Characterization of 4-hydroxy-2-nonenal-modified peptides by liquid chromatography-tandem mass spectrometry using data-dependent acquisition: neutral loss-driven MS3 versus neutral loss-driven electron capture dissociation.

Characterization of 4-hydroxy-2-nonenal-modified peptides by liquid chromatography-tandem mass spectrometry using data-dependent acquisition: neutral loss-driven MS3 versus neutral loss-driven electron capture dissociation.

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http://www.wikidata.org/entity/Q33391997

Q33391997

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Protein lipoxidation: Detection strategies and challenges Protein modifications by electrophilic lipoxidation products: adduct formation, chemical strategies and tandem mass spectrometry for their detection and identification Protein adducts of aldehydic lipid peroxidation products identification and characterization of protein adducts using an aldehyde/keto-reactive probe in combination with mass spectrometry Detection and identification of 4-hydroxy-2-nonenal Schiff-base adducts along with products of Michael addition using data-dependent neutral loss-driven MS3 acquisition: method evaluation through an in vitro study on cytochrome c oxidase modificatio Site-specific protein adducts of 4-hydroxy-2(E)-nonenal in human THP-1 monocytic cells: protein carbonylation is diminished by ascorbic acid.Effects of ionizing radiation on biological molecules--mechanisms of damage and emerging methods of detection A mass spectrometric analysis of 4-hydroxy-2-(E)-nonenal modification of cytochrome c.Targeted 18O-labeling for improved proteomic analysis of carbonylated peptides by mass spectrometry Proteomic identification of carbonylated proteins and their oxidation sites A comparative 'bottom up' proteomics strategy for the site-specific identification and quantification of protein modifications by electrophilic lipids.Qualitative and quantitative evaluation of derivatization reagents for different types of protein-bound carbonyl groups.The lipid peroxidation product 4-hydroxy-2-nonenal: Advances in chemistry and analysis Selective chemoprecipitation and subsequent release of tagged species for the analysis of nitropeptides by liquid chromatography-tandem mass spectrometry Exploring the biology of lipid peroxidation-derived protein carbonylation.Isotope-coded dimethyl tagging for differential quantification of posttranslational protein carbonylation by 4-hydroxy-2-nonenal, an end-product of lipid peroxidation.Site-specific proteomic analysis of lipoxidation adducts in cardiac mitochondria reveals chemical diversity of 2-alkenal adduction To tag or not to tag: a comparative evaluation of immunoaffinity-labeling and tandem mass spectrometry for the identification and localization of posttranslational protein carbonylation by 4-hydroxy-2-nonenal, an end-product of lipid peroxidation.Protein targets for carbonylation by 4-hydroxy-2-nonenal in rat liver mitochondria.Selective chemoprecipitation to enrich nitropeptides from complex proteomes for mass-spectrometric analysis Cardiovascular redox and ox stress proteomics.Relative quantitation of protein nitration by liquid chromatography-mass spectrometry using isotope-coded dimethyl labeling and chemoprecipitation.The reactivity of human serum albumin toward trans-4-hydroxy-2-nonenal.An overview of the chemistry and biology of reactive aldehydes.Carbonylation of mitochondrial aconitase with 4-hydroxy-2-(E)-nonenal: localization and relative reactivity of addition sites.Phenolic compounds protect cultured hippocampal neurons against ethanol-withdrawal induced oxidative stress.Advances in methods for the determination of biologically relevant lipid peroxidation products.Protein carbonylation as a major hallmark of oxidative damage: update of analytical strategies.Redox proteomics: Methods for the identification and enrichment of redox-modified proteins and their applications.Mechanisms of 4-hydroxy-2-nonenal induced pro- and anti-apoptotic signaling.4-HNE adduct stability characterized by collision-induced dissociation and electron transfer dissociation mass spectrometry.Conversion of 3-nitrotyrosine to 3-aminotyrosine residues facilitates mapping of tyrosine nitration in proteins by electrospray ionization-tandem mass spectrometry using electron capture dissociation.

P2860

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P2860

Characterization of 4-hydroxy-2-nonenal-modified peptides by liquid chromatography-tandem mass spectrometry using data-dependent acquisition: neutral loss-driven MS3 versus neutral loss-driven electron capture dissociation.

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http://www.wikidata.org/entity/Q33391997

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2009 nî lūn-bûn

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2009 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2009 թվականի հունվարին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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