Evidence map›Paper›PMID 15971080›Full record

ArticlePflugers Archiv : European journal of physiology2005

Homo- and heteromeric assembly of TRP channel subunits.

Michael Schaefer

Abstract read
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In one paragraph

Article in Pflugers Archiv : European journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

58 citing papers in PubMed, 141 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. TRPV3 Ion Channel: From Gene to Pharmacology.International journal of molecular sciences · 2023
    Review
  5. Review
  6. Article
  7. Ion channels alterations in the forebrain of high-fat diet fed rats.European journal of histochemistry : EJH · 2021
    Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. Sensitization of small-diameter sensory neurons is controlled by TRPV1 and TRPA1 association.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  14. Review
  15. Review
  16. Review
  17. A focus on extracellular CaExperimental & molecular medicine · 2017
    Review
  18. Article
  19. Review
  20. Mustard vesicant-induced lung injury: Advances in therapy.Toxicology and applied pharmacology · 2016
    Review
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

1 author at 1 institution in 2 countries.

Michael SchaeferInstitut für Pharmakologie, Charité, Universitätsmedizin Berlin, Campus Benjamin Franklin, Thielallee 67-73, 14195 Berlin, Germany. m.schaefer@charite.de
Franklin University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mammalian homologues of the Drosophila melanogaster transient receptor potential (TRP) channels are the second largest cation channel family within the superfamily of hexahelical cation channels. Most mammalian TRP channels function as homooligomers and mediate mono- or divalent cation entry upon activation by a variety of stimuli. Because native TRP channels may be multimeric proteins of possibly complex composition, it is difficult to compare cation conductances in native tissues to those of clearly defined homomeric TRP channel complexes in living cells. Therefore, the possibility of heteromeric TRP channel assembly has been investigated in recent years by several groups. As a major conclusion of these studies, most heteromeric TRP channel complexes appear to consist of subunit combinations only within relatively narrow confines of phylogenetic subfamilies. Although the general capability of heteromer formation between closely related TRP channel subunits is now clearly established, we are only beginning to understand whether these heteromeric complexes are of physiological significance. This review summarizes the current knowledge on the promiscuity and specificity of the assembly of channel complexes composed of TRPC-, TRPV- and TRPM-subunits of mammalian TRP channels.

Indexed as

AnimalsDrosophila melanogasterFluorescence Resonance Energy TransferHumansPhylogenyProtein Structure, QuaternaryTransient Receptor Potential ChannelsTRPC Cation ChannelsTRPM Cation ChannelsTRPV Cation ChannelsTransient Receptor Potential ChannelsTRPC Cation ChannelsTRPM Cation ChannelsTRPV Cation Channels

Identifiers

PMID15971080
OpenAlexW2073214440

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.