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Edge Strand Dissociation and Conformational Changes in Transthyretin under Amyloidogenic Conditions
During amyloidogenesis, proteins undergo conformational changes that allow them to aggregate and assemble into insoluble, fibrillar structures. Soluble oligomers that form during this process typically contain 2–24 monomeric subunits and are cytotoxic. Before the formation of these soluble oligomers...
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| Udgivet i: | Biophys J |
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| Main Authors: | , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
The Biophysical Society
2020
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7732750/ https://ncbi.nlm.nih.gov/pubmed/33091379 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpj.2020.08.043 |
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