Structure of human O-GlcNAc transferase and its complex with a peptide substrate - Test2 - elhamkhani - TriplyDB

Structure of human O-GlcNAc transferase and its complex with a peptide substrate

Structure of human O-GlcNAc transferase and its complex with a peptide substrate

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TMTC1 and TMTC2 are novel endoplasmic reticulum tetratricopeptide repeat-containing adapter proteins involved in calcium homeostasis Glucose regulates mitochondrial motility via Milton modification by O-GlcNAc transferase.TET2 promotes histone O-GlcNAcylation during gene transcription Structure of human POFUT2: insights into thrombospondin type 1 repeat fold and O-fucosylation Glycosyltransferase-mediated Sweet Modification in Oral Streptococci Proteolysis of HCF-1 by Ser/Thr glycosylation-incompetent O-GlcNAc transferase:UDP-GlcNAc complexes.X-ray structure of a bacterial oligosaccharyltransferase Structural Insights into the Glycosyltransferase Activity of the Actinobacillus pleuropneumoniae HMW1C-like Protein Structural Insights into the Mechanism of Protein O-Fucosylation 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 Synergy of Peptide and Sugar in O-GlcNAcase Substrate Recognition Structure of a bacterial putative acetyltransferase defines the fold of the human O-GlcNAcase C-terminal domain HCF-1 Is Cleaved in the Active Site of O-GlcNAc Transferase Structure of a Novel O -Linked N -Acetyl-d-glucosamine ( O -GlcNAc) Transferase, GtfA, Reveals Insights into the Glycosylation of Pneumococcal Serine-rich Repeat Adhesins O-GlcNAcylation and oxidation of proteins: is signalling in the cardiovascular system becoming sweeter?How the glycosyltransferase OGT catalyzes amide bond cleavage Glycosyltransferase structural biology and its role in the design of catalysts for glycosylation The molecular basis of emerin-emerin and emerin-BAF interactions Distinct OGT-Binding Sites Promote HCF-1 Cleavage Global identification and characterization of both O-GlcNAcylation and phosphorylation at the murine synapse The Arabidopsis O-fucosyltransferase SPINDLY activates nuclear growth repressor DELLA O-GlcNAcylation of master growth repressor DELLA by SECRET AGENT modulates multiple signaling pathways in Arabidopsis.Evidence for a Functional O-Linked N-Acetylglucosamine (O-GlcNAc) System in the Thermophilic Bacterium Thermobaculum terrenum Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK)The putative eukaryote-like O-GlcNAc transferase of the cyanobacterium Synechococcus elongatus PCC 7942 hydrolyzes UDP-GlcNAc and is involved in multiple cellular processes.O-GlcNAc transferase (OGT) as a placental biomarker of maternal stress and reprogramming of CNS gene transcription in development.Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives Mechanistic study of CMP-Neu5Ac hydrolysis by α2,3-sialyltransferase from Pasteurella dagmatis.Extension of research data repository system to support direct compute access to biomedical datasets: enhancing Dataverse to support large datasets.The role of O-GlcNAc signaling in the pathogenesis of diabetic retinopathy.Targeted placental deletion of OGT recapitulates the prenatal stress phenotype including hypothalamic mitochondrial dysfunction.Substrate specificity of cytoplasmic N-glycosyltransferase Changes in metabolic chemical reporter structure yield a selective probe of O-GlcNAc modification A structural motif is the recognition site for a new family of bacterial protein O-glycosyltransferases.O-GlcNAc signaling in cancer metabolism and epigenetics Versatile O-GlcNAc transferase assay for high-throughput identification of enzyme variants, substrates, and inhibitors.Aberrant O-GlcNAcylated Proteins: New Perspectives in Breast and Colorectal Cancer.Locating sweet spots for screening hits and evaluating pan-assay interference filters from the performance analysis of two lead-like libraries

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Structure of human O-GlcNAc transferase and its complex with a peptide substrate

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2011 nî lūn-bûn

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2011 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2011年の論文

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name

Structure of human O-GlcNAc transferase and its complex with a peptide substrate

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Structure of human O-GlcNAc transferase and its complex with a peptide substrate

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Structure of human O-GlcNAc transferase and its complex with a peptide substrate

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Structure of human O-GlcNAc transferase and its complex with a peptide substrate

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Structure of human O-GlcNAc transferase and its complex with a peptide substrate

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Structure of human O-GlcNAc transferase and its complex with a peptide substrate

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Structure of human O-GlcNAc transferase and its complex with a peptide substrate

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Structure of human O-GlcNAc transferase and its complex with a peptide substrate

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Structure of human O-GlcNAc transferase and its complex with a peptide substrate

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Structure of human O-GlcNAc transferase and its complex with a peptide substrate

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Structure of human O-GlcNAc transferase and its complex with a peptide substrate

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Structure of human O-GlcNAc transferase and its complex with a peptide substrate

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Structure of human O-GlcNAc transferase and its complex with a peptide substrate

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Suzanne Walker

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Yunsun Nam

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P2860

Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression

Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats

O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats

Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance

The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny

The 1.9 Å crystal structure ofEscherichia coliMurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis

Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases

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

Structural insights into mechanism and specificity of O-GlcNAc transferase

Biochemistry and molecular cell biology of diabetic complications

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10.1038/NATURE09638

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Michael B Lazarus

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O-linked N-acetylglucosamine (GlcNAc) transferase

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3064491

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