Golgi -mannosidase II cleaves two sugars sequentially in the same catalytic site
about
Structure and kinetic investigation of Streptococcus pyogenes family GH38 alpha-mannosidaseThe Molecular Basis of Inhibition of Golgi α-Mannosidase II by Mannostatin AGlycan fragment database: a database of PDB-based glycan 3D structures.Mutations in four glycosyl hydrolases reveal a highly coordinated pathway for rhodopsin biosynthesis and N-glycan trimming in Drosophila melanogaster.A long-wavelength fluorescent substrate for continuous fluorometric determination of alpha-mannosidase activity: resorufin alpha-D-mannopyranoside.Neural-specific α3-fucosylation of N-linked glycans in the Drosophila embryo requires fucosyltransferase A and influences developmental signaling associated with O-glycosylationEngineering β1,4-galactosyltransferase I to reduce secretion and enhance N-glycan elongation in insect cells.Reduced immunogenicity of Arabidopsis hgl1 mutant N-glycans caused by altered accessibility of xylose and core fucose epitopes.Preferred conformations of N-glycan core pentasaccharide in solution and in glycoproteins.A human embryonic kidney 293T cell line mutated at the Golgi alpha-mannosidase II locus.Developing inhibitors of glycan processing enzymes as tools for enabling glycobiology.The multivalent effect in glycosidase inhibition: a new, rapidly emerging topic in glycoscience.Cloning, Expression, and Characterization of Capra hircus Golgi α-Mannosidase II.In-depth analysis of site-specific N-glycosylation in vitronectin from human plasma by tandem mass spectrometry with immunoprecipitation.Potent Glycosidase Inhibition with Heterovalent Fullerenes: Unveiling the Binding Modes Triggering Multivalent Inhibition.Human lysosomal alpha-mannosidases exhibit different inhibition and metal binding properties'Click chemistry' synthesis of 1-(α-D-mannopyranosyl)-1,2,3-triazoles for inhibition of α-mannosidases.Fullerene-sp2-iminosugar balls as multimodal ligands for lectins and glycosidases: a mechanistic hypothesis for the inhibitory multivalent effect.Characterisation of class I and II α-mannosidases from Drosophila melanogaster.Human N-acetylglucosaminyltransferase II substrate recognition uses a modular architecture that includes a convergent exosite.In silico analysis of interaction pattern switching in ligandreceptor binding in Golgi α-mannosidase II induced by the protonated states of inhibitors.
P2860
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P2860
Golgi -mannosidase II cleaves two sugars sequentially in the same catalytic site
description
2008 nî lūn-bûn
@nan
2008 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Golgi -mannosidase II cleaves two sugars sequentially in the same catalytic site
@ast
Golgi -mannosidase II cleaves two sugars sequentially in the same catalytic site
@en
Golgi -mannosidase II cleaves two sugars sequentially in the same catalytic site
@nl
type
label
Golgi -mannosidase II cleaves two sugars sequentially in the same catalytic site
@ast
Golgi -mannosidase II cleaves two sugars sequentially in the same catalytic site
@en
Golgi -mannosidase II cleaves two sugars sequentially in the same catalytic site
@nl
prefLabel
Golgi -mannosidase II cleaves two sugars sequentially in the same catalytic site
@ast
Golgi -mannosidase II cleaves two sugars sequentially in the same catalytic site
@en
Golgi -mannosidase II cleaves two sugars sequentially in the same catalytic site
@nl
P2093
P2860
P356
P1476
Golgi -mannosidase II cleaves two sugars sequentially in the same catalytic site
@en
P2093
David R Rose
Douglas A Kuntz
Niket Shah
P2860
P304
P356
10.1073/PNAS.0802206105
P407
P577
2008-07-15T00:00:00Z