Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases-Reference-Cited by-同舟云学术

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Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases

Published:2016-09-13 Issue:1 Volume:6 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Evangelisti Elisa,Cascella Roberta,Becatti Matteo,Marrazza Giovanna,Dobson Christopher M.,Chiti Fabrizio,Stefani Massimo,Cecchi Cristina

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/srep32721.pdf

Reference55 articles.

1. Bemporad, F. & Chiti, F. Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships. Chem. Biol. 19, 315–327 (2012).

2. Martins, I. C. et al. Lipids revert inert Abeta amyloid fibrils to neurotoxic protofibrils that affect learning in mice. EMBO J. 27, 224–233 (2008).

3. Cohen, S. I. et al.Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism. Proc. Natl. Acad. Sci. USA. 110, 9758–9763 (2013).

4. Kinnunen, P. J. K. Amyloid formation on lipid membrane surfaces. Open Biol. J. 2, 163–175 (2009).

5. Lukiw, W. J. Alzheimer’s disease (AD) as a disorder of the plasma membrane. Front Physiol. 4, 24 (2013).

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