Results 21 to 30 of about 1,224 (162)
Protein Persulfidation in Plants: Function and Mechanism [PDF]
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
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Persulfides and the cellular thiol landscape [PDF]
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.
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Persulfidation of DJ-1 : Mechanism and Consequences
Abstract DJ-1 (also called PARK7) is a ubiquitously expressed protein involved in the etiology of Parkinson disease and cancers. At least one of its three cysteine residue is functionally essential, and its oxidation state determines the specific function of the enzyme.
Erwan Galardon +5 more
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Contribution of NRF2 to sulfur metabolism and mitochondrial activity
NF-E2-related factor 2 (NRF2) plays a crucial role in the maintenance of cellular homeostasis by regulating various enzymes and proteins that are involved in the redox reactions utilizing sulfur.
Md Morshedul Alam +7 more
doaj +1 more source
AbstractProtein persulfides (R‐S‐SH) have emerged as a common post‐translational modification. Detection and quantitation of protein persulfides requires trapping with alkylating agents. Here we show that alkylating agents differ dramatically in their ability to conserve the persulfide's sulfur–sulfur bond for subsequent detection by mass spectrometry.
Danny Schilling +5 more
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Acidity and nucleophilic reactivity of glutathione persulfide [PDF]
Les persulfures (RSSH/RSS−) participent au trafic de soufre et aux processus métaboliques, et sont proposés pour médier les effets de signalisation du sulfure d'hydrogène (H2S). Malgré leur pertinence croissante, leurs propriétés chimiques sont mal comprises.
Dayana Benchoam +10 more
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Hydrogen sulfide (H2S) is endogenously produced by enzymes and via reactive persulfide/polysulfide degradation; it participates in a variety of biological processes under physiological and pathological conditions. H2S levels in biological fluids, such as
Shingo Kasamatsu +4 more
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Enzymatic Regulation and Biological Functions of Reactive Cysteine Persulfides and Polysulfides
Cysteine persulfide (CysSSH) and cysteine polysulfides (CysSSnH, n > 1) are cysteine derivatives that have sulfane sulfur atoms bound to cysteine thiol. Advances in analytical methods that detect and quantify persulfides and polysulfides have shown that ...
Tomohiro Sawa +3 more
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Direct Proteomic Mapping of Cysteine Persulfidation [PDF]
Aims: Cysteine persulfidation (also called sulfhydration or sulfuration) has emerged as a potential redox mechanism to regulate protein functions and diverse biological processes in hydrogen sulfide (H2S) signaling. Due to its intrinsically unstable nature, working with this modification has proven to be challenging.
Ling, Fu +5 more
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Hydrogen Sulfide and Persulfides Oxidation by Biologically Relevant Oxidizing Species
Hydrogen sulfide (H2S/HS⁻) can be formed in mammalian tissues and exert physiological effects. It can react with metal centers and oxidized thiol products such as disulfides (RSSR) and sulfenic acids (RSOH).
Dayana Benchoam +3 more
doaj +1 more source

