Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes. Mechanistic studies identifying labile intermediates along the reaction pathway.
about
Site-specific AGE modifications in the extracellular matrix: a role for glyoxal in protein damage in diabetesEndogenous Generation of Singlet Oxygen and Ozone in Human and Animal Tissues: Mechanisms, Biological Significance, and Influence of Dietary ComponentsReactions of hypochlorous acid with tyrosine and peptidyl-tyrosyl residues give dichlorinated and aldehydic products in addition to 3-chlorotyrosineMyeloperoxidase: a front-line defender against phagocytosed microorganismsNitric oxide is a physiological substrate for mammalian peroxidasesProduction of brominating intermediates by myeloperoxidase. A transhalogenation pathway for generating mutagenic nucleobases during inflammation.Lysine residues direct the chlorination of tyrosines in YXXK motifs of apolipoprotein A-I when hypochlorous acid oxidizes high density lipoprotein.Evaluation of a multi-parameter biomarker set for oxidative damage in man: increased urinary excretion of lipid, protein and DNA oxidation products after one hour of exercise.Potential role of tryptophan and chloride in the inhibition of human myeloperoxidase.The myeloperoxidase system of human phagocytes generates Nepsilon-(carboxymethyl)lysine on proteins: a mechanism for producing advanced glycation end products at sites of inflammation.Role of eosinophil peroxidase in the origins of protein oxidation in asthma.Myeloperoxidase-derived oxidation: mechanisms of biological damage and its preventionThe myeloperoxidase product hypochlorous acid generates irreversible high-density lipoprotein receptor inhibitorsThe impact of polyether chain length on the iron clearing efficiency and physiochemical properties of desferrithiocin analogues.Characterization of methionine oxidation and methionine sulfoxide reduction using methionine-rich cysteine-free proteins.The promotion of functional urinary bladder regeneration using anti-inflammatory nanofibersMyeloperoxidase-mediated protein oxidation: its possible biological functions.Eosinophils generate brominating oxidants in allergen-induced asthma.Effect of exposure of human monocyte-derived macrophages to high, versus normal, glucose on subsequent lipid accumulation from glycated and acetylated low-density lipoproteins.Metabolic Response of Escherichia coli upon Treatment with Hypochlorite at Sub-Lethal ConcentrationsDesferrithiocin analogue iron chelators: iron clearing efficiency, tissue distribution, and renal toxicityMetabolically programmed iron chelatorsReactive oxygen species-targeted therapeutic interventions for atrial fibrillation.Oxidized proteins and their contribution to redox homeostasis.Pyridoxamine protects proteins from damage by hypohalous acids in vitro and in vivo.Substituent effects on desferrithiocin and desferrithiocin analogue iron-clearing and toxicity profiles.The design, synthesis, and evaluation of organ-specific iron chelators.Impact of the 3,6,9-trioxadecyloxy group on desazadesferrithiocin analogue iron clearance and organ distribution.Gas signatures from Escherichia coli and Escherichia coli-inoculated human whole blood.Acetaldehyde and hexanaldehyde from cultured white cellsDesign, synthesis, and testing of non-nephrotoxic desazadesferrithiocin polyether analogues.Desferrithiocin analogues and nephrotoxicity.Hypochlorous acid converts the gamma-glutamyl group of glutathione disulfide to 5-hydroxybutyrolactam, a potential marker for neutrophil activation.Neutrophil-generated oxidative stress and protein damage in Staphylococcus aureus.Biosynthesis of floral scent 2-phenylethanol in rose flowers.Defence against methylglyoxal in Group A Streptococcus: a role for Glyoxylase I in bacterial virulence and survival in neutrophils?Proteomic analysis of oxidative stress-resistant cells: a specific role for aldose reductase overexpression in cytoprotection.Evidence that endogenous formaldehyde produces immunogenic and atherogenic adduct epitopesVitamin C protects against and reverses specific hypochlorous acid- and chloramine-dependent modifications of low-density lipoprotein.Characterization of non-covalent oligomers of proteins treated with hypochlorous acid.
