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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...
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| Pubblicato in: | Sci Rep |
|---|---|
| Autori principali: | , , , , , , , , , , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Nature Publishing Group
2017
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| Soggetti: | |
| Accesso online: | 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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