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Structure and topology around the cleavage site regulate post-translational cleavage of the HIV-1 gp160 signal peptide
Like all other secretory proteins, the HIV-1 envelope glycoprotein gp160 is targeted to the endoplasmic reticulum (ER) by its signal peptide during synthesis. Proper gp160 folding in the ER requires core glycosylation, disulfide-bond formation and proline isomerization. Signal-peptide cleavage occur...
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| Gepubliceerd in: | eLife |
|---|---|
| Hoofdauteurs: | , , , , , , , , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
eLife Sciences Publications, Ltd
2017
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5577925/ https://ncbi.nlm.nih.gov/pubmed/28753126 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.7554/eLife.26067 |
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