ArticleBiochemical Society transactions2006
The structural biology of voltage-gated calcium channel function and regulation.
Article in Biochemical Society transactions, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 50 citations in OpenAlex.
- Magnesium Ions as Modulators of Voltage-Gated and Ligand-Gated Ion Channels in Central Neurons.International journal of molecular sciences · 2025Review
- Selective posttranslational inhibition of CaNature communications · 2022Article
- An Improved Method for Modeling Voltage-Gated Ion Channels at Atomic Accuracy Applied to Human CaCell reports · 2018Article
- Proteolytic cleavage of the hydrophobic domain in the CaThe Journal of biological chemistry · 2017Article
- Stapled Voltage-Gated Calcium Channel (CaACS chemical neuroscience · 2017Article
- Zn(2+) at a cellular crossroads.Current opinion in chemical biology · 2016Review
- Apo states of calmodulin and CaBP1 control CaV1 voltage-gated calcium channel function through direct competition for the IQ domain.Journal of molecular biology · 2013Article
- Bivariate genome-wide association analysis of the growth and intake components of feed efficiency.PloS one · 2013Article
- A quartet of leucine residues in the guanylate kinase domain of CaVβ determines the plasma membrane density of the CaV2.3 channel.The Journal of biological chemistry · 2012Article
- The Discovery and Characterization of ML218: A Novel, Centrally Active T-Type Calcium Channel Inhibitor with Robust Effects in STN Neurons and in a Rodent Model of Parkinson's Disease.ACS chemical neuroscience · 2011Article
- Structural basis for the differential effects of CaBP1 and calmodulin on Ca(V)1.2 calcium-dependent inactivation.Structure (London, England : 1993) · 2010Article
- Multiple C-terminal tail Ca(2+)/CaMs regulate Ca(V)1.2 function but do not mediate channel dimerization.The EMBO journal · 2010Article
- The N terminus of a schistosome beta subunit regulates inactivation and current density of a Cav2 channel.The Journal of biological chemistry · 2010Article
- Molecular determinants of the CaVbeta-induced plasma membrane targeting of the CaV1.2 channel.The Journal of biological chemistry · 2010Article
- Calmodulin is a functional regulator of Cav1.4 L-type Ca2+ channels.The Journal of biological chemistry · 2009Article
- Disruption of the IS6-AID linker affects voltage-gated calcium channel inactivation and facilitation.The Journal of general physiology · 2009Article
- Structures of CaV2 Ca2+/CaM-IQ domain complexes reveal binding modes that underlie calcium-dependent inactivation and facilitation.Structure (London, England : 1993) · 2008Article
- Alanine-scanning mutagenesis defines a conserved energetic hotspot in the CaValpha1 AID-CaVbeta interaction site that is critical for channel modulation.Structure (London, England : 1993) · 2008Article
- Review
- Progress in the structural understanding of voltage-gated calcium channel (CaV) function and modulation.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
2 authors at 1 institution in 1 country.
Funding
Abstract
Voltage-gated calcium channels (CaVs) are large (approximately 0.5 MDa), multisubunit, macromolecular machines that control calcium entry into cells in response to membrane potential changes. These molecular switches play pivotal roles in cardiac action potentials, neurotransmitter release, muscle contraction, calcium-dependent gene transcription and synaptic transmission. CaVs possess self-regulatory mechanisms that permit them to change their behaviour in response to activity, including voltage-dependent inactivation, calcium-dependent inactivation and calcium-dependent facilitation. These processes arise from the concerted action of different channel domains with CaV beta-subunits and the soluble calcium sensor calmodulin. Until recently, nothing was known about the CaV structure at high resolution. Recent crystallographic work has revealed the first glimpses at the CaV molecular framework and set a new direction towards a detailed mechanistic understanding of CaV function.
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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.