메뉴 건너뛰기




Volumn 73, Issue 12, 1999, Pages 9695-9701

Effect of cytoplasmic tail truncations on the activity of the M2 ion channel of influenza A virus

Author keywords

[No Author keywords available]

Indexed keywords

ION CHANNEL;

EID: 0032736043     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.73.12.9695-9701.1999     Document Type: Article
Times cited : (62)

References (49)
  • 1
    • 0033073762 scopus 로고    scopus 로고
    • 2 ion channel protein: Probing the structure of the transmembrane domain in intact cells by using engineered disulfide cross-linking
    • 2 ion channel protein: probing the structure of the transmembrane domain in intact cells by using engineered disulfide cross-linking. Virology 254:195-209.
    • (1999) Virology , vol.254 , pp. 195-209
    • Bauer, C.M.1    Pinto, L.H.2    Cross, T.A.3    Lamb, R.A.4
  • 4
    • 0026772384 scopus 로고
    • 2-mediated conversion of influenza A virus hemagglutinin to the low pH conformation occurs in an acidic trans Golgi compartment
    • 2-mediated conversion of influenza A virus hemagglutinin to the low pH conformation occurs in an acidic trans Golgi compartment. Virology 188:14-24.
    • (1992) Virology , vol.188 , pp. 14-24
    • Ciampor, F.1    Bayley, P.M.2    Nermut, M.V.3    Hirst, E.M.4    Sugrue, R.J.5    Hay, A.J.6
  • 5
    • 0026785994 scopus 로고
    • 2 protein forms amantadine-sensitive proton channels in planar lipid bilayers
    • 2 protein forms amantadine-sensitive proton channels in planar lipid bilayers. Virology 190:485-489.
    • (1992) Virology , vol.190 , pp. 485-489
    • Duff, K.C.1    Ashley, R.H.2
  • 8
    • 0022508657 scopus 로고
    • Sequence determinants of cytosolic N-terminal protein processing
    • Flinta, C., B. Persson, H. Jornvall, and G. von Heijne. 1986. Sequence determinants of cytosolic N-terminal protein processing. Eur. J. Biochem. 154:193-196.
    • (1986) Eur. J. Biochem. , vol.154 , pp. 193-196
    • Flinta, C.1    Persson, B.2    Jornvall, H.3    Von Heijne, G.4
  • 14
    • 0002988267 scopus 로고
    • 2 ion channel protein
    • 2 ion channel protein. Semin. Virol. 3:21-30.
    • (1992) Semin. Virol. , vol.3 , pp. 21-30
    • Hay, A.J.1
  • 15
    • 0022157043 scopus 로고
    • The molecular basis of the specific anti-influenza action of amantadine
    • Hay, A. J., A. J. Wolstenhohne, J. J. Skehel, and M. H. Smith. 1985. The molecular basis of the specific anti-influenza action of amantadine. EMBO J. 4:3021-3024.
    • (1985) EMBO J. , vol.4 , pp. 3021-3024
    • Hay, A.J.1    Wolstenhohne, A.J.2    Skehel, J.J.3    Smith, M.H.4
  • 16
    • 0025923280 scopus 로고
    • 2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds
    • 2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds. Virology 183:32-43.
    • (1991) Virology , vol.183 , pp. 32-43
    • Holsinger, L.J.1    Lamb, R.A.2
  • 20
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivation
    • Hoshi, T., W. N. Zagotta, and R. W. Aldrich. 1990. Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science 250:533-538.
    • (1990) Science , vol.250 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 21
    • 0026049511 scopus 로고
    • + channels: Effects of alterations in the carboxy-terminal region
    • + channels: effects of alterations in the carboxy-terminal region. Neuron 7:547-556.
    • (1991) Neuron , vol.7 , pp. 547-556
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 22
    • 0031038307 scopus 로고    scopus 로고
    • + channel inactivation mediated by the concerted action of the cytoplasmic N- and C-terminal domains
    • + channel inactivation mediated by the concerted action of the cytoplasmic N- and C-terminal domains. Biophys. J. 72:163-174.
    • (1997) Biophys. J. , vol.72 , pp. 163-174
    • Jerng, H.H.1    Covarrubias, M.2
  • 23
    • 0030777711 scopus 로고    scopus 로고
    • 2 protein channel: Structural implications from helix tilt and orientation
