Evidence map›Paper›PMID 12609873›Full record

ArticleBiophysical journal2003

Control of ion conduction in L-type Ca2+ channels by the concerted action of S5-6 regions.

Susan M Cibulsky, William A Sather

Abstract readComparative Study
In one paragraph

Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from 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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Susan M CibulskyDepartment of Pharmacology and Program in Neuroscience, University of Colorado Health Sciences Center, Denver 80262, USA.
William A Sather

Funding

Structural Basis of Ion Selectivity in Calciumn ChannelsR01NS035245 · NINDS · UNIVERSITY OF COLORADO DENVER · PI SATHER, WILLIAM A · 1996 to 2004
$1.2M
CA++ CHANNEL BETA SUBUNITS IN CA++ CHANNEL MODULATIONF31MH011717 · NIMH · UNIVERSITY OF COLORADO DENVER · PI CIBULSKY, SUSAN M · 1997 to 1999
–
NIMH NIH HHS F31 MH011717NIMH NIH HHS MH11717NINDS NIH HHS NS35245NINDS NIH HHS R01 NS035245
6 · The paper itself

Abstract

Voltage-gated L-type Ca(2+) channels from cardiac (alpha(1C)) and skeletal (alpha(1S)) muscle differ from one another in ion selectivity and permeation properties, including unitary conductance. In 110 mM Ba(2+), unitary conductance of alpha(1S) is approximately half that of alpha(1C). As a step toward understanding the mechanism of rapid ion flux through these highly selective ion channels, we used chimeras constructed between alpha(1C) and alpha(1S) to identify structural features responsible for the difference in conductance. Combined replacement of the four pore-lining P-loops in alpha(1C) with P-loops from alpha(1S) reduced unitary conductance to a value intermediate between those of the two parent channels. Combined replacement of four larger regions that include sequences flanking the P-loops (S5 and S6 segments along with the P-loop-containing linker between these segments (S5-6)) conferred alpha(1S)-like conductance on alpha(1C). Likewise, substitution of the four S5-6 regions of alpha(1C) into alpha(1S) conferred alpha(1C)-like conductance on alpha(1S). These results indicate that, comparing alpha(1C) with alpha(1S), the differences in structure that are responsible for the difference in ion conduction are housed within the S5-6 regions. Moreover, the pattern of unitary conductance values obtained for chimeras in which a single P-loop or single S5-6 region was replaced suggest a concerted action of pore-lining regions in the control of ion conduction.

Indexed as

Amino Acid SequenceAnimalsCalcium Channels, L-TypeCells, CulturedElectric ConductivityHeartIon Channel GatingMembrane PotentialsMolecular Sequence DataMuscle, SkeletalMyocardiumOocytesProtein ConformationProtein Structure, TertiaryProtein SubunitsRecombinant Fusion ProteinsCalcium Channels, L-TypeProtein SubunitsRecombinant Fusion ProteinsRecombinant Proteins

Identifiers

PMID12609873
PMCPMC1302740

What OpenQuestion holds

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Registered trials

None linked

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.