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

The effect of the Asp175Asn and Glu180Gly TPM1 mutations on actin-myosin interaction during the ATPase cycle.

Biochimica et biophysica acta - 1 Feb 2012

Rysev Nikita A, Karpicheva Olga E, Redwood Charles S, Borovikov Yurii S

Abstract excerpt

Hypertrophic cardiomyopathy (HCM), characterized by cardiac hypertrophy and contractile dysfunction, is a major cause of heart failure. HCM can result from mutations in the gene encoding cardiac α-tropomyosin (TM). To understand how the HCM-causing Asp175Asn and Glu180Gly mutations in α-tropomyosin affect on actin-myosin interaction during the ATPase cycle, we labeled the SH1 helix of myosin subfragment-1 and the...

Read the complete abstract on PubMed

Topics

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

Share to Actomyosin
Share to Asparagine
Share to Aspartic Acid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cardiomyopathy, Hypertrophic

Share to Fluorescent Dyes

Share to Muscle Contraction

Share to Spectrometry, Fluorescence

Share to Tropomyosin

Source

Identifiers

PMID: 22155441
DOI: 10.1016/j.bbapap.2011.11.004

Genes

TPM1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The effect of the Asp175Asn and Glu180Gly TPM1 mutations on actin-myosin interaction during the ATPase cycle.PMID 22155441Read ↗

Hypertrophic cardiomyopathy-causing Asp175asn and Glu180gly Tpm1 mutations shift tropomyosin strands further towards the open position during the ATPase cycle.Semantic proximity Read ↗

Dilated cardiomyopathy mutations in alpha-tropomyosin inhibit its movement during the ATPase cycle.Semantic proximity Read ↗

Myopathy-causing Q147P TPM2 mutation shifts tropomyosin strands further towards the open position and increases the proportion of strong-binding cross-bridges during the ATPase cycle.Semantic proximity Read ↗

[Abnormal tropomyosin function in ATPase cycle in hypertrophic and dilated cardiomyopathies].Semantic proximity Read ↗

Aberrant movement of β-tropomyosin associated with congenital myopathy causes defective response of myosin heads and actin during the ATPase cycle.Semantic proximity Read ↗

Molecular mechanisms of deregulation of the thin filament associated with the R167H and K168E substitutions in tropomyosin Tpm1.1.Semantic proximity Read ↗

Abnormal movement of tropomyosin and response of myosin heads and actin during the ATPase cycle caused by the Arg167His, Arg167Gly and Lys168Glu mutations in TPM1 gene.Semantic proximity Read ↗

The E117K mutation in β-tropomyosin disturbs concerted conformational changes of actomyosin in muscle fibers.Semantic proximity Read ↗

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

Cardiomyopathy-associated mutations in tropomyosin differently affect actin-myosin interaction at single-molecule and ensemble levels.Semantic proximity Read ↗

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

The effects of the tropomyosin cardiomyopathy mutations on the calcium regulation of actin-myosin interaction in the atrium and ventricle differ.Semantic proximity Read ↗

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