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Exposure of Cys of mitochondrially encoded subunit ND3 makes the D-form susceptible for modification by reactive oxygen species and nitric oxide metabolites which arrests the reactivation of the D-form and inhibits the enzyme.
In addition, both the protein and polysaccharide constituents undergo modification by reactive oxygen species (ROS) which can lead to chain fragmentation.
Functional amino acids that play critical roles in catalysis and regulation are known to display elevated nucleophilicity and can be selectively targeted for covalent modification by reactive electrophiles.
S-nitrosylation of critical protein thiols has been shown to protect them from further oxidative modification by reactive oxygen species.
Particularly the polyunsaturated fatty acid side chains of membrane phospholipids are highly susceptible to modification by reactive oxygen intermediates, which potentially yields an enormous array of distinct lipid oxidation products with diverse biological effects (Leitinger, 2003; Berliner & Watson, 2005; Bochkov et al, 2010; Lee et al, 2012).
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A second process is via chemical modification of contractile elements through kinase-mediated phosphorylation reactions or sidegroup modifications by reactive species (for example, nitrosylation of tyrosine residues by peroxynitrite or carbonyl formation in response to reaction with ROS species).
Some of these processes occur during cell culture, such as modifications by reactive metabolites (e.g., methylglyoxal and homocysteine thiolactone), glycosylation and sialic acid incorporation, while others can occur through production, purification, and storage, such as oxidation, deamidation, cross-linking, protein protein interactions, and fragmentation.
(5) Oxidation of protein thiols under nitrosative stress has been proposed to be the dominant protein modification caused by reactive nitrogen species formed from NO and NO2–, such as N2O3, NO2, and peroxynitrite.
DNA modification by these reactive estrogen metabolites might explain some of the structural and numeric chromosomal changes observed in response to estrogen exposure [ 42].
Herein we hypothesize that mitochondrial defects induced by exposure to a HFD (high fat diet) contribute to a hypoxic state in liver and this is associated with increased protein modification by RNS (reactive nitrogen species).
Myosin molecules have a slow turnover rate, that is, 1 2% per day (Smith & Rennie, 1996) which makes them preferential targets for different types of post-translational modifications (PTMs) by reactive oxygen or nitrogen species.
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