Toxicity of Protein Oligomers Is Rationalized by a Function Combining Size and Surface Hydrophobicity-Reference-Cited by-同舟云学术

Toxicity of Protein Oligomers Is Rationalized by a Function Combining Size and Surface Hydrophobicity

Published:2014-08-11 Issue:10 Volume:9 Page:2309-2317
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Mannini Benedetta¹,Mulvihill Estefania¹,Sgromo Caterina¹,Cascella Roberta¹,Khodarahmi Reza²,Ramazzotti Matteo¹,Dobson Christopher M.³,Cecchi Cristina¹,Chiti Fabrizio¹

Affiliation:

1. Department of Biomedical Experimental and Clinical Sciences, Section of Biochemistry, University of Florence, 50134 Florence, Italy

2. Medical Biology Research Center, Kermanshah University of Medical Sciences, Kermanshah, Iran

3. Department of Chemistry, University of Cambridge, CB2 1EW Cambridge, United Kingdom

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/cb500505m

Reference33 articles.

1. Protein Misfolding, Functional Amyloid, and Human Disease

2. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

3. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

4. Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein

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