Evidence map›Paper›PMID 31892199›Full record

ReviewCells2019

Structure-Function Relationship and Physiological Roles of Transient Receptor Potential Canonical (TRPC) 4 and 5 Channels.

Jinsung Kim, Juyeon Ko, Chansik Hong, Insuk So

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.8field-weighted citation impact, top 33% 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

10 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Thermosensing ability of TRPC5: current knowledge and unsettled questions.The journal of physiological sciences : JPS · 2024
    Review
  4. Review
  5. Article
  6. The odyssey of the TR(i)P journey to the cellular membrane.Frontiers in cell and developmental biology · 2024
    Review
  7. Article
  8. Review
  9. Article
  10. 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

4 authors at 2 institutions in 1 country.

Jinsung KimDepartment of Physiology, College of Medicine, Seoul National University, Seoul 03080, Korea.ORCID 0000-0001-5135-3699
Juyeon KoDepartment of Physiology, College of Medicine, Seoul National University, Seoul 03080, Korea.
Chansik HongDepartment of Physiology, College of Medicine, Chosun University, Gwangju 61452, Korea.
Insuk SoDepartment of Physiology, College of Medicine, Seoul National University, Seoul 03080, Korea.
Seoul National University · KRChosun University · KR

Funding

Ministry of Science, ICT, and Future Planing (MSIP) of the Korean Government 2018R1A4A1023822Seoul National University Hospital Education and Research Encouragement Fund
6 · The paper itself

Abstract

The study of the structure-function relationship of ion channels has been one of the most challenging goals in contemporary physiology. Revelation of the three-dimensional (3D) structure of ion channels has facilitated our understanding of many of the submolecular mechanisms inside ion channels, such as selective permeability, voltage dependency, agonist binding, and inter-subunit multimerization. Identifying the structure-function relationship of the ion channels is clinically important as well since only such knowledge can imbue potential therapeutics with practical possibilities. In a sense, recent advances in the understanding of the structure-relationship of transient receptor potential canonical (TRPC) channels look promising since human TRPC channels are calcium-permeable, non-selective cation channels expressed in many tissues such as the gastrointestinal (GI) tract, kidney, heart, vasculature, and brain. TRPC channels are known to regulate GI contractility and motility, pulmonary hypertension, right ventricular hypertrophy, podocyte injury, seizure, fear, anxiety-like behavior, and many others. In this article, we tried to elaborate recent findings of Cryo-EM (cryogenic-electron microscopy) based structural information of TRPC 4 and 5 channels and domain-specific functions of the channel, such as G-protein mediated activation mechanism, extracellular modification of the channel, homo/hetero-tetramerization, and pharmacological gating mechanisms.

Indexed as

Structure-Activity RelationshipAmino Acid SequenceAnimalsCysteineGTP-Binding ProteinsHumansIon Channel GatingModels, MolecularMultigene FamilyProtein BindingProtein ConformationProtein Interaction Domains and MotifsProtein MultimerizationSesquiterpenes, GuaianeSignal TransductionTRPC Cation ChannelsCysteineenglerin AGTP-Binding ProteinsSesquiterpenes, GuaianeTRPC Cation Channelsstructure–function relationshiptransient receptor potential canonicalTRPC

Identifiers

PMID31892199
PMCPMC7017149
OpenAlexW2997184163

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.