A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation-Reference-Cited by-同舟云学术

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A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation

Published:2018-04 Issue: Volume:14 Page:566-575
ISSN:2213-2317
Container-title:Redox Biology
language:en
Short-container-title:Redox Biology

Author:

Marinelli Patrizia,Navarro Susanna,Graña-Montes Ricardo,Bañó-Polo Manuel,Fernández María Rosario,Papaleo Elena,Ventura Salvador

Funder

Spanish Ministry of Economy and Competitiveness

ICREA

Publisher

Elsevier BV

Subject

Organic Chemistry,Biochemistry,Clinical Biochemistry

Reference47 articles.

1. Protein aggregation: mechanisms and functional consequences;Invernizzi;Int. J. Biochem. Cell Biol.,2012

2. Protein Misfolding, Functional Amyloid, and Human Disease;Chiti;Annu. Rev. Biochem.,2006

3. Prevention of amyloid-like aggregation as a driving force of protein evolution;Monsellier;EMBO Rep.,2007

4. Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses;Johnson;Acc. Chem. Res.,2005

5. Thermal stability threshold for amyloid formation in light chain amyloidosis;Poshusta;Int. J. Mol. Sci.,2013

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