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THERMAL INSTABILITY OF ΔF508 CFTR CHANNEL FUNCTION: PROTECTION BY SINGLE SUPPRESSOR MUTATIONS AND INHIBITING CHANNEL ACTIVITY
Deletion of Phe508 from CFTR results in a temperature-sensitive folding defect that impairs protein maturation and chloride channel function. Both of these adverse effects, however, can be mitigated to varying extents by second-site, suppressor mutations. To better understand the impact of second-si...
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| Huvudupphovsmän: | , , , , |
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| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
2012
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3402225/ https://ncbi.nlm.nih.gov/pubmed/22680785 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi300018e |
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