Results 11 to 20 of about 7,062 (200)
Isolable Cysteine Sulfenyl Iodide: Stabilization by a Molecular Cradle, Crystal Structure, and Biologically Relevant Reactivity. [PDF]
ChembiochemAn isolable cysteine sulfenyl iodide (Cys–SI) stabilized by a molecular cradle is reported. X‐ray analysis and reactivity studies reveal hydrolysis to sulfenic acid, electrophilic substitution with indoles, and high reactivity toward amines and dimedone, providing direct evidence for long‐standing proposals on iodine‐mediated protein modification ...
Otaka S +4 more
europepmc +2 more sources
H<sub>2</sub>S Is a Potential Universal Reducing Agent for Prx6-Type Peroxiredoxins. [PDF]
Adv Sci (Weinh)We report the identification of H2S as reducing agent for Prx6‐type peroxiredoxins. In contrast to common physiological reducing agents of other peroxiredoxins, HS− is small enough to access the active site of oxidized Prx6‐type enzymes in the fully‐folded protein conformation.
Lang L, Leiskau L, Bambach L, Deponte M.
europepmc +2 more sources
Frontiers in Plant Science, 2020 In proteins, hydrogen peroxide (H2O2) reacts with redox-sensitive cysteines to form cysteine sulfenic acid, also known as S-sulfenylation. These cysteine oxidation events can steer diverse cellular processes by altering protein interactions, trafficking,
Bo Wei +15 more
doaj +1 more source
The Active Site Sulfenic Acid Ligand in Nitrile Hydratases Can Function as a Nucleophile [PDF]
, 2014 Nitrile hydratase (NHase) catalyzes the hydration of nitriles to their corresponding commercially valuable amides at ambient temperatures and physiological pH.
Holz, Richard C. +4 more
core +3 more sources
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
core +2 more sources
Brazilian Journal of Medical and Biological Research, 2009 Human serum albumin (HSA) is the most abundant protein in the intravascular compartment. It possesses a single thiol, Cys34, which constitutes ~80% of the total thiols in plasma. This thiol is able to scavenge plasma oxidants.
L. Turell +4 more
doaj +1 more source
Molecules, 2019 Glutathione-based products, GSnX, of the reaction of hydrogen sulfide, H2S, S-nitroso glutathione, and GSNO, at varied stoichiometries have been analyzed by liquid chromatography high-resolution mass spectrometry (LC-HRMS) and chemical trapping ...
Murugaeson R Kumar, Patrick J Farmer
doaj +1 more source
Synthesis of Curcumin Derivatives and Analysis of Their Antitumor Effects in Triple Negative Breast Cancer (TNBC) Cell Lines [PDF]
, 2019 We analyzed antitumor effects of a series of curcumin analogues. Some of them were obtained by reaction of substitution involving the two phenolic OH groups of curcumin while the analogues with a substituent at C-4 was prepared following an original ...
Barattucci A +5 more
core +1 more source
Antioxidants, 2018 Cysteine and methionine residues are the amino acids most sensitive to oxidation by reactive oxygen species. However, in contrast to other amino acids, certain cysteine and methionine oxidation products can be reduced within proteins by dedicated ...
Sofia Lourenço dos Santos +2 more
doaj +1 more source
Measurement of Protein Sulfenic Acid Content [PDF]
Current Protocols in Toxicology, 2003 AbstractProtein sulfenic acids are reactive, reversibly oxidized, cysteinyl residues with roles in redox catalysis and regulation. Detection and quantitation of these species in proteins is accomplished through chemical modification by reagents such as 7‐chloro‐4‐nitrobenzo‐2‐oxa‐1,3‐diazole (NBD chloride), 2‐nitro‐5‐thiobenzoate (TNB) or dimedone ...
openaire +2 more sources