ArticleCommunications biology2026
Ancestral protein reconstruction reveals the mechanism of substrate specificity in FN3K-mediated deglycation.
Article in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
- Update of
- Update of
Authors and funding
4 authors.
Funding
Abstract
Protein glycation is a detrimental byproduct of carbohydrate metabolism, and nearly all organisms encode kinases that facilitate the removal of early glycation products. In humans, these repair functions are performed by Fructosamine-3 and Ketosamine-3 kinases (FN3K, KT3K). Recent structural studies identified conserved residues essential for FN3K activity, but the molecular basis for substrate discrimination between FN3K and KT3K remains unknown. Here, we show that substrate-binding residues are highly conserved and do not confer specificity in the FN3K family. Using APR, we resurrected four ancestral fructosamine kinases that recapitulate the distinct substrate preferences of FN3K and KT3K. Through mutational studies and structural analysis, we identify an evolutionarily tuned allosteric network that modulates substrate selection through long-range intramolecular interactions. Our findings define the mechanism of substrate selectivity within the FN3K family and establish a framework for the development of selective FN3K inhibitors.
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.