ReviewBiopolymers2014
Chemical and biological methods to detect post-translational modifications of arginine.
Review in Biopolymers, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
40 citing papers in PubMed, 72 citations in OpenAlex.
- Differential histone tail citrullination by PAD Enzymes observed via NMR spectroscopy.bioRxiv : the preprint server for biology · 2026Article
- Metabolic Origin, Role and Fate of the Denaturant Guanidine.Microbial biotechnology · 2025Article
- Citrullination of NF-κB p65 by PAD2 as a Novel Therapeutic Target for Modulating Macrophage Polarization in Acute Lung Injury.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- The Role and Mechanism of Protein Post‑Translational Modification in Rheumatoid Arthritis.Journal of inflammation research · 2025Review
- StackGlyEmbed: prediction of N-linked glycosylation sites using protein language models.Bioinformatics advances · 2025Article
- Targeting Peptidylarginine Deiminase 3 to Efficiently Suppress Herpes Simplex Virus Type 2 Infection.International journal of molecular sciences · 2024Article
- A quantitative and site-specific atlas of the citrullinome reveals widespread existence of citrullination and insights into PADI4 substrates.Nature structural & molecular biology · 2024Article
- Characterizing citrullination by mass spectrometry-based proteomics.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023Review
- Beyond metabolic waste: lysine lactylation and its potential roles in cancer progression and cell fate determination.Cellular oncology (Dordrecht, Netherlands) · 2023Review
- Chemical Conjugation to Less Targeted Proteinogenic Amino Acids.Chembiochem : a European journal of chemical biology · 2022Review
- The virtues and vices of protein citrullination.Royal Society open science · 2022Review
- Inhibition ofSaudi journal of biological sciences · 2022Article
- Citrullination in the pathology of inflammatory and autoimmune disorders: recent advances and future perspectives.Cellular and molecular life sciences : CMLS · 2022Review
- pH/Acetonitrile-Gradient Reversed-Phase Fractionation of Enriched Hyper-Citrullinated Library in Combination with LC-MS/MS Analysis for Confident Identification of Citrullinated Peptides.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Covalent Chemical Tools for Profiling Post-Translational Modifications.Frontiers in chemistry · 2022Review
- Characterization of Monoclonal Antibodies Recognizing Citrulline-Modified Residues.Frontiers in immunology · 2022Article
- DeepNGlyPred: A Deep Neural Network-Based Approach for Human N-Linked Glycosylation Site Prediction.Molecules (Basel, Switzerland) · 2021Article
- On the Need to Tell Apart Fraternal Twins eEF1A1 and eEF1A2, and Their Respective Outfits.International journal of molecular sciences · 2021Review
- A deep learning based approach for prediction of Chlamydomonas reinhardtii phosphorylation sites.Scientific reports · 2021Article
- A comprehensive guide to genetic variants and post-translational modifications of cardiac troponin C.Journal of muscle research and cell motility · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Post-translational modifications (PTMs) of protein embedded arginines are increasingly being recognized as playing an important role in both prokaryotic and eukaryotic biology, and it is now clear that these PTMs modulate a number of cellular processes including DNA binding, gene transcription, protein-protein interactions, immune system activation, and proteolysis. There are currently four known enzymatic PTMs of arginine (i.e., citrullination, methylation, phosphorylation, and ADP-ribosylation), and two non-enzymatic PTMs [i.e., carbonylation, advanced glycation end-products (AGEs)]. Enzymatic modification of arginine is tightly controlled during normal cellular function, and can be drastically altered in response to various second messengers and in different disease states. Non-enzymatic arginine modifications are associated with a loss of metabolite regulation during normal human aging. This abnormally large number of modifications to a single amino acid creates a diverse set of structural perturbations that can lead to altered biological responses. While the biological role of methylation has been the most extensively characterized of the arginine PTMs, recent advances have shown that the once obscure modification known as citrullination is involved in the onset and progression of inflammatory diseases and cancer. This review will highlight the reported arginine PTMs and their methods of detection, with a focus on new chemical methods to detect protein citrullination.
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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.