Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells.
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Targeting Selectins and Their Ligands in CancerCancer metabolism and elevated O-GlcNAc in oncogenic signalingProteolysis of HCF-1 by Ser/Thr glycosylation-incompetent O-GlcNAc transferase:UDP-GlcNAc complexes.Structural snapshots of the reaction coordinate for O-GlcNAc transferaseO-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysisA neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferaseBase-modified Donor Analogues Reveal Novel Dynamic Features of a GlycosyltransferaseBisubstrate UDP–peptide conjugates as human O-GlcNAc transferase inhibitorsHCF-1 Is Cleaved in the Active Site of O-GlcNAc TransferaseO-GlcNAcylation and oxidation of proteins: is signalling in the cardiovascular system becoming sweeter?Glycomimetics Targeting Glycosyltransferases: Synthetic, Computational and Structural Studies of Less-Polar ConjugatesDistinct OGT-Binding Sites Promote HCF-1 CleavageDiscovery of inhibitors of Leishmania β-1,2-mannosyltransferases using a click-chemistry-derived guanosine monophosphate librarySpindle pole cohesion requires glycosylation-mediated localization of NuMA.Advancement of Sialyltransferase Inhibitors: Therapeutic Challenges and OpportunitiesGlycosidase inhibitors: a patent review (2008-2013).Evidence for a Functional O-Linked N-Acetylglucosamine (O-GlcNAc) System in the Thermophilic Bacterium Thermobaculum terrenumHyper-O-GlcNAcylation is anti-apoptotic and maintains constitutive NF-κB activity in pancreatic cancer cellsThe role of O-GlcNAc signaling in the pathogenesis of diabetic retinopathy.O-GlcNAcylation stabilizes β-catenin through direct competition with phosphorylation at threonine 41.O-GlcNAcylation regulates cancer metabolism and survival stress signaling via regulation of the HIF-1 pathway.Iminosugar C-glycoside analogues of α-D-GlcNAc-1-phosphate: synthesis and bacterial transglycosylase inhibition.Development of inhibitors as research tools for carbohydrate-processing enzymes.Versatile O-GlcNAc transferase assay for high-throughput identification of enzyme variants, substrates, and inhibitors.O-GlcNAcase Expression is Sensitive to Changes in O-GlcNAc Homeostasis.The making of a sweet modification: structure and function of O-GlcNAc transferase.Systemic blockade of sialylation in mice with a global inhibitor of sialyltransferases.The non-metabolizable glucose analog D-glucal inhibits aflatoxin biosynthesis and promotes kojic acid production in Aspergillus flavusA small molecule that inhibits OGT activity in cells.mTOR/MYC Axis Regulates O-GlcNAc Transferase Expression and O-GlcNAcylation in Breast Cancer.The active site of O-GlcNAc transferase imposes constraints on substrate sequenceA common sugar-nucleotide-mediated mechanism of inhibition of (glycosamino)glycan biosynthesis, as evidenced by 6F-GalNAc (Ac3)O-GlcNAc modification of transcription factor Sp1 mediates hyperglycemia-induced VEGF-A upregulation in retinal cells.The roles of O-linked β-N-acetylglucosamine in cardiovascular physiology and disease.5-thiomannosides block the biosynthesis of dolichol-linked oligosaccharides and mimic class I congenital disorders of glycosylationNovel UDP-GalNAc Derivative Structures Provide Insight into the Donor Specificity of Human Blood Group Glycosyltransferase.Dual functionality of O-GlcNAc transferase is required for Drosophila development.Post-translational O-GlcNAcylation is essential for nuclear pore integrity and maintenance of the pore selectivity filter.Serum-stimulated cell cycle entry promotes ncOGT synthesis required for cyclin D expressionDevelopment of orally active inhibitors of protein and cellular fucosylation
P2860
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P2860
Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells.
description
2011 nî lūn-bûn
@nan
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
2011年论文
@zh
2011年论文
@zh-cn
name
Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells.
@en
type
label
Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells.
@en
prefLabel
Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells.
@en
P2093
P2860
P356
P1476
Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells
@en
P2093
David L Shen
Julia E Heinonen
Lehua Deng
Tracey M Gloster
Wesley F Zandberg
P2860
P2888
P304
P356
10.1038/NCHEMBIO.520
P577
2011-01-23T00:00:00Z