메뉴 건너뛰기




Volumn 183, Issue 2, 2008, Pages 177-179

The pH sensor for flavivirus membrane fusion

Author keywords

[No Author keywords available]

Indexed keywords

FLAVIVIRUS; MEMBRANE FUSION; MUTATIONAL ANALYSIS; NOTE; PH MEASUREMENT; PRIORITY JOURNAL; PROTON TRANSPORT; VIRUS ENVELOPE; VIRUS MORPHOLOGY; CHEMISTRY; METABOLISM; PH; PROTEIN CONFORMATION;

EID: 55949125587     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200809175     Document Type: Note
Times cited : (37)

References (15)
  • 1
    • 0029162425 scopus 로고
    • Synthesis and secretion of recombinant tick-borne encephalitis virus protein E in soluble and particulate form
    • Allison, S.L., K. Stadler, C.W. Mandl, C. Kunz, and F.X. Heinz. 1995. Synthesis and secretion of recombinant tick-borne encephalitis virus protein E in soluble and particulate form. J. Virol. 69:5816-5820.
    • (1995) J. Virol , vol.69 , pp. 5816-5820
    • Allison, S.L.1    Stadler, K.2    Mandl, C.W.3    Kunz, C.4    Heinz, F.X.5
  • 3
    • 0034732136 scopus 로고    scopus 로고
    • Membrane fusion activity of tick-borne encephalitis virus and recombinant subviral particles in a liposomal model system
    • Corver, J., A. Ortiz, S.L. Allison, J. Schalich, F.X. Heinz, and J. Wilschut. 2000. Membrane fusion activity of tick-borne encephalitis virus and recombinant subviral particles in a liposomal model system. Virology. 269:37-46.
    • (2000) Virology , vol.269 , pp. 37-46
    • Corver, J.1    Ortiz, A.2    Allison, S.L.3    Schalich, J.4    Heinz, F.X.5    Wilschut, J.6
  • 5
    • 55949108725 scopus 로고    scopus 로고
    • Identification of specific histidines as pH sensors in flavivirus membrane fusion
    • Fritz, E, K. Stiasny, and F.X. Heinz. 2008. Identification of specific histidines as pH sensors in flavivirus membrane fusion. J. Cell Biol. 183:353-361.
    • (2008) J. Cell Biol , vol.183 , pp. 353-361
    • Fritz, E.1    Stiasny, K.2    Heinz, F.X.3
  • 7
    • 33749266195 scopus 로고    scopus 로고
    • The role of histidine residues in low-pH-mediated viral membrane fusion
    • Kampmann, T., D.S. Mueller, A.E. Mark, P.R. Young, and B. Kobe. 2006. The role of histidine residues in low-pH-mediated viral membrane fusion. Structure. 14:1481-1487.
    • (2006) Structure , vol.14 , pp. 1481-1487
    • Kampmann, T.1    Mueller, D.S.2    Mark, A.E.3    Young, P.R.4    Kobe, B.5
  • 8
    • 26444506252 scopus 로고    scopus 로고
    • Domain III from class II fusion proteins functions as a dominant-negative inhibitor of virus membrane fusion
    • Liao, M., and M. Kielian. 2005. Domain III from class II fusion proteins functions as a dominant-negative inhibitor of virus membrane fusion. J. Cell Biol. 171:111-120.
    • (2005) J. Cell Biol , vol.171 , pp. 111-120
    • Liao, M.1    Kielian, M.2
  • 9
    • 34748873170 scopus 로고    scopus 로고
    • Flaviviruses: The viruses and their replication
    • D.M. Knipe and P.M. Howley, editors. Lippincott Williams & Wilkins, Philadelphia
    • Lindenbach, B.D., H.-J. Thiel, and C.M. Rice. 2007. Flaviviruses: the viruses and their replication. In Fields' Virology. D.M. Knipe and P.M. Howley, editors. Lippincott Williams & Wilkins, Philadelphia. 1102-1152.
    • (2007) Fields' Virology , pp. 1102-1152
    • Lindenbach, B.D.1    Thiel, H.-J.2    Rice, C.M.3
  • 10
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 å resolution
    • Rey, F.A., F.X. Heinz, C. Mandl, C. Kunz, and S.C. Harrison. 1995. The envelope glycoprotein from tick-borne encephalitis virus at 2 å resolution. Nature. 375:291-298.
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 11
    • 0023836405 scopus 로고
    • The Bohr effect
    • Riggs, A.F. 1988. The Bohr effect. Annu. Rev. Physiol. 50:181-204.
    • (1988) Annu. Rev. Physiol , vol.50 , pp. 181-204
    • Riggs, A.F.1
  • 12
    • 0029888374 scopus 로고    scopus 로고
    • Recombinant subviral particles from tick-borne encephalitis virus are fusogenic and provide a model system for studying flavivirus envelope glycoprotein functions
    • Schalich, J., S.L. Allison, K. Stiasny, C.W. Mandl, C. Kunz, and F.X. Heinz. 1996. Recombinant subviral particles from tick-borne encephalitis virus are fusogenic and provide a model system for studying flavivirus envelope glycoprotein functions. J. Virol. 70:4549-4557.
    • (1996) J. Virol , vol.70 , pp. 4549-4557
    • Schalich, J.1    Allison, S.L.2    Stiasny, K.3    Mandl, C.W.4    Kunz, C.5    Heinz, F.X.6
  • 13
    • 35148859259 scopus 로고    scopus 로고
    • Probing the flavivirus membrane fusion mechanism by using monoclonal antibodies
    • Stiasny, K., S. Brandler, C. Kossl, and F.X. Heinz. 2007. Probing the flavivirus membrane fusion mechanism by using monoclonal antibodies. J. Virol. 81:11526-11531.
    • (2007) J. Virol , vol.81 , pp. 11526-11531
    • Stiasny, K.1    Brandler, S.2    Kossl, C.3    Heinz, F.X.4
  • 14
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: Multiple variations on a common theme
    • White, J.M., S.E. Delos, M. Brecher, and K. Schornberg. 2008. Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit. Rev. Biochem. Mol. Biol. 43:189-219.
    • (2008) Crit. Rev. Biochem. Mol. Biol , vol.43 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.