Stability matters, too - the thermodynamics of amyloid fibril formation
Chemical Science, ISSN: 2041-6539, Vol: 13, Issue: 35, Page: 10177-10192
2022
- 49Citations
- 79Captures
- 2Mentions
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Metrics Details
- Citations49
- Citation Indexes49
- 49
- CrossRef34
- Captures79
- Readers79
- 79
- Mentions2
- Blog Mentions1
- Blog1
- News Mentions1
- News1
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Stability matters, too - the thermodynamics of amyloid fibril formation.
Chem Sci. 2022 Sep 14;13(35):10177-10192. Epub 2022 Feb 2 Authors: Buell AK PubMed: 36277637 Submit Comment
Review Description
Amyloid fibrils are supramolecular homopolymers of proteins that play important roles in biological functions and disease. These objects have received an exponential increase in attention during the last few decades, due to their role in the aetiology of a range of severe disorders, most notably some of a neurodegenerative nature. While an overwhelming number of experimental studies exist that investigate how, and how fast, amyloid fibrils form and how their formation can be inhibited, a much more limited body of experimental work attempts to answer the question as to why these types of structures form (i.e. the thermodynamic driving force) and how stable they actually are. In this review, I attempt to give an overview of the types of experiments that have been performed to-date to answer these questions, and to summarise our current understanding of amyloid thermodynamics.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85138835076&origin=inward; http://dx.doi.org/10.1039/d1sc06782f; http://www.ncbi.nlm.nih.gov/pubmed/36277637; https://xlink.rsc.org/?DOI=D1SC06782F; https://dx.doi.org/10.1039/d1sc06782f; https://pubs.rsc.org/en/content/articlelanding/2022/sc/d1sc06782f
Royal Society of Chemistry (RSC)
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