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Structure of an open K ATP channel reveals tandem PIP 2 binding sites mediating the Kir6.2 and SUR1 regulatory interface

bioRxiv (Cold Spring Harbor Laboratory)(2023)10.1101/2023.08.01.551546Source: DataRank Database

Structure of an open K ATP channel reveals tandem PIP 2 binding sites mediating the Kir6.2 and SUR1 regulatory interface is a research paper published in bioRxiv (Cold Spring Harbor Laboratory) (2023). On theSindex it has a DataRank of 0. It has been cited 5 times.

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Open Access5 citations

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datarank_citation_only_1hop_v6· scope data_onlyMethodology

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Enrichment:Funding (3 grants)OA: greenTopics (55)IDs (PubMed, OpenAlex)SDGs (1)

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Findable (1/2)

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Accessible (1/2)

Open Access

Interoperable (0/2)

Reusable (0/3)

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Authors (5)

Yi‐Ying Kuo ORCID,Phillip Zhu ORCID,Assmaa ElSheikh ORCID,Show‐Ling Shyng ORCID,Camden Driggers ORCID

Live enrichment

PubMed:37577494 OpenAlex:https://openalex.org/W4385495396

National Institutes of Health

Grant: 2R01DK066485-13

Structural basis of KATP channel gating

National Institutes of Health

Grant: 5U24GM129547-03

Pacific Northwest Center for Cryo-EM

National Institutes of Health

Grant: 3R01GM145784-02S1

Correlating structure and function in KATP channel isoforms

greenLicense: CC BY

repositoryhttps://www.biorxiv.org/content/biorxiv/early/2023/08/01/2023.08.01.551546.full.pdf

publisherhttps://syndication.highwire.org/content/doi/10.1101/2023.08.01.551546

repositoryhttps://doi.org/10.1101/2023.08.01.551546

repositoryhttps://pubmed.ncbi.nlm.nih.gov/37577494

Fields of Study

RNA Interference and Gene DeliveryRNA Research and SplicingMass Spectrometry Techniques and Applications03 medical and health sciences0303 health sciences

Keywords

TandemKir6.2Interface (matter)Channel (broadcasting)ChemistryComputer scienceMaterials scienceGeneticsBiologyProtein subunitComputer networkGeneBiochemistryCell biologyPathophysiology of Myocardial Reperfusion InjuryScienceMechanical Circulatory Support SystemsBiomedical EngineeringBiophysicsSulfonylurea ReceptorsFOS: Medical engineeringArticlePathology and Forensic MedicineTransmembrane domainBinding siteAdenosine TriphosphateEngineeringKATP ChannelsSulfonylurea receptorHealth SciencesInward-rectifier potassium ion channelDiabetes MellitusHumansATPasePotassium channelPotassium Channels, Inwardly RectifyingBinding SitesATP-Sensitive Potassium ChannelsManagement of Cardiac Arrest and ResuscitationQWalker motifsInfant, NewbornEnzymeATP hydrolysisPhysical SciencesEmergency MedicineMedicineIon channelGatingReceptor

Sustainable Development Goals

SDG 0: Good health and well-being