    • 2 protein channel: structural implications from helix tilt and orientation. Biophys. J. 73:2511-2517.
    • (1997) Biophys. J. , vol.73 , pp. 2511-2517
    • Kovacs, F.A.1    Cross, T.A.2
  • 25
    • 0003156040 scopus 로고
    • 2 ion channel protein and its role in the influenza virus life cycle
    • E. Wimmer (ed.). Cold Spring Harbor Press, Cold Spring Harbor, N.Y.
    • 2 ion channel protein and its role in the influenza virus life cycle, p. 303-321. In E. Wimmer (ed.), Receptor-mediated virus entry into cells. Cold Spring Harbor Press, Cold Spring Harbor, N.Y.
    • (1994) Receptor-mediated Virus Entry into Cells , pp. 303-321
    • Lamb, R.A.1    Holsinger, L.J.2    Pinto, L.H.3
  • 26
    • 0019859896 scopus 로고
    • Sequences of mRNAs derived from genome RNA segment 7 of influenza virus: Colinear and interrupted mRNAs code for overlapping proteins
    • Lamb, R. A., C.-J. Lai, and P. W. Choppin. 1981. Sequences of mRNAs derived from genome RNA segment 7 of influenza virus: colinear and interrupted mRNAs code for overlapping proteins. Proc. Natl. Acad. Sci. USA 78:4170-4174.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4170-4174
    • Lamb, R.A.1    Lai, C.-J.2    Choppin, P.W.3
  • 27
    • 0021893484 scopus 로고
    • 2 protein is an integral membrane protein expressed on the infected-cell surface
    • 2 protein is an integral membrane protein expressed on the infected-cell surface. Cell 40:627-633.
    • (1985) Cell , vol.40 , pp. 627-633
    • Lamb, R.A.1    Zebedee, S.L.2    Richardson, C.D.3
  • 28
    • 0027172696 scopus 로고
    • A structural basis for the unequal sensitivity of the major cardiac and liver gap junctions to intracellular acidification: The carboxyl tail length
    • Liu, S., S. Taffet, L. Stoner, M. Delmar, M. L. Vallano, and J. Jalife. 1993. A structural basis for the unequal sensitivity of the major cardiac and liver gap junctions to intracellular acidification: the carboxyl tail length. Biophys. J. 64:1422-1433.
    • (1993) Biophys. J. , vol.64 , pp. 1422-1433
    • Liu, S.1    Taffet, S.2    Stoner, L.3    Delmar, M.4    Vallano, M.L.5    Jalife, J.6
  • 38
    • 0028783338 scopus 로고
    • Viral and cellular small integral membrane proteins can modify ion channels endogenous to Xenopus oocytes
    • Shimbo, K., D. L. Brassard, R A. Lamb, and L. H. Pinto. 1995. Viral and cellular small integral membrane proteins can modify ion channels endogenous to Xenopus oocytes. Biophys. J. 69:1819-1829.
    • (1995) Biophys. J. , vol.69 , pp. 1819-1829
    • Shimbo, K.1    Brassard, D.L.2    Lamb, R.A.3    Pinto, L.H.4
  • 40
    • 0026008031 scopus 로고
    • 2 protein of the influenza A viruses: Evidence that it forms a tetrameric channel
    • 2 protein of the influenza A viruses: evidence that it forms a tetrameric channel. Virology 180:617-624.
    • (1991) Virology , vol.180 , pp. 617-624
    • Sugrue, R.J.1    Hay, A.J.2
  • 43
    • 0028980598 scopus 로고
    • 2 ion channel of influenza virus: A role for the transmembrane domain histidine residue
    • 2 ion channel of influenza virus: a role for the transmembrane domain histidine residue. Biophys. J. 69:1363-1371.
    • (1995) Biophys. J. , vol.69 , pp. 1363-1371
    • Wang, C.1    Lamb, R.A.2    Pinto, L.H.3
  • 44
    • 0028100022 scopus 로고
    • 2 protein ion channel activity in mammalian cells
    • 2 protein ion channel activity in mammalian cells. Virology 205:133-140.
    • (1994) Virology , vol.205 , pp. 133-140
    • Wang, C.1    Lamb, R.A.2    Pinto, L.H.3
  • 48
    • 0022345295 scopus 로고
    • 2 integral membrane protein and expression at the infected-cell surface from cloned cDNA
    • 2 integral membrane protein and expression at the infected-cell surface from cloned cDNA. J. Virol. 56:502-511.
    • (1985) J. Virol. , vol.56 , pp. 502-511
    • Zebedee, S.L.1    Richardson, C.D.2    Lamb, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.