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

Functional dissection of myosin binding protein C phosphorylation.

Journal of molecular and cellular cardiology - 1 Nov 2013

Gupta Manish K, Gulick James, James Jeanne, Osinska Hanna, Lorenz John N, Robbins Jeffrey

Abstract excerpt

Cardiac myosin binding protein C (cMyBP-C) phosphorylation is differentially regulated in the normal heart and during disease development. Our objective was to examine in detail three phosphorylatable sites (Ser-273, Ser-282, and Ser-302) present in the protein's cardiac-specific sequences, as these residues are differentially and reversibly phosphorylated during normal and abnormal cardiac function. Three...

Read the complete abstract on PubMed

Topics

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

Share to Cardiomyopathy, Dilated
Share to Codon
Share to Echocardiography

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Electrocardiography

Share to Fibrosis

Share to Hemodynamics

Share to Myocardium

Share to Serine

Source

Open in PubMed Open full text

Identifiers

PMID: 24001940
DOI: 10.1016/j.yjmcc.2013.08.006
PMCID: PMC3847820

Genes

ADA
SDS

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

Functional dissection of myosin binding protein C phosphorylation.PMID 24001940Read ↗

Cardiac myosin binding protein C phosphorylation is cardioprotective.Semantic proximity Read ↗

Phosphorylation of cMyBP-C affects contractile mechanisms in a site-specific manner.Semantic proximity Read ↗

Identification of novel protein kinase A phosphorylation sites in the M-domain of human and murine cardiac myosin binding protein-C using mass spectrometry analysis.Semantic proximity Read ↗

The contribution of cardiac myosin binding protein-c Ser282 phosphorylation to the rate of force generation and in vivo cardiac contractility.Semantic proximity Read ↗

Phosphorylation of cardiac Myosin-binding protein-C is a critical mediator of diastolic function.Semantic proximity Read ↗

Cardiac myosin binding protein C phosphorylation in cardiac disease.Semantic proximity Read ↗

Signaling and myosin-binding protein C.Semantic proximity Read ↗

In vivo definition of cardiac myosin-binding protein C's critical interactions with myosin.Semantic proximity Read ↗

Cardiac myosin-binding protein C N-terminal interactions with myosin and actin filaments: Opposite effects of phosphorylation and M-domain mutations.Semantic proximity Read ↗

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

Myosin Binding Protein-C Slow Phosphorylation is Altered in Duchenne Dystrophy and Arthrogryposis Myopathy in Fast-Twitch Skeletal Muscles.Semantic proximity Read ↗

Cardiac myosin binding protein C phosphorylation affects cross-bridge cycle's elementary steps in a site-specific manner.Semantic proximity Read ↗

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