Tyrosine 192 in apolipoprotein A-I is the major site of nitration and chlorination by myeloperoxidase, but only chlorination markedly impairs ABCA1-dependent cholesterol transport.
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Preparation and Characterization of a Polyclonal Antibody against Brominated ProteinRole of Myeloperoxidase in Patients with Chronic Kidney DiseaseStructural Insights into High Density Lipoprotein: Old Models and New FactsTyrosine modifications in agingSequence conservation of apolipoprotein A-I affords novel insights into HDL structure-function3-nitrotyrosine modified proteins in atherosclerosisProteomics of citrullination in cardiovascular diseaseHuman apolipoprotein A-I-derived amyloid: its association with atherosclerosisHDL-apoA-I exchange: rapid detection and association with atherosclerosisAcrolein impairs ATP binding cassette transporter A1-dependent cholesterol export from cells through site-specific modification of apolipoprotein A-I.Specific sequence motifs direct the oxygenation and chlorination of tryptophan by myeloperoxidase.Enhanced nitrosative stress during Trypanosoma cruzi infection causes nitrotyrosine modification of host proteins: implications in Chagas' disease.HDL in humans with cardiovascular disease exhibits a proteomic signature.Dysfunctional HDL as a diagnostic and therapeutic targetIn vitro and in vivo protein-bound tyrosine nitration characterized by diagonal chromatographyEffects of protein oxidation on the structure and stability of model discoidal high-density lipoproteinsSite-specific nitration of apolipoprotein A-I at tyrosine 166 is both abundant within human atherosclerotic plaque and dysfunctional.Myeloperoxidase: an oxidative pathway for generating dysfunctional high-density lipoproteinHumans with atherosclerosis have impaired ABCA1 cholesterol efflux and enhanced high-density lipoprotein oxidation by myeloperoxidase.Myeloperoxidase-dependent inactivation of surfactant protein D in vitro and in vivoModifying apolipoprotein A-I by malondialdehyde, but not by an array of other reactive carbonyls, blocks cholesterol efflux by the ABCA1 pathwayExchange of apolipoprotein A-I between lipid-associated and lipid-free states: a potential target for oxidative generation of dysfunctional high density lipoproteinsOxidation of apolipoprotein A-I by myeloperoxidase impairs the initial interactions with ABCA1 required for signaling and cholesterol exportNeutrophil extracellular trap-derived enzymes oxidize high-density lipoprotein: an additional proatherogenic mechanism in systemic lupus erythematosus.High density lipoprotein is targeted for oxidation by myeloperoxidase in rheumatoid arthritis.Crystal structure of human apolipoprotein A-I: insights into its protective effect against cardiovascular diseases.Plasma levels of HDL and carotenoids are lower in dementia patients with vascular comorbidities.Effects of a novel pharmacologic inhibitor of myeloperoxidase in a mouse atherosclerosis model.Nitrated apolipoprotein A-I, a potential new cardiovascular marker, is markedly increased in low high-density lipoprotein cholesterol subjects.Distinct HDL subclasses present similar intrinsic susceptibility to oxidation by HOCl.Selective chemoprecipitation and subsequent release of tagged species for the analysis of nitropeptides by liquid chromatography-tandem mass spectrometryImpact of HDL oxidation by the myeloperoxidase system on sterol efflux by the ABCA1 pathwayImpact of self-association on function of apolipoprotein A-ISite-specific oxidation of apolipoprotein A-I impairs cholesterol export by ABCA1, a key cardioprotective function of HDL.Myeloperoxidase targets apolipoprotein A-I, the major high density lipoprotein protein, for site-specific oxidation in human atherosclerotic lesionsA Novel Anti-Inflammatory Effect for High Density Lipoprotein.HDL dysfunction in diabetes: causes and possible treatments.Plasma Nitration of High-Density and Low-Density Lipoproteins in Chronic Kidney Disease Patients Receiving Kidney Transplants.Lipid peroxyl radicals mediate tyrosine dimerization and nitration in membranesSerum amyloid A impairs the antiinflammatory properties of HDL
P2860
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P2860
Tyrosine 192 in apolipoprotein A-I is the major site of nitration and chlorination by myeloperoxidase, but only chlorination markedly impairs ABCA1-dependent cholesterol transport.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh
2004年學術文章
@zh-hant
name
Tyrosine 192 in apolipoprotein ...... pendent cholesterol transport.
@en
type
label
Tyrosine 192 in apolipoprotein ...... pendent cholesterol transport.
@en
prefLabel
Tyrosine 192 in apolipoprotein ...... pendent cholesterol transport.
@en
P2093
P356
P1476
Tyrosine 192 in apolipoprotein ...... ependent cholesterol transport
@en
P2093
Constanze Bergt
Jay W Heinecke
John F Oram
Michael N Oda
Pattie Green
Xiaoyun Fu
P304
P356
10.1074/JBC.M411484200
P407
P577
2004-11-30T00:00:00Z