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

Several cardiomyopathy causing mutations on tropomyosin either destabilize the active state of actomyosin or alter the binding properties of tropomyosin.

Biochemical and biophysical research communications - 4 Mar 2011

Mathur Mohit C, Chase P Bryant, Chalovich Joseph M

Abstract excerpt

We examined the cardiomyopathy-causing tropomyosin mutations E180G, D175N, and V95A to determine their effects on actomyosin regulation. V95A reduced the ATPase rate when filaments were saturated with regulatory proteins both in the presence and absence of calcium, indicating either a stabilization of the inactive state or an inability to fully populate the active state. Effects of E180G and D175N were more...

Read the complete abstract on PubMed

Topics

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

Share to Actomyosin
Share to Adenosine Triphosphatases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Calcium

Share to Cardiomyopathies

Share to Mutation

Share to Rabbits

Share to Tropomyosin

Source

Open in PubMed Open full text

Identifiers

PMID: 21295541
DOI: 10.1016/j.bbrc.2011.01.112
PMCID: PMC3057449

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Several cardiomyopathy causing mutations on tropomyosin either destabilize the active state of actomyosin or alter the binding properties of tropomyosin.PMID 21295541Read ↗

Enhanced active cross-bridges during diastole: molecular pathogenesis of tropomyosin's HCM mutations.Semantic proximity Read ↗

Some cardiomyopathy-causing troponin I mutations stabilize a functional intermediate actin state.Semantic proximity Read ↗

Dilated and hypertrophic cardiomyopathy mutations in troponin and alpha-tropomyosin have opposing effects on the calcium affinity of cardiac thin filaments.Semantic proximity Read ↗

Long-range effects of familial hypertrophic cardiomyopathy mutations E180G and D175N on the properties of tropomyosin.Semantic proximity Read ↗

Troponin C Mutations Partially Stabilize the Active State of Regulated Actin and Fully Stabilize the Active State When Paired with Δ14 TnT.Semantic proximity Read ↗

Mechanistic Heterogeneity in Contractile Properties of α-Tropomyosin (TPM1) Mutants Associated with Inherited CardiomyopathiesSemantic proximity Read ↗

Alterations in thin filament regulation induced by a human cardiac troponin T mutant that causes dilated cardiomyopathy are distinct from those induced by troponin T mutants that cause hypertrophic cardiomyopathy.Semantic proximity Read ↗

The flexibility of two tropomyosin mutants, D175N and E180G, that cause hypertrophic cardiomyopathy.Semantic proximity Read ↗

Molecular mechanisms and structural features of cardiomyopathy-causing troponin T mutants in the tropomyosin overlap region.Semantic proximity Read ↗

Dilated cardiomyopathy mutations in three thin filament regulatory proteins result in a common functional phenotype.Semantic proximity Read ↗

Effect of Cardiomyopathic Mutations in Tropomyosin on Calcium Regulation of the Actin-Myosin Interaction in Skeletal Muscle.Semantic proximity Read ↗

Structure-function relationship of muscle thin filament regulatory proteins : tropomyosin and troponinSemantic proximity Read ↗

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