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

Role of troponin I phosphorylation in protein kinase C-mediated enhanced contractile performance of rat myocytes.

The Journal of biological chemistry - 5 Sept 2003

Westfall Margaret V, Borton Andrea R

Abstract excerpt

Our goal was to define the role of phosphorylated cardiac troponin-I in the adult myocyte contractile performance response to activated protein kinase C. In agreement with earlier work, endothelin enhanced both adult rat myocyte contractile performance and cardiac troponin-I phosphorylation. Protein kinase C participated in both responses. The role of cardiac troponin-I phosphorylation in the contractile function...

Read the complete abstract on PubMed

Topics

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

Share to Adenoviridae
Share to Gene Transfer Techniques
Share to Muscle Contraction

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Myocardium

Share to Protein Isoforms

Share to Protein Kinase C

Share to Threonine

Share to Troponin I

Source

Identifiers

PMID: 12815045
DOI: 10.1074/jbc.M305404200

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

Role of troponin I phosphorylation in protein kinase C-mediated enhanced contractile performance of rat myocytes.PMID 12815045Read ↗

Left ventricular and myocardial function in mice expressing constitutively pseudophosphorylated cardiac troponin I.Semantic proximity Read ↗

Phosphorylation of troponin I controls cardiac twitch dynamics: evidence from phosphorylation site mutants expressed on a troponin I-null background in mice.Semantic proximity Read ↗

Molecular biology of protein kinase C signaling in cardiac myocytes.Semantic proximity Read ↗

Protein kinase C and A sites on troponin I regulate myofilament Ca2+ sensitivity and ATPase activity in the mouse myocardium.Semantic proximity Read ↗

Cardiotrophic Effects of Protein Kinase C εSemantic proximity Read ↗

Allele and species dependent contractile defects by restrictive and hypertrophic cardiomyopathy-linked troponin I mutants.Semantic proximity Read ↗

Gene transfer of troponin I isoforms, mutants, and chimeras.Semantic proximity Read ↗

PKCepsilon activation induces dichotomous cardiac phenotypes and modulates PKCepsilon-RACK interactions and RACK expression.Semantic proximity Read ↗

PKA phosphorylation of cardiac troponin I modulates activation and relaxation kinetics of ventricular myofibrils.Semantic proximity Read ↗

Protein kinase C phosphomimetics alter thin filament Ca2+ binding properties.Semantic proximity Read ↗

Interplay between the effects of a Protein Kinase C phosphomimic (T204E) and a dilated cardiomyopathy mutation (K211Δ or R206W) in rat cardiac troponin T blunts the magnitude of muscle length-mediated crossbridge recruitment against the β-myosin heavy chain background.Semantic proximity Read ↗

Impaired cardiomyocyte relaxation and diastolic function in transgenic mice expressing slow skeletal troponin I in the heart.Semantic proximity Read ↗

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