ArticleThe Journal of biological chemistry2017
Structural Insights into the Broad Substrate Specificity of a Novel Endoglycoceramidase I Belonging to a New Subfamily of GH5 Glycosidases.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Biocatalytic Approaches to Building Blocks for Enzymatic and Chemical Glycan Synthesis.JACS Au · 2023Review
- Roles of Sialyl Glycans in HCoV-OC43, HCoV-HKU1, MERS-CoV and SARS-CoV-2 Infections.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Structure and inhibition of Cryptococcus neoformans sterylglucosidase to develop antifungal agents.Nature communications · 2021Article
- The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata.Scientific reports · 2020Article
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- Distinguishing the differences in β-glycosylceramidase folds, dynamics, and actions informs therapeutic uses.Journal of lipid research · 2018Article
- Carbohydrate active enzyme domains from extreme thermophiles: components of a modular toolbox for lignocellulose degradation.Extremophiles : life under extreme conditions · 2018Review
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Endoglycoceramidases (EGCases) specifically hydrolyze the glycosidic linkage between the oligosaccharide and the ceramide moieties of various glycosphingolipids, and they have received substantial attention in the emerging field of glycosphingolipidology. However, the mechanism regulating the strict substrate specificity of these GH5 glycosidases has not been identified. In this study, we report a novel EGCase I from
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Registered trials
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