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Inhibition of succinic dehydrogenase and F0F1-ATP synthase by 4,4 '-diisothiocyanatostilbene-2,2 '-disulfonic acid (DIDS)
(Verlag Z NaturforschTubingenAlemanha, 1997)
Ca2+-independent permeabilization of the inner mitochondrial membrane by peroxynitrite is mediated by membrane protein thiol cross-linking and lipid peroxidation
(Academic Press Inc Jnl-comp SubscriptionsSan Diego, 1997)
Oligomerization of the cysteinyl-rich oligopeptidase EP24.15 is triggered by S-glutathionylation
(ELSEVIER SCIENCE INC, 2008)
Thimet oligopeptidase (EC 3.4.24.15; EP24.15) is a thiol-rich metallopeptidase ubiquitously distributed in mammalian tissues and involved in oligopeptide metabolism both within and outside cells. Fifteen Cys residues are ...
OXIDATIVE DAMAGE OF MITOCHONDRIA INDUCED BY 5-AMINOLEVULINIC ACID - ROLE OF CA2+ AND MEMBRANE-PROTEIN THIOLS
(Elsevier Science BvAmsterdamHolanda, 1994)
CA2+-DEPENDENT PERMEABILIZATION OF THE INNER MITOCHONDRIAL-MEMBRANE BY 4,4'-DIISOTHIOCYANATOSTILBENE-2,2'-DISULFONIC ACID (DIDS)
(Elsevier Science BvAmsterdamHolanda, 1994)
Multiscale Modeling of Thiol Overoxidation in Peroxiredoxins by Hydrogen Peroxide
(American Chemical Society, 2019-11)
In this work, we employ a multiscale quantum-classical mechanics (QM/MM) scheme to investigate the chemical reactivity of sulfenic acids toward hydrogen peroxide, both in aqueous solution and in the protein environment of ...
Evaluation of a protein deficient diet in rats through blood oxidative stress biomarkers
(2003-12-01)
Protein malnutrition leads to functional impairment in several organs, which is not fully restored with nutritional recovery. Little is known about the role of oxidative stress in the genesis of these alterations. This ...
Evaluation of a protein deficient diet in rats through blood oxidative stress biomarkers
(2003-12-01)
Protein malnutrition leads to functional impairment in several organs, which is not fully restored with nutritional recovery. Little is known about the role of oxidative stress in the genesis of these alterations. This ...