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Intermolecular disulfide bonds are not required for the expression of the dimeric state and functional activity of the transferrin receptor.
The human transferrin receptor is expressed as a disulfide-linked dimer at the cell surface. The sites of intermolecular disulfide bonds are Cys-89 and Cys-98. We have examined the functional significance of the covalent dimeric structure of the transferrin receptor by substitution of Cys-89 and Cys...
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| Gepubliceerd in: | EMBO J |
|---|---|
| Hoofdauteurs: | , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
Nature Publishing Group
1989
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC401153/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2507316/ https://ncbi.nlm.nih.govhttps://doi.org/10.1002/j.1460-2075.1989.tb08347.x |
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