ArticleCell reports2014
Arginylation of myosin heavy chain regulates skeletal muscle strength.
Article in Cell reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT06660784 (Mechanism of Nitric Oxide on Ventilator-induced Diaphragm Dysfunction with Extracorporeal Membrane Lung Assistance), which is not on this map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Mechanism of Nitric Oxide on Ventilator-induced Diaphragm Dysfunction with Extracorporeal Membrane Lung Assistance
Who cites it
21 citing papers in PubMed, 36 citations in OpenAlex.
- Method Overview for Discovering ATE1 Substrates and their Arginylation Sites.Chembiochem : a European journal of chemical biology · 2025Review
- Identification of Arginylated Proteins by Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Arginylation Regulates Cytoskeleton Organization and Cell Division and Affects Mitochondria in Fission Yeast.Molecular and cellular biology · 2022Article
- Functional Interplay between Arginyl-tRNA Synthetases and Arginyltransferase.International journal of molecular sciences · 2022Article
- Nitric oxide and skeletal muscle contractile function.Nitric oxide : biology and chemistry · 2022Review
- Availability of Arg, but Not tRNA, Is a Rate-Limiting Factor for Intracellular Arginylation.International journal of molecular sciences · 2021Article
- ATE1 Inhibits Liver Cancer Progression through RGS5-Mediated Suppression of Wnt/β-Catenin Signaling.Molecular cancer research : MCR · 2021Article
- Dietary nitrate supplementation increases diaphragm peak power in old mice.The Journal of physiology · 2020Article
- Regulation of actin isoforms in cellular and developmental processes.Seminars in cell & developmental biology · 2020Review
- The load dependence and the force-velocity relation in intact myosin filaments from skeletal and smooth muscles.American journal of physiology. Cell physiology · 2020Article
- Protein arginylation of cytoskeletal proteins in the muscle: modifications modifying function.American journal of physiology. Cell physiology · 2019Review
- Ate1-mediated posttranslational arginylation affects substrate adhesion and cell migration in Dictyostelium discoideum.Molecular biology of the cell · 2019Article
- Target site specificity and in vivo complexity of the mammalian arginylome.Scientific reports · 2018Article
- N-terminal arginylation generates a bimodal degron that modulates autophagic proteolysis.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Thick Filament Protein Network, Functions, and Disease Association.Comprehensive Physiology · 2018Review
- Arginyltransferase ATE1 is targeted to the neuronal growth cones and regulates neurite outgrowth during brain development.Developmental biology · 2017Article
- Protein arginylation targets alpha synuclein, facilitates normal brain health, and prevents neurodegeneration.Scientific reports · 2017Article
- Tampering with springs: phosphorylation of titin affecting the mechanical function of cardiomyocytes.Biophysical reviews · 2017Review
- Analyzing N-terminal Arginylation through the Use of Peptide Arrays and Degradation Assays.The Journal of biological chemistry · 2016Article
- Reduced passive force in skeletal muscles lacking protein arginylation.American journal of physiology. Cell physiology · 2016Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
Abstract
Protein arginylation is a posttranslational modification with an emerging global role in the regulation of actin cytoskeleton. To test the role of arginylation in the skeletal muscle, we generated a mouse model with Ate1 deletion driven by the skeletal muscle-specific creatine kinase (Ckmm) promoter. Ckmm-Ate1 mice were viable and outwardly normal; however, their skeletal muscle strength was significantly reduced in comparison to controls. Mass spectrometry of isolated skeletal myofibrils showed a limited set of proteins, including myosin heavy chain, arginylated on specific sites. Atomic force microscopy measurements of contractile strength in individual myofibrils and isolated myosin filaments from these mice showed a significant reduction of contractile forces, which, in the case of myosin filaments, could be fully rescued by rearginylation with purified Ate1. Our results demonstrate that arginylation regulates force production in muscle and exerts a direct effect on muscle strength through arginylation of myosin.
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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.