Mutations Phe785Leu and Thr618Met in Na+,K+-ATPase, Associated with Familial Rapid-onset Dystonia Parkinsonism, Interfere with Na+ Interaction by Distinct Mechanisms
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference45 articles.
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1. Crystal structures of Na+,K+‐ATPase reveal the mechanism that converts the K+‐bound form to Na+‐bound form and opens and closes the cytoplasmic gate;FEBS Letters;2023-07-06
2. ATP1A3 mutation in rapid-onset dystonia parkinsonism: New data and genotype-phenotype correlation analysis;Frontiers in Aging Neuroscience;2022-08-01
3. Cryo‐electron microscopy of Na + ,K + ‐ ATPase reveals how the extracellular gate locks in the E2 · 2K + state;FEBS Letters;2022-07-06
4. Auditory Neuropathy as the Initial Phenotype for Patients With ATP1A3 c.2452 G > A: Genotype–Phenotype Study and CI Management;Frontiers in Cell and Developmental Biology;2021-10-08
5. Comparative description of the mRNA expression profile of Na + /K + ‐ ATPase isoforms in adult mouse nervous system;Journal of Comparative Neurology;2021-09-15
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