ReviewEuropean biophysics journal : EBJ2009
The voltage-gated calcium-channel beta subunit: more than just an accessory.
Review in European biophysics journal : EBJ, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed.
- Elucidating the role ofFrontiers in immunology · 2025Article
- The Yin and Yang of Breast Cancer: Ion Channels as Determinants of Left-Right Functional Differences.International journal of molecular sciences · 2023Article
- Co-Silencing of the Voltage-Gated Calcium Channel β Subunit and High-Voltage Activated αInternational journal of molecular sciences · 2022Article
- Regulatory mechanisms of ryanodine receptor/CaJournal of muscle research and cell motility · 2021Review
- Structure and Function of the Human Ryanodine Receptors and Their Association with Myopathies-Present State, Challenges, and Perspectives.Molecules (Basel, Switzerland) · 2020Review
- Excitation-contraction coupling in skeletal muscle: recent progress and unanswered questions.Biophysical reviews · 2020Review
- Conformational ensembles of non-peptide ω-conotoxin mimetics and CaComputational and structural biotechnology journal · 2020Article
- Fluorescence Resonance Energy Transfer-based Structural Analysis of the Dihydropyridine Receptor α1S Subunit Reveals Conformational Differences Induced by Binding of the β1a Subunit.The Journal of biological chemistry · 2016Article
- Troponin T3 regulates nuclear localization of the calcium channel Cavβ1a subunit in skeletal muscle.Experimental cell research · 2015Article
- Article
- β1a490-508, a 19-residue peptide from C-terminal tail of Cav1.1 β1a subunit, potentiates voltage-dependent calcium release in adult skeletal muscle fibers.Biophysical journal · 2014Article
- A shortcut to a skeletal muscle DHPR knock-in?The Journal of physiology · 2011Article
- Functional coupling of Rab3-interacting molecule 1 (RIM1) and L-type Ca2+ channels in insulin release.The Journal of biological chemistry · 2011Article
- Functional expression of transgenic 1sDHPR channels in adult mammalian skeletal muscle fibres.The Journal of physiology · 2011Article
- The β(1a) subunit of the skeletal DHPR binds to skeletal RyR1 and activates the channel via its 35-residue C-terminal tail.Biophysical journal · 2011Article
- The N terminus of a schistosome beta subunit regulates inactivation and current density of a Cav2 channel.The Journal of biological chemistry · 2010Article
- Forward trafficking of ion channels: what the clinician needs to know.Heart rhythm · 2010Review
- Calcium channel functions in pain processing.Channels (Austin, Tex.)Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Voltage-gated Ca(2+) channels (VGCCs) are involved in a number of excitatory processes in the cell that regulate muscle contraction, neurotransmitter release, gene regulation, and neuronal migration. They consist of a central pore-forming alpha(1) subunit together with a number of associated auxiliary subunits including a cytoplasmic beta subunit. With the aid of X-ray crystallography, it has been found that the beta subunits of VGCCs (beta(2a), beta(3), and beta(4)) interact strongly with the I-II loop of the pore-forming alpha(1) subunit. Here we discuss the potential interaction sites of beta(1a) with its alpha(1) subunit as well as the skeletal ryanodine receptor. We suggest that not only can beta(1a) interact with the alpha(1) subunit I-II loop, but more subtle interactions may be possible through the II-III loop via the beta(1a) SH3 domain. Such findings could have important implications with respect to EC coupling.
Indexed as
Identifiers
19455319What 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.