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Freezing of meat and aquatic food: Underlying mechanisms and implications on protein oxidation [PDF]
Over the recent decades,protein oxidation in muscle foods has gained increasing research interests as it is known that protein oxidation can affect eating quality and nutritional value of meat and aquatic products.
Ruichang Gao, Per Ertbjerg, Li Yuan
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Annals of the New York Academy of Sciences, 2000
Abstract: The oxidative modification of proteins by reactive species, especially reactive oxygen species, is implicated in the etiology or progression of a panoply of disorders and diseases. These reactive species form through a large number of physiological and non‐physiological reactions.
E R, Stadtman, R L, Levine
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Abstract: The oxidative modification of proteins by reactive species, especially reactive oxygen species, is implicated in the etiology or progression of a panoply of disorders and diseases. These reactive species form through a large number of physiological and non‐physiological reactions.
E R, Stadtman, R L, Levine
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Protein oxidation in aging and the removal of oxidized proteins
Journal of Proteomics, 2013Reactive oxygen species (ROS) are generated constantly within cells at low concentrations even under physiological conditions. During aging the levels of ROS can increase due to a limited capacity of antioxidant systems and repair mechanisms. Proteins are among the main targets for oxidants due to their high rate constants for several reactions with ...
Annika, Höhn +2 more
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Experimental Gerontology, 2001
Organisms produce reactive oxygen species (ROS) throughout their lives. The activities of a number of key antioxidant enzymes, such as catalase, superoxide dismutase and glutathione peroxidase, which protect against the damaging effects of ROS, have been reported to decrease with increasing age, though this is not unequivocal.
Linton, S +2 more
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Organisms produce reactive oxygen species (ROS) throughout their lives. The activities of a number of key antioxidant enzymes, such as catalase, superoxide dismutase and glutathione peroxidase, which protect against the damaging effects of ROS, have been reported to decrease with increasing age, though this is not unequivocal.
Linton, S +2 more
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Protein oxidation and proteolysis
bchm, 2006Abstract One of the hallmarks of chronic or severe oxidative stress is the accumulation of oxidized proteins, which tend to form high-molecular-weight aggregates. The major proteolytic system responsible for the removal of oxidized cytosolic and nuclear proteins is the proteasome.
Nicolle, Bader, Tilman, Grune
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Photochemical & Photobiological Sciences, 2012
Photo-induced damage to proteins occurs via multiple pathways. Direct damage induced by UVB (λ 280-320 nm) and UVA radiation (λ 320-400 nm) is limited to a small number of amino acid residues, principally tryptophan (Trp), tyrosine (Tyr), histidine (His) and disulfide (cystine) residues, with this occurring via both excited state species and radicals ...
David I, Pattison +2 more
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Photo-induced damage to proteins occurs via multiple pathways. Direct damage induced by UVB (λ 280-320 nm) and UVA radiation (λ 320-400 nm) is limited to a small number of amino acid residues, principally tryptophan (Trp), tyrosine (Tyr), histidine (His) and disulfide (cystine) residues, with this occurring via both excited state species and radicals ...
David I, Pattison +2 more
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Accounts of Chemical Research, 2000
The oxidative folding of proteins is reviewed and illustrated with bovine pancreatic ribonuclease A (RNase A). The mutual effects of conformational folding and disulfide bond regeneration are emphasized, particularly the "locking in" of native disulfide bonds by stable tertiary structure in disulfide intermediates.
M, Narayan +3 more
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The oxidative folding of proteins is reviewed and illustrated with bovine pancreatic ribonuclease A (RNase A). The mutual effects of conformational folding and disulfide bond regeneration are emphasized, particularly the "locking in" of native disulfide bonds by stable tertiary structure in disulfide intermediates.
M, Narayan +3 more
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Oxidative Stress and Protein Oxidation in Pseudoexfoliation Syndrome
Current Eye Research, 2006To investigate the oxidant/antioxidant status and protein oxidation in pseudoexfoliation syndrome.The activity of serum superoxide dismutase (SOD) and the levels of serum malondialdehyde (MDA) and protein carbonyl (PC) were measured in 50 patients with pseudoexfoliation (PEX) and in 55 healthy controls.There was significant difference in the SOD ...
Ibrahim Ersoz +6 more
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SUMO: a (Oxidative) Stressed Protein
NeuroMolecular Medicine, 2013Redox species are produced during the physiological cellular metabolism of a normal tissue. In turn, their presence is also attributed to pathological conditions including neurodegenerative diseases. Many are the molecular changes that occur during the unbalance of the redox homeostasis.
Feligioni, M, NISTICO', ROBERT GIOVANNI
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Protein oxidation and proteolysis during aging and oxidative stress
Archives of Biochemistry and Biophysics, 1989Previous studies in this laboratory have shown that glutamine synthetase (GS) and other key metabolic enzymes are inactivated by metal-catalyzed oxidation reactions in vitro. Oxidative inactivation renders these proteins highly susceptible to proteolysis, especially to a class of newly identified alkaline proteases which exhibit little or no activity ...
P E, Starke-Reed, C N, Oliver
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