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Cavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregation
More than a hundred different Transthyretin (TTR) mutations are associated with fatal systemic amyloidoses. They destabilize the protein tetrameric structure and promote the extracellular deposition of TTR as pathological amyloid fibrils. So far, only mutations R104H and T119M have been shown to sta...
Shranjeno v:
| izdano v: | Sci Rep |
|---|---|
| Main Authors: | , , , , , , , , , , , , |
| Format: | Artigo |
| Jezik: | Inglês |
| Izdano: |
Nature Publishing Group
2017
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| Teme: | |
| Online dostop: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5364509/ https://ncbi.nlm.nih.gov/pubmed/28338000 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/srep44709 |
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