Oligomeric and Conformational Properties of a Proteolytically Mature, Disulfide-Stabilized Human Immunodeficiency Virus Type 1 gp140 Envelope Glycoprotein

We describe the further properties of a protein, designated SOS gp140, wherein the association of the gp120 and gp41 subunits of the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein is stabilized by an intersubunit disulfide bond. HIV-1(JR-FL) SOS gp140, proteolytically uncleaved gp...

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में प्रकाशित:	J Virol
मुख्य लेखकों:	Schülke, Norbert, Vesanen, Mika S., Sanders, Rogier W., Zhu, Ping, Lu, Min, Anselma, Deborah J., Villa, Anthony R., Parren, Paul W. H. I., Binley, James M., Roux, Kenneth H., Maddon, Paul J., Moore, John P., Olson, William C.
स्वरूप:	Artigo
भाषा:	Inglês
प्रकाशित:	American Society for Microbiology (ASM) 2002
विषय:	Structure and Assembly
ऑनलाइन पहुंच:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC136400/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/12097589/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/JVI.76.15.7760-7776.2002
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