The Effect of Nanoparticles on Amyloid Aggregation Depends on the Protein Stability and Intrinsic Aggregation Rate-Reference-Cited by-同舟云学术

The Effect of Nanoparticles on Amyloid Aggregation Depends on the Protein Stability and Intrinsic Aggregation Rate

Published:2012-01-11 Issue:3 Volume:28 Page:1852-1857
ISSN:0743-7463
Container-title:Langmuir
language:en
Short-container-title:Langmuir

Author:

Cabaleiro-Lago C.¹,Szczepankiewicz O.¹,Linse S.¹

Affiliation:

1. Department of Biochemistry and Structural Biology and ‡Department of Biophysical Chemistry, Center for Molecular Protein Science (CMPS), Lund University, Lund, Sweden

Publisher

American Chemical Society (ACS)

Subject

Electrochemistry,Spectroscopy,Surfaces and Interfaces,Condensed Matter Physics,General Materials Science

Link

https://pubs.acs.org/doi/pdf/10.1021/la203078w

Reference47 articles.

1. Designing conditions for in vitro formation of amyloid protofilaments and fibrils

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3. Protein misfolding, evolution and disease

4. Mutagenic analysis of the nucleation propensity of oxidized Alzheimer's β-amyloid peptide

5. Rationalization of the effects of mutations on peptide andprotein aggregation rates

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