Results 11 to 20 of about 1,944 (186)

Hydrogen Sulfide: From a Toxic Molecule to a Key Molecule of Cell Life [PDF]

open access: yesAntioxidants, 2020
Hydrogen sulfide (H2S) has always been considered toxic, but a huge number of articles published more recently showed the beneficial biochemical properties of its endogenous production throughout all regna.
Angeles Aroca   +3 more
doaj   +4 more sources

Dual Roles of Reducing Systems in Protein Persulfidation and Depersulfidation [PDF]

open access: yesAntioxidants
The oxidative modification of specific cysteine residues to persulfides is thought to be the main way by which hydrogen sulfide (H2S) exerts its biological and signaling functions. Therefore, protein persulfidation represents an important thiol-switching
Zhichao Liu   +2 more
doaj   +2 more sources

A persulfidation-based mechanism controls aquaporin-8 conductance [PDF]

open access: yesScience Advances, 2018
Upon engagement of tyrosine kinase receptors, nicotinamide adenine dinucleotide phosphate (NADPH)-oxidases release H2O2 in the extracellular space.
Bestetti, Stefano   +8 more
core   +5 more sources

Cysteine-rich zinc finger proteins and the nuclear factor kappa-B pathway [PDF]

open access: yesFrontiers in Chemical Biology
Inflammation-related disorders, such as autoimmune diseases and cancer, impose a significant global health burden. Zinc finger proteins (ZFs) are ubiquitous metalloproteins which regulate inflammation and many biological signaling pathways related to ...
Andrew T. Stoltzfus, Sarah L. J. Michel
doaj   +2 more sources

Reactive Sulfur Species and Protein Persulfidation: An Emerging Redox Axis in Human Health and Disease [PDF]

open access: yesCurrent Issues in Molecular Biology
Reactive sulfur species (RSS)—hydrogen sulfide (H2S), low-molecular-weight persulfides/polysulfides and protein persulfidation—constitute a third redox axis alongside ROS and RNS.
Celia María Curieses Andrés   +5 more
doaj   +2 more sources

Persulfidation of Human Cystathionine γ-Lyase Inhibits Its Activity: A Negative Feedback Regulation Mechanism for H2S Production [PDF]

open access: yesAntioxidants
Cystathionine γ-lyase (CSE) is the second enzyme in the trans-sulfuration pathway that converts cystathionine to cysteine. It is also one of three major enzymes responsible for the biosynthesis of hydrogen sulfide (H2S).
Guanya Jia   +8 more
doaj   +2 more sources

Persulfidation of DJ-1: Mechanism and Consequences

open access: yesBiomolecules, 2022
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 residues is functionally essential, and its oxidation state determines the specific function of the
Erwan Galardon   +5 more
doaj   +3 more sources

Plant catalases as NO and H2S targets [PDF]

open access: yesRedox Biology, 2020
Catalase is a powerful antioxidant metalloenzyme located in peroxisomes which also plays a central role in signaling processes under physiological and adverse situations. Whereas animals contain a single catalase gene, in plants this enzyme is encoded by
José M. Palma   +6 more
doaj   +5 more sources

Hydrogen sulfide protects against spinal cord pyroptosis via persulfidation of Rac1 after lumbosacral plexus nerve injury [PDF]

open access: yesCell Death Discovery
Pyroptosis, a form of lytic and inflammatory programmed cell death mediated by gasdermin proteins, contributes to progressive spinal cord neurodegeneration following neural trauma.
Jianyu Mao   +9 more
doaj   +2 more sources

Profiling the landscape of cysteine posttranslational modifications in brain aging and neurodegeneration [PDF]

open access: yesNeurotherapeutics
Cysteine residues occupy a unique position in the proteome: their thiolate side chain combines high nucleophilicity with redox sensitivity, making them prime targets for a diverse and ever-expanding array of post-translational modifications (PTMs).
Milos R. Filipovic
doaj   +2 more sources

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