Results 31 to 40 of about 3,419 (230)

2-Thiouridine formation in Escherichia coli: a critical review [PDF]

open access: yesJournal of Bacteriology
Modifications of transfer RNA (tRNA) have been shown to play critical roles in the biogenesis, metabolism, structural stability, and function of RNA molecules, and the specific modifications of nucleobases with sulfur atoms in tRNA are present in ...
Silke Leimkühler
doaj   +2 more sources

Identification of persulfide-binding and disulfide-forming cysteine residues in the NifS-like domain of the molybdenum cofactor sulfurase ABA3 by cysteine-scanning mutagenesis [PDF]

open access: green, 2012
The Moco (molybdenum cofactor) sulfurase ABA3 from Arabidopsis thaliana catalyses the sulfuration of the Moco of aldehyde oxidase and xanthine oxidoreductase, which represents the final activation step of these enzymes.
Wissing, Josef   +11 more
core   +2 more sources

Toxic Tear Gas 2-Chloroacetophenone (CN) Forms Adducts With Endogenous Plasma Thiols In Vitro Valuable as Biomarkers of Exposure. [PDF]

open access: yesDrug Test Anal
Incubation of human plasma with the tear gas 2‐chloroacetophenone (CN) led to the formation of acetophenone (AcPhen)‐adducts with the small plasma thiols glutathione, homocysteine, and cysteine persulfide. The AcPhen‐adducts were either bound to an organic thiol‐group or to an organic persulfide. The adducts were detected with a mass spectrometry‐based
Sieber PH, Steinritz D, Worek F, John H.
europepmc   +2 more sources

Cysteine trisulfide oxidizes protein thiols and induces electrophilic stress in human cells

open access: yesRedox Biology, 2021
The cellular effects of hydrogen sulfide (H2S) signaling may be partially mediated by the formation of alkyl persulfides from thiols, such as glutathione and protein cysteine residues.
Christopher H. Switzer   +3 more
doaj   +1 more source

Therapeutic Efficacy of the Supersulfide Donor NAC-S2 in Influenza Virus Pneumonia via Suppression of Excessive Inflammatory Responses. [PDF]

open access: yesMicrobiol Immunol
ABSTRACT Influenza pneumonia is characterized by excessive inflammatory responses that contribute to severe lung injury and mortality. Supersulfides, endogenously produced cysteine‐derived persulfides and polysulfides, exert potent antioxidant, anti‐ferroptotic, and anti‐inflammatory activities; however, their therapeutic potential after disease onset ...
Hossen F   +9 more
europepmc   +2 more sources

The mercaptopyruvate sulfurtransferase of trichomonas vaginalis links cysteine catabolism to the production of thioredoxin persulfide [PDF]

open access: hybrid, 2009
Trichomonas vaginalis is a protozoan parasite of humans that is able to synthesize cysteine de novo using cysteine synthase but does not produce glutathione. In this study, high pressure liquid chromatography analysis confirmed that cysteine is the major
Coombs, G.H.   +8 more
core   +2 more sources

Saccharomyces cerevisiae Rhodanese RDL2 Uses the Arg Residue of the Active-Site Loop for Thiosulfate Decomposition

open access: yesAntioxidants, 2021
Persulfide, polysulfide and thiosulfate are examples of sulfane sulfur containing chemicals that play multiple functions in biological systems. Rhodaneses are widely present in all three kingdoms of life, which catalyze sulfur transfer among these ...
Qingda Wang   +4 more
doaj   +1 more source

Protein Persulfidation in Plants: Function and Mechanism [PDF]

open access: yesAntioxidants, 2021
As an endogenous gaseous transmitter, the function of hydrogen sulfide (H2S) has been extensively studied in plants. Once synthesized, H2S may be involved in almost all life processes of plants. Among them, a key route for H2S bioactivity occurs via protein persulfidation, in which process oxidizes cysteine thiol (R-SH) groups into persulfide (R-SSH ...
Peng Wang   +3 more
openaire   +3 more sources

Persulfides and the cellular thiol landscape [PDF]

open access: yesProceedings of the National Academy of Sciences, 2014
The biochemistry of sulfur touches on every aspect of cellular biology, from protein structure and function to redox regulation to defense against chemical stress. Over the last decade, posttranslational modification of protein thiols by reactive oxygen or nitrogen species has emerged as a major component of signal transduction, leading to both ...
Miranda, Katrina M., Wink, David A.
openaire   +4 more sources

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