ArticleThe Journal of biological chemistry2011
Constraint-based, homology model of the extracellular domain of the epithelial Na+ channel α subunit reveals a mechanism of channel activation by proteases.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
50 citing papers in PubMed, 71 citations in OpenAlex.
- Epithelial NaComprehensive Physiology · 2024Review
- Role of αENaC in root resorption of adjacent teeth due to entirely impacted mandibular third molars.BMC oral health · 2024Article
- The Epithelial Sodium Channel-An Underestimated Drug Target.International journal of molecular sciences · 2023Review
- The epithelial sodium channel in inflammation and blood pressure modulation.Frontiers in cardiovascular medicine · 2023Review
- Epithelial Sodium Channel Alpha Subunit (αENaC) Is Associated with Inverse Salt Sensitivity of Blood Pressure.Biomedicines · 2022Article
- The Effect of Dynasore Upon the Negative Interaction Between ENaC and CFTR Channels in Xenopus laevis Oocytes.The Journal of membrane biology · 2022Article
- Activation by cleavage of the epithelial NaeLife · 2022Article
- Hypertension: Do Inflammation and Immunity Hold the Key to Solving this Epidemic?Circulation research · 2021Review
- Regulating ENaC's gate.American journal of physiology. Cell physiology · 2020Review
- Murine epithelial sodium (NaThe Journal of biological chemistry · 2019Article
- New insights regarding epithelial Na+ channel regulation and its role in the kidney, immune system and vasculature.Current opinion in nephrology and hypertension · 2019Review
- Thumb domains of the three epithelial NaThe Journal of biological chemistry · 2018Article
- The epithelial NaThe Journal of biological chemistry · 2018Article
- Conserved cysteines in the finger domain of the epithelial NaThe Journal of biological chemistry · 2018Article
- Liddle Syndrome: Review of the Literature and Description of a New Case.International journal of molecular sciences · 2018Review
- N-linked glycans are required on epithelial NaAmerican journal of physiology. Renal physiology · 2018Article
- Epithelial NaAnnual review of physiology · 2018Review
- The Epithelial Sodium Channel Is a Modifier of the Long-Term Nonprogressive Phenotype Associated with F508del CFTR Mutations.American journal of respiratory cell and molecular biology · 2017Article
- Interactions between intersubunit transmembrane domains regulate the chaperone-dependent degradation of an oligomeric membrane protein.The Biochemical journal · 2017Article
- TNF Lectin-Like Domain Restores Epithelial Sodium Channel Function in Frameshift Mutants Associated with Pseudohypoaldosteronism Type 1B.Frontiers in immunology · 2017Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
The epithelial Na(+) channel (ENaC) mediates Na(+) transport across high resistance epithelia. This channel is assembled from three homologous subunits with the majority of the protein's mass found in the extracellular domains. Acid-sensing ion channel 1 (ASIC1) is homologous to ENaC, but a key functional domain is highly divergent. Here we present molecular models of the extracellular region of α ENaC based on a large data set of mutations that attenuate inhibitory peptide binding in combination with comparative modeling based on the resolved structure of ASIC1. The models successfully rationalized the data from the peptide binding screen. We engineered new mutants that had not been tested based on the models and successfully predict sites where mutations affected peptide binding. Thus, we were able to confirm the overall general fold of our structural models. Further analysis suggested that the α subunit-derived inhibitory peptide affects channel gating by constraining motions within two major domains in the extracellular region, the thumb and finger domains.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.