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Synthesis and Biological Activity of Unsymmetrical Monoterpenylhetaryl Disulfides [PDF]
Molecules, 2022 New unsymmetrical monoterpenylhetaryl disulfides based on heterocyclic disulfides and monoterpene thiols were synthesized for the first time in 48–88% yields.
Oksana Shevchenko +2 more
exaly +4 more sources
A novel method for the mechanochemical synthesis of unsymmetrical disulfides using phosphorodithioic acid derivatives [PDF]
Scientific ReportsIn this study, we report the efficient synthesis of unsymmetrical disulfides using a mechanochemical ball-milling approach. This research successfully yielded alkyl-alkyl, alkyl-aryl, and aryl-aryl unsymmetrical disulfides without any detectable ...
Mikołaj Walter +4 more
doaj +2 more sources
Photocatalytic Bilateral Disulfuration of Thioethers Toward α‐Sulfide Disulfides With Antibacterial Activity [PDF]
Advanced Scienceα−Sulfide disulfides represent valuable motifs in organic and pharmaceutical chemistry. However, the limited availability of synthetic approaches for α−sulfide disulfides has impeded progress in this field.
Qingqiang Tian +4 more
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Thiol Isomerases: Enzymatic Mechanisms, Models of Oxidation, and Antagonism by Galloylated Polyphenols [PDF]
AntioxidantsThiol isomerases are a family of enzymes that participate in oxidative protein folding. They contain highly reactive vicinal thiols in a CXXC motif within their catalytic domains to mediate thiol-disulfide switching as part of their reductase, oxidase ...
Osamede C. Owegie +3 more
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Identification of allosteric disulfides from labile bonds in X-ray structures [PDF]
Royal Society Open Science, 2018 Protein disulfide bonds link pairs of cysteine sulfur atoms and are either structural or functional motifs. The allosteric disulfides control the function of the protein in which they reside when cleaved or formed.
Aster E. Pijning +4 more
doaj +1 more source
NO, thiols and disulfides [PDF]
FEBS Letters, 1993 The chemical nature of the messenger molecule, nitric oxide (NO), and especially its reactivity towards thiol groups and disuifides, could explain, at least partly, its intervention in so many different biological processes. NO can be regarded as the smallest molecule suitable for electron transport in biological systems. The S‐nitrosation reaction and
Girard, Pierre, Potier, Pierre
openaire +2 more sources
The effect of tensile stress on the conformational free energy landscape of disulfide bonds. [PDF]
PLoS ONE, 2014 Disulfide bridges are no longer considered to merely stabilize protein structure, but are increasingly recognized to play a functional role in many regulatory biomolecular processes.
Padmesh Anjukandi +3 more
doaj +1 more source
Protein disulfides and protein disulfide oxidoreductases in hyperthermophiles [PDF]
The FEBS Journal, 2006 Disulfide bonds are required for the stability and function of a large number of proteins. Recently, the results from genome analysis have suggested an important role for disulfide bonds concerning the structural stabilization of intracellular proteins from hyperthermophilic Archaea and Bacteria, contrary to the conventional view that structural ...
Rudolf, Ladenstein, Bin, Ren
openaire +2 more sources
Advanced Energy & Sustainability Research, 2023 Selective coupling of thiols to produce disulfides is one very important and classic type of coupling reactions. Herein, an environmentally friendly and practical photocatalytic system for oxidative coupling of thiols to disulfides is developed.
Fengyun Su +8 more
doaj +1 more source
Scientific Reports, 2022 In this research, a simple, efficient and novel protocol is eveloped for the direct synthesis of symmetrical disulfides using dipotassium 1,3,4-thiadiazole-2,5-bis(thiolate) as a new, low toxicity, inexpensive, stable solid and free of foul-smelling ...
Mohammad Soleiman-Beigi +3 more
doaj +1 more source