Ligand binding to distinct states diverts aggregation of an amyloid-forming protein-Reference-Cited by-同舟云学术

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Ligand binding to distinct states diverts aggregation of an amyloid-forming protein

Published:2011-08-28 Issue:10 Volume:7 Page:730-739
ISSN:1552-4450
Container-title:Nature Chemical Biology
language:en
Short-container-title:Nat Chem Biol

Author:

Woods Lucy A,Platt Geoffrey W,Hellewell Andrew L,Hewitt Eric W,Homans Steve W,Ashcroft Alison E,Radford Sheena E

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology

Link

http://www.nature.com/articles/nchembio.635.pdf

Reference50 articles.

1. Sipe, J.D. et al. Amyloid fibril protein nomenclature: 2010 recommendations from the nomenclature committee of the International Society of Amyloidosis. Amyloid 17, 101–104 (2010).

2. Chiti, F. & Dobson, C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333–366 (2006).

3. Bernstein, S.L. et al. Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease. Nat. Chem. 1, 326–331 (2009).

4. Glabe, C.G. Structural classification of toxic amyloid oligomers. J. Biol. Chem. 283, 29639–29643 (2008).

5. Necula, M., Kayed, R., Milton, S. & Glabe, C.G. Small molecule inhibitors of aggregation indicate that Aβ oligomerization and fibrillization pathways are independent and distinct. J. Biol. Chem. 282, 10311–10324 (2007).

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