Metal-free Superoxide Dismutase-1 and Three Different Amyotrophic Lateral Sclerosis Variants Share a Similar Partially Unfolded β-Barrel at Physiological Temperature

The structure and unfolding of metal-free (apo) human wild-type SOD1 and three pathogenic variants of SOD1 (A4V, G93R, and H48Q) that cause familial amyotrophic lateral sclerosis have been studied with amide hydrogen/deuterium exchange and mass spectrometry. The results indicate that a significant p...

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Bibliographische Detailangaben
Hauptverfasser: Durazo, Armando, Shaw, Bryan F., Chattopadhyay, Madhuri, Faull, Kym F., Nersissian, Aram M., Valentine, Joan Selverstone, Whitelegge, Julian P.
Format: Artigo
Sprache:Inglês
Veröffentlicht: American Society for Biochemistry and Molecular Biology 2009
Schlagworte:
Protein Structure and Folding
Online Zugang:https://ncbi.nlm.nih.gov/pmc/articles/PMC2797206/
https://ncbi.nlm.nih.gov/pubmed/19805550
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.052076
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