Altered voltage‐dependence of slowly activating chloride‐proton antiport by late endosomal ClC‐6 explains distinct neurological disorders
Author:
Affiliation:
1. Institute of Biophysics, CNR Genoa Italy
2. Department of Anatomy and Physiology Kansas State University College of Veterinary Medicine Manhattan Kansas USA
Funder
Associazione Italiana per la Ricerca sul Cancro
Publisher
Wiley
Subject
Physiology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1113/JP282737
Reference41 articles.
1. Not so transport incompetent after all: Revisiting a CLC-7 mutant sheds new mechanistic light on lysosomal physiology
2. Synergism Between Halide Binding and Proton Transport in a CLC-type Exchanger
3. Secondary active transport mediated by a prokaryotic homologue of ClC Cl- channels
4. Separate Ion Pathways in a Cl−/H+ Exchanger
5. ClC-6 and ClC-7 are two novel broadly expressed members of the CLC chloride channel family
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1. Structural basis of pH-dependent activation in a CLC transporter;Nature Structural & Molecular Biology;2024-01-26
2. Distinct ClC‐6 and ClC‐7 Cl− sensitivities provide insight into ClC‐7's role in lysosomal Cl− homeostasis;The Journal of Physiology;2023-11-08
3. Vesicular CLC chloride/proton exchangers in health and diseases;Frontiers in Pharmacology;2023-11-07
4. Molecular basis of ClC-6 function and its impairment in human disease;Science Advances;2023-10-13
5. The chloride antiporter CLCN7 is a modifier of lysosome dysfunction in FIG4 and VAC14 mutants;PLOS Genetics;2023-06-26
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