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Allosteric activation or inhibition of PI3Kγ mediated through conformational changes in the p110γ helical domain

(2023)10.7554/elife.88058.2Source: DataRank Database

Allosteric activation or inhibition of PI3Kγ mediated through conformational changes in the p110γ helical domain is a research paper (2023). On theSindex it has a DataRank of 0.

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0DataRank · unranked

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Open Access0 citations

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›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Pipeline:MetadataData-paper checkEnrichmentCitation networkScoring

Enrichment:Funding (6 grants)OA: goldTopics (13)IDs (PubMed, OpenAlex)SDGs (1)

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 (12)

Meredith L. Jenkins ORCID,Sung-Eun Nam ORCID,Manoj Kumar Rathinaswamy ORCID,Matthew AH Parson ORCID,Harish Ranga-Prasad

Live enrichment

PubMed:21097893 OpenAlex:https://openalex.org/W4380360534

Canadian Institutes of Health Research

Grant: FDN-143228

Canadian Institutes of Health Research

Grant: PJT-168907

Natural Sciences and Engineering Research Council of Canada

Grant: RGPIN-2018-03951

National Science Foundation

Grant: MCB-2048060

Canadian Institutes of Health Research

Grant: 168998

Michael Smith Health Research BC

Grant: 17686

goldLicense: cc-by

https://doi.org/10.7554/elife.88058.2

publisherhttps://cdn.elifesciences.org/preprints/88058/elife-preprint-88058-v2.pdf

publisherhttps://cdn.elifesciences.org/preprints/88058/elife-preprint-88058-v2.xml

publisherhttps://elifesciences.org/reviewed-preprints/88058v2/pdf

Fields of Study

PI3K/AKT/mTOR signaling in cancerCytokine Signaling Pathways and InteractionsProtein Tyrosine Phosphatases

Keywords

Allosteric regulationDomain (mathematical analysis)ChemistryConformational changeBiophysicsStereochemistryBiochemistryBiologyEnzymeMathematics

Sustainable Development Goals

SDG 0: Good health and well-being