Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity
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Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated beta-lactam resistanceElevation of Global O-GlcNAc Levels in 3T3-L1 Adipocytes by Selective Inhibition of O-GlcNAcase Does Not Induce Insulin ResistanceStreptococcus pneumoniae Endohexosaminidase D, Structural and Mechanistic Insight into Substrate-assisted Catalysis in Family 85 Glycoside HydrolasesPortrait of an Enzyme, a Complete Structural Analysis of a Multimodular -N-Acetylglucosaminidase from Clostridium perfringensGlcNAcstatins are nanomolar inhibitors of human O -GlcNAcase inducing cellular hyper- O -GlcNAcylationN-Acetylglucosamine Recognition by a Family 32 Carbohydrate-Binding Module from Clostridium perfringens NagHInsight into a strategy for attenuating AmpC-mediated β-lactam resistance: Structural basis for selective inhibition of the glycoside hydrolase NagZScreening-based discovery of drug-likeO-GlcNAcase inhibitor scaffoldsSubstrate and product analogues as human O-GlcNAc transferase inhibitorsInhibition of a bacterial O-GlcNAcase homologue by lactone and lactam derivatives: structural, kinetic and thermodynamic analysesThe structure of a family GH25 lysozyme fromAspergillus fumigatusInhibition of O-GlcNAcase Using a Potent and Cell-Permeable Inhibitor Does Not Induce Insulin Resistance in 3T3-L1 AdipocytesHuman OGA binds substrates in a conserved peptide recognition grooveSynergy of Peptide and Sugar in O-GlcNAcase Substrate RecognitionGaining insight into the inhibition of glycoside hydrolase family 20 exo-β-N-acetylhexosaminidases using a structural approachStructure of a bacterial putative acetyltransferase defines the fold of the human O-GlcNAcase C-terminal domainMetabolism of Vertebrate Amino Sugars with N-Glycolyl Groups: INTRACELLULAR -O-LINKED N-GLYCOLYLGLUCOSAMINE (GlcNGc), UDP-GlcNGc, AND THE BIOCHEMICAL AND STRUCTURAL RATIONALE FOR THE SUBSTRATE TOLERANCE OF -O-LINKED -N-ACETYLGLUCOSAMINIDASEThree-dimensional structure of aStreptomyces sviceusGNAT acetyltransferase with similarity to the C-terminal domain of the human GH84O-GlcNAcaseA Convenient Approach to Stereoisomeric Iminocyclitols: Generation of Potent Brain-Permeable OGA InhibitorsStructural and Biochemical Insights into the Peptidoglycan Hydrolase Domain of FlgJ from Salmonella typhimuriumO-GlcNAcase: promiscuous hexosaminidase or key regulator of O-GlcNAc signaling?Evidence for a Functional O-Linked N-Acetylglucosamine (O-GlcNAc) System in the Thermophilic Bacterium Thermobaculum terrenumThe putative eukaryote-like O-GlcNAc transferase of the cyanobacterium Synechococcus elongatus PCC 7942 hydrolyzes UDP-GlcNAc and is involved in multiple cellular processes.Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway.The hexosamine signaling pathway: O-GlcNAc cycling in feast or famineO-linked beta-N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stressOGA inhibition by GlcNAc-selenazolineDiscovery of selective small-molecule activators of a bacterial glycoside hydrolase.A lipid-droplet-targeted O-GlcNAcase isoform is a key regulator of the proteasomeCross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease.Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates.O-GlcNAc transferase and O-GlcNAcase: achieving target substrate specificity.By their genes ye shall know them: genomic signatures of predatory bacteriaDefining the structural origin of the substrate sequence independence of O-GlcNAcase using a combination of molecular docking and dynamics simulation.O-GlcNAc cycling: implications for neurodegenerative disorders.Nutrient-driven O-GlcNAc cycling - think globally but act locally.Site-specific interplay between O-GlcNAcylation and phosphorylation in cellular regulation.Providing β-lactams a helping hand: targeting the AmpC β-lactamase induction pathway.Developing inhibitors of glycan processing enzymes as tools for enabling glycobiology.Recent biotechnological progress in enzymatic synthesis of glycosides.
P2860
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P2860
Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity
description
2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2006
@ast
im April 2006 veröffentlichter wissenschaftlicher Artikel
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scientific journal article
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vedecký článok (publikovaný 2006/04/01)
@sk
vědecký článek publikovaný v roce 2006
@cs
wetenschappelijk artikel (gepubliceerd op 2006/04/01)
@nl
наукова стаття, опублікована у квітні 2006
@uk
مقالة علمية (نشرت في أبريل 2006)
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name
Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity
@ast
Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity
@en
Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity
@nl
type
label
Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity
@ast
Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity
@en
Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity
@nl
prefLabel
Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity
@ast
Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity
@en
Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity
@nl
P2093
P2860
P3181
P356
P1476
Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity
@en
P2093
David J. Vocadlo
Edward J. Taylor
Gary N. Black
Gideon J. Davies
Johan P. Turkenburg
Matthew S. Macauley
Rebecca J. Dennis
Samuel J. Hart
P2860
P2888
P304
P3181
P356
10.1038/NSMB1079
P577
2006-04-01T00:00:00Z