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Structure-informed theoretical modeling defines principles governing avidity in bivalent protein interactions

bioRxiv (Cold Spring Harbor Laboratory)(2025)10.1101/2025.05.13.653723Source: DataRank Database

Structure-informed theoretical modeling defines principles governing avidity in bivalent protein interactions is a research paper published in bioRxiv (Cold Spring Harbor Laboratory) (2025). On theSindex it has a DataRank of 0.

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›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

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Enrichment:Funding (3 grants)OA: greenTopics (28)IDs (PubMed, OpenAlex)

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Open Access

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Authors (4)

Anqi Wu ORCID,Alekhya Kandoor ORCID,Kristen M. Naegle ORCID,Reagan Portelance

Live enrichment

PubMed:40463177 OpenAlex:https://openalex.org/W4410344882

National Institute of General Medical Sciences

Grant: R35GM138127

National Institute of General Medical Sciences

Grant: T32GM008715

NCI NIH HHS

Grant: R33 CA259451

greenLicense: cc-by-nc-nd

repositoryhttps://www.biorxiv.org/content/biorxiv/early/2025/05/13/2025.05.13.653723.full.pdf

publisherhttps://syndication.highwire.org/content/doi/10.1101/2025.05.13.653723

repositoryhttps://doi.org/10.1101/2025.05.13.653723

repositoryhttps://pubmed.ncbi.nlm.nih.gov/40463177

Fields of Study

Protein Kinase Regulation and GTPase SignalingProtein Tyrosine PhosphatasesPI3K/AKT/mTOR signaling in cancer

Keywords

AviditySH2 domainTandemAffinitiesComputational biologyDomain (mathematical analysis)Protein–protein interactionTandem repeatProtein domainBiologyChemistryComputer scienceCell biologySignal transductionGeneticsBiochemistryProto-oncogene tyrosine-protein kinase SrcMathematicsAntibodyBLISH2 domainsbiolayer interferometrybivalentphosphotyrosineprotein interactions