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Ligand-independent EGFR oligomers do not rely on the active state asymmetric kinase dimer

bioRxiv (Cold Spring Harbor Laboratory)(2020)10.1101/2020.04.24.056077Source: DataRank Database

Ligand-independent EGFR oligomers do not rely on the active state asymmetric kinase dimer is a research paper published in bioRxiv (Cold Spring Harbor Laboratory) (2020). On theSindex it has a DataRank of 0. It has been cited 2 times.

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Open Access2 citations

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datarank_citation_only_1hop_v6· scope data_onlyMethodology

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Enrichment:Funding (2 grants)OA: greenTopics (22)IDs (PubMed, OpenAlex)

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Authors (3)

Kalina Hristova ORCID,Daniel J. Leahy ORCID,Patrick O. Byrne ORCID

Live enrichment

PubMed:23304386 OpenAlex:https://openalex.org/W3018024898

National Science Foundation

Grant: 1712740

Biophysics of protein interactions on membrane surfaces

National Institutes of Health

Grant: 5R01GM099321-17

Structural Studies of Growth Factor Receptor Function

greenLicense: cc-by-nc-nd

repositoryhttps://www.biorxiv.org/content/biorxiv/early/2020/04/25/2020.04.24.056077.full.pdf

publisherhttps://syndication.highwire.org/content/doi/10.1101/2020.04.24.056077

repositoryhttps://doi.org/10.1101/2020.04.24.056077

https://dx.doi.org/10.1101/2020.04.24.056077

Fields of Study

HER2/EGFR in Cancer ResearchMonoclonal and Polyclonal Antibodies ResearchGlycosylation and Glycoproteins Research0301 basic medicine0303 health sciences03 medical and health sciences

Keywords

Förster resonance energy transferLigand (biochemistry)OligomerDimerEpidermal growth factor receptorChemistryTyrosine kinaseBiophysicsReceptor tyrosine kinaseEpidermal growth factorRaftReceptorBiochemistryFluorescenceBiologyPolymerization