About: Selective Detection and Site-Analysis of O-GlcNAc-Modified Glycopeptides by β-Elimination and Tandem Electrospray Mass Spectrometry

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About: Selective Detection and Site-Analysis of O-GlcNAc-Modified Glycopeptides by β-Elimination and Tandem Electrospray Mass Spectrometry Goto Sponge NotDistinct Permalink

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scientific article published on 01 February 1996

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в лютому 1996 (uk) im Februar 1996 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en febreru de 1996 (ast) artikull shkencor i botuar më 01 shkurt 1996 (sq) scientific article published on 01 February 1996 (en)
publication date	wds:Q63361145-32CB594E-72CA-4653-AA2D-A67807702117
publication date	1996-02-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q63361145-47BBD32F-90F6-4886-A30E-235D8ADDA046
language of work or name	English
author name string	wds:Q63361145-183E0351-7E97-4246-A76E-D44C561E3D2F wds:Q63361145-52698F0A-3E8B-41DB-B8B4-6420D9E501C6 wds:Q63361145-57858363-AE48-46B0-A6A4-BBDD6F3F678B wds:Q63361145-7E6AB22A-EF3D-4AC9-B0A9-B908B70912D2 wds:Q63361145-C8674FD1-C425-4987-A27D-0D935F8959B6
author name string	Barnes S Kirk M Hart GW Hayes BK Comer FI
rdfs:label	Selective Detection and Site-Analysis of O-GlcNAc-Modified Glycopeptides by β-Elimination and Tandem Electrospray Mass Spectrometry (en) Selective Detection and Site-Analysis of O-GlcNAc-Modified Glycopeptides by β-Elimination and Tandem Electrospray Mass Spectrometry (nl) Selective Detection and Site-Analysis of O-GlcNAc-Modified Glycopeptides by β-Elimination and Tandem Electrospray Mass Spectrometry (sq)
skos:prefLabel	Selective Detection and Site-Analysis of O-GlcNAc-Modified Glycopeptides by β-Elimination and Tandem Electrospray Mass Spectrometry (en) Selective Detection and Site-Analysis of O-GlcNAc-Modified Glycopeptides by β-Elimination and Tandem Electrospray Mass Spectrometry (nl) Selective Detection and Site-Analysis of O-GlcNAc-Modified Glycopeptides by β-Elimination and Tandem Electrospray Mass Spectrometry (sq)
name	Selective Detection and Site-Analysis of O-GlcNAc-Modified Glycopeptides by β-Elimination and Tandem Electrospray Mass Spectrometry (en) Selective Detection and Site-Analysis of O-GlcNAc-Modified Glycopeptides by β-Elimination and Tandem Electrospray Mass Spectrometry (nl) Selective Detection and Site-Analysis of O-GlcNAc-Modified Glycopeptides by β-Elimination and Tandem Electrospray Mass Spectrometry (sq)
author	wds:Q63361145-0B0924B5-CC83-4158-B80F-F0F2A3C98345 wds:Q63361145-F90D3A02-94ED-46D8-8E47-1FF295D3A7DA
author	Todd L. Lowary Kenneth D. Greis
title	wds:Q63361145-43554FB8-E232-46CD-BF01-8F31617479F8
title	Selective detection and site-analysis of O-GlcNAc-modified glycopeptides by beta-elimination and tandem electrospray mass spectrometry (en)
page(s)	wds:Q63361145-706B336C-F79B-42B6-903F-82058FF0E5E3
page(s)	38-49
instance of	wds:Q63361145-FE9AFA04-9B33-4FDC-8E5B-20DD00AB7E3F
instance of	scholarly article
main subject	wds:Q63361145-00810EFC-E6E7-4325-905D-3D33362C3DA0
main subject	mass spectrometry
PubMed ID	wds:Q63361145-B04523D0-B5ED-49D1-B228-7CBDC913854A
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8742080
PubMed ID	8742080
published in	wds:Q63361145-BD8C54F3-F3FE-4F85-AEF3-8CB5084B4B7B
published in	Analytical Biochemistry
issue	wds:Q63361145-264B236B-D472-4917-BF41-3286CBA6D1F6
volume	wds:Q63361145-8C5376EF-EE19-4953-A860-DA99289BEE1C
issue	1
volume	234
DOI	wds:Q63361145-9B80A37B-E4B3-48CA-9111-37464ABBD8CD
DOI	http://dx.doi.org/10.1006/ABIO.1996.0047
DOI	10.1006/ABIO.1996.0047
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q63361145
is cites work of	The diversity of O-linked glycans expressed during Drosophila melanogaster development reflects stage- and tissue-specific requirements for cell signaling Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: a new paradigm for metabolic control of signal transduction and transcription Probing mucin-type O-linked glycosylation in living animals O-sulfonation of serine and threonine: mass spectrometric detection and characterization of a new posttranslational modification in diverse proteins throughout the eukaryotes. O-GlcNAc: a regulatory post-translational modification. Synthetic methods of glycopeptide assembly, and biological analysis of glycopeptide products Mapping posttranslational modifications of proteins by MS-based selective detection: application to phosphoproteomics Phosphospecific proteolysis for mapping sites of protein phosphorylation Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-specific O-GlcNAc transferase targets Identification of protein O-GlcNAcylation sites using electron transfer dissociation mass spectrometry on native peptides O-GlcNAc and the control of gene expression Identification of novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry. Nucleocytoplasmic O-glycosylation: O-GlcNAc and functional proteomics Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease Proteome analysis of glycoforms: a review of strategies for the microcharacterisation of glycoproteins separated by two-dimensional polyacrylamide gel electrophoresis. High-sensitivity analytical approaches for the structural characterization of glycoproteins Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Detection and analysis of proteins modified by O-linked N-acetylglucosamine Identification of phosphorylated and glycosylated sites in peptides by chemically targeted proteolysis. Protein analysis by shotgun/bottom-up proteomics Identification of the major site of O-linked beta-N-acetylglucosamine modification in the C terminus of insulin receptor substrate-1. The E2F-1 associated retinoblastoma-susceptibility gene product is modified by O-GlcNAc Glycosylation of the nuclear pore O-GlcNAc signaling in the cardiovascular system Proteomics: the first decade and beyond Artifactual sulfation of silver-stained proteins: implications for the assignment of phosphorylation and sulfation sites Mass spectrometry based glycoproteomics--from a proteomics perspective Glycobiology and proteomics: is mass spectrometry the Holy Grail? Detection and analysis of proteins modified by O-linked N-acetylglucosamine A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation Phagocytosis stimulates alternative glycosylation of macrosialin (mouse CD68), a macrophage-specific endosomal protein Nuclear and cytoplasmic glycosylation. Determination of glycosylation sites and site-specific heterogeneity in glycoproteins. O-GlcNAc and the cardiovascular system. Comparative proteomics based on stable isotope labeling and affinity selection Studying simple epithelial keratins in cells and tissues. Automated glycopeptide analysis--review of current state and future directions Chemical arsenal for the study of O-GlcNAc. O-GlcNAc profiling: from proteins to proteomes The glycomics of glycan glucuronylation in Drosophila melanogaster The combination of electron capture dissociation and fixed charge derivatization increases sequence coverage for O-glycosylated and O-phosphorylated peptides Direct Monitoring of Protein O-GlcNAcylation by High-Resolution Native Mass Spectrometry Isotope Targeted Glycoproteomics (IsoTaG) to Characterize Intact, Metabolically Labeled Glycopeptides from Complex Proteomes Chip-based CE coupled to a quadrupole TOF mass spectrometer for the analysis of a glycopeptide

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