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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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Bibliografische gegevens
Hoofdauteurs: Lim, Kwang Hun, Dyson, H. Jane, Kelly, Jeffery W., Wright, Peter E.
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: 2013
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Online toegang: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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