ArticleTrends in glycoscience and glycotechnology : TIGG2011
The Amazing Transglycosylation Activity of Endo-β-N-acetylglucosaminidases.
Article in Trends in glycoscience and glycotechnology : TIGG, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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
27 citing papers in PubMed.
- Enzyme-Mediated Dynamic Combinatorial Chemistry Enables Large-Scale Synthesis of δ-Cyclodextrin.Journal of the American Chemical Society · 2025Article
- Chemical tools to track and perturb the expression of sialic acid and fucose monosaccharides.Chemical communications (Cambridge, England) · 2022Review
- Heterologous expression of 4α-glucanotransferase: overproduction and properties for industrial applications.World journal of microbiology & biotechnology · 2022Review
- GH18 endo-β-N-acetylglucosaminidases use distinct mechanisms to process hybrid-type N-linked glycans.The Journal of biological chemistry · 2021Article
- Pro4 prolyl peptide bond isomerization in human galectin-7 modulates the monomer-dimer equilibrum to affect function.The Biochemical journal · 2020Article
- Synthesis and photoinitiated thiol-ene reactions ofRSC advances · 2020Article
- Structural insights into the mechanisms and specificities of IgG-active endoglycosidases.Glycobiology · 2020Review
- Obtaining and Investigation of theScientifica · 2020Article
- Chemoenzymatic Methods for the Synthesis of Glycoproteins.Chemical reviews · 2018Review
- Acceptor range of endo-β-Royal Society open science · 2018Article
- Silyl-protective groups influencing the reactivity and selectivity in glycosylations.Beilstein journal of organic chemistry · 2017Review
- Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017Review
- Chemical Methods for Encoding and Decoding of Posttranslational Modifications.Cell chemical biology · 2016Review
- Endoglycosidases for the Synthesis of Polysaccharides and Glycoconjugates.Advances in carbohydrate chemistry and biochemistry · 2016Review
- Chemoenzymatic synthesis of α-dystroglycan core M1 O-mannose glycans.Chemical communications (Cambridge, England) · 2015Article
- Transglycosylation Activity of Glycosynthase Mutants of Endo-β-N-Acetylglucosaminidase from Coprinopsis cinerea.PloS one · 2015Article
- A 3,4-trans-fused cyclic protecting group facilitates α-selective catalytic synthesis of 2-deoxyglycosides.Angewandte Chemie (International ed. in English) · 2014Article
- Regioselective chemoenzymatic synthesis of ganglioside disialyl tetrasaccharide epitopes.Journal of the American Chemical Society · 2014Article
- Chemical and chemoenzymatic synthesis of glycoproteins for deciphering functions.Chemistry & biology · 2014Review
- Molecular modeling and analysis of human and plant endo-β-N-acetyl- glucosaminidases for mutations effects on function.Bioinformation · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
Abstract
Major advances have been made in exploring the transglycosylation activity of endo-β-N-acetylglucosaminidases (ENGases) for synthetic purpose. The exploration of synthetic sugar oxazolines as donor substrates for the ENGase-catalyzed transglycosylation has expanded the substrate availability and significantly enhanced the overall transglycosylation efficiency. On the other hand, site-directed mutagenesis in combination with activity screening has led to the discovery of the first generation ENGase-based glycosynthases that can use highly active sugar oxazolines as substrates for transglycosylation but lack hydrolytic activity on the ground-state products. ENGases have shown amazing flexibility in transglycosylation and possess much broader substrate specificity than previously thought. Now the ENGase-based chemoenzymatic method has been extended to the synthesis of a range of complex carbohydrates, including homogeneous glycopeptides, glycoproteins carrying well-defined glycans, novel oligosaccharide clusters, unusually glycosylated natural products, and even polysaccharides. This article highlights recent advances related to ENGase-catalyzed transglycosylation with a focus on their synthetic potential.
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.