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

Divergent effects of α- and β-myosin heavy chain isoforms on the N terminus of rat cardiac troponin T.

The Journal of general physiology - 1 Oct 2013

Mamidi Ranganath, Chandra Murali

Abstract excerpt

Divergent effects of α- and β-myosin heavy chain (MHC) isoforms on contractile behavior arise mainly because of their impact on thin filament cooperativity. The N terminus of cardiac troponin T (cTnT) also modulates thin filament cooperativity. Our hypothesis is that the impact of the N terminus of cTnT on thin filament activation is modulated by a shift from α- to β-MHC isoform. We engineered two recombinant...

Read the complete abstract on PubMed

Topics

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

Share to Muscle Contraction
Share to Myosin Heavy Chains
Share to Propylthiouracil

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Isoforms

Share to Rats, Sprague-Dawley

Share to Sarcomeres

Share to Troponin T

Share to Ventricular Myosins

Source

Open in PubMed Open full text

Identifiers

PMID: 24043862
DOI: 10.1085/jgp.201310971
PMCID: PMC3787779

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

Divergent effects of α- and β-myosin heavy chain isoforms on the N terminus of rat cardiac troponin T.PMID 24043862Read ↗

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

Rat cardiac troponin T mutation (F72L)-mediated impact on thin filament cooperativity is divergently modulated by α- and β-myosin heavy chain isoforms.Semantic proximity Read ↗

L71F mutation in rat cardiac troponin T augments crossbridge recruitment and detachment dynamics against α-myosin heavy chain, but not against β-myosin heavy chain.Semantic proximity Read ↗

The effect of cardiomyopathy mutation (R97L) in mouse cardiac troponin T on the muscle length-mediated recruitment of crossbridges is modified divergently by α- and β-myosin heavy chain.Semantic proximity Read ↗

Functional consequence of mutation in rat cardiac troponin T is affected differently by myosin heavy chain isoforms.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 ↗

Interplay Between the Effects of Dilated Cardiomyopathy Mutation (R206L) and the Protein Kinase C Phosphomimic (T204E) of Rat Cardiac Troponin T Are Differently Modulated by α- and β-Myosin Heavy Chain Isoforms.Semantic proximity Read ↗

Thin filament interaction and Ca2+-desensitization effect of the C-terminal end peptide of cardiac troponin T and loss of function in hypertrophic cardiomyopathy mutants.Semantic proximity Read ↗

Hypertrophic cardiomyopathy mutation in cardiac troponin T (R95H) attenuates length-dependent activation in guinea pig cardiac muscle fibers.Semantic proximity Read ↗

Modulating the tension-time integral of the cardiac twitch prevents dilated cardiomyopathy in murine hearts.Semantic proximity Read ↗

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 ↗

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