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Nanoscale inhibition of polymorphic and ambidextrous IAPP amyloid aggregation with small molecules

Understanding how small molecules interface amyloid fibrils on the nanoscale is of importance for developing therapeutic treatment against amyloid-based diseases. Here we show, for the first time, that human islet amyloid polypeptide (IAPP) in the fibrillar form is polymorphic and ambidextrous posse...

詳細記述

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書誌詳細
出版年:Nano Res
主要な著者: Kakinen, Aleksandr, Adamcik, Jozef, Wang, Bo, Ge, Xinwei, Mezzenga, Raffaele, Davis, Thomas P., Ding, Feng, Ke, Pu Chun
フォーマット: Artigo
言語:Inglês
出版事項: 2018
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC6162064/
https://ncbi.nlm.nih.gov/pubmed/30275931
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1007/s12274-017-1930-7
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