ReviewMass spectrometry reviews
Uncommon posttranslational modifications in proteomics: ADP-ribosylation, tyrosine nitration, and tyrosine sulfation.
Review in Mass spectrometry reviews. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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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
13 citing papers in PubMed.
- Are Sulfates of the Hydroxyl Amino Acids Threonine and Serine Truly Extremely Rare or Do They Simply Escape Detection?Life (Basel, Switzerland) · 2026Article
- Discovery of chirally dependent protein modifications by D- and L-2-hydroxyglutarates.Nature chemistry · 2026Article
- Threonine sulfation: a rare post translational modification in insect adipokinetic hormones.Scientific reports · 2026Article
- Review
- Reply to: Mass spectrometry and enzyme assays refute histone tyrosine sulfation.Nature chemical biology · 2025Article
- Impact of Microwave Time on the Structure and Functional Properties of Glycosylated Soy 7S Globulins.Foods (Basel, Switzerland) · 2025Article
- Post-translational modifications of proteins in cardiovascular diseases examined by proteomic approaches.The FEBS journal · 2025Review
- An updated overview of the search for biomarkers of osteoporosis based on human proteomics.Journal of orthopaedic translation · 2024Review
- Acetylation, ADP-ribosylation and methylation of malate dehydrogenase.Essays in biochemistry · 2024Review
- Proteomics of the heart.Physiological reviews · 2024Review
- Mass Spectrometry Strategies forCells · 2024Review
- Tyrosine Sulfation at Antibody Light Chain CDR-1 Increases Binding Affinity and Neutralization Potency to Interleukine-4.International journal of molecular sciences · 2024Article
- Special Issue "Deployment of Proteomics Approaches in Biomedical Research".International journal of molecular sciences · 2024Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Posttranslational modifications (PTMs) are covalent modifications of proteins that modulate the structure and functions of proteins and regulate biological processes. The development of various mass spectrometry-based proteomics workflows has facilitated the identification of hundreds of PTMs and aided the understanding of biological significance in a high throughput manner. Improvements in sample preparation and PTM enrichment techniques, instrumentation for liquid chromatography-tandem mass spectrometry (LC-MS/MS), and advanced data analysis tools enhance the specificity and sensitivity of PTM identification. Highly prevalent PTMs like phosphorylation, glycosylation, acetylation, ubiquitinylation, and methylation are extensively studied. However, the functions and impact of less abundant PTMs are not as well understood and underscore the need for analytical methods that aim to characterize these PTMs. This review focuses on the advancement and analytical challenges associated with the characterization of three less common but biologically relevant PTMs, specifically, adenosine diphosphate-ribosylation, tyrosine sulfation, and tyrosine nitration. The advantages and disadvantages of various enrichment, separation, and MS/MS techniques utilized to identify and localize these PTMs are described.
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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.