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An Additional Ca2+ Binding Site Allosterically Controls TMEM16A Activation

Cell Reports(2020)10.1016/j.celrep.2020.108570Source: DataRank Database

An Additional Ca2+ Binding Site Allosterically Controls TMEM16A Activation is a research paper published in Cell Reports (2020). On theSindex it has a DataRank of 0. It has been cited 41 times.

N/A

0DataRank · unranked

Scored on demand from live citation data

Open Access41 citations

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›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Pipeline:MetadataData-paper checkEnrichmentCitation networkScoring

Enrichment:Funding (4 grants)Impact (FWCI 1.79)OA: goldTopics (76)IDs (PubMed, OpenAlex)

FAIR Checklist

Context only (not used in score)

Findable (1/2)

Has DOI

Accessible (1/2)

Open Access

Interoperable (0/2)

Reusable (0/3)

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Authors (2)

Huanghe Yang ORCID,Son C. Le ORCID

Live enrichment

PubMed:33378669 OpenAlex:https://openalex.org/W3115634737

National Institutes of Health

Grant: DP2-GM126898

American Heart Association

Grant: 19PRE34380456

National Institutes of Health

Grant: 1DP2GM126898-01

Manipulating TMEM16F lipid scramblase to understand the transbilayer phospholipid transport phenomenon

NIGMS NIH HHS

Grant: DP2 GM126898

FWCI

1.79

Citation Percentile

0.9%

Citation Trend

2021

2022

2023

2024

2025

2026

goldLicense: cc-by-nc-nd

journalhttp://www.cell.com/article/S221112472031559X/pdf

publisherhttp://www.cell.com/article/S221112472031559X/pdf

publisherhttps://api.elsevier.com/content/article/PII:S221112472031559X?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S221112472031559X?httpAccept=text/plain

journalhttps://doi.org/10.1016/j.celrep.2020.108570

Fields of Study

Ion channel regulation and functionIon Transport and Channel RegulationNeuroscience and Neuropharmacology Research0301 basic medicine0303 health sciences03 medical and health sciencesAnoctamin-1Binding SitesCadmiumCalciumCell MembraneChloride ChannelsElectrophysiologyHEK293 CellsHumansIon Channel GatingIon TransportModels, MolecularMutationPhospholipid Transfer ProteinsProtein ConformationProtein Domains

MeSH Terms

Protein DomainsAnoctamin-1Binding SitesCadmiumCalciumCell MembraneElectrophysiologyHumansModels, MolecularMutationProtein ConformationIon Channel GatingIon TransportChloride ChannelsPhospholipid Transfer ProteinsHEK293 Cells

Keywords

Allosteric regulationGatingBinding siteChemistryBiophysicsTransmembrane proteinIntracellularTransmembrane domainBiochemistryCell biologyBiologyReceptorModels, MolecularBinding SitesIon TransportProtein ConformationCell MembraneArticleElectrophysiologyHEK293 CellsProtein DomainsChloride ChannelsMutationHumansCalciumPhospholipid Transfer ProteinsIon Channel GatingAnoctamin-1CadmiumCa(2+) binding sitesCa(2+)-activated chloride channelsCaCCTMEM16allosteric modulationchannel activation and inhibitionchannel gatingphospholipid scramblasestransmembrane protein 16