ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2025
The important interplay between metal ions and the intermediate filament protein vimentin.
Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 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
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
1 citing paper in PubMed.
- Metal Ion Binding of Vimentin Tail Domain Fragments.Chembiochem : a European journal of chemical biology · 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
Vimentin is a principal intermediate filament (IF) protein that is essential for maintaining cytoskeleton architecture and cellular mechanical integrity. Growing evidence is revealing that metal ions play critical roles in modulating the structure, assembly, and mechanics of vimentin IFs. Despite this, a detailed molecular-level understanding of vimentin-metal interactions and its functional consequences remains incomplete. This review summarizes the current knowledge of metal-induced effects on the structural and mechanical properties of vimentin and highlights how post-translational modifications and cytoskeletal dynamics may alter these metal-protein interactions. Advancing our understanding of the interplay between metal ions and vimentin IFs will enhance our comprehension of the complex mechanisms governing the versatile functions of vimentin and other IF proteins in health and disease.
Indexed as
Identifiers
What Socratic 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 Socratic graph.