Evidence map›Paper›PMID 32560560›Full record

ArticleInternational journal of molecular sciences2020

Mapping of CaM, S100A1 and PIP2-Binding Epitopes in the Intracellular N- and C-Termini of TRPM4.

Kristyna Bousova, Ivan Barvik, Petr Herman, Kateřina Hofbauerová, Lenka Monincova, Pavel Majer, Monika Zouharova, Veronika Vetyskova, Klara Postulkova, Jiri Vondrasek

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.5field-weighted citation impact, top 39% 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

8 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Interaction of Calmodulin with TRPM: An Initiator of Channel Modulation.International journal of molecular sciences · 2023
    Review
  6. Article
  7. Review
  8. 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

10 authors at 3 institutions in 1 country.

Kristyna BousovaInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 2, 16000 Prague, Czech Republic.
Ivan BarvikFaculty of Mathematics and Physics, Charles University, Ke Karlovu 5, 12116 Prague, Czech Republic.
Petr HermanFaculty of Mathematics and Physics, Charles University, Ke Karlovu 5, 12116 Prague, Czech Republic.ORCID 0000-0001-6918-2576
Kateřina HofbauerováFaculty of Mathematics and Physics, Charles University, Ke Karlovu 5, 12116 Prague, Czech Republic.ORCID 0000-0001-7608-793X
Lenka MonincovaInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 2, 16000 Prague, Czech Republic.
Pavel MajerInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 2, 16000 Prague, Czech Republic.
Monika ZouharovaInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 2, 16000 Prague, Czech Republic.
Veronika VetyskovaInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 2, 16000 Prague, Czech Republic.
Klara PostulkovaInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 2, 16000 Prague, Czech Republic.
Jiri VondrasekInstitute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 2, 16000 Prague, Czech Republic.ORCID 0000-0002-6066-973X
Czech Academy of Sciences, Institute of Organic Chemistry and Biochemistry · CZCharles University · CZCzech Academy of Sciences · CZ

Funding

Czech Science Foundation GACR 19-04099SEU Operational Program OP VaVpICZ.1.05/4.1.00/16.0340Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences RVO: 61388963
6 · The paper itself

Abstract

Molecular determinants of the binding of various endogenous modulators to transient receptor potential (TRP) channels are crucial for the understanding of necessary cellular pathways, as well as new paths for rational drug designs. The aim of this study was to characterise interactions between the TRP cation channel subfamily melastatin member 4 (TRPM4) and endogenous intracellular modulators-calcium-binding proteins (calmodulin (CaM) and S100A1) and phosphatidylinositol 4, 5-bisphosphate (PIP

Indexed as

Binding SitesProtein Interaction Domains and MotifsAmino Acid SequenceAquaporinsCalmodulinHumansKineticsModels, MolecularMultiprotein ComplexesPeptide FragmentsProtein BindingProtein ConformationS100 ProteinsStructure-Activity RelationshipTRPM Cation ChannelsAquaporinsCalmodulinMultiprotein ComplexesPeptide FragmentsS100A1 proteinS100 ProteinsTRPM4 protein, humanTRPM Cation Channelsbinding epitopeCaMdockingfluorescence anisotropymolecular dynamics simulationsPIP2S100A1TRPM4 channel

Identifiers

PMID32560560
PMCPMC7352223
OpenAlexW3036010672

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.