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Localized structural fluctuations promote amyloidogenic conformations in transthyretin
The process of transthyretin (TTR) misfolding and aggregation, including amyloid formation, appears to cause a number of degenerative diseases. During amyloid formation, the native protein undergoes a tetramer-to-folded monomer transition, followed by local unfolding of the monomer to an assembly-co...
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| Hlavní autoři: | , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2013
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3594634/ https://ncbi.nlm.nih.gov/pubmed/23318953 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2013.01.008 |
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