ArticleNature communications2026
Plant fucosyltransferase FUT11 distorts the sugar acceptor to catalyze via a transient oxocarbenium intermediate mechanism.
Article in Nature communications, 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
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
Abstract
Glycosyltransferases catalyze glycosidic bond formation by activating the donor sugar, while the sugar acceptor substrate is considered passive, maintaining a chair conformation during catalysis. We challenge this through a multidisciplinary study of Arabidopsis thaliana FUT11, a core α1,3-fucosyltransferase essential for plant development and reproduction. AtFUT11 adopts a GT-B fold with an additional N-terminal subdomain that anchors the G0 N-glycan, while the α1,3 arm is mainly recognized by the acceptor Rossmann subdomain. The α1,6 arm remains solvent-exposed, allowing diverse modifications, while solvent exposure of the central mannose's OH2 explains tolerance for β1,2-xylose. Remarkably, simulations suggest the catalytic base Glu158 may promote the innermost GlcNAc's transient puckering distortion to align the hydroxyl for nucleophilic attack. This enables an asynchronous S
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.