A Role of Mixed‐Function Oxidation Reactions in the Accumulation of Altered Enzyme Forms During Aging
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- Type
- review
- Published
- 1987-10-01
- Cited by
- 95
- References
- 66
- OpenAlex
- https://openalex.org/W1966490843
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:31020359
Keywords
Medicine, Gerontology, National laboratory, Library science
References
- Mixed-function oxidation of histidine residues.
- Heat-labile enzymes in circulating erythrocytes of a progeria family.
- Oxidative modification of glutamine synthetase. I. Inactivation is due to loss of one histidine residue.
- Age-related changes in oxidized proteins.
- Inactivation of yeast fructose-1,6-bisphosphatase. In vivo phosphorylation of the enzyme.
- Nonenzymatic cleavage of proteins by reactive oxygen species generated by dithiothreitol and iron.
- Purification of a liver alkaline protease which degrades oxidatively modified glutamine synthetase. Characterization as a high molecular weight cysteine proteinase.
- Oxidative modification of glutamine synthetase. II. Characterization of the ascorbate model system.
- Altered phosphoglycerate kinase in aging rats.
- Purification of a protease from Escherichia coli with specificity for oxidized glutamine synthetase.
- Preferential degradation of the oxidatively modified form of glutamine synthetase by intracellular mammalian proteases.
- Glutathione disulfide inactivates, destabilizes, and enhances proteolytic susceptibility of fructose-1,6-bisphosphate aldolase.
- The in vivo regulation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A reductase. Phosphorylation of the enzyme as an early regulatory response following cholesterol feeding.
- Sequence of a peptide susceptible to mixed-function oxidation. Probable cation binding site in glutamine synthetase.
- A correlation between protein thermostability and resistance to proteolysis.
- Protein turnover and growth in the whole body, liver and kidney of the rat from the foetus to senility.
- Role of Protein Molecular and Metabolic Aberrations in Aging, in the Physiologic Decline of the Aged, and in Age‐Associated Diseases
- Regulation of fructose-1,6-bisphosphatase in yeast by phosphorylation/dephosphorylation.
- Effect of a single amino acid substitution on stability of conformation of a protein
- Inactivation of glutamine synthetase by a purified rabbit liver microsomal cytochrome P-450 system.
Cited by
- Site-specific oxidation of angiotensin I by copper(II) and L-ascorbate: conversion of histidine residues to 2-imidazolones.
- Proteasome-dependent turnover of protein disulfide isomerase in oxidatively stressed cells.
- Ginsenoside Re Protects Trimethyltin-Induced Neurotoxicity via Activation of IL-6-Mediated Phosphoinositol 3-Kinase/Akt Signaling in Mice
- Oxidative damage to proteins: spectrophotometric method for carbonyl assay.
- Oxidative modification of cytochrome c by hydrogen peroxide.
- Rickettsial Infection and Immunity
- Spinal Cord Monitoring
- ANALYTICAL METHOD DEVELOPMENT FOR THE DETECTION AND ANALYSIS OF PROTEIN CARBONYLS
- Possible involvement of histidine residues in the loss of enzymatic activity of rat liver malic enzyme during aging.
- Determination of carbonyl content in oxidatively modified proteins.
- Infection of human endothelial cells by Rickettsia rickettsii causes a significant reduction in the levels of key enzymes involved in protection against oxidative injury
- Modulation of the hydrophobicity of glutamine synthetase by mixed‐function oxidation
- Hemoglobin: a mechanism for the generation of hydroxyl radicals.
- Metal-catalyzed oxidation of Escherichia coli glutamine synthetase: correlation of structural and functional changes.
- Covalent modification reactions are marking steps in protein turnover.
- Acrolein, A Reactive Product of Lipid Peroxidation, Induces Oxidative Modification of Cytochrome c
- Advances in age pigment research.
- Oxidative stress in vivo and in vitro: modulation by quartz dust and hyperbaric atmosphere.
- Identification of the Major Oxidatively Damaged Proteins inEscherichia coli Cells Exposed to Oxidative Stress*
- Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences.
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