A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo - Wikidata - awgldk - TriplyDB

A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo

A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo

http://www.wikidata.org/entity/Q27650997

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O-GlcNAcylation: a bridge between glucose and cell differentiation Diverse molecular targets for therapeutic strategies in Alzheimer's disease Developing therapeutic approaches to tau, selected kinases, and related neuronal protein targets Functional O-GlcNAc modifications: implications in molecular regulation and pathophysiology Glycotherapy: new advances inspire a reemergence of glycans in medicine Elevation of Global O-GlcNAc Levels in 3T3-L1 Adipocytes by Selective Inhibition of O-GlcNAcase Does Not Induce Insulin Resistance GlcNAcstatins are nanomolar inhibitors of human O -GlcNAcase inducing cellular hyper- O -GlcNAcylation Insight into a strategy for attenuating AmpC-mediated β-lactam resistance: Structural basis for selective inhibition of the glycoside hydrolase NagZ Screening-based discovery of drug-likeO-GlcNAcase inhibitor scaffolds Substrate and product analogues as human O-GlcNAc transferase inhibitors Inhibition of a bacterial O-GlcNAcase homologue by lactone and lactam derivatives: structural, kinetic and thermodynamic analyses Inhibition of O-GlcNAcase Using a Potent and Cell-Permeable Inhibitor Does Not Induce Insulin Resistance in 3T3-L1 Adipocytes Cell-Penetrant, Nanomolar O-GlcNAcase Inhibitors Selective against Lysosomal Hexosaminidases Synergy of Peptide and Sugar in O-GlcNAcase Substrate Recognition Gaining insight into the inhibition of glycoside hydrolase family 20 exo-β-N-acetylhexosaminidases using a structural approach Structure of a bacterial putative acetyltransferase defines the fold of the human O-GlcNAcase C-terminal domain Structural snapshots illustrate the catalytic cycle of β-galactocerebrosidase, the defective enzyme in Krabbe disease.Three-dimensional structure of aStreptomyces sviceusGNAT acetyltransferase with similarity to the C-terminal domain of the human GH84O-GlcNAcase Gaining insight into the catalysis by GH20 lacto-N-biosidase using small molecule inhibitors and structural analysis A Convenient Approach to Stereoisomeric Iminocyclitols: Generation of Potent Brain-Permeable OGA Inhibitors N-Acetyl glycals are tight-binding and environmentally insensitive inhibitors of hexosaminidases Interplay between troponin T phosphorylation and O-N-acetylglucosaminylation in ischaemic heart failure Mutations in EOGT confirm the genetic heterogeneity of autosomal-recessive Adams-Oliver syndrome Increasing brain protein O-GlcNAc-ylation mitigates breathing defects and mortality of Tau.P301L mice O-linked β-N-acetylglucosamine supports p38 MAPK activation by high glucose in glomerular mesangial cells Differential effects of an O-GlcNAcase inhibitor on tau phosphorylation O-GlcNAcase: promiscuous hexosaminidase or key regulator of O-GlcNAc signaling?Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK)O-Linked β-N-acetylglucosamine (O-GlcNAc) regulates emerin binding to barrier to autointegration factor (BAF) in a chromatin- and lamin B-enriched "niche".Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-specific O-GlcNAc transferase targets.Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway.O-GlcNAc cycling mutants modulate proteotoxicity in Caenorhabditis elegans models of human neurodegenerative diseases.The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine O-linked beta-N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress Activation of AKT by O-linked N-acetylglucosamine induces vascular calcification in diabetes mellitus The role of O-GlcNAc signaling in the pathogenesis of diabetic retinopathy.Inhibition of O-GlcNAcase leads to elevation of O-GlcNAc tau and reduction of tauopathy and cerebrospinal fluid tau in rTg4510 mice Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.Mechanisms of tau-induced neurodegeneration.Acute regulation of cardiac metabolism by the hexosamine biosynthesis pathway and protein O-GlcNAcylation.

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A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo

http://www.wikidata.org/entity/Q27650997

description

2008 nî lūn-bûn

@nan

2008 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2008年の論文

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2008年論文

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2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

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2008年論文

@zh-tw

2008年论文

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name

A potent mechanism-inspired O- ...... phosphorylation of tau in vivo

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A potent mechanism-inspired O- ...... phosphorylation of tau in vivo

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A potent mechanism-inspired O- ...... phosphorylation of tau in vivo

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A potent mechanism-inspired O- ...... phosphorylation of tau in vivo

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A potent mechanism-inspired O- ...... phosphorylation of tau in vivo

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A potent mechanism-inspired O- ...... phosphorylation of tau in vivo

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A potent mechanism-inspired O- ...... phosphorylation of tau in vivo

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Nature Chemical Biology

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A potent mechanism-inspired O- ...... phosphorylation of tau in vivo

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Ernest J McEachern

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Garrett E Whitworth

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Julia E Heinonen

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Rebecca J Dennis

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Scott A Yuzwa

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Xiaoyang Shan

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483-90

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scholarly article

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1286903

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10.1038/NCHEMBIO.96

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8

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4

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Matthew S Macauley

David J Vocadlo

Keith A. Stubbs

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2008-08-01T00:00:00Z

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5267334

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1050435297

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18587388

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phosphorylation