei, N.2    Doan, D.N.3    Paradkar, P.N.4    Chong, Y.5    Davidson, A.D.6    Kotaka, M.7    Lescar, J.8    Vasudevan, S.G.9
  • 96
    • 33846005485 scopus 로고    scopus 로고
    • Evidence for the formation of a heptameric ion channel complex by the hepatitis C virus p7 protein in vitro
    • Clarke D, Griffin S, Beales L, Gelais CS, Burgess S, Harris M, Rowlands D. 2006. Evidence for the formation of a heptameric ion channel complex by the hepatitis C virus p7 protein in vitro. J. Biol. Chem. 281: 37057-37068. http://dx.doi.org/10.1074/jbc.M602434200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 37057-37068
    • Clarke, D.1    Griffin, S.2    Beales, L.3    Gelais, C.S.4    Burgess, S.5    Harris, M.6    Rowlands, D.7
  • 98
    • 33747452685 scopus 로고    scopus 로고
    • Structure of the catalytic domain of the hepatitis C virus NS2-3 protease
    • Lorenz IC, Marcotrigiano J, Dentzer TG, Rice CM. 2006. Structure of the catalytic domain of the hepatitis C virus NS2-3 protease. Nature 442:831-835. http://dx.doi.org/10.1038/nature04975.
    • (2006) Nature , vol.442 , pp. 831-835
    • Lorenz, I.C.1    Marcotrigiano, J.2    Dentzer, T.G.3    Rice, C.M.4
  • 99
    • 78649398569 scopus 로고    scopus 로고
    • Amphipathic alpha-helix AH2 is a major determinant for the oligomerization of hepatitis C virus nonstructural protein 4B
    • Gouttenoire J, Roingeard P, Penin F, Moradpour D. 2010. Amphipathic alpha-helix AH2 is a major determinant for the oligomerization of hepatitis C virus nonstructural protein 4B. J. Virol. 84:12529-12537. http://dx.doi.org/10.1128/JVI.01798-10.
    • (2010) J. Virol. , vol.84 , pp. 12529-12537
    • Gouttenoire, J.1    Roingeard, P.2    Penin, F.3    Moradpour, D.4
  • 100
    • 79960406328 scopus 로고    scopus 로고
    • NS4B self-interaction through conserved C-terminal elements is required for the establishment of functional hepatitis C virus replication complexes
    • Paul D, Romero-Brey I, Gouttenoire J, Stoitsova S, Krijnse-Locker J, Moradpour D, Bartenschlager R. 2011. NS4B self-interaction through conserved C-terminal elements is required for the establishment of functional hepatitis C virus replication complexes. J. Virol. 85:6963-6976. http://dx.doi.org/10.1128/JVI.00502-11.
    • (2011) J. Virol. , vol.85 , pp. 6963-6976
    • Paul, D.1    Romero-Brey, I.2    Gouttenoire, J.3    Stoitsova, S.4    Krijnse-Locker, J.5    Moradpour, D.6    Bartenschlager, R.7
  • 101
    • 78649430973 scopus 로고    scopus 로고
    • Hepatitis C virus nonstructural protein 5A: biochemical characterization of a novel structural class of RNA-binding proteins
    • Hwang J, Huang L, Cordek DG, Vaughan R, Reynolds SL, Kihara G, Raney KD, Kao CC, Cameron CE. 2010. Hepatitis C virus nonstructural protein 5A: biochemical characterization of a novel structural class of RNA-binding proteins. J. Virol. 84:12480-12491. http://dx.doi.org/10 .1128/JVI.01319-10.
