Evidence map›Paper›PMID 23677990›Full record

ArticleThe Journal of biological chemistry2013

Conserved gating elements in TRPC4 and TRPC5 channels.

Andreas Beck, Tilman Speicher, Christof Stoerger, Thomas Sell, Viviane Dettmer, Siti A Jusoh, Ammar Abdulmughni, Adolfo Cavalié, Stephan E Philipp, Michael X Zhu and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.9field-weighted citation impact, top 9% of its field
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

22 citing papers in PubMed, 54 citations in OpenAlex.

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  10. Englerin A-sensing charged residues for transient receptor potential canonical 5 channel activation.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2019
    Article
  11. Structure of the mouse TRPC4 ion channel.Nature communications · 2018
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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

13 authors at 4 institutions in 3 countries.

Andreas BeckExperimentelle und Klinische Pharmakologie und Toxikologie, Universität des Saarlandes, 66421 Homburg, Germany. andreas.beck@uniklinikum-saarland.de
Tilman Speicher
Christof Stoerger
Thomas Sell
Viviane Dettmer
Siti A Jusoh
Ammar Abdulmughni
Adolfo Cavalié
Stephan E Philipp
Michael X Zhu
Volkhard Helms
Ulrich Wissenbach
Veit Flockerzi
Universitätsklinikum des Saarlandes · DESaarland University · DEThe University of Texas Health Science Center at Houston · USUniversiti Teknologi MARA · MY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TRPC4 and TRPC5 proteins share 65% amino acid sequence identity and form Ca(2+)-permeable nonselective cation channels. They are activated by stimulation of receptors coupled to the phosphoinositide signaling cascade. Replacing a conserved glycine residue within the cytosolic S4-S5 linker of both proteins by a serine residue forces the channels into an open conformation. Expression of the TRPC4G503S and TRPC5G504S mutants causes cell death, which could be prevented by buffering the Ca(2+) of the culture medium. Current-voltage relationships of the TRPC4G503S and TRPC5G504S mutant ion channels resemble that of fully activated TRPC4 and TRPC5 wild-type channels, respectively. Modeling the structure of the transmembrane domains and the pore region (S4-S6) of TRPC4 predicts a conserved serine residue within the C-terminal sequence of the predicted S6 helix as a potential interaction site. Introduction of a second mutation (S623A) into TRPC4G503S suppressed the constitutive activation and partially rescued its function. These results indicate that the S4-S5 linker is a critical constituent of TRPC4/C5 channel gating and that disturbance of its sequence allows channel opening independent of any sensor domain.

Indexed as

Amino Acid SubstitutionAnimalsHEK293 CellsHumansIon Channel GatingMiceModels, MolecularMutation, MissensePeptide MappingProtein Structure, SecondaryProtein Structure, TertiaryRatsTRPC Cation ChannelsTRPC4 ion channelTRPC5 protein, humanTrpc5 protein, mouseTrpc5 protein, ratTRPC Cation ChannelsCalcium ImagingCalcium InfluxChannel GatingIon ChannelsPatch ClampSignal TransductionTRP Channels

Identifiers

PMID23677990
PMCPMC3707650
OpenAlexW2014504388

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.