ArticleACS catalysis2020
Synthetic Glycosidase Distinguishing Glycan and Glycosidic Linkage in Its Catalytic Hydrolysis.
Article in ACS catalysis, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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
7 citing papers in PubMed, 21 citations in OpenAlex.
- Molecularly imprinted materials for glycan recognition and processing.Journal of materials chemistry. B · 2022Review
- Rational design of allosteric switchable catalysts.Exploration (Beijing, China) · 2022Review
- Dynamic Tuning in Synthetic Glycosidase for Selective Hydrolysis of Alkyl and Aryl Glycosides.The Journal of organic chemistry · 2022Article
- Environmental Modulation of Chiral Prolinamide Catalysts for Stereodivergent Conjugate Addition.Journal of catalysis · 2022Article
- Substrate Protection in Controlled Enzymatic Transformation of Peptides and Proteins.Chembiochem : a European journal of chemical biology · 2021Article
- Tandem Aldol Reaction from Acetal Mixtures by an Artificial Enzyme with Site-Isolated Acid and Base Functionalities.ACS applied polymer materials · 2021Article
- Selective Hydrolysis of Aryl Esters under Acidic and Neutral Conditions by a Synthetic Aspartic Protease Mimic.ACS catalysis · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Selective hydrolysis of carbohydrates is vital to the processing of these molecules in biology but has rarely been achieved with synthetic catalysts. The challenge is especially difficult because the catalyst needs to distinguish the inversion of a single hydroxyl and the α or β glycosidic bonds that join monosaccharide building blocks. Here we report synthetic glycosidase prepared through molecular imprinting within a cross-linked micelle. The nanoparticle catalyst resembles natural enzymes in dimension, water-solubility, and a hydrophilic/hydrophobic surface-core topology. Its boronic acid-functionalized active site binds its targeted glycoside substrate and an acid cofactor simultaneously, with the acidic group in close proximity to the exocyclic glycosidic oxygen. The hydrophobically anchored acid cofactor is tunable in acidity and causes selective cleavage of the targeted glycoside in mildly acidic water. Selectivity for both the glycan and the α/β glycosidic bond can be rationally designed through the molecular imprinting process.
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.