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Volumn 74, Issue 24, 2000, Pages 11717-11723

Mutational analysis of conserved domains within the cytoplasmic tail of gp41 from human immunodeficiency virus type 1: Effects on glycoprotein incorporation and infectivity

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; GLYCOPROTEIN GP 41;

EID: 0034467955     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.74.24.11717-11723.2000     Document Type: Article
Times cited : (63)

References (38)
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  • 13
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    • Domains of the human immunodeficiency virus type 1 matrix and gp41 cytoplasmic tail required for envelope incorporation into virions
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    • Freed, E.O.1    Martin, M.A.2
  • 14
    • 0028819071 scopus 로고
    • Virion incorporation of envelope glycoproteins with long but not short cytoplasmic tails is blocked by specific, single amino acid substitutions in the human immunodeficiency virus type 1 matrix
    • (1995) J. Virol. , vol.69 , pp. 1984-1989
    • Freed, E.O.1    Martin, M.A.2
  • 17
    • 0003321617 scopus 로고    scopus 로고
    • gp41, a multifunctional protein involved in HIV entry and pathogenesis
    • B. Korber, B. Hahn, B. Foley, J. W. Mellors, T. Leitner, G. Myers, F. McCutchan, and C. L. Kuiken (ed.), Human retroviruses and AIDS 1997: a compilation and analysis of nucleic acid and amino acid sequences. Theoretical Biology and Biophysics Group, Los Alamos National Laboratory, Los Alamos, N.Mex.
    • (1997)
    • Hunter, E.1
  • 33
  • 35
    • 0026741425 scopus 로고
    • Retained in vitro infectivity and cytopathogenicity of HIV-1 despite truncation of the C-terminal tail of the env gene product
    • (1992) Virology , vol.189 , pp. 167-177
    • Wilk, T.1    Pfeiffer, T.2    Bosch, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.