ArticlePLoS biology2007
Global analysis of posttranslational protein arginylation.
Article in PLoS biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 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.
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Who cites it
93 citing papers in PubMed, 151 citations in OpenAlex.
- Trypsin exhibits exopeptidase-like activity toward N-terminal arginine that biases proteomic analyses.bioRxiv : the preprint server for biology · 2026Article
- Review
- Methods to Study Arginylation of Tubulin.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Implementing N-terminomics and machine learning to probe Nt-arginylation.Nature communications · 2025Article
- An unbiased proteomic platform for ATE1-based arginylation profiling.Nature chemical biology · 2025Article
- Method Overview for Discovering ATE1 Substrates and their Arginylation Sites.Chembiochem : a European journal of chemical biology · 2025Review
- Arginyltransferase1 drives a mitochondria-dependent program to induce cell death.Cell death & disease · 2025Article
- Top-Down Proteomics for the Characterization and Quantification of Calreticulin Arginylation.Analytical chemistry · 2025Article
- Arginylation of ⍺-tubulin at E77 regulates microtubule dynamics via MAP1S.The Journal of cell biology · 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
- Impact of Protein NLife (Basel, Switzerland) · 2023Review
- Iron-sulfur clusters are involved in post-translational arginylation.Nature communications · 2023Article
- Article
- Identification of Arginylated Proteins by Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Development of New Tools for the Studies of Protein Arginylation.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Identification of Protein Arginylation by Encapsulated N-Terminal Peptide Enrichment Method.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Identification of Arginylated Proteins by Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Assaying ATE1 Activity In Vitro.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Assaying the Posttranslational Arginylation of Proteins in Cultured Cells.Methods in molecular biology (Clifton, N.J.) · 2023Article
33 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 4 institutions in 1 country.
Funding
Abstract
Posttranslational arginylation is critical for embryogenesis, cardiovascular development, and angiogenesis, but its molecular effects and the identity of proteins arginylated in vivo are largely unknown. Here we report a global analysis of this modification on the protein level and identification of 43 proteins arginylated in vivo on highly specific sites. Our data demonstrate that unlike previously believed, arginylation can occur on any N-terminally exposed residue likely defined by a structural recognition motif on the protein surface, and that it preferentially affects a number of physiological systems, including cytoskeleton and primary metabolic pathways. The results of our study suggest that protein arginylation is a general mechanism for regulation of protein structure and function and outline the potential role of protein arginylation in cell metabolism and embryonic development.
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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.