Protein-bound 3,4-dihydroxyphenylalanine is a major reductant formed during hydroxyl radical damage to proteins.
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Tyrosine modifications in agingNovel inter-protein cross-link identified in the GGH-ecotin D137Y dimerReactivity of peptidyl-tyrosine to hydroxylation and cross-linkingNorepinephrine and its metabolites are involved in the synthesis of neuromelanin derived from the locus coeruleusCurrent understanding on the role of retinal pigment epithelium and its pigmentation.Endogenous 3,4-dihydroxyphenylalanine and dopaquinone modifications on protein tyrosine: links to mitochondrially derived oxidative stress via hydroxyl radicalQuantification and significance of protein oxidation in biological samples.Tough coating proteins: subtle sequence variation modulates cohesionThe yeast heat shock transcription factor changes conformation in response to superoxide and temperature.Disease stage-dependent accumulation of lipid and protein oxidation products in human atherosclerosis.Major chorion proteins and their crosslinking during chorion hardening in Aedes aegypti mosquitoes.Chemical modifications in aggregates of recombinant human insulin induced by metal-catalyzed oxidation: covalent cross-linking via michael addition to tyrosine oxidation products.Cardiovascular redox and ox stress proteomics.Biomedical and Clinical Importance of Mussel-Inspired Polymers and MaterialsUnderstanding and applying tyrosine biochemical diversity.Redox control of enzymatic functions: The electronics of life's circuitry.Exploring oxidative modifications of tyrosine: an update on mechanisms of formation, advances in analysis and biological consequences.High level protein-purification allows the unambiguous polypeptide determination of latent isoform PPO4 of mushroom tyrosinase.Evidence for L-dopa incorporation into cell proteins in patients treated with levodopa.Proteins containing oxidized amino acids induce apoptosis in human monocytes.Metabolism-induced oxidative stress is a mediator of glucose toxicity in HT22 neuronal cells.Functional food science and defence against reactive oxidative species.Biochemistry and pathology of radical-mediated protein oxidation.The protein oxidation product 3,4-dihydroxyphenylalanine (DOPA) mediates oxidative DNA damage.Superoxide-mediated formation of tyrosine hydroperoxides and methionine sulfoxide in peptides through radical addition and intramolecular oxygen transfer.Histone H1- and other protein- and amino acid-hydroperoxides can give rise to free radicals which oxidize DNA.Structural characterization of the products of hydroxyl-radical damage to leucine and their detection on proteins.Biological fate of amino acid, peptide and protein hydroperoxides.Antioxidant activities of a peptide derived from chicken dark meat.Protein hydroperoxides can give rise to reactive free radicalsPresence of dopa and amino acid hydroperoxides in proteins modified with advanced glycation end products (AGEs): amino acid oxidation products as a possible source of oxidative stress induced by AGE proteins.Evidence for roles of radicals in protein oxidation in advanced human atherosclerotic plaque.Protection of erythrocytes by the macrophage synthesized antioxidant 7,8 dihydroneopterin.Inhibition of protein oxidation by the macrophage-synthesised antioxidant 7,8-dihydroneopterin.Protection of U937 cells from free radical damage by the macrophage synthesized antioxidant 7,8-dihydroneopterin.A highly sensitive method for the determination of protein bound 3,4-dihydroxyphenylalanine as a marker for post-translational protein hydroxylation in human tissues ex vivo.Iron binding β-hairpin peptides.Hypocaloric diet and regular moderate aerobic exercise is an effective strategy to reduce anthropometric parameters and oxidative stress in obese patients.Serum protein-bound 3,4-dihydroxyphenylalanine and related products of protein oxidation and chronic hemodialysis.Protein hydroperoxides are a major product of low density lipoprotein oxidation during copper, peroxyl radical and macrophage-mediated oxidation.
P2860
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P2860
Protein-bound 3,4-dihydroxyphenylalanine is a major reductant formed during hydroxyl radical damage to proteins.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh-hant
name
Protein-bound 3,4-dihydroxyphe ...... yl radical damage to proteins.
@en
Protein-bound 3,4-dihydroxyphe ...... yl radical damage to proteins.
@nl
type
label
Protein-bound 3,4-dihydroxyphe ...... yl radical damage to proteins.
@en
Protein-bound 3,4-dihydroxyphe ...... yl radical damage to proteins.
@nl
prefLabel
Protein-bound 3,4-dihydroxyphe ...... yl radical damage to proteins.
@en
Protein-bound 3,4-dihydroxyphe ...... yl radical damage to proteins.
@nl
P2093
P356
P1433
P1476
Protein-bound 3,4-dihydroxyphe ...... yl radical damage to proteins.
@en
P2093
P304
P356
10.1021/BI00069A012
P407
P577
1993-05-01T00:00:00Z