Results 251 to 260 of about 221,664 (312)

Disulfide modification and thiol protection via tris(trimethylsilyl)silane-mediated hydrosilylation of disulfides. [PDF]

Nat Commun
Zhang Y, Lin K, Zang Z, Chen J, Zhu T.
europepmc   +1 more source

Controlling Macrophage Uptake of Gold Nanoparticles through the Design of an Effective Heterogeneous Coating. [PDF]

ACS Appl Mater Interfaces
Siani P, Eguskiza A, Frigerio G, Donadoni E, Ossanna R, Volk M, Brust M, Giovannone B, Fiammengo R, Di Valentin C.   +9 more
europepmc   +1 more source

Built-in thiol mesoporous carbon immunosensor to detect carcinoembryonic antigen in human serum. [PDF]

Mikrochim Acta
Echeverri D, Laverde J, Restrepo LG, Llinás-Quintero N, López D, Orozco J.   +5 more
europepmc   +1 more source

Synthesis and Immunological Evaluation of Pel-Derived Glycoconjugate Vaccine Candidates against <i>Pseudomonas aeruginosa</i>. [PDF]

JACS Au
Wu DY, Bino LD, Romagnoli G, van der Marel GA, Adamo R, Romano MR, Codée JDC.   +6 more
europepmc   +1 more source

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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, D, Gelvan, P, Burda, P, Saltman   +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, Dean P, Jones   +1 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, Hamilton, Chris J, Messens, Joris   +2 more
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