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The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species.

Abstract:

We have studied the effects of the extracellular molecular chaperone, clusterin, on the in vitro aggregation of mutational variants of human lysozyme, including one associated with familial amyloid disease. The aggregation of the amyloidogenic variant I56T is inhibited significantly at clusterin to lysozyme ratios as low as 1:80 (i.e. one clusterin molecule per 80 lysozyme molecules). Experiments indicate that under the conditions where inhibition of aggregation occurs, clusterin does not bin...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2007.02.095

Authors


Kumita, JR More by this author
Dumoulin, M More by this author
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Journal:
Journal of molecular biology
Volume:
369
Issue:
1
Pages:
157-167
Publication date:
2007-05-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:f1e8b47f-bfeb-48f5-a1a3-bafb639229ef
Source identifiers:
59300
Local pid:
pubs:59300

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