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Structural basis of closed groove scrambling by a TMEM16 protein

bioRxiv (Cold Spring Harbor Laboratory)(2023)10.1101/2023.08.11.553029Source: DataRank Database

Structural basis of closed groove scrambling by a TMEM16 protein is a research paper published in bioRxiv (Cold Spring Harbor Laboratory) (2023). On theSindex it has a DataRank of 0. It has been cited 1 time.

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Enrichment:Funding (4 grants)OA: greenTopics (30)IDs (PubMed, OpenAlex)

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Authors (3)

Omar E. Alvarenga ORCID,Alessio Accardi ORCID,Zhang Feng ORCID

Live enrichment

PubMed:37609346 OpenAlex:https://openalex.org/W4385785468

National Institutes of Health

Grant: 5R01GM106717-06

Ca2+-dependent lipid scrambling and ion transport by TMEM16 proteins

National Institutes of Health

Grant: 1R35GM152012-01

Structure and function of chloride channels, transporters and scramblases

National Science Foundation

Grant: 1746886

Graduate Research Fellowship Program (GRFP)

National Institutes of Health

Grant: 7P41GM103310-14

National Resource for Automated Molecular Microscopy

greenLicense: cc-by-nc-nd

repositoryhttps://www.biorxiv.org/content/biorxiv/early/2023/08/12/2023.08.11.553029.full.pdf

publisherhttps://syndication.highwire.org/content/doi/10.1101/2023.08.11.553029

repositoryhttps://doi.org/10.1101/2023.08.11.553029

repositoryhttps://pubmed.ncbi.nlm.nih.gov/37609346

Fields of Study

Erythrocyte Function and PathophysiologyCaveolin-1 and cellular processesCellular transport and secretion0301 basic medicine03 medical and health sciences

Keywords

Groove (engineering)PhosphatidylserinePhospholipid scramblaseBiophysicsScramblingHelix (gastropod)ChemistryCrystallographyCell biologyBiologyBiochemistryMembraneComputer sciencePhospholipidMaterials scienceModels, MolecularProtein ConformationCryoelectron MicroscopyAnoctaminsHumansCalciumPhosphatidylserinesPhospholipid Transfer ProteinsArticleProtein Binding