The B1 Subunit of the H+ATPase Is a PDZ Domain-binding Protein
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference39 articles.
1. Protein trafficking and polarity in kidney epithelium: from cell biology to physiology
2. A C-terminal motif found in the 2-adrenergic receptor, P2Y1 receptor and cystic fibrosis transmembrane conductance regulator determines binding to the Na+/H+ exchanger regulatory factor family of PDZ proteins
3. The β2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange
4. Cloning and Characterization of Postsynaptic Density 93, a Nitric Oxide Synthase Interacting Protein
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1. Pendrin abundance, subcellular distribution, and function are unaffected by either αENaC gene ablation or by increasing ENaC channel activity;Pflügers Archiv - European Journal of Physiology;2023-03-29
2. Evidence for the involvement of branchial Vacuolar-type H+-ATPase in the acidification of the external medium by the West African lungfish, Protopterus annectens, exposed to ammonia-loading conditions;Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology;2022-11
3. The H+-ATPase (V-ATPase): from proton pump to signaling complex in health and disease;American Journal of Physiology-Cell Physiology;2021-03-01
4. Emerging insights on the role of V‐ATPase in human diseases: Therapeutic challenges and opportunities;Medicinal Research Reviews;2021-01-23
5. In vivo crystals reveal critical features of the interaction between cystic fibrosis transmembrane conductance regulator (CFTR) and the PDZ2 domain of Na+/H+ exchange cofactor NHERF1;Journal of Biological Chemistry;2020-04
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