ReviewChemical reviews2026
Catalyzing Carbohydrate Cleavage: Glycosidases and Their Mechanisms.
Review in Chemical reviews, 2026. 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-Free Electrochemical Construction of Oxygen Heterocycles.Accounts of chemical research · 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
No grant is acknowledged in the PubMed record.
Abstract
Glycoside hydrolases, "glycosidases", catalyze carbohydrate catabolism, remodeling, and signaling by accelerating glycosidic-bond cleavage by more than 17 orders of magnitude. Distributed across every kingdom of life and grouped into over 180 sequence-defined families, these enzymes exhibit exceptional diversity in fold, mechanism, and physiological function, and many also catalyze transglycosylation or phosphorolysis. The classical Koshland paradigms─stereochemical inversion, enzymatic nucleophile-assisted retention, and substrate-assisted retention─are analyzed with an emphasis on the conformational itineraries and oxocarbenium ion-like transition states revealed by kinetic isotope effects, linear free-energy relationships, and high-resolution three-dimensional structures. Attention then turns to noncanonical enzymes that employ NAD
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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.