Free radical-mediated oxidation of free amino acids and amino acid residues in proteins

By E. Stadtman, R. Levine. Amino Acids, 2003

1,874 citations recorded by the source corpus.

Subfields: Clinical Biochemistry, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/45d6930d034e84e02026c7915793b0a4af07a706

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Citations in the corpus

Measurement and Clinical Significance of Biomarkers of Oxidative Stress in Humans (2017, background): “Also, the attack of HO radicals on proline, lysine, arginine, and threonine side chains generates carbonyl groups [193].”
Protein oxidation in muscle foods: a review. (2011, background): “In fact, peroxyl radicals formed during lipid oxidation has been reported to abstract hydrogen atoms from protein molecules leading to a radicalmediated chain reaction similar to that of lipid oxidation [64].”
Oral multispecies biofilm development and the key role of cell–cell distance (2010, background): “As a result, carbonyl groups can be introduced into the side chains of arginine, proline, lysine and threonine residues and thereby target the protein for degradatio”
Molecular events associated with reactive oxygen species and cell cycle progression in mammalian cells. (2004, background): “These modifications might result in catalytically less active enzymes that are more susceptible to proteolytic degradation, although the oxidation of methionines and cysteines is reversible (Stadtman, 2001; Davies, 2000; Stadtman and Levine, 2003).”
Protein carbonylation, cellular dysfunction, and disease progression (2006, background): “3) [10, 11].”
Oxidative Stress and Antioxidant Defense (2012, background): “For example, methionine can be oxidized methionine sulfoxide 126 and phenylalanine to o -tyrosine 127 ; sulfhydryl groups can be oxidized to form disul ﬁ de bonds; 128 and carbonyl groups may be introduced into the side chains of proteins.”
Oxygen, oxidative stress, hypoxia, and heart failure. (2005, background): “Modification of proteins by ROS can cause inactivation of critical enzymes and can induce denaturation that renders proteins nonfunctional (41, 42).”
Antioxidant Activity of Proteins and Peptides (2008, background): “These include electron paramagnetic resonance (EPR), protein fragmentation and/or polymerization rates, changes in proteolytic susceptibility, and the detection of specific amino acid oxidation products (Stadtman and Levine, 2003).”
Radical-free biology of oxidative stress. (2008, background): “Oxidation of Met to methionine sulfoxide occurs in association with oxidative stress and aging (169, 170).”
Chemical Basis of Reactive Oxygen Species Reactivity and Involvement in Neurodegenerative Diseases (2019, background): “(A) the mechanism of 4-HNE formation from ROS-induced polyunsaturated omega-6 fatty acid peroxidation (from Pryor and Porter [125]); 4-HNE is able to form adducts with lipoic acid, proteins (C, H and K residues) and DNA bases; (B) ROS-induced protein carbonylation and cleavage (from Stadtman and Lev”
Oxidative stress and the amyloid beta peptide in Alzheimer’s disease (2017, background): “Asp1 is also subject to a backbone cleavage on the α-position of the peptide [141,153], leading to an isocyanate function in a reaction mechanism proceeding through the diamine pathway [177].”