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Disulfide Bond That Constrains the HIV-1 gp120 V3 Domain Is Cleaved by Thioredoxin
A functional disulfide bond in both the HIV envelope glycoprotein, gp120, and its immune cell receptor, CD4, is involved in viral entry, and compounds that block cleavage of the disulfide bond in these proteins inhibit HIV entry and infection. The disulfide bonds in both proteins are cleaved at the...
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| Главные авторы: | , , , , |
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| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
American Society for Biochemistry and Molecular Biology
2010
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3000989/ https://ncbi.nlm.nih.gov/pubmed/20943653 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M110.185371 |
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