Enrichment and site mapping of O-linked N-acetylglucosamine by a combination of chemical/enzymatic tagging, photochemical cleavage, and electron transfer dissociation mass spectrometry.
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Functional O-GlcNAc modifications: implications in molecular regulation and pathophysiologyProteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometryHuman OGA binds substrates in a conserved peptide recognition grooveTau physiology and pathomechanisms in frontotemporal lobar degenerationA critical perspective of the diverse roles of O-GlcNAc transferase in chromatinSynthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational ModificationsProteomics of protein post-translational modifications implicated in neurodegenerationElectron transfer dissociation mass spectrometry in proteomicsCell signaling, post-translational protein modifications and NMR spectroscopyIdentification of Glycopeptides as Posttranslationally Modified Neoantigens in Leukemia.Quantitative proteomic analysis of histone modificationsO-Linked β-N-acetylglucosamine (O-GlcNAc) regulates emerin binding to barrier to autointegration factor (BAF) in a chromatin- and lamin B-enriched "niche".Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-specific O-GlcNAc transferase targets.Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesisMetabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway.Memory and synaptic plasticity are impaired by dysregulated hippocampal O-GlcNAcylation.The use of biophysical proteomic techniques in advancing our understanding of diseases.The role of O-GlcNAc signaling in the pathogenesis of diabetic retinopathy.Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.dbOGAP - an integrated bioinformatics resource for protein O-GlcNAcylation.Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.O-GlcNAc signaling: a metabolic link between diabetes and cancer?Mapping of O-GlcNAc sites of 20 S proteasome subunits and Hsp90 by a novel biotin-cystamine tag.Beta-N-acetylglucosamine (O-GlcNAc) is part of the histone codeIncorporation of unnatural sugars for the identification of glycoproteins.Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrilsThe E2F-1 associated retinoblastoma-susceptibility gene product is modified by O-GlcNAc.O-GlcNAcylation: a novel pathway contributing to the effects of endothelin in the vasculature.Protein analysis by shotgun/bottom-up proteomicsThe emerging link between O-GlcNAc and Alzheimer disease.Proteomic approaches for site-specific O-GlcNAcylation analysis.Characterization and diagnostic value of amino acid side chain neutral losses following electron-transfer dissociation.Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1Reversible hydrazide chemistry-based enrichment for O-GlcNAc-modified peptides and glycopeptides having non-reducing GlcNAc residues.Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells.Characterization and identification of protein O-GlcNAcylation sites with substrate specificity.Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease.A two-layered machine learning method to identify protein O-GlcNAcylation sites with O-GlcNAc transferase substrate motifs.The dynamic stress-induced "O-GlcNAc-ome" highlights functions for O-GlcNAc in regulating DNA damage/repair and other cellular pathways.Activity Based High-Throughput Screening for Novel O-GlcNAc Transferase Substrates Using a Dynamic Peptide Microarray
P2860
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P2860
Enrichment and site mapping of O-linked N-acetylglucosamine by a combination of chemical/enzymatic tagging, photochemical cleavage, and electron transfer dissociation mass spectrometry.
description
2009 nî lūn-bûn
@nan
2009 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Enrichment and site mapping of ...... issociation mass spectrometry.
@ast
Enrichment and site mapping of ...... issociation mass spectrometry.
@en
type
label
Enrichment and site mapping of ...... issociation mass spectrometry.
@ast
Enrichment and site mapping of ...... issociation mass spectrometry.
@en
prefLabel
Enrichment and site mapping of ...... issociation mass spectrometry.
@ast
Enrichment and site mapping of ...... issociation mass spectrometry.
@en
P2093
P2860
P1476
Enrichment and site mapping of ...... issociation mass spectrometry.
@en
P2093
Donald F Hunt
Gerald W Hart
Meaghan O'Malley
Namrata D Udeshi
Zihao Wang
P2860
P304
P356
10.1074/MCP.M900268-MCP200
P577
2009-08-19T00:00:00Z