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Protein oxidation in aging and the removal of oxidized proteins

Journal of Proteomics, 2013
Reactive 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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SUMO: a (Oxidative) Stressed Protein

NeuroMolecular Medicine, 2013
Redox 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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Oxidative Stress and Protein Oxidation in Pseudoexfoliation Syndrome

Current Eye Research, 2006
To 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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Immunohistochemical Detection of Protein Oxidation

2003
The oxidative modification of proteins by reactive oxygen species (ROS) and other reactive compounds is associated with a number of disease and pathophysiological processes as well as aging (1). Under physiological conditions, almost all oxidative modifications of proteins are resulting in an increase of carbonylated proteins.
FRANK J, POMPELLA, ALFONSO, BIESALSKI HK
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Oxidative Protein Folding Using trans-3,4-Dihydroxyselenolane Oxide

2019
trans-3,4-Dihydroxyselenolane oxide (DHSox), a water-soluble cyclic selenoxide reagent, is useful for rapid and quantitative formation of disulphide (SS) bonds in a reduced state of SS-containing proteins because the selenoxide is a strong but selective oxidant for thiol substrates (RSH) in a wide range of pH.
Kenta, Arai, Michio, Iwaoka
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Genetically Encoding Protein Oxidative Damage

Journal of the American Chemical Society, 2008
Posttranslational modification of tyrosine residues in proteins, to produce 3-nitrotyrosine (3-NT), is associated with over 50 disease states including transplant rejection, lung infection, central nervous system and ocular inflammation shock, cancer, and neurological disorders (for example, Alzheimer's disease, Parkinson's disease, and stroke).
Heinz, Neumann   +4 more
openaire   +2 more sources

Plant proteins under oxidative attack

PROTEOMICS, 2013
Reactive oxygen and nitrogen species can modify various biomolecules, including proteins. The resulting protein modifications are highly diverse, can be reversible as well as irreversible, and might affect protein structure and function. Besides random modifications, targeted modifications at specific amino acids in surface‐accessible protein regions ...
Silke, Jacques   +3 more
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Protein Oxidative Modifications

2011
Proteins are molecules especially susceptible to oxidative modifications owing to their abundance and reactivity to radicals. Amongst the protein oxidative (redox) changes, carbonylation of the molecules represents an irreversible process that leads to the lost of protein functionality.
Liliana Beatriz Pena   +3 more
openaire   +1 more source

Aging and protein oxidative damage

Mechanisms of Ageing and Development, 1994
The hypothesis that aging is associated with the accumulation of oxidative damage was tested in the adult male housefly by monitoring the loss of membrane protein -SH groups, and activities of glucose-6-phosphate dehydrogenase and alcohol dehydrogenase, the cytosolic enzymes that are particularly susceptible to oxidative damage.
S, Agarwal, R S, Sohal
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Hemodialysis and Protein Oxidation Products

Annals of the New York Academy of Sciences, 2007
Abstract:  The presence of a chronic inflammatory state has also been widely documented in end‐stage renal disease patients receiving maintenance hemodialysis (HD). It is commonly attributed to the constantly renewed activation of circulating neutrophils and monocytes following blood passage through dialysis circuits and subsequent generation of ...
Cihan, Coskun   +6 more
openaire   +2 more sources

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