The Toxicity of Misfolded Protein Oligomers Is Independent of Their Secondary Structure-Reference-Cited by-同舟云学术

The Toxicity of Misfolded Protein Oligomers Is Independent of Their Secondary Structure

Published:2019-05-10 Issue:7 Volume:14 Page:1593-1600
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Vivoli Vega Mirella¹,Cascella Roberta¹,Chen Serene W²,Fusco Giuliana³^ORCID,De Simone Alfonso²^ORCID,Dobson Christopher M.³,Cecchi Cristina¹,Chiti Fabrizio¹^ORCID

Affiliation:

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

2. Department of Life Sciences, Imperial College London, London SW7 2AZ, U.K.

3. Centre for Misfolding disease, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.

Funder

Regione Toscana

Progetto Dipartimento di Eccellenza

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acschembio.9b00324

Reference53 articles.

1. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade

2. The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes

3. Amyloid-β Annular Protofibrils Evade Fibrillar Fate in Alzheimer Disease Brain

4. Structure and assembly-disassembly properties of wild-type transthyretin amyloid protofibrils observed with atomic force microscopy

5. Toxic fibrillar oligomers of amyloid- have cross- structure

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