Results 251 to 260 of about 242,358 (312)
Disulfidptosis in heart failure: an emerging mechanism awaiting exploration. [PDF]
Ding S +8 more
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Chemical Devulcanization of Crosslinked Nitrile Rubber Using Tetra-<i>n</i>-Butylammonium Fluoride (TBAF) as a Devulcanization Aid. [PDF]
Wręczycki J +3 more
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Thiols, Thiol Depletion, and Thermosensitivity
Radiation Research, 1983Hyperthermia 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, 1993The 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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Thiol-addition reactions and their applications in thiol recognition
Chemical Society Reviews, 2013Because of the biological importance of thiols, the development of probes for thiols has been an active research area in recent years. In this review, we summarize the results of recent exciting reports regarding thiol-addition reactions and their applications in thiol recognition.
Yin, Caixia +6 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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Low-Molecular-Weight Thiols in Thiol–Disulfide Exchange
Antioxidants & Redox Signaling, 2013Oxidative 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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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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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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Chemically Induced Vinylphosphonothiolate Electrophiles for Thiol–Thiol Bioconjugations
Journal of the American Chemical Society, 2020Herein 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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