Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells. - Wikidata - wikimedia - TriplyDB

Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells.

Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells.

http://www.wikidata.org/entity/Q38845236

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Targeting Selectins and Their Ligands in Cancer Cancer metabolism and elevated O-GlcNAc in oncogenic signaling Proteolysis of HCF-1 by Ser/Thr glycosylation-incompetent O-GlcNAc transferase:UDP-GlcNAc complexes.Structural snapshots of the reaction coordinate for O-GlcNAc transferase O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysis A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase Base-modified Donor Analogues Reveal Novel Dynamic Features of a Glycosyltransferase Bisubstrate UDP–peptide conjugates as human O-GlcNAc transferase inhibitors HCF-1 Is Cleaved in the Active Site of O-GlcNAc Transferase O-GlcNAcylation and oxidation of proteins: is signalling in the cardiovascular system becoming sweeter?Glycomimetics Targeting Glycosyltransferases: Synthetic, Computational and Structural Studies of Less-Polar Conjugates Distinct OGT-Binding Sites Promote HCF-1 Cleavage Discovery of inhibitors of Leishmania β-1,2-mannosyltransferases using a click-chemistry-derived guanosine monophosphate library Spindle pole cohesion requires glycosylation-mediated localization of NuMA.Advancement of Sialyltransferase Inhibitors: Therapeutic Challenges and Opportunities Glycosidase inhibitors: a patent review (2008-2013).Evidence for a Functional O-Linked N-Acetylglucosamine (O-GlcNAc) System in the Thermophilic Bacterium Thermobaculum terrenum Hyper-O-GlcNAcylation is anti-apoptotic and maintains constitutive NF-κB activity in pancreatic cancer cells The 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 flavus A 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 sequence A 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 glycosylation Novel 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 expression Development of orally active inhibitors of protein and cellular fucosylation

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P2860

Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells.

http://www.wikidata.org/entity/Q38845236

description

2011 nî lūn-bûn

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2011年の論文

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2011年論文

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2011年論文

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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.

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type

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Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells.

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prefLabel

Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells.

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Nature Chemical Biology

P1476

Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells

@en

P2093

David L Shen

http://www.w3.org/2001/XMLSchema#string

Julia E Heinonen

http://www.w3.org/2001/XMLSchema#string

Lehua Deng

http://www.w3.org/2001/XMLSchema#string

Tracey M Gloster

http://www.w3.org/2001/XMLSchema#string

Wesley F Zandberg

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P2860

Molecular cloning and characterization of murine and human N-acetylglucosamine kinase

Functional cloning and mutational analysis of the human cDNA for phosphoacetylglucosamine mutase: identification of the amino acid residues essential for the catalysis

Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance

Nuclear pore complex contains a family of glycoproteins that includes p62: glycosylation through a previously unidentified cellular pathway

Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation

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

Structural and mechanistic basis for a new mode of glycosyltransferase inhibition

Cell surface engineering by a modified Staudinger reaction

Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin

Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins

P2888

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174-181

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scholarly article

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10.1038/NCHEMBIO.520

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3

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7

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David J Vocadlo

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2011-01-23T00:00:00Z

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49777531

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21258330

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3202988

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