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

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

The Journal of physiology - 1 Nov 2003

Pi YeQing, Zhang Dahua, Kemnitz Kara R, Wang Hao, Walker Jeffery W

Abstract excerpt

Cardiac troponin I (cTnI) is a phosphoprotein subunit of the troponin-tropomyosin complex that is thought to inhibit cardiac muscle contraction during diastole. To investigate the contributions of cTnI phosphorylation to cardiac regulation, transgenic mice were created with the phosphorylation sites of cTnI mutated to alanine. Activation of protein kinase C (PKC) by perfusion of hearts with...

Topics

Join the communities discussing this publication.

Actin Cytoskeleton
Adrenergic beta-Agonists
Endothelin-1
Isometric Contraction
Isoproterenol

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Myocardial Contraction

Tetradecanoylphorbol Acetate

Source

Open in PubMed Open full text

Identifiers

PMID: 12923217
DOI: 10.1113/jphysiol.2003.045260
PMCID: PMC2343448

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Protein kinase C and A sites on troponin I regulate myofilament Ca2+ sensitivity and ATPase activity in the mouse myocardium.PMID 12923217Read ↗

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 ↗

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

The dilated cardiomyopathy-causing mutation ACTC E361G in cardiac muscle myofibrils specifically abolishes modulation of Ca(2+) regulation by phosphorylation of troponin I.Semantic proximity Read ↗

alpha-Adrenergic response and myofilament activity in mouse hearts lacking PKC phosphorylation sites on cardiac TnI.Semantic proximity Read ↗

Phosphoregulation of Cardiac Inotropy via Myosin Binding Protein-C During Increased Pacing Frequency or β1-Adrenergic Stimulation.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 ↗

Mutations in Troponin that cause HCM, DCM AND RCM: what can we learn about thin filament function?Semantic proximity Read ↗

Acceleration of crossbridge kinetics by protein kinase A phosphorylation of cardiac myosin binding protein C modulates cardiac function.Semantic proximity Read ↗

Differential regulation of cardiac actomyosin S-1 MgATPase by protein kinase C isozyme-specific phosphorylation of specific sites in cardiac troponin I and its phosphorylation site mutants.Semantic proximity Read ↗

Heart Failure-Related Hyperphosphorylation in the Cardiac Troponin I C Terminus Has Divergent Effects on Cardiac Function In Vivo.Semantic proximity Read ↗

Mouse Models of Cardiomyopathies Caused by Mutations in Troponin C.Semantic proximity Read ↗

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