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Negative cooperativity underlies dynamic assembly of the Par complex regulators Cdc42 and Par-3

bioRxiv (Cold Spring Harbor Laboratory)(2022)10.1101/2022.08.12.503756Source: DataRank Database

Negative cooperativity underlies dynamic assembly of the Par complex regulators Cdc42 and Par-3 is a research paper published in bioRxiv (Cold Spring Harbor Laboratory) (2022). 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 (26)IDs (PubMed, OpenAlex)

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Open Access

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Authors (2)

Kenneth E. Prehoda ORCID,Elizabeth Vargas ORCID

Live enrichment

PubMed:21097893 OpenAlex:https://openalex.org/W4291168592

National Institutes of Health

Grant: 5R35GM127092-08

Molecular mechanisms that control polarity and asymmetric cell division

National Institutes of Health

Grant: 5T32HD007348-18

Developmental Biology Training Program

greenLicense: cc-by-nc-nd

repositoryhttps://www.biorxiv.org/content/biorxiv/early/2022/08/12/2022.08.12.503756.full.pdf

publisherhttps://syndication.highwire.org/content/doi/10.1101/2022.08.12.503756

repositoryhttps://doi.org/10.1101/2022.08.12.503756

https://doi.org/10.1016/j.jbc.2022.102749

Fields of Study

Hippo pathway signaling and YAP/TAZHeat shock proteins researchWnt/β-catenin signaling in development and cancer0301 basic medicine0303 health sciences03 medical and health sciences

Keywords

PDZ domainCDC42CooperativityTernary complexGTPaseCooperative bindingCell biologyBiophysicsBiologyChemistryBinding siteBiochemistryEnzymerho GTP-Binding ProteinsAnimalsCell PolarityHumansNerve Tissue Proteinscdc42 GTP-Binding ProteinResearch Article