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Hsp70 inhibits the nucleation and elongation of tau and sequesters tau aggregates with high affinity

Abstract:

As a key player of the protein quality control network of the cell, the molecular chaperone Hsp70 inhibits the aggregation of the amyloid protein tau. To date, the mechanism of this inhibition and the tau species targeted by Hsp70 remain unknown. This is partly due to the inherent difficulty of studying amyloid aggregates because of their heterogeneous and transient nature. Here, we used ensemble and single-molecule fluorescence measurements to dissect how Hsp70 counteracts the self-assembly ...

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Publication status:
Published
Peer review status:
Peer reviewed

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Role:
Author
ORCID:
0000-0001-5013-0004
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Role:
Author
ORCID:
0000-0003-1675-0773
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Role:
Author
ORCID:
0000-0002-1204-5340
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Role:
Author
ORCID:
0000-0002-7020-9366
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Name:
Medical Research Council
Grant:
UKDRI-2003
Publisher:
American Chemical Society
Journal:
ACS Chemical Biology More from this journal
Volume:
13
Issue:
3
Pages:
636-646
Publication date:
2018-01-04
Acceptance date:
2018-01-04
DOI:
EISSN:
1554-8937
ISSN:
1554-8929
Pmid:
29300447
Language:
English
Keywords:
Pubs id:
pubs:867843
UUID:
uuid:244218a5-9f23-472d-96c9-04eff107014c
Local pid:
pubs:867843
Source identifiers:
867843
Deposit date:
2019-06-11

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