Cargando…
Mutations associated with Dent's disease affect gating and voltage dependence of the human anion/proton exchanger ClC-5
Dent's disease is associated with impaired renal endocytosis and endosomal acidification. It is linked to mutations in the membrane chloride/proton exchanger ClC-5; however, a direct link between localization in the protein and functional phenotype of the mutants has not been established until...
Autor principal: | Alekov, Alexi K. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4436585/ https://www.ncbi.nlm.nih.gov/pubmed/26042048 http://dx.doi.org/10.3389/fphys.2015.00159 |
Ejemplares similares
-
Channel-like slippage modes in the human anion/proton exchanger ClC-4
por: Alekov, Alexi K., et al.
Publicado: (2009) -
The CLC-5 2Cl(−)/H(+) exchange transporter in endosomal function and Dent's disease
por: Lippiat, Jonathan D., et al.
Publicado: (2012) -
Metabolic energy sensing by mammalian CLC anion/proton exchangers
por: Grieschat, Matthias, et al.
Publicado: (2020) -
Barttin Regulates the Subcellular Localization and Posttranslational Modification of Human Cl(-)/H(+) Antiporter ClC-5
por: Wojciechowski, Daniel, et al.
Publicado: (2018) -
Overexpression of the Endosomal Anion/Proton Exchanger ClC-5 Increases Cell Susceptibility toward Clostridium difficile Toxins TcdA and TcdB
por: Ruhe, Frederike, et al.
Publicado: (2017)