ReviewJournal of muscle research and cell motility2001
Vertebrate tropomyosin: distribution, properties and function.
Review in Journal of muscle research and cell motility, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 174 papers.
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174 citing papers in PubMed, 463 citations in OpenAlex.
- Characterization and evaluation of a Sarcoptes scabiei allergen as a candidate vaccine.Parasites & vectors · 2012Trial
- Temperature dependence of activation of thick and thin filaments in skeletal and cardiac muscles.Journal of muscle research and cell motility · 2026Review
- Comparative transcriptome analysis reveals the patterns of gene expression in different venison cuts of sika deer (Cervus nippon).Animal bioscience · 2025Article
- Actin Filament Pointed Ends: Assays for Regulation of Assembly and Disassembly by Tropomodulin and Tropomyosin.Cytoskeleton (Hoboken, N.J.) · 2025Article
- ELF3 regulates epithelial-mesenchymal transition through TPM1 and promotes the development of endometrial cancer.Cytotechnology · 2025Article
- The Twisting and Untwisting of Actin and Tropomyosin Filaments Are Involved in the Molecular Mechanisms of Muscle Contraction, and Their Disruption Can Result in Muscle Disorders.International journal of molecular sciences · 2025Review
- Article
- Novel Mutation Lys30Glu in theInternational journal of molecular sciences · 2024Article
- Integrin subunit beta 6 is a potential diagnostic marker for acute kidney injury in patients with diabetic kidney disease: a single cell sequencing data analysis.Renal failure · 2024Article
- CYB561 is a potential therapeutic target for breast cancer and is associated with immune cell infiltration.European journal of medical research · 2024Article
- Nucleus Mechanosensing in Cardiomyocytes.International journal of molecular sciences · 2023Review
- Alternative polyadenylation regulation in cardiac development and cardiovascular disease.Cardiovascular research · 2023Review
- Structural and Functional Properties of Kappa Tropomyosin.International journal of molecular sciences · 2023Article
- A novel variant in the tropomyosin 3 gene presenting as an adult-onset distal myopathy - a case report.BMC neurology · 2023Article
- Molecular Mechanisms of Deregulation of Muscle Contractility Caused by the R168H Mutation in TPM3 and Its Attenuation by Therapeutic Agents.International journal of molecular sciences · 2023Article
- Impact of Troponin in Cardiomyopathy Development Caused by Mutations in Tropomyosin.International journal of molecular sciences · 2022Article
- mNG-tagged fusion proteins and nanobodies to visualize tropomyosins in yeast and mammalian cells.Journal of cell science · 2022Article
- The prognostic value of TPM1-4 in hepatocellular carcinoma.Cancer medicine · 2022Article
- Nanopore sequencing reveals full-length Tropomyosin 1 isoforms and their regulation by RNA-binding proteins during rat heart development.Journal of cellular and molecular medicine · 2021Article
- The R168G heterozygous mutation of tropomyosin 3 (TPM3) was identified in three family members and has manifestations ranging from asymptotic to serve scoliosis and respiratory complications.Genes & diseases · 2021Article
114 more citing papers are in PubMed but not listed here.
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Authors and funding
1 author at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Tropomyosin (TM) is widely distributed in all cell types associated with actin as a fibrous molecule composed of two alpha-helical chains arranged as a coiled-coil. It is localised, polymerised end to end, along each of the two grooves of the F-actin filament providing structural stability and modulating the filament function. To accommodate the wide range of functions associated with actin filaments that occur in eucaryote cells TM exists in a large number isoforms, over 20 of which have been identified. These isoforms which are expressed by alternative promoters and alternative RNA processing of four genes, TPM1, 2, 3 and 4, all conform to a general pattern of structure. Their amino acid sequences consist of an integral number, six or seven in vertebrates, of quasiequivalent regions of about 40 residues that are considered to represent the actin-binding regions of the molecule. In addition to the variable regions a large part of the polypeptide chains of the TM isoforms, mainly centrally located and expressed by five exons, is invariant. Many of the isoforms are tissue and filament specific in their distribution implying that the exons expressed in them and the regions of the molecule they represent are of significance for the function of the filament system with which they are associated. In the case of muscle there is clear evidence that the TM moves its position on the F-actin filament during contraction and it is therefore considered to play an important part in the regulation of the process. It is uncertain how the role of TM in muscle compares to that in non-muscle systems and if its function in the former tissue is unique to muscle.
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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.