ArticleJournal of muscle research and cell motility2007
Role of tropomyosin isoforms in the calcium sensitivity of striated muscle thin filaments.
Article in Journal of muscle research and cell motility, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 46 citations in OpenAlex.
- Back pain exercise therapy remodels human epigenetic profiles in buccal and human peripheral blood mononuclear cells: an exploratory study in young male participants.Frontiers in sports and active living · 2024Article
- Functional outcomes of structural peculiarities of striated muscle tropomyosin.Journal of muscle research and cell motility · 2020Review
- A Novel Homozygous Intronic Variant in TNNT2 Associates With Feline Cardiomyopathy.Frontiers in physiology · 2020Article
- The mechanism of thin filament regulation: Models in conflict?The Journal of general physiology · 2019Review
- Computational Tool to Study Perturbations in Muscle Regulation and Its Application to Heart Disease.Biophysical journal · 2019Article
- Investigating the effects of tropomyosin mutations on its flexibility and interactions with filamentous actin using molecular dynamics simulation.Journal of muscle research and cell motility · 2016Article
- The impact of tropomyosins on actin filament assembly is isoform specific.Bioarchitecture · 2016Article
- Predicting Effects of Tropomyosin Mutations on Cardiac Muscle Contraction through Myofilament Modeling.Frontiers in physiology · 2016Article
- Impact of tropomyosin isoform composition on fast skeletal muscle thin filament regulation and force development.Journal of muscle research and cell motility · 2015Article
- The myosin-activated thin filament regulatory state, M⁻-open: a link to hypertrophic cardiomyopathy (HCM).Journal of muscle research and cell motility · 2014Review
- Polymorphism in tropomyosin structure and function.Journal of muscle research and cell motility · 2013Review
- α-Tropomyosin with a D175N or E180G mutation in only one chain differs from tropomyosin with mutations in both chains.Biochemistry · 2012Article
- Cooperative regulation of myosin-S1 binding to actin filaments by a continuous flexible Tm-Tn chain.European biophysics journal : EBJ · 2012Article
- Familial hypertrophic cardiomyopathy related E180G mutation increases flexibility of human cardiac α-tropomyosin.FEBS letters · 2012Article
- In vitro formation and characterization of the skeletal muscle α·β tropomyosin heterodimers.Biochemistry · 2012Article
- Long-range effects of familial hypertrophic cardiomyopathy mutations E180G and D175N on the properties of tropomyosin.Biochemistry · 2012Article
- The Hill model for binding myosin S1 to regulated actin is not equivalent to the McKillop-Geeves model.Journal of molecular biology · 2012Article
- Tropomyosin flexural rigidity and single ca(2+) regulatory unit dynamics: implications for cooperative regulation of cardiac muscle contraction and cardiomyocyte hypertrophy.Frontiers in physiology · 2012Article
- Tropomyosin is in a reduced state in rabbit psoas muscle.Journal of muscle research and cell motility · 2011Article
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
Abstract
We have expressed alpha & beta isoforms of mammalian striated muscle tropomyosin (Tm) and alpha-Tm carrying the D175N or E180G cardiomyopathy mutations. In each case the Tm carries an Ala-Ser N-terminal extension to mimic the acetylation of the native Tm. We show that these Ala-Ser modified proteins are good analogues of the native Tm in the assays used here. We go on to use an in vitro kinetic approach to define the assembly of actin filaments with the Tm isoforms with either a cardiac or a skeletal muscle troponin (cTn, skTn). With skTn the calcium sensitivity of the actin filament is the same for alpha & beta-Tm and there is little change with the mutant Tms. For cTn switching from alpha to beta-Tm causes an increase of calcium sensitivity of 0.2 pCa units. D175N is very similar to the wild type alpha-Tm and E180G shows a small increase in calcium sensitivity of about 0.1 pCa unit. The formation of the switched-off blocked-state of the actin filament is independent of the Tm isoform but does differ for cardiac versus skeletal Tn. The in vitro assays developed here provide a novel, simple and efficient method for assaying the behaviour of expressed thin filament proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.