ReviewAmino acids2022
Current status of PTMs structural databases: applications, limitations and prospects.
Review in Amino acids, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed.
- Biomarkers in Clinical Medicine Research: A Literature Survey in the PubMed Database and a Critical Evaluation.Journal of clinical medicine · 2026Review
- PTMFusionNet: A Deep Learning Approach for Predicting Disease Related Post-translational Modification and Classifying Disease Subtypes.Molecular & cellular proteomics : MCP · 2025Article
- Follicular metabolic dysfunction, oocyte aneuploidy and ovarian aging: a review.Journal of ovarian research · 2025Review
- Investigating the Key Trends in Applying Artificial Intelligence to Health Technologies: A Scoping Review.PloS one · 2025Article
- ProCaliper: functional and structural analysis, visualization, and annotation of proteins.Bioinformatics advances · 2025Article
- TRIM21 Promotes Rabies Virus Production by Degrading IRF7 through Ubiquitination.International journal of molecular sciences · 2023Article
- Lysine N-methyltransferase SETD7 promotes bladder cancer progression and immune escape via STAT3/PD-L1 cascade.International journal of biological sciences · 2023Article
- Article
- Post-translational modifications of the apelin receptor regulate its functional expression.AIMS neuroscience · 2023Article
- Implications of Post-Translational Modifications in Autoimmunity with Emphasis on Citrullination, Homocitrullination and Acetylation for the Pathogenesis, Diagnosis and Prognosis of Rheumatoid Arthritis.International journal of molecular sciences · 2022Review
- Editorial.Amino acids · 2022Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Protein 3D structures, determined by their amino acid sequences, are the support of major crucial biological functions. Post-translational modifications (PTMs) play an essential role in regulating these functions by altering the physicochemical properties of proteins. By virtue of their importance, several PTM databases have been developed and released in decades, but very few of these databases incorporate real 3D structural data. Since PTMs influence the function of the protein and their aberrant states are frequently implicated in human diseases, providing structural insights to understand the influence and dynamics of PTMs is crucial for unraveling the underlying processes. This review is dedicated to the current status of databases providing 3D structural data on PTM sites in proteins. Some of these databases are general, covering multiple types of PTMs in different organisms, while others are specific to one particular type of PTM, class of proteins or organism. The importance of these databases is illustrated with two major types of in silico applications: predicting PTM sites in proteins using machine learning approaches and investigating protein structure-function relationships involving PTMs. Finally, these databases suffer from multiple problems and care must be taken when analyzing the PTMs data.
Indexed as
Identifiers
35020020What 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.