Modification of histidine residues in proteins by reaction with 4-hydroxynonenal.
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Alcohol, aldehydes, adducts and airwaysRadiation Metabolomics: Current Status and Future DirectionsNew insights into the role of fatty acids in the pathogenesis and resolution of inflammatory bowel diseaseInhibitors of the Hydrolytic Enzyme Dimethylarginine Dimethylaminohydrolase (DDAH): Discovery, Synthesis and DevelopmentOxidative Stress and Carbonyl Lesions in Ulcerative Colitis and Associated Colorectal CancerProtein carbonylation, cellular dysfunction, and disease progressionReactions of electrophiles with nucleophilic thiolate sites: relevance to pathophysiological mechanisms and remediationT-REX on-demand redox targeting in live cells.Reactive oxygen species-induced molecular damage and its application in pathology.Two dimensional blue native/SDS-PAGE to identify mitochondrial complex I subunits modified by 4-hydroxynonenal (HNE).Convergence of nitric oxide and lipid signaling: anti-inflammatory nitro-fatty acids.Characterization of 4-HNE modified L-FABP reveals alterations in structural and functional dynamics.Nitrated fatty acids: Endogenous anti-inflammatory signaling mediatorsReversible post-translational modification of proteins by nitrated fatty acids in vivo.Effect of 4-hydroxy-2-nonenal modification on alpha-synuclein aggregation.The oxidative stress metabolite 4-hydroxynonenal promotes Alzheimer protofibril formation.Age-related alterations in oxidatively damaged proteins of mouse skeletal muscle mitochondrial electron transport chain complexes.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 modificatioOxidatively modified proteins in Alzheimer's disease (AD), mild cognitive impairment and animal models of AD: role of Abeta in pathogenesis.Activation of aldehyde dehydrogenase 2 (ALDH2) confers cardioprotection in protein kinase C epsilon (PKCvarepsilon) knockout mice.Effects of ionizing radiation on biological molecules--mechanisms of damage and emerging methods of detectionAldehyde dehydrogenase 2 in cardiac protection: a new therapeutic target?Retinol dehydrogenase 12 detoxifies 4-hydroxynonenal in photoreceptor cells.Post-translational protein modification by carotenoid cleavage products.Modifying apolipoprotein A-I by malondialdehyde, but not by an array of other reactive carbonyls, blocks cholesterol efflux by the ABCA1 pathwayAre ancient proteins responsible for the age-related decline in health and fitness?Oxidation of hepatic carnitine palmitoyl transferase-I (CPT-I) impairs fatty acid beta-oxidation in rats fed a methionine-choline deficient dietPathological aspects of lipid peroxidation.Ibuprofen attenuates oxidative damage through NOX2 inhibition in Alzheimer's diseaseChemical probes for analysis of carbonylated proteins: a review.Inactivation of ethanol-inducible cytochrome P450 and other microsomal P450 isozymes by trans-4-hydroxy-2-nonenal, a major product of membrane lipid peroxidation.Targeting aldehyde dehydrogenase 2: new therapeutic opportunities.Mn (III) tetrakis (4-benzoic acid) porphyrin protects against neuronal and glial oxidative stress and death after spinal cord injuryModifications of proteins by polyunsaturated fatty acid peroxidation productsFormation of 4-hydroxy-2-nonenal-modified proteins in the renal proximal tubules of rats treated with a renal carcinogen, ferric nitrilotriacetate.Impaired self-renewal and increased colitis and dysplastic lesions in colonic mucosa of AKR1B8-deficient mice.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.Application of the Hard and Soft, Acids and Bases (HSAB) theory to toxicant--target interactions.Site-specific oxidation of apolipoprotein A-I impairs cholesterol export by ABCA1, a key cardioprotective function of HDL.
P2860
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P2860
Modification of histidine residues in proteins by reaction with 4-hydroxynonenal.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on May 1992
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Modification of histidine residues in proteins by reaction with 4-hydroxynonenal.
@en
Modification of histidine residues in proteins by reaction with 4-hydroxynonenal.
@nl
type
label
Modification of histidine residues in proteins by reaction with 4-hydroxynonenal.
@en
Modification of histidine residues in proteins by reaction with 4-hydroxynonenal.
@nl
prefLabel
Modification of histidine residues in proteins by reaction with 4-hydroxynonenal.
@en
Modification of histidine residues in proteins by reaction with 4-hydroxynonenal.
@nl
P2860
P356
P1476
Modification of histidine residues in proteins by reaction with 4-hydroxynonenal.
@en
P2093
E R Stadtman
P2860
P304
P356
10.1073/PNAS.89.10.4544
P407
P577
1992-05-01T00:00:00Z