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

New insights into the functional significance of the acidic region of the unique N-terminal extension of cardiac troponin I.

Biochimica et biophysica acta - 1 Apr 2013

Henze Marcus, Patrick Stacey E, Hinken Aaron, Scruggs Sarah B, Goldspink Paul, de Tombe Pieter P, Kobayashi Minae, Ping Peipei, Kobayashi Tomoyoshi, Solaro R John

Abstract excerpt

Previous structural studies indicated a special functional role for an acidic region composed of residues 1-10 in the unique N-terminal peptide of cardiac troponin I (cTnI). Employing LC-MS/MS, we determined the presence of phosphorylation sites at S5/S6 in cTnI from wild type mouse hearts as well as in hearts of mice chronically expressing active protein kinase C-ε (PKCε) and exhibiting severe dilated...

Topics

Join the communities discussing this publication.

Adenosine Triphosphatases
Cardiomyopathy, Dilated
Isometric Contraction
Myocardium
Myofibrils

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Isoforms

Protein Kinase C-epsilon

Source

Open in PubMed Open full text

Identifiers

PMID: 22940544
DOI: 10.1016/j.bbamcr.2012.08.012
PMCID: PMC3548050

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

New insights into the functional significance of the acidic region of the unique N-terminal extension of cardiac troponin I.PMID 22940544Read ↗

Pathogenesis associated with a restrictive cardiomyopathy mutant in cardiac troponin T is due to reduced protein stability and greatly increased myofilament Ca2+ sensitivity.Semantic proximity Read ↗

Cardiac troponin structure-function and the influence of hypertrophic cardiomyopathy associated mutations on modulation of contractility.Semantic proximity Read ↗

Engineered troponin C constructs correct disease-related cardiac myofilament calcium sensitivity.Semantic proximity Read ↗

Identification of two new regions in the N-terminus of cardiac troponin T that have divergent effects on cardiac contractile function.Semantic proximity Read ↗

Troponin I Mutations R146G and R21C Alter Cardiac Troponin Function, Contractile Properties, and Modulation by Protein Kinase A (PKA)-mediated Phosphorylation.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 ↗

Cardiomyopathy-related mutation (A30V) in mouse cardiac troponin T divergently alters the magnitude of stretch activation in α- and β-myosin heavy chain fibers.Semantic proximity Read ↗

Troponins, intrinsic disorder, and cardiomyopathy.Semantic proximity Read ↗

Effects of Cardiac Troponin I Mutation P83S on Contractile Properties and the Modulation by PKA-Mediated Phosphorylation.Semantic proximity Read ↗

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

Significance of troponin dynamics for Ca2+-mediated regulation of contraction and inherited cardiomyopathy.Semantic proximity Read ↗

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

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