ArticleMolecular and cellular biochemistry2003
Genetic characterization of a new splice variant of the beta2 subunit of the voltage-dependent calcium channel.
Article in Molecular and cellular biochemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed, 6 citations in OpenAlex.
- The calcium channel beta2 (CACNB2) subunit repertoire in teleosts.BMC molecular biology · 2008Article
- Structures of the murine genes for the beta1- and beta4-subunits of the voltage-dependent calcium channel.Journal of molecular neuroscience : MN · 2003Article
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
No grant is acknowledged in the PubMed record.
Abstract
This study reports a novel splice variant form of the voltage-dependent calcium channel beta2 subunit (beta2g). This variant is composed of the conserved amino-terminal sequences of the beta2a subunit, but lacks the beta-subunit interaction domain (BID), which is thought essential for interactions with the alpha1 subunit. Gene structure analysis revealed that this gene was composed of 13 translated exons spread over 107 kb of the genome. The gene structure of the beta2 subunit was similar in exon-intron organization to the murine beta3 and human beta4 subunits. Electrophysiological evaluation revealed that beta2a and 2g affected channel properties in different ways. The beta2a subunit increased the peak amplitude, but failed to increase channel inactivation, while beta2g had no significant effects on either the peak current amplitude or channel inactivation. Other beta3 subunits, such as beta3 and beta4, significantly increased the peak current and accelerated current inactivation.
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.