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Volumn 79, Issue 3, 2000, Pages 1415-1427

Delay of influenza hemagglutinin refolding into a fusion-competent conformation by receptor binding: A hypothesis

Author keywords

[No Author keywords available]

Indexed keywords

HEMAGGLUTININ; LYSOPHOSPHATIDYLCHOLINE; MEMBRANE RECEPTOR; SIALIC ACID; SIALIC ACID DERIVATIVE; SIALIDASE;

EID: 0033855432     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76393-4     Document Type: Article
Times cited : (25)

References (9)
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  • 2
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    • Minimal aggregate size and minimal fusion unit for the first fusion pore of influenza hemagglutinin mediated membrane fusion
    • Bentz, J. 1999. Minimal aggregate size and minimal fusion unit for the first fusion pore of influenza hemagglutinin mediated membrane fusion. Biophys. J. 78:227-245.
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    • Bentz, J.1
  • 3
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    • Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events
    • Blumenthal, R., D. P. Sarkar, S. Durell, D. E. Howard, and S. J. Morris. 1996. Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events. J. Cell Biol. 135:63-71.
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    • Blumenthal, R.1    Sarkar, D.P.2    Durell, S.3    Howard, D.E.4    Morris, S.J.5
  • 4
    • 0026389193 scopus 로고
    • A dissection of steps leading to viral envelope protein-mediated membrane fusion
    • Blumenthal, R., C. Schoch, A. Puri, and M. J. Clague. 1991. A dissection of steps leading to viral envelope protein-mediated membrane fusion. Ann. N.Y. Acad. Sci. 635:285-296.
    • (1991) Ann. N.Y. Acad. Sci. , vol.635 , pp. 285-296
    • Blumenthal, R.1    Schoch, C.2    Puri, A.3    Clague, M.J.4
  • 5
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P. A., F. M. Hughson, J. J. Skehel, and D. C. Wiley. 1994. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature. 371:37-43.
    • (1994) Nature. , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 6
    • 0031460632 scopus 로고    scopus 로고
    • Influenza hemagglutinin is spring-loaded by a metastable native conformation
    • Carr, C. M., C. Chaudhry, and P. S. Kim. 1997. Influenza hemagglutinin is spring-loaded by a metastable native conformation. Proc. Natl. Acad. Sci. USA. 94:14306-14313.
    • (1997) Proc. Natl. Acad. Sci. USA. , vol.94 , pp. 14306-14313
    • Carr, C.M.1    Chaudhry, C.2    Kim, P.S.3
  • 7
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr, C. M., and P. S. Kim. 1993. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell. 73:823-832.
    • (1993) Cell. , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 8
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    • N- And C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil
    • Chen, J., J. J. Skehel, and D. C. Wiley. 1999. N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil. Proc. Natl. Acad. Sci. USA. 96:8967-8972.
    • (1999) Proc. Natl. Acad. Sci. USA. , vol.96 , pp. 8967-8972
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  • 9
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    • A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation
    • Chen, J., S. A. Wharton, W. Weissenhorn, L. J. Calder, F. M. Hughson, J. J. Skehel, and D. C. Wiley. 1995. A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation. Proc. Natl. Acad. Sci. USA. 92:12205-12209.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.