ReviewActa crystallographica. Section D, Structural biology2024
Post-translational modifications in the Protein Data Bank.
Review in Acta crystallographica. Section D, Structural biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
16 citing papers in PubMed.
- Post-translational modification-regulating biomaterials for regeneration.Bioactive materials · 2026Review
- Beyond the Capsid: How Can Post-Translational Modifications Modulate the Multifunctionality of the Orthoflavivirus Capsid Protein?Molecules (Basel, Switzerland) · 2026Review
- N-glycosylation of ERLIN2 promotes hepatocellular carcinoma progression by enhancing CCNB1 stability.Molecular and cellular biochemistry · 2026Article
- Modulation of Intravenous Immunoglobulin Aggregation, Subvisible Particle Formation, and Viscosity by Acetylated Amino Acids.Pharmaceutics · 2026Article
- Global Profiling of Post-Translationally Modified Crustacean Neuropeptidome Trends Affiliated with Feeding Activity.Journal of the American Society for Mass Spectrometry · 2026Article
- Tumor cell cycle regulation: integrated perspective of stage characteristics, regulatory networks, and signaling pathway intervention strategies.Molecular biomedicine · 2026Review
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- Research advances in key genes and regulatory mechanisms of posttranslational modifications in Parkinson's disease.PloS one · 2026Article
- Unveiling the hidden regulators: how post-translational modifications influence the progression and treatment of hepatocellular carcinoma.Frontiers in oncology · 2026Review
- Integrated bioinformatics and experimental validation identifies SOX2 as a key therapeutic target for chronic atrophic gastritis/gastric cancer-depression comorbidity.Frontiers in oncology · 2026Article
- Novel Respiratory Disease Diagnosis Tool: Development of an Au-ReSSmall science · 2026Article
- Reconstructing biological molecules with help from video gamers.Acta crystallographica. Section D, Structural biology · 2025Article
- Methods for detecting, building, and improving tryptophan mannosylation in glycoprotein structures.Protein science : a publication of the Protein Society · 2025Article
- Impact of Microwave Time on the Structure and Functional Properties of Glycosylated Soy 7S Globulins.Foods (Basel, Switzerland) · 2025Article
- Article
- Association of inflammation and protein carbamylation in patients with COVID-19.Frontiers in medicine · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Proteins frequently undergo covalent modification at the post-translational level, which involves the covalent attachment of chemical groups onto amino acids. This can entail the singular or multiple addition of small groups, such as phosphorylation; long-chain modifications, such as glycosylation; small proteins, such as ubiquitination; as well as the interconversion of chemical groups, such as the formation of pyroglutamic acid. These post-translational modifications (PTMs) are essential for the normal functioning of cells, as they can alter the physicochemical properties of amino acids and therefore influence enzymatic activity, protein localization, protein-protein interactions and protein stability. Despite their inherent importance, accurately depicting PTMs in experimental studies of protein structures often poses a challenge. This review highlights the role of PTMs in protein structures, as well as the prevalence of PTMs in the Protein Data Bank, directing the reader to accurately built examples suitable for use as a modelling reference.
Indexed as
Identifiers
What OpenQuestion holds
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.