A chemical approach for identifying O-GlcNAc-modified proteins in cells. - sprookjes - yvandenbroek - TriplyDB

A chemical approach for identifying O-GlcNAc-modified proteins in cells.

A chemical approach for identifying O-GlcNAc-modified proteins in cells.

http://www.wikidata.org/entity/Q35242785

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Exploring the O-GlcNAc proteome: direct identification of O-GlcNAc-modified proteins from the brain Modification-specific proteomics: strategies for characterization of post-translational modifications using enrichment techniques Bioorthogonal chemistry: fishing for selectivity in a sea of functionality Copper-free click chemistry for dynamic in vivo imaging Large-scale approaches for glycobiology.Chemical Lectinology: Tools for Probing the Ligands and Dynamics of Mammalian Lectins In Vivo Specific and quantitative labeling of biomolecules using click chemistry Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometry O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysis Metabolism 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-ACETYLGLUCOSAMINIDASE Development and Applications of the Copper-Catalyzed Azide-Alkyne Cycloaddition (CuAAC) as a Bioorthogonal Reaction The hexosamine signaling pathway: deciphering the "O-GlcNAc code"Discovery and confirmation of O-GlcNAcylated proteins in rat liver mitochondria by combination of mass spectrometry and immunological methods CYP450 Enzymes Effect Oxygen-Dependent Reduction of Azide-Based Fluorogenic Dyes Imaging the glycome in living systems Bioorthogonal labeling cell-surface proteins expressed in pancreatic cancer cells to identify potential diagnostic/therapeutic biomarkers O-GlcNAcylation of master growth repressor DELLA by SECRET AGENT modulates multiple signaling pathways in Arabidopsis.Enzymatic labeling of proteins: techniques and approaches Quantitative proteomic analysis of histone modifications Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway.Staudinger ligation of peptides at non-glycyl residues.In vivo imaging of Caenorhabditis elegans glycans The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine Targeted metabolic labeling of yeast N-glycans with unnatural sugars O-GlcNAc-ylation in the Nuclear Pore Complex.Chemoselective attachment of small molecule effector functionality to human adenoviruses facilitates gene delivery to cancer cells.Real-time bioluminescence imaging of glycans on live cells.Bioorthogonal chemistry: recent progress and future directions.Bioorthogonal Chemistry-A Covalent Strategy for the Study of Biological Systems.Chemoenzymatic synthesis of uridine 5'-diphospho-2-acetonyl-2-deoxy-alpha-D-glucose as C(2)-carbon isostere of UDP-GlcNAc O-GlcNAc signaling in the cardiovascular system.Changes in metabolic chemical reporter structure yield a selective probe of O-GlcNAc modification Discovery of O-GlcNAc-6-phosphate modified proteins in large-scale phosphoproteomics data.A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation.Probing mucin-type O-linked glycosylation in living animals Assignment of protein function in the postgenomic era.O-GlcNAcylation: a novel post-translational mechanism to alter vascular cellular signaling in health and disease: focus on hypertension.Substrate specificity provides insights into the sugar donor recognition mechanism of O-GlcNAc transferase (OGT).Proteomic approaches for site-specific O-GlcNAcylation analysis.Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1

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P2860

A chemical approach for identifying O-GlcNAc-modified proteins in cells.

http://www.wikidata.org/entity/Q35242785

description

2003 nî lūn-bûn

@nan

2003 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի հուլիսին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

A chemical approach for identifying O-GlcNAc-modified proteins in cells.

@ast

A chemical approach for identifying O-GlcNAc-modified proteins in cells.

@en

type

label

A chemical approach for identifying O-GlcNAc-modified proteins in cells.

@ast

A chemical approach for identifying O-GlcNAc-modified proteins in cells.

@en

prefLabel

A chemical approach for identifying O-GlcNAc-modified proteins in cells.

@ast

A chemical approach for identifying O-GlcNAc-modified proteins in cells.

@en

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Proceedings of the National Academy of Sciences of the United States of America

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A chemical approach for identifying O-GlcNAc-modified proteins in cells.

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David J Vocadlo

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Eun-Ju Kim

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Howard C Hang

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John A Hanover

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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

Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain

O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation

Insulin-dependent activation of endothelial nitric oxide synthase is impaired by O-linked glycosylation modification of signaling proteins in human coronary endothelial cells

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

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

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

Cell surface engineering by a modified Staudinger reaction

Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications

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9116-9121

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16

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100

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Carolyn Bertozzi

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2003-07-21T00:00:00Z

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10651205

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171382

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