Structural analyses of enzymes involved in the O-GlcNAc modification.
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Inhibition 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 AdipocytesMetabolism 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-ACETYLGLUCOSAMINIDASEIncreasing brain protein O-GlcNAc-ylation mitigates breathing defects and mortality of Tau.P301L miceEvidence for a Functional O-Linked N-Acetylglucosamine (O-GlcNAc) System in the Thermophilic Bacterium Thermobaculum terrenumStructure-based evolutionary relationship of glycosyltransferases: a case study of vertebrate β1,4-galactosyltransferase, invertebrate β1,4-N-acetylgalactosaminyltransferase and α-polypeptidyl-N-acetylgalactosaminyltransferaseO-GlcNAcylation of the Plum pox virus capsid protein catalyzed by SECRET AGENT: characterization of O-GlcNAc sites by electron transfer dissociation mass spectrometry.O-GlcNAc protein modification in plants: Evolution and function.Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.The making of a sweet modification: structure and function of O-GlcNAc transferase.Comparative analysis of plant carbohydrate active enZymes and their role in xylogenesis.Chemical approaches to study O-GlcNAcylation.Chemical tools to probe cellular O-GlcNAc signalling.Dissecting conformational contributions to glycosidase catalysis and inhibition.Damaging effects of hyperglycemia on cardiovascular function: spotlight on glucose metabolic pathways.Direct evidence of O-GlcNAcylation in the apicomplexan Toxoplasma gondii: a biochemical and bioinformatic study.Exploring the sequence context of phosphorylatable amino acids: the contribution of the upgraded MAPRes tool.The Arabidopsis O-linked N-acetylglucosamine transferase SPINDLY interacts with class I TCPs to facilitate cytokinin responses in leaves and flowers.Computational evidence for the substrate-assisted catalytic mechanism of O-GlcNAcase. A DFT investigation
P2860
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P2860
Structural analyses of enzymes involved in the O-GlcNAc modification.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 30 July 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Structural analyses of enzymes involved in the O-GlcNAc modification.
@en
Structural analyses of enzymes involved in the O-GlcNAc modification.
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type
label
Structural analyses of enzymes involved in the O-GlcNAc modification.
@en
Structural analyses of enzymes involved in the O-GlcNAc modification.
@nl
prefLabel
Structural analyses of enzymes involved in the O-GlcNAc modification.
@en
Structural analyses of enzymes involved in the O-GlcNAc modification.
@nl
P1476
Structural analyses of enzymes involved in the O-GlcNAc modification.
@en
P2093
Carlos Martinez-Fleites
P304
P356
10.1016/J.BBAGEN.2009.07.019
P407
P577
2009-07-30T00:00:00Z