The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β1−40 peptide-Reference-Cited by-同舟云学术

The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β1−40 peptide

Published:2011-12-18 Issue:1 Volume:19 Page:79-83
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Narayan Priyanka,Orte Angel,Clarke Richard W,Bolognesi Benedetta,Hook Sharon,Ganzinger Kristina A,Meehan Sarah,Wilson Mark R,Dobson Christopher M,Klenerman David

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.2191.pdf

Reference44 articles.

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2. Bucciantini, M. et al. Prefibrillar amyloid protein aggregates share common features of cytotoxicity. J. Biol. Chem. 279, 31374–31382 (2004).

3. Cleary, J.P. et al. Natural oligomers of the amyloid-β protein specifically disrupt cognitive function. Nat. Neurosci. 8, 79–84 (2005).

4. Lesné, S. et al. A specific amyloid-β protein assembly in the brain impairs memory. Nature 440, 352–357 (2006).

5. Selkoe, D.J. Soluble oligomers of the amyloid-β protein impair synaptic plasticity and behavior. Behav. Brain Res. 192, 106–113 (2008).

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