Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags. - Wikidata - wikimedia - TriplyDB

Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.

Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.

http://www.wikidata.org/entity/Q34075637

about

Phosphofructokinase 1 glycosylation regulates cell growth and metabolism Glycan Engineering for Cell and Developmental Biology MeCP2 post-translational modifications: a mechanism to control its involvement in synaptic plasticity and homeostasis?Functional O-GlcNAc modifications: implications in molecular regulation and pathophysiology Global identification and characterization of both O-GlcNAcylation and phosphorylation at the murine synapse Mass-tag labeling reveals site-specific and endogenous levels of protein S-fatty acylation Quantitative proteomic analysis of histone modifications Evidence for a Functional O-Linked N-Acetylglucosamine (O-GlcNAc) System in the Thermophilic Bacterium Thermobaculum terrenum Mammalian protein glycosylation--structure versus function.Quantitative investigation of human cell surface N-glycoprotein dynamics.Activation of the transcriptional function of the NF-κB protein c-Rel by O-GlcNAc glycosylation Tools for Studying Glycans: Recent Advances in Chemoenzymatic Glycan Labeling A novel deconvolution method for modeling UDP-N-acetyl-D-glucosamine biosynthetic pathways based on (13)C mass isotopologue profiles under non-steady-state conditions Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates Akt signaling.O-GlcNAc modification of the runt-related transcription factor 2 (Runx2) links osteogenesis and nutrient metabolism in bone marrow mesenchymal stem cells.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 Mechanisms of specificity in neuronal activity-regulated gene transcription Dynamic O-GlcNAc modification regulates CREB-mediated gene expression and memory formation Metabolic labeling enables selective photocrosslinking of O-GlcNAc-modified proteins to their binding partners.Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates.The roles of O-linked β-N-acetylglucosamine in cardiovascular physiology and disease.Enhanced transfer of a photocross-linking N-acetylglucosamine (GlcNAc) analog by an O-GlcNAc transferase mutant with converted substrate specificity.Overview: the maturing of proteomics in cardiovascular research.Chemical Methods for Encoding and Decoding of Posttranslational Modifications Chemical approaches to study O-GlcNAcylation.Dynamic O-GlcNAcylation and its roles in the cellular stress response and homeostasis.Identification of PSD-95 Depalmitoylating Enzymes.GlycoMine(struct): a new bioinformatics tool for highly accurate mapping of the human N-linked and O-linked glycoproteomes by incorporating structural features.Global Analysis of O-GlcNAc Glycoproteins in Activated Human T Cells O-GlcNAcomics--Revealing roles of O-GlcNAcylation in disease mechanisms and development of potential diagnostics.Visualization of O-GlcNAc glycosylation stoichiometry and dynamics using resolvable poly(ethylene glycol) mass tags.O-GlcNAcylation of ATG4B positively regulates autophagy by increasing its hydroxylase activity Microarray discovery of new OGT substrates: the medulloblastoma oncogene OTX2 is O-GlcNAcylated.Carbohydrate chemistry in drug discovery.Protein O-linked β-N-acetylglucosamine: a novel effector of cardiomyocyte metabolism and function.Recent progress in quantitative glycoproteomics.Chemical reporters for biological discovery.Glycosylation of the nuclear pore.O-GlcNAc profiling: from proteins to proteomes.

P2860

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P2860

Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.

http://www.wikidata.org/entity/Q34075637

description

2010 nî lūn-bûn

@nan

2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հուլիսին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.

@ast

Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.

@en

Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.

@nl

type

label

Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.

@ast

Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.

@en

Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.

@nl

prefLabel

Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.

@ast

Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.

@en

Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.

@nl

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Nature Chemical Biology

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Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.

@en

P2093

Claude J Rogers

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

Jessica E Rexach

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

Jifang Tao

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

Linda C Hsieh-Wilson

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

Seok-Ho Yu

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

Yi E Sun

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

P2860

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

Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance

Exploring the O-GlcNAc proteome: direct identification of O-GlcNAc-modified proteins from the brain

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

Structure-based design of beta 1,4-galactosyltransferase I (beta 4Gal-T1) with equally efficient N-acetylgalactosaminyltransferase activity: point mutation broadens beta 4Gal-T1 donor specificity

Transcriptional regulation by the phosphorylation-dependent factor CREB

SV40 large T antigen is modified with O-linked N-acetylglucosamine but not with other forms of glycosylation

PEGylation, successful approach to drug delivery

Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H

Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine

P2888

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645-651

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scholarly article

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10.1038/NCHEMBIO.412

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9

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6

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2010-07-25T00:00:00Z

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45288469

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20657584

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P932

2924450

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