    • (2010) J. Virol. , vol.84 , pp. 12480-12491
    • Hwang, J.1    Huang, L.2    Cordek, D.G.3    Vaughan, R.4    Reynolds, S.L.5    Kihara, G.6    Raney, K.D.7    Kao, C.C.8    Cameron, C.E.9
  • 102
    • 0037127306 scopus 로고    scopus 로고
    • Oligomeric interaction of hepatitis C virus NS5B is critical for catalytic activity of RNA-dependent RNA polymerase
    • Qin W, Luo H, Nomura T, Hayashi N, Yamashita T, Murakami S. 2002. Oligomeric interaction of hepatitis C virus NS5B is critical for catalytic activity of RNA-dependent RNA polymerase. J. Biol. Chem. 277:2132-2137. http://dx.doi.org/10.1074/jbc.M106880200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2132-2137
    • Qin, W.1    Luo, H.2    Nomura, T.3    Hayashi, N.4    Yamashita, T.5    Murakami, S.6
  • 106
    • 33144471074 scopus 로고    scopus 로고
    • Production of infectious genotype 1a hepatitis C virus (Hutchinson strain) in cultured human hepatoma cells
    • Yi M, Villanueva RA, Thomas DL, Wakita T, Lemon SM. 2006. Production of infectious genotype 1a hepatitis C virus (Hutchinson strain) in cultured human hepatoma cells. Proc. Natl. Acad. Sci. U. S. A. 103:2310-2315. http://dx.doi.org/10.1073/pnas.0510727103.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 2310-2315
    • Yi, M.1    Villanueva, R.A.2    Thomas, D.L.3    Wakita, T.4    Lemon, S.M.5
  • 110
    • 0036568229 scopus 로고    scopus 로고
    • Interhelical hydrogen bonds and spatial motifs in membrane proteins: polar clamps and serine zippers
    • Adamian L, Liang J. 2002. Interhelical hydrogen bonds and spatial motifs in membrane proteins: polar clamps and serine zippers. Proteins 47:209-218. http://dx.doi.org/10.1002/prot.10071.
    • (2002) Proteins , vol.47 , pp. 209-218
    • Adamian, L.1    Liang, J.2
  • 111
    • 34250865507 scopus 로고    scopus 로고
    • In vivo study of the HC-TN strain of hepatitis C virus recovered from a patient with fulminant hepatitis: RNA transcripts of a molecular clone (pHC-TN) are infectious in chimpanzees but not in Huh7.5
    • Sakai A, Takikawa S, Thimme R, Meunier JC, Spangenberg HC, Govindarajan S, Farci P, Emerson SU, Chisari FV, Purcell RH, Bukh J. 2007. In vivo study of the HC-TN strain of hepatitis C virus recovered from a patient with fulminant hepatitis: RNA transcripts of a molecular clone (pHC-TN) are infectious in chimpanzees but not in Huh7.5 cells. J. Virol. 81:7208-7219. http://dx.doi.org/10.1128/JVI.01774-06.
    • (2007) cells. J. Virol. , vol.81 , pp. 7208-7219
    • Sakai, A.1    Takikawa, S.2    Thimme, R.3    Meunier, J.C.4    Spangenberg, H.C.5    Govindarajan, S.6    Farci, P.7    Emerson, S.U.8    Chisari, F.V.9    Purcell, R.H.10    Bukh, J.11
  • 112
    • 0033568548 scopus 로고    scopus 로고
    • Hepatitis C virus: an infectious molecular clone of a second major genotype (2a) and lack of viability of intertypic 1a and 2a chimeras
    • Yanagi M, Purcell RH, Emerson SU, Bukh J. 1999. Hepatitis C virus: an infectious molecular clone of a second major genotype (2a) and lack of viability of intertypic 1a and 2a chimeras. Virology 262:250-263. http: //dx.doi.org/10.1006/viro.1999.9889.
    • (1999) Virology , vol.262 , pp. 250-263
    • Yanagi, M.1    Purcell, R.H.2    Emerson, S.U.3    Bukh, J.4
  • 113
    • 84863264794 scopus 로고    scopus 로고
    • Control of innate immune signaling and membrane targeting by the hepatitis C virus NS3/4A protease are governed by the NS3 helix alpha0
    • Horner SM, Park HS, Gale M, Jr. 2012. Control of innate immune signaling and membrane targeting by the hepatitis C virus NS3/4A protease are governed by the NS3 helix alpha0. J. Virol. 86:3112-3120. http: //dx.doi.org/10.1128/JVI.06727-11.
    • (2012) J. Virol. , vol.86 , pp. 3112-3120
    • Horner, S.M.1    Park, H.S.2    Gale, M.3
  • 115
    • 77956623666 scopus 로고    scopus 로고
    • Receptor tyrosine kinase transmembrane domain interactions: potential target for "interceptor" therapy
    • jc6
    • Najumudeen AK. 2010. Receptor tyrosine kinase transmembrane domain interactions: potential target for "interceptor" therapy. Sci. Signal. 3:jc6. http://dx.doi.org/10.1126/scisignal.3138jc6.
    • (2010) Sci. Signal. , vol.3
    • Najumudeen, A.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.