P2860
Q26865565-070D7ADD-8E70-42A8-A6C3-BCC92188DA2AQ28078168-7747DF2E-C366-4CAC-AA6E-AD412A9E7A69Q28375883-27B9B7FA-FF47-4D54-A580-A7866A6E9EE5Q28393101-DE22C20A-8769-43D0-80FE-567A3F8DEE9AQ28645799-2ACA7F05-560A-4C44-A2F8-BEC39F4786DCQ31628322-3ADEF1F4-D5F1-4E14-9179-0EF72DD0D0ABQ33195740-F65C07D6-D75F-45EC-82C6-71DA891D8EB4Q33433041-B1AE2CAA-8BD1-4B6B-A5D3-02E56949C16FQ33818264-B70FC1CE-1880-41CE-BD7F-171B3A991D9EQ33853348-0D6FB6B8-8C2B-4F84-BB04-030F346F0D2DQ34037726-2CAF13B0-B6CA-4B03-86B9-5A1253E4992FQ34162955-A6F662C5-0090-45BF-BDB0-B3BD4D3E51B8Q34178582-F29863A2-614D-46F9-9B50-B7CC90F08B7BQ34181082-E76F08B2-0188-48F6-9835-4D75399887DDQ34454225-F0523391-5E10-4895-94F0-B85010E5995BQ34722403-848F6A4E-B943-4319-B7FA-E02A76AF9A7DQ34734560-806ED2E0-925F-4136-9EB8-2CFA1F8CE4A3Q35160027-409E49A5-4B06-4A93-AF9A-3E98FD7D48F5Q35195762-BF5ED38F-A415-4EF4-A9C6-F7A009698D85Q35620078-868999A5-75C1-4037-AFC4-DAE718A7A58EQ35896606-01643527-2F93-4EEE-B57C-72E0A2BF083DQ36170377-920C0056-5AFC-467E-8855-5EF569C80D30Q36193817-9341F23E-BDC4-4C49-897E-ECFBF649A35FQ36301722-6940B31E-B01A-47C9-ACB4-933E9736024BQ36386384-1DEA5C0C-C5DC-4EB2-B4A2-445D6C5D978DQ36642048-65081B49-26D2-485F-8917-5BEEF340AC3DQ36837342-F69EA5A1-0954-4D09-9C42-8391E703A848Q36857692-485CFC39-19DA-4B2A-B7B1-48225865D522Q37028444-40C07718-E950-4CF8-A11A-6F75329A5E68Q37196373-92D65E91-C3D9-46FD-BC7D-9560ADDFB826Q37381807-99E84D1B-0936-48FD-9DE1-91CAE4D84BF2Q37423512-AEF1C434-C227-4C0F-901B-2766CEF956D3Q37446863-9526ED1B-F28D-4D9F-8CF8-7807FE5C6860Q38847411-48B0BF26-D154-4CE3-8094-4DBD5EC7CFACQ38864106-7743BE99-1F16-448E-A732-16C8323B6278Q40172795-CC0E5870-A5A9-4704-9841-0B3CED6DBE64Q40607273-2C93BBEB-E18A-47F2-8EB7-22CE162F2296Q41535735-546C7692-8B32-4864-9085-2273088A8F8FQ41998801-55649591-F8DA-4E22-B6B9-8FD7EAA8EA35Q42028055-E9315278-B50D-43C4-BA88-A0EA43983B57
P2860
Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes. Mechanistic studies identifying labile intermediates along the reaction pathway.
description
1998 nî lūn-bûn
@nan
1998 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Human neutrophils employ the m ...... es along the reaction pathway.
@ast
Human neutrophils employ the m ...... es along the reaction pathway.
@en
Human neutrophils employ the m ...... es along the reaction pathway.
@nl
type
label
Human neutrophils employ the m ...... es along the reaction pathway.
@ast
Human neutrophils employ the m ...... es along the reaction pathway.
@en
Human neutrophils employ the m ...... es along the reaction pathway.
@nl
prefLabel
Human neutrophils employ the m ...... es along the reaction pathway.
@ast
Human neutrophils employ the m ...... es along the reaction pathway.
@en
Human neutrophils employ the m ...... es along the reaction pathway.
@nl
P2093
P2860
P356
P1476
Human neutrophils employ the m ...... es along the reaction pathway.
@en
P2093
A d'Avignon
J W Heinecke
M M Anderson
P2860
P304
P356
10.1074/JBC.273.9.4997
P407
P577
1998-02-01T00:00:00Z