Amphipathic domains in the C terminus of the transmembrane protein (gp41) permeabilize HIV-1 virions: A molecular mechanism underlying natural endogenous reverse transcription

Proceedings of the National Academy of Sciences of the United States of America

Volumn 93, Issue 22, 1996, Pages 12519-12524

  Zhang, Hui ^a   Dornadula, Geethanjali ^a   Alur, Prasad ^a   Laughlin, Mark A ^a   Pomerantz, Roger J ^a  

^a THOMAS JEFFERSON UNIVERSITY   (United States)

Author keywords

deoxyribonucleoside triphosphates; lentivirus lytic peptide; polyamines; reverse transcription inhibitors

Indexed keywords

2',3' DIDEOXYTHYMIDINE TRIPHOSPHATE; GLYCOPROTEIN GP 41; VIRUS DNA; ZIDOVUDINE 5' TRIPHOSPHATE;

CONFERENCE PAPER; DRUG PENETRATION; HUMAN IMMUNODEFICIENCY VIRUS 1; MEMBRANE PERMEABILITY; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; PROTEIN TRANSPORT; VIRUS ENVELOPE; VIRUS TRANSCRIPTION; VIRUS TRANSMISSION;

DNA VIRUSES; HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1; LENTIVIRUS;

EID: 0029970774     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.93.22.12519     Document Type: Article

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