ReviewPhysiological reviews2010
The ß subunit of voltage-gated Ca2+ channels.
Review in Physiological reviews, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 243 papers, 1 of them a synthesis that pooled it.
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
243 citing papers in PubMed, 1 synthesis or guideline pooled it.
- N-Type Ca Channel in Epileptic Syndromes and Epilepsy: A Systematic Review of Its Genetic Variants.International journal of molecular sciences · 2023Pooled it
- A brief guideline for the studies of structure-function relationship of ion channels using AlphaFold3.Fundamental research · 2026Review
- Sudden death-associated KCNH2 variants exert opposing effects on a nuclear subdomain of the cardiac potassium channel hERG1.The Journal of biological chemistry · 2026Article
- Molecular Partners of Voltage-Gated Calcium Channel β and αThe Journal of membrane biology · 2026Review
- N-terminal truncating variants in CACNB1 cause a new congenital muscular disorder.European journal of human genetics : EJHG · 2026Article
- Human neuronal networks on micro-electrode arrays as a tool to assess genotype-phenotype correlation in CACNA1A-related disorders.Stem cell reports · 2026Article
- Age-related changes in calcium ion influx and efflux capacity of human dermal fibroblasts.Cell communication and signaling : CCS · 2026Article
- Identification of Hub Neutrophil Coexpressed Genes in Acute PancreatitisEndocrine, metabolic & immune disorders drug targets · 2026Article
- Unveiling β Subunit-Dependent Gating Defects in CaNeuroscience bulletin · 2026Article
- Article
- AHeartRhythm case reports · 2025Article
- Noise-Induced Hearing Loss Enhances CaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2025Article
- Interactive Role of the DHPR βBiomolecules · 2025Article
- A Pharmacological Perspective on Targeting the Voltage-Gated Calcium Channel Subunit αNeurochemical research · 2025Review
- CaMKII clusters neuronal LTCCs in biomolecular condensates to gate excitation-transcription coupling.bioRxiv : the preprint server for biology · 2025Article
- Modulating ion channels with nanobodies.Synthetic and systems biotechnology · 2025Review
- Mapping the interaction surface between CaNature communications · 2025Article
- Electrosome assembly: Structural insights from high voltage-activated calcium channel (CaV)-chaperone interactions.Biochemical Society transactions · 2025Review
- Inhibition of NMDA receptors and other ion channel types by membrane-associated drugs.Frontiers in pharmacology · 2025Review
- The membrane-associated β2e-subunit of voltage-gated calcium channels translocates to the nucleus and regulates gene expression.Frontiers in physiology · 2025Article
183 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Calcium regulates a wide spectrum of physiological processes such as heartbeat, muscle contraction, neuronal communication, hormone release, cell division, and gene transcription. Major entryways for Ca(2+) in excitable cells are high-voltage activated (HVA) Ca(2+) channels. These are plasma membrane proteins composed of several subunits, including α(1), α(2)δ, β, and γ. Although the principal α(1) subunit (Ca(v)α(1)) contains the channel pore, gating machinery and most drug binding sites, the cytosolic auxiliary β subunit (Ca(v)β) plays an essential role in regulating the surface expression and gating properties of HVA Ca(2+) channels. Ca(v)β is also crucial for the modulation of HVA Ca(2+) channels by G proteins, kinases, and the Ras-related RGK GTPases. New proteins have emerged in recent years that modulate HVA Ca(2+) channels by binding to Ca(v)β. There are also indications that Ca(v)β may carry out Ca(2+) channel-independent functions, including directly regulating gene transcription. All four subtypes of Ca(v)β, encoded by different genes, have a modular organization, consisting of three variable regions, a conserved guanylate kinase (GK) domain, and a conserved Src-homology 3 (SH3) domain, placing them into the membrane-associated guanylate kinase (MAGUK) protein family. Crystal structures of Ca(v)βs reveal how they interact with Ca(v)α(1), open new research avenues, and prompt new inquiries. In this article, we review the structure and various biological functions of Ca(v)β, with both a historical perspective as well as an emphasis on recent advances.
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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.