Results 21 to 30 of about 8,975 (219)
Redox Biology, 2018 Small oxoacids of sulfur (SOS) are elusive molecules like sulfenic acid, HSOH, and sulfinic acid, HS(O)OH, generated during the oxidation of hydrogen sulfide, H2S, in aqueous solution.
Murugaeson R. Kumar, Patrick J. Farmer
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A cell-permeable biscyclooctyne as a novel probe for the identification of protein sulfenic acids [PDF]
, 2016 Reactive oxygen species act as important second messengers in cell signaling and homeostasis through the oxidation of protein thiols. However, the dynamic nature of protein oxidation and the lack of sensitivity of existing molecular probes have hindered ...
Hartley, Richard C. +4 more
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Transient Sulfenic Acids in the Synthesis of Biologically Relevant Products
Molecules, 2018 Sulfenic acids as small molecules are too unstable to be isolated and their transient nature offers the possibility to involve them in concerted processes that lead to the obtainment of functional groups such as sulfoxides, sulfones, and disulfides.
Anna Barattucci +4 more
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Reactivity of Small Oxoacids of Sulfur
Molecules, 2019 Oxidation of sulfide to sulfate is known to consist of several steps. Key intermediates in this process are the so-called small oxoacids of sulfur (SOS)—sulfenic HSOH (hydrogen thioperoxide, oxadisulfane, or sulfur hydride hydroxide) and sulfoxylic
Sergei V. Makarov +2 more
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A novel reaction of peroxiredoxin 4 towards substrates in oxidative protein folding. [PDF]
PLoS ONE, 2014 Peroxiredoxin 4 (Prx4) is the only endoplasmic reticulum localized peroxiredoxin. It functions not only to eliminate peroxide but also to promote oxidative protein folding via oxidizing protein disulfide isomerase (PDI).
Li Zhu +4 more
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Cysteine perthiosulfenic acid (Cys-SSOH): A novel intermediate in thiol-based redox signaling?
Redox Biology, 2018 The reversible oxidation of protein cysteine residues (Cys-SH) is a key reaction in cellular redox signaling involving initial formation of sulfenic acids (Cys-SOH), which are commonly detected using selective dimedone-based probes.
David E. Heppner +11 more
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Protein topology determines cysteine oxidation fate: the case of sulfenyl amide formation among protein families. [PDF]
PLoS Computational Biology, 2015 Cysteine residues have a rich chemistry and play a critical role in the catalytic activity of a plethora of enzymes. However, cysteines are susceptible to oxidation by Reactive Oxygen and Nitrogen Species, leading to a loss of their catalytic function ...
Lucas A Defelipe +4 more
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Endogenous SO2-dependent Smad3 redox modification controls vascular remodeling
Redox Biology, 2021 Sulfur dioxide (SO2) has emerged as a physiological relevant signaling molecule that plays a prominent role in regulating vascular functions. However, molecular mechanisms whereby SO2 influences its upper-stream targets have been elusive.
Yaqian Huang +20 more
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Detecting peroxiredoxin hyperoxidation by one-dimensional isoelectric focusing [PDF]
, 2015 The activity of typical 2-cys peroxiredoxin (Prxs) can be regulated by hyperoxidation with a consequent loss of redox activity. Here we developed a simple assay to monitor the level of hyperoxidation of different typical 2-cys prxs simultaneously.
Bulleid, Neil J., Cao, Zhenbo
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Kinetic Studies of Antioxidant Properties of Ovothiol A
Antioxidants, 2021 Ovothiol A (OSH) is one of the strongest natural antioxidants. So far, its presence was found in tissues of marine invertebrates, algae and fish. Due to very low pKa value of the SH group, under physiological conditions, this compound is almost entirely ...
Nataliya A. Osik +2 more
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