A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase
about
Conformational analysis of Clostridium difficile toxin B and its implications for substrate recognitionO-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysisRational Design of Fatty Acid Amide Hydrolase Inhibitors That Act by Covalently Bonding to Two Active Site ResiduesBisubstrate UDP–peptide conjugates as human O-GlcNAc transferase inhibitorsHCF-1 Is Cleaved in the Active Site of O-GlcNAc TransferaseDesign of glycosyltransferase inhibitors: pyridine as a pyrophosphate surrogateGlycomimetics Targeting Glycosyltransferases: Synthetic, Computational and Structural Studies of Less-Polar ConjugatesModulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectivesVersatile O-GlcNAc transferase assay for high-throughput identification of enzyme variants, substrates, and inhibitors.Monitoring of Intracellular Tau Aggregation Regulated by OGA/OGT Inhibitors.The making of a sweet modification: structure and function of O-GlcNAc transferase.A small molecule that inhibits OGT activity in cells.O-GlcNAc modification of transcription factor Sp1 mediates hyperglycemia-induced VEGF-A upregulation in retinal cells.Enhanced transfer of a photocross-linking N-acetylglucosamine (GlcNAc) analog by an O-GlcNAc transferase mutant with converted substrate specificity.Chemical approaches to study O-GlcNAcylation.O-GlcNAc and the cardiovascular system.Viable screening targets related to the bacterial cell wall.Chemical tools to probe cellular O-GlcNAc signalling.Chemical tools to explore nutrient-driven O-GlcNAc cycling.Advances in understanding glycosyltransferases from a structural perspective.Biosynthetic Machinery Involved in Aberrant Glycosylation: Promising Targets for Developing of Drugs Against CancerDiscovery of a Low Toxicity O-GlcNAc Transferase (OGT) Inhibitor by Structure-based Virtual Screening of Natural ProductsChemical biologists rush to San Francisco for the ICBS.Electrophilic probes for deciphering substrate recognition by O-GlcNAc transferase.Thio-Linked UDP-Peptide Conjugates as O-GlcNAc Transferase Inhibitors.
P2860
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P2860
A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase
description
2011 nî lūn-bûn
@nan
2011 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase
@ast
A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase
@en
A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase
@nl
type
label
A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase
@ast
A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase
@en
A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase
@nl
prefLabel
A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase
@ast
A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase
@en
A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase
@nl
P2093
P2860
P356
P1476
A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase
@en
P2093
Jiaoyang Jiang
Lincoln Pasquina
Suzanne Walker
P2860
P2888
P356
10.1038/NCHEMBIO.711
P577
2011-11-13T00:00:00Z
P5875
P6179
1043170429