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A novel bivalent interaction mode underlies a non-catalytic mechanism for Pin1-mediated Protein Kinase C regulation

bioRxiv (Cold Spring Harbor Laboratory)(2023)10.1101/2023.09.18.558341Source: DataRank Database

A novel bivalent interaction mode underlies a non-catalytic mechanism for Pin1-mediated Protein Kinase C regulation is a research paper published in bioRxiv (Cold Spring Harbor Laboratory) (2023). On theSindex it has a DataRank of 0.

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Enrichment:Funding (2 grants)OA: greenTopics (19)IDs (PubMed)

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Authors (7)

Karuna Dixit ORCID,Yuan Yang ORCID,Mark I. McDermott ORCID,Hasan Imam ORCID,Vytas A. Bankaitis ORCID

Live enrichment

PubMed:37781616

National Institutes of Health

Grant: 3R35GM131804-03S1

The Biology and Biochemistry of Lipid Transfer Protein-Regulated Phosphoinositide Signaling

National Institutes of Health

Grant: 5R01GM108998-05

Structural and functional studies of protein kinase C regulation

greenLicense: CC BY

repositoryhttps://www.biorxiv.org/content/biorxiv/early/2023/09/26/2023.09.18.558341.full.pdf

publisherhttps://syndication.highwire.org/content/doi/10.1101/2023.09.18.558341

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/10541119

https://doi.org/10.1101/2023.09.18.558341

https://doi.org/10.7554/elife.92884

Fields of Study

0301 basic medicine03 medical and health sciences

Keywords

protein kinase C degradationbivalent bindingQH301-705.5Protein ConformationScienceStructural Biology and Molecular BiophysicsQRnon-catalytic mechanismPin1 peptidyl-prolyl isomeraseNIMA-Interacting Peptidylprolyl IsomeraseMedicineHumansBiology (General)signalingProtein Kinase CProtein Binding