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

Global consequences of activation loop phosphorylation on protein kinase A.

The Journal of biological chemistry - 5 Feb 2010

Steichen Jon M, Iyer Ganesh H, Li Sheng, Saldanha S Adrian, Deal Michael S, Woods Virgil L, Taylor Susan S

Abstract excerpt

Phosphorylation of the activation loop is one of the most common mechanisms for regulating protein kinase activity. The catalytic subunit of cAMP-dependent protein kinase autophosphorylates Thr(197) in the activation loop when expressed in Escherichia coli. Although mutation of Arg(194) to Ala prevents autophosphorylation, phosphorylation of Thr(197) can still be achieved by a heterologous protein kinase,...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Cyclic AMP-Dependent Protein Kinases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Deuterium Exchange Measurement

Share to Hydrophobic and Hydrophilic Interactions

Share to Oligopeptides

Share to Protein Denaturation

Share to Threonine

Source

Open in PubMed Open full text

Identifiers

PMID: 19965870
DOI: 10.1074/jbc.M109.061820
PMCID: PMC2823524

Genes

PDK1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Global consequences of activation loop phosphorylation on protein kinase A.PMID 19965870Read ↗

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 ↗

Allosteric network of cAMP-dependent protein kinase revealed by mutation of Tyr204 in the P+1 loop.Semantic proximity Read ↗

Folding and activity of cAMP-dependent protein kinase mutants.Semantic proximity Read ↗

Phosphorylation of the catalytic subunit of protein kinase A. Autophosphorylation versus phosphorylation by phosphoinositide-dependent kinase-1.Semantic proximity Read ↗

How does activation loop phosphorylation modulate catalytic activity in the cAMP-dependent protein kinase: a theoretical study.Semantic proximity Read ↗

Decoding the Interactions Regulating the Active State Mechanics of Eukaryotic Protein Kinases.Semantic proximity Read ↗

Structures of PKA-phospholamban complexes reveal a mechanism of familial dilated cardiomyopathySemantic proximity Read ↗

Dissecting interdomain communication within cAPK regulatory subunit type IIbeta using enhanced amide hydrogen/deuterium exchange mass spectrometry (DXMS).Semantic proximity Read ↗

Regulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains.Semantic proximity Read ↗

Consequences of cAMP-binding site mutations on the structural stability of the type I regulatory subunit of cAMP-dependent protein kinase.Semantic proximity Read ↗

Dysfunctional conformational dynamics of protein kinase A induced by a lethal mutant of phospholamban hinder phosphorylation.Semantic proximity Read ↗

Mapping the Free Energy Landscape of PKA Inhibition and Activation: A Double-Conformational Selection Model for the Tandem cAMP-Binding Domains of PKA RIα.Semantic proximity Read ↗

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