Polyalanine expansions drive a shift into α-helical clusters without amyloid-fibril formation

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Polling, Saskia, Ormsby, Angelique R, Wood, Rebecca J, Lee, Kristie, Shoubridge, Cheryl, Hughes, James N, Thomas, Paul Q, Griffin, Michael DW, Hill, Andrew F ORCID: 0000-0001-5581-2354, Bowden, Quill, Böcking, Till and Hatters, Danny M ORCID: 0000-0002-9965-2847 (2015) Polyalanine expansions drive a shift into α-helical clusters without amyloid-fibril formation. Nature Structural and Molecular Biology, 22. pp. 1008-1015. ISSN 1545-9993

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Item type Article
URI https://vuir.vu.edu.au/id/eprint/45588
DOI 10.1038/nsmb.3127
Official URL https://www.nature.com/articles/nsmb.3127
Subjects Current > FOR (2020) Classification > 3207 Medical microbiology
Current > Division/Research > Chancellery
Keywords polyglutamine, human proteins, physiology, proteins, amyloid
Citations in Scopus 33 - View on Scopus
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