Impaired Cu–Zn Superoxide Dismutase (SOD1) and Calcineurin (Cn) Interaction in ALS: A Presumed Consequence for TDP-43 and Zinc Aggregation in Tg SOD1G93A Rodent Spinal Cord Tissue
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Title
Impaired Cu–Zn Superoxide Dismutase (SOD1) and Calcineurin (Cn) Interaction in ALS: A Presumed Consequence for TDP-43 and Zinc Aggregation in Tg SOD1G93A Rodent Spinal Cord Tissue
Authors
Keywords
ALS, TDP-43, SOD1<sup>G93A</sup>, Calcineurin, Spinal cord
Journal
NEUROCHEMICAL RESEARCH
Volume -, Issue -, Pages -
Publisher
Springer Nature
Online
2018-01-04
DOI
10.1007/s11064-017-2461-z
References
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Note: Only part of the references are listed.- The Role of Metal Binding in the Amyotrophic Lateral Sclerosis-Related Aggregation of Copper-Zinc Superoxide Dismutase
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- The ALS-Associated Mutation G93A in Human Copper-Zinc Superoxide Dismutase Selectively Destabilizes the Remote Metal Binding Region
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