ArticleNeurochemical research2006
Protein arginylation in rat brain cytosol: a proteomic analysis.
Article in Neurochemical research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- Trypsin exhibits exopeptidase-like activity toward N-terminal arginine that biases proteomic analyses.bioRxiv : the preprint server for biology · 2026Article
- Method Overview for Discovering ATE1 Substrates and their Arginylation Sites.Chembiochem : a European journal of chemical biology · 2025Review
- Top-Down Proteomics for the Characterization and Quantification of Calreticulin Arginylation.Analytical chemistry · 2025Article
- Top-down Proteomics for the Characterization and Quantification of Calreticulin Arginylation.bioRxiv : the preprint server for biology · 2024Article
- Arginyltransferase 1 modulates p62-driven autophagy via mTORC1/AMPk signaling.Cell communication and signaling : CCS · 2024Article
- Assaying the Posttranslational Arginylation of Proteins in Cultured Cells.Methods in molecular biology (Clifton, N.J.) · 2023Article
- The evolutionarily conserved arginyltransferase 1 mediates a pVHL-independent oxygen-sensing pathway in mammalian cells.Developmental cell · 2022Article
- The Final Maturation State of β-actin Involves N-terminal Acetylation by NAA80, not N-terminal Arginylation by ATE1.Journal of molecular biology · 2022Article
- Posttranslational Arginylation Enzyme Arginyltransferase1 Shows Genetic Interactions With Specific Cellular PathwaysFrontiers in physiology · 2020Article
- Reduced Arginyltransferase 1 is a driver and a potential prognostic indicator of prostate cancer metastasis.Oncogene · 2019Article
- Protein arginylation targets alpha synuclein, facilitates normal brain health, and prevents neurodegeneration.Scientific reports · 2017Article
- Posttranslational arginylation enzyme Ate1 affects DNA mutagenesis by regulating stress response.Cell death & disease · 2016Article
- Calreticulin and Arginylated Calreticulin Have Different Susceptibilities to Proteasomal Degradation.The Journal of biological chemistry · 2015Article
- Characterization of arginylation branch of N-end rule pathway in G-protein-mediated proliferation and signaling of cardiomyocytes.The Journal of biological chemistry · 2012Article
- The N-end rule pathway: emerging functions and molecular principles of substrate recognition.Nature reviews. Molecular cell biology · 2011Review
- Arginylation regulates intracellular actin polymer level by modulating actin properties and binding of capping and severing proteins.Molecular biology of the cell · 2010Article
- Arginylation-dependent neural crest cell migration is essential for mouse development.PLoS genetics · 2010Article
- Arginyltransferase regulates alpha cardiac actin function, myofibril formation and contractility during heart development.Development (Cambridge, England) · 2008Article
- Global analysis of posttranslational protein arginylation.PLoS biology · 2007Article
- Post-translational arginylation of calreticulin: a new isospecies of calreticulin component of stress granules.The Journal of biological chemistry · 2007Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Arginine can be post-translationally incorporated from arginyl-tRNA into the N-terminus of soluble acceptor proteins in a reaction catalyzed by arginyl-tRNA protein transferase. In the present study, several soluble rat brain proteins that accepted arginine were identified after arginine incorporation by two dimensional electrophoresis and mass spectrometry. They were identified as: contrapsin-like protease inhibitor-3, alpha-1-antitrypsin, apolipoprotein E, hemopexin, calreticulin and apolipoprotein A-I. All of these proteins shared a signal sequence for the translocation of proteins across endoplasmic reticulum membranes. After losing the signal peptide, these proteins expose amino acids described as compatible for post-translational arginylation. Although the enzymatic system involved in arginylation is confined mainly in cytosol and nucleus, all the substrates described herein enter to the exocytic pathway co-translationally. Therefore, we postulate that the substrates for arginylation could reach the cytosol by retro-translocation and be then arginylated.
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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.