ReviewAnatomical record (Hoboken, N.J. : 2007)2014
Protein arginylation, a global biological regulator that targets actin cytoskeleton and the muscle.
Review in Anatomical record (Hoboken, N.J. : 2007), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 1 synthesis or guideline pooled it, 33 citations in OpenAlex.
- Multi-epigenome-wide analyses and meta-analysis of child maltreatment in judicial autopsies and intervened children and adolescents.Molecular psychiatry · 2026Pooled it
- The C-terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity.FEBS open bio · 2026Article
- Actin arginylation alters myosin engagement and F-actin patterning despite structural conservation.The Journal of cell biology · 2026Article
- The divergent intron-containing actin in sponge morphogenetic processes.NAR genomics and bioinformatics · 2025Article
- Reconstitution of the Arginyltransferase (ATE1) Iron-Sulfur Cluster.Methods in molecular biology (Clifton, N.J.) · 2023Article
- The preparation of recombinant arginyltransferase 1 (ATE1) for biophysical characterization.Methods in enzymology · 2023Article
- Arginylation Regulates Cytoskeleton Organization and Cell Division and Affects Mitochondria in Fission Yeast.Molecular and cellular biology · 2022Article
- Specialization of actin isoforms derived from the loss of key interactions with regulatory factors.The EMBO journal · 2022Article
- ATE1-Mediated Post-Translational Arginylation Is an Essential Regulator of Eukaryotic Cellular Homeostasis.ACS chemical biology · 2020Article
- A Label-Free Assay for Aminoacylation of tRNA.Genes · 2020Article
- Diversity from similarity: cellular strategies for assigning particular identities to actin filaments and networks.Open biology · 2020Article
- Downregulation of the Arg/N-degron Pathway Sensitizes Cancer Cells to Chemotherapy In Vivo.Molecular therapy : the journal of the American Society of Gene Therapy · 2020Article
- Protein arginylation of cytoskeletal proteins in the muscle: modifications modifying function.American journal of physiology. Cell physiology · 2019Review
- tRNA 3'-amino-tailing for stable amino acid attachment.RNA (New York, N.Y.) · 2018Article
- Actin's N-terminal acetyltransferase uncovered.Cytoskeleton (Hoboken, N.J.) · 2018Article
- Arginyltransferase ATE1 is targeted to the neuronal growth cones and regulates neurite outgrowth during brain development.Developmental biology · 2017Article
- Reduced passive force in skeletal muscles lacking protein arginylation.American journal of physiology. Cell physiology · 2016Article
- Recent advances in muscle research.Anatomical record (Hoboken, N.J. : 2007) · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Posttranslational addition of Arg to proteins, mediated by arginyltransferase ATE1 has been first observed in 1963 and remained poorly understood for decades since its original discovery. Recent work demonstrated the global nature of arginylation and its essential role in multiple physiological pathways during embryogenesis and adulthood and identified over a hundred of proteins arginylated in vivo. Among these proteins, the prominent role belongs to the actin cytoskeleton and the muscle, and follow up studies strongly suggests that arginylation constitutes a novel biological regulator of contractility. This review presents an overview of the studies of protein arginylation that led to the discovery of its major role in the muscle.
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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.