ReviewFEBS letters2014
Gap junction regulation by calmodulin.
Review in FEBS letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
35 citing papers in PubMed, 60 citations in OpenAlex.
- History of Gap Junction Architecture and Potential Role of Calmodulin in Channel Arrays.International journal of molecular sciences · 2025Review
- Calmodulin D133H Disrupts CaCells · 2025Article
- Cx47 Phosphorylation Exacerbates White Matter Damage and Kainic Acid Induced Epilepsy.CNS neuroscience & therapeutics · 2025Article
- Intracellular CaBiologia futura · 2025Review
- The genetic and molecular basis of a connexin-linked skin disease.The Biochemical journal · 2024Review
- The rectification of heterotypic Cx46/Cx50 gap junction channels depends on intracellular magnesium.Biophysics reports · 2024Article
- Calcium Role in Gap Junction Channel Gating: Direct Electrostatic or Calmodulin-Mediated?International journal of molecular sciences · 2024Review
- Calmodulin: a highly conserved and ubiquitous CaProceedings of the Japan Academy. Series B, Physical and biological sciences · 2024Review
- CaInternational journal of molecular sciences · 2023Article
- CaFrontiers in cellular neuroscience · 2023Article
- Anesthetics and Cell-Cell Communication: Potential CaInternational journal of molecular sciences · 2022Review
- Connexons Coupling to Gap Junction Channel: Potential Role for Extracellular Protein Stabilization Centers.Biomolecules · 2021Article
- Calmodulin-Connexin Partnership in Gap Junction Channel Regulation-Calmodulin-Cork Gating Model.International journal of molecular sciences · 2021Review
- New Insights on the Role of Connexins and Gap Junctions Channels in Adipose Tissue and Obesity.International journal of molecular sciences · 2021Review
- Gap Junction Channelopathies and Calmodulinopathies. Do Disease-Causing Calmodulin Mutants Affect Direct Cell-Cell Communication?International journal of molecular sciences · 2021Review
- Structural Aspects and Prediction of Calmodulin-Binding Proteins.International journal of molecular sciences · 2020Review
- Regulation of Connexin Gap Junctions and Hemichannels by Calcium and Calcium Binding Protein Calmodulin.International journal of molecular sciences · 2020Review
- Article
- Calmodulin Binding to Connexin 35: Specializations to Function as an Electrical Synapse.International journal of molecular sciences · 2020Article
- Calmodulin-Cork Model of Gap Junction Channel Gating-One Molecule, Two Mechanisms.International journal of molecular sciences · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Intracellular Ca(2+) activated calmodulin (CaM) inhibits gap junction channels in the low nanomolar to high micromolar range of [Ca(2+)]i. This regulation plays an essential role in numerous cellular processes that include hearing, lens transparency, and synchronized contractions of the heart. Previous studies have indicated that gap junction mediated cell-to-cell communication was inhibited by CaM antagonists. More recent evidence indicates a direct role of CaM in regulating several members of the connexin family. Since the intracellular loop and carboxyl termini of connexins are largely "invisible" in electron microscopy and X-ray crystallographic structures due to disorder in these domains, peptide models encompassing the putative CaM binding sites of several intracellular domains of connexins have been used to identify the Ca(2+)-dependent CaM binding sites of these proteins. This approach has been used to determine the CaM binding affinities of peptides derived from a number of different connexin-subfamilies.
Indexed as
Identifiers
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.