Rapid amyloid fibril formation by a winter flounder antifreeze protein requires specific interaction with ice
Author:
Affiliation:
1. Department of Biochemistry and Molecular Biology; Dalhousie University; Halifax Canada
2. Aquatic and Crop Resource Development; National Research Council; Halifax Canada
3. Department of Biology; Dalhousie University; Halifax Canada
Funder
NSERC Discovery Grant
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Reference44 articles.
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5. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis;Kayed;Science,2003
Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Paradoxical effects on ice nucleation are intrinsic to a small winter flounder antifreeze protein;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2024-01
2. An extract of the marine alga Alaria esculenta modulates α-synuclein folding and amyloid formation;Neuroscience Letters;2017-03
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