ReviewMedComm2026
Post-translational Modifications in Proteins: Prediction Methods, Biological Functions, and Diseases.
Review in MedComm, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed.
- Post-Translational Modifications in Traumatic Brain Injury: Decoding the Proteomic Landscape and Molecular Mechanisms of Secondary Injury.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Review
- Protein Posttranslational Modifications in Immunity: Molecular Mechanisms and Therapeutic Targets.MedComm · 2026Review
- Beyond the Capsid: How Can Post-Translational Modifications Modulate the Multifunctionality of the Orthoflavivirus Capsid Protein?Molecules (Basel, Switzerland) · 2026Review
- Deep learning-driven decoding of ubiquitination: from regulatory mechanisms to targeted protein degradation.Biology direct · 2026Review
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
No grant is acknowledged in the PubMed record.
Abstract
Posttranslational modifications (PTMs) act as rapid, reversible switches that reshape protein activity, stability, and interactome, thereby governing virtually every physiological cue from signal transduction to epigenetic memory. Mass spectrometry-based proteomics has considerably extended our knowledge about the occurrence and dynamics of PTMs. Pinpointing disease- or physiology-specific PTM sites remains an open challenge. As a biological process with well-defined stage-specific markers and a precise endpoint, erythropoiesis is orchestrated by the complex interplay of multiple PTM-regulatory networks, making it an ideal model for dissecting the spatiotemporal dynamics, quantitative thresholds, and crosstalk of PTMs. This review delineates the applications, detection, and prediction technologies of PTMs, with an emphasis on the mechanisms of phosphorylation, ubiquitination, methylation, SUMOylation, glycosylation, and acetylation in both physiological and pathological processes. Dissecting PTM circuitry driving erythroid specification and maturation, we show how its perturbation triggers disease, clarifying PTM roles. Additionally, we have investigated the progress made in the clinical translation and drug development of the PTMs field, emphasizing the potential of PTMs in the field of precision medicine as well as the existing challenges. This review aims to provide new insights and perspectives for the study of PTMs.
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.