Small Heat-shock Proteins Prevent α-Synuclein Aggregation via Transient Interactions and Their Efficacy Is Affected by the Rate of Aggregation-Reference-Cited by-同舟云学术

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Small Heat-shock Proteins Prevent α-Synuclein Aggregation via Transient Interactions and Their Efficacy Is Affected by the Rate of Aggregation

Published:2016-10 Issue:43 Volume:291 Page:22618-22629
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Cox Dezerae,Selig Emily,Griffin Michael D.W.,Carver John A.,Ecroyd Heath

Funder

National Health and Medical Research Council

Australian Research Council

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference92 articles.

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2. Stabilization of α-synuclein secondary structure upon binding to synthetic membranes;Davidson;J. Biol. Chem,1998

3. Regulation of phospholipase D2: selective inhibition of mammalian phospholipase D isoenzymes by α- and β-synucleins;Jenco;Biochemistry,1998

4. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded;Weinreb;Biochemistry,1996

5. Why are “natively unfolded” proteins unstructured under physiologic conditions?;Uversky;Proteins Struct. Funct. Bioinformat,2000

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