ReviewAmino acids2025
Post-translational modifications of ezrin: a crucial regulator for diseases.
Review in Amino acids, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
- Transcriptomic analysis reveals and validates lipid raft-associated biomarkers and functional networks in Alzheimer's disease.IBRO neuroscience reports · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Ezrin is a crucial structural protein that connects the plasma membrane to the actin cytoskeleton to maintain cell shape, adhesion, and motility. Post-translational modifications (PTMs) play a key role in the regulation of various biological functions and have been implicated in a range of pathological conditions. With the help of PTMs, ezrin not only plays a structural role in connecting the cell membrane to F-actin, but also participates in transmitting cellular signals including those related to inflammatory responses. In this study, we reviewed the key sites and domains involved in the different PTMs of ezrin, including acetylation, lactylation and phosphorylation. We analyzed the regulation of biological processes mediated by different PTMs of ezrin, such as cell migration, inflammation regulation and cell stiffness. In addition, we examined the mutual regulatory effects of different modifications of ezrin, including regulation of ezrin phosphorylation by kinases and phosphatases, and so on. Increasing evidence suggests that PTMs of ezrin are involved in cancer, respiratory diseases and urological diseases. These studies provide novel insights into the design of new disease treatment strategies targeting ezrin.
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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.