ArticleJournal of muscle research and cell motility2016
Comprehensive analysis of tropomyosin isoforms in skeletal muscles by top-down proteomics.
Article in Journal of muscle research and cell motility, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 39 citations in OpenAlex.
- Postmortem interval estimation through skeletal muscle protein degradation: a comprehensive review.International journal of legal medicine · 2026Review
- Fluorescent protein tags for human tropomyosin isoform comparison.Biology open · 2025Article
- CHOIR improves significance-based detection of cell types and states from single-cell data.Nature genetics · 2025Article
- Screening and validation of key microRNAs regulating muscle development in Hanper sheep.PloS one · 2025Article
- Top-down proteomics.Nature reviews. Methods primers · 2024Article
- Tropomyosin 3 (TPM3) function in skeletal muscle and in myopathy.Skeletal muscle · 2023Review
- High sensitivity top-down proteomics captures single muscle cell heterogeneity in large proteoforms.Proceedings of the National Academy of Sciences of the United States of America · 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
- Defining the Sarcomeric Proteoform Landscape in Ischemic Cardiomyopathy by Top-Down Proteomics.Journal of proteome research · 2023Article
- Fourier-transform ion cyclotron resonance mass spectrometry for characterizing proteoforms.Mass spectrometry reviews · 2022Review
- Application of ATAC-Seq for genome-wide analysis of the chromatin state at single myofiber resolution.eLife · 2022Article
- Molecular Mechanisms of the Deregulation of Muscle Contraction Induced by the R90P Mutation in Tpm3.12 and the Weakening of This Effect by BDM and W7.International journal of molecular sciences · 2021Article
- Vitamin D ameliorates adipose browning in chronic kidney disease cachexia.Scientific reports · 2020Article
- Thin filament dysfunctions caused by mutations in tropomyosin Tpm3.12 and Tpm1.1.Journal of muscle research and cell motility · 2020Review
- Functional outcomes of structural peculiarities of striated muscle tropomyosin.Journal of muscle research and cell motility · 2020Review
- Top-Down Proteomics Reveals Myofilament Proteoform Heterogeneity among Various Rat Skeletal Muscle Tissues.Journal of proteome research · 2020Article
- Top-down Mass Spectrometry of Sarcomeric Protein Post-translational Modifications from Non-human Primate Skeletal Muscle.Journal of the American Society for Mass Spectrometry · 2019Article
- Intact-Mass Analysis Facilitating the Identification of Large Human Heart Proteoforms.Analytical chemistry · 2019Article
- Characterization of Contractile Proteins from Skeletal Muscle Using Gel-Based Top-Down Proteomics.Proteomes · 2019Review
- Review
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Authors and funding
8 authors at 2 institutions in 3 countries.
Funding
Abstract
Mammalian skeletal muscles are heterogeneous in nature and are capable of performing various functions. Tropomyosin (Tpm) is a major component of the thin filament in skeletal muscles and plays an important role in controlling muscle contraction and relaxation. Tpm is known to consist of multiple isoforms resulting from different encoding genes and alternative splicing, along with post-translational modifications. However, a systematic characterization of Tpm isoforms in skeletal muscles is still lacking. Therefore, we employed top-down mass spectrometry (MS) to identify and characterize Tpm isoforms present in different skeletal muscles from multiple species, including swine, rat, and human. Our study revealed that Tpm1.1 and Tpm2.2 are the two major Tpm isoforms in swine and rat skeletal muscles, whereas Tpm1.1, Tpm2.2, and Tpm3.12 are present in human skeletal muscles. Tandem MS was utilized to identify the sequences of the major Tpm isoforms. Furthermore, quantitative analysis revealed muscle-type specific differences in the abundance of un-modified and modified Tpm isoforms in rat and human skeletal muscles. This study represents the first systematic investigation of Tpm isoforms in skeletal muscles, which not only demonstrates the capabilities of top-down MS for the comprehensive characterization of skeletal myofilament proteins but also provides the basis for further studies on these Tpm isoforms in muscle-related diseases.
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Registered trials
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