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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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| 主要な著者: | , , , , , , , , , , , , |
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| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
American Society for Microbiology
2002
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| 主題: | |
| オンライン・アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC136400/ https://ncbi.nlm.nih.gov/pubmed/12097589 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/JVI.76.15.7760-7776.2002 |
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