Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Decoding the Interactions Regulating the Active State Mechanics of Eukaryotic Protein Kinases.

PLoS biology - 1 Nov 2016

Meharena Hiruy S, Fan Xiaorui, Ahuja Lalima G, Keshwani Malik M, McClendon Christopher L, Chen Angela M, Adams Joseph A, Taylor Susan S

Abstract excerpt

Eukaryotic protein kinases regulate most cellular functions by phosphorylating targeted protein substrates through a highly conserved catalytic core. In the active state, the catalytic core oscillates between open, intermediate, and closed conformations. Currently, the intramolecular interactions that regulate the active state mechanics are not well understood. Here, using cAMP-dependent protein kinase as a...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalysis
Share to Hydrophobic and Hydrophilic Interactions

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Protein Kinases

Share to Static Electricity

Source

Open in PubMed Open full text

Identifiers

PMID: 27902690
DOI: 10.1371/journal.pbio.2000127
PMCID: PMC5130182

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Decoding the Interactions Regulating the Active State Mechanics of Eukaryotic Protein Kinases.PMID 27902690Read ↗

Allosteric regulation of kinase activity in living cellsSemantic proximity Read ↗

Switching of the folding-energy landscape governs the allosteric activation of protein kinase A.Semantic proximity Read ↗

A template for the protein kinase family.Semantic proximity Read ↗

Extended regulation interface coupled to the allosteric network and disease mutations in the PP2A-B56δ holoenzymeSemantic proximity Read ↗

Disease mutations and phosphorylation alter the allosteric pathways involved in autoinhibition of protein phosphatase 2A.Semantic proximity Read ↗

Catalytic independent functions of a protein kinase as revealed by a kinase-dead mutant: study of the Lys72His mutant of cAMP-dependent kinase.Semantic proximity Read ↗

Unveiling the Complexity of cis-Regulation Mechanisms in Kinases: A Comprehensive AnalysisSemantic proximity Read ↗

Unveiling the Complexity of cis-Regulation Mechanisms in Kinases: A Comprehensive Analysis.Semantic proximity Read ↗

Mutation of a kinase allosteric node uncouples dynamics linked to phosphotransfer.Semantic proximity Read ↗

Conformational changes in protein kinase A along its activation cycle are rooted in the folding energetics of cyclic-nucleotide binding domains.Semantic proximity Read ↗

Mechanism of Epac activation: structural and functional analyses of Epac2 hinge mutants with constitutive and reduced activities.Semantic proximity Read ↗

Evolution and Engineering of Allosteric Regulation in Protein KinasesSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.