Site-specific protein adducts of 4-hydroxy-2(E)-nonenal in human THP-1 monocytic cells: protein carbonylation is diminished by ascorbic acid. - Wikidata - awgldk - TriplyDB

Site-specific protein adducts of 4-hydroxy-2(E)-nonenal in human THP-1 monocytic cells: protein carbonylation is diminished by ascorbic acid.

Site-specific protein adducts of 4-hydroxy-2(E)-nonenal in human THP-1 monocytic cells: protein carbonylation is diminished by ascorbic acid.

http://www.wikidata.org/entity/Q33674371

about

Alcohol, aldehydes, adducts and airways Vitamins C and E: beneficial effects from a mechanistic perspective 4-Hydroxy-nonenal-A Bioactive Lipid Peroxidation Product Protein lipoxidation: Detection strategies and challenges Human genetic variation influences vitamin C homeostasis by altering vitamin C transport and antioxidant enzyme function 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 Label-Free Proteomics Assisted by Affinity Enrichment for Elucidating the Chemical Reactivity of the Liver Mitochondrial Proteome toward Adduction by the Lipid Electrophile 4-hydroxy-2-nonenal (HNE)Redox proteomics in selected neurodegenerative disorders: from its infancy to future applications.Chemical probes for analysis of carbonylated proteins: a review.Stereoselective effects of 4-hydroxynonenal in cultured mouse hepatocytes.A targeted mass spectrometry-based approach for the identification and characterization of proteins containing α-aminoadipic and γ-glutamic semialdehyde residues.Identification of protein succination as a novel modification of tubulin Catabolism of 4-hydroxy-2-trans-nonenal by THP1 monocytes/macrophages and inactivation of carboxylesterases by this lipid electrophile.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.Vimentin filament organization and stress sensing depend on its single cysteine residue and zinc binding.Formation and signaling actions of electrophilic lipids A novel strategy for global analysis of the dynamic thiol redox proteome.Increased hepatocellular protein carbonylation in human end-stage alcoholic cirrhosis Comparing the efficiencies of hydrazide labels in the study of protein carbonylation in human serum albumin Alkylation damage by lipid electrophiles targets functional protein systems.Target molecules of food phytochemicals: food science bound for the next dimension.Modification of cysteine residues by cyclopentenone prostaglandins: interplay with redox regulation of protein function.Protein carbonylation as a major hallmark of oxidative damage: update of analytical strategies.New criteria for supplementation of selected micronutrients in the era of nutrigenetics and nutrigenomics.Gel-free proteomic methodologies to study reversible cysteine oxidation and irreversible protein carbonyl formation.The lipid peroxidation product 4-hydroxynonenal contributes to oxidative stress-mediated deterioration of the ageing oocyte.Mass spectrometry-based proteomics of oxidative stress: Identification of 4-hydroxy-2-nonenal (HNE) adducts of amino acids using lysozyme and bovine serum albumin as model proteins.Mass spectrometry-based quantification of myocardial protein adducts with acrolein in an in vivo model of oxidative stress.Ube2V2 Is a Rosetta Stone Bridging Redox and Ubiquitin Codes, Coordinating DNA Damage Responses.

P2860

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P2860

Site-specific protein adducts of 4-hydroxy-2(E)-nonenal in human THP-1 monocytic cells: protein carbonylation is diminished by ascorbic acid.

http://www.wikidata.org/entity/Q33674371

description

2010 nî lūn-bûn

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2010 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունվարին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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Site-specific protein adducts ...... s diminished by ascorbic acid.

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Site-specific protein adducts ...... s diminished by ascorbic acid.

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Site-specific protein adducts ...... s diminished by ascorbic acid.

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Site-specific protein adducts ...... s diminished by ascorbic acid.

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Site-specific protein adducts ...... s diminished by ascorbic acid.

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Chemical Research in Toxicology

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Site-specific protein adducts ...... is diminished by ascorbic acid

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Cristobal L Miranda

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Juan Chavez

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Mudita Singhal

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Woon-Gye Chung

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P2860

Sequence analysis and chromosomal localization of human Cap Z. Conserved residues within the actin-binding domain may link Cap Z to gelsolin/severin and profilin protein families

Multifunctional alpha-enolase: its role in diseases

Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes

Oxidative post-translational modification of tryptophan residues in cardiac mitochondrial proteins.

Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal.

Proteomic changes in renal cancer and co-ordinate demonstration of both the glycolytic and mitochondrial aspects of the Warburg effect.

New role for an old probe: affinity labeling of oxylipid protein conjugates by N'-aminooxymethylcarbonylhydrazino d-biotin.

Protein adducts generated from products of lipid oxidation: focus on HNE and one.

Design, synthesis, and application of a hydrazide-functionalized isotope-coded affinity tag for the quantification of oxylipid-protein conjugates.

Rapid characterization of covalent modifications to rat brain mitochondrial proteins after ex vivo exposure to 4-hydroxy-2-nonenal by liquid chromatography-tandem mass spectrometry using data-dependent and neutral loss-driven MS3 acquisition.

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37-47

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10.1021/TX9002462

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1

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40820882

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20043646

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2825578

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