Associated Papers
Analysis of CLCNKB mutations at dimer-interface, calcium-binding site, and pore reveals a variety of functional alterations in ClC-Kb channel leading to Bartter syndrome.
Bignon Y et al.
Human Mutation, 2020
Functional Study of Novel Bartter's Syndrome Mutations in ClC-Kb and Rescue by the Accessory Subunit Barttin Toward Personalized Medicine.
Sahbani D et al.
Frontiers in Pharmacology, 2020
Learning Physiology From Inherited Kidney Disorders.
van der Wijst J et al.
Physiological Reviews, 2019
Carboxyl-terminal Truncations of ClC-Kb Abolish Channel Activation by Barttin Via Modified Common Gating and Trafficking.
Stölting G et al.
The Journal of Biological Chemistry, 2015
Genomic epidemiology of blood pressure salt sensitivity.
Kelly TN et al.
Journal of Hypertension, 2012
Physiology and pathophysiology of ClC-K/barttin channels.
Fahlke C et al.
Frontiers in Physiology, 2010
Molecular mechanisms of Bartter syndrome caused by mutations in the BSND gene.
Hayama A et al.
Histochemistry and Cell Biology, 2003
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