Results 261 to 270 of about 114,000 (315)
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Thiols, Thiol Depletion, and Thermosensitivity

Radiation Research, 1983
Hyperthermia sensitization or tolerance is subject to cellular events that may occur at membrane, nuclear, and cytoplasmic sites. We have studied the effects of elevated temperatures on the oxidative-reductive state of the cell by measuring and altering glutathione (GSH) concentrations. GSH plays a pivotal role in maintaining the overall cellular redox
J B, Mitchell, A, Russo
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Thiols, gold-thiols, zinc-thiols and the redox state of hemoglobin

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1993
The beta subunit of human hemoglobin can be oxidized site-specifically through beta-Cys-93 by Cu(II)(His)2. A series of thiol ligands, gold thiols and zinc(II) inhibit this oxidation. The thiol inhibitors formed a transient ternary intermediate involving Cu(I) with consequent inhibition of electron transfer from the Fe(II)-heme. The intermediate led to
S, Potuznik   +3 more
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EXTRACELLULAR THIOLS AND THIOL/DISULFIDE REDOX IN METABOLISM

Annual Review of Nutrition, 2004
▪ Abstract  Many proteins present on cell surfaces and located in extracellular fluids contain cysteine and methionine residues that are subject to oxidation. These proteins, which include transporters, receptors, and enzymes, respond to variations in the extracellular thiol/disulfide redox environment.
Siobhan E, Moriarty-Craige   +1 more
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Chemically Induced Vinylphosphonothiolate Electrophiles for Thiol–Thiol Bioconjugations

Journal of the American Chemical Society, 2020
Herein we introduce vinylphosphonothiolates as a new class of cysteine-selective electrophiles for protein labeling and the formation of stable protein-protein conjugates. We developed a straightforward synthetic route to convert nucleophilic thiols into electrophilic, thiol-selective vinylphosphonothiolates: In this protocol, intermediately formed ...
Alice L, Baumann   +7 more
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Low-Molecular-Weight Thiols in Thiol–Disulfide Exchange

Antioxidants & Redox Signaling, 2013
Oxidative stress is widely invoked in inflammation, aging, and complex diseases. To avoid unwanted oxidations, the redox environment of cellular compartments needs to be tightly controlled. The complementary action of oxidoreductases and of high concentrations of low-molecular-weight (LMW) nonprotein thiols plays an essential role in maintaining the ...
Van Laer, Koen   +2 more
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Reactions of thiols

Russian Journal of Organic Chemistry, 2007
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
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Immune system and thiols: Some peculiarities of thiol exchange

Comparative Immunology, Microbiology and Infectious Diseases, 2010
We show that for the system of SH-containing compounds of the organism (cysteine, in particular) there are conditions leading to immunosuppression, which occurs when the level of amino acid cysteine in blood serum increases. The arising "overload" of free sulfhydryl groups inactivates antibodies of the IgM class of any specificity restoring disulphide ...
N K, Rodosskaia, G M, Chernousova
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New Thiols for Photoinitiator‐Free Thiol‐Acrylate Polymerization

Macromolecular Chemistry and Physics, 2013
AbstractNew thiols for efficient thiol‐ene polymerization reactions are presented. They do not exhibit any unpleasant odor, are characterized by quite good light‐absorption properties at λ > 300 nm, and generate thiyl radicals upon UV‐light exposure.
Mohamad‐Ali Tehfe   +8 more
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ROS, thiols and thiol-regulating systems in male gametogenesis

Biochimica et Biophysica Acta (BBA) - General Subjects, 2015
During maturation and storage, spermatozoa generate substantial amounts of reactive oxygen species (ROS) and are thus forced to cope with an increasingly oxidative environment that is both needed and detrimental to their biology. Such a janus-faceted intermediate needs to be tightly controlled and this is done by a wide array of redox enzymes.
Conrad, M.   +4 more
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Thiol-dependent and non-thiol-dependent stimulations of insulin release

Diabetes, 1984
The effects of reduced glutathione (GSH) and diamide (an oxidant of GSH) on insulin release induced by glucose, glyceraldehyde, leucine, tolbutamide, glibenclamide, Ca-ionophore A-23187, isoprenaline, and db-cAMP were studied using isolated rat pancreatic islets.
H P, Ammon   +3 more
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