Results 31 to 40 of about 6,975 (121)

S-glutathionylation reactions in mitochondrial function and disease

open access: yesFrontiers in Cell and Developmental Biology, 2014
Mitochondria are highly efficient energy-transforming organelles that convert energy stored in carbon bonds into the universal energy currency ATP. The production of ATP by mitochondria is dependent on oxidation of nutrients and coupling of exergonic ...
Ryan J. Mailloux, William G. Willmore
doaj   +1 more source

Novel control of cardiac myofilament response to calcium by S-glutahionylation at specific sites of myosin binding protein C

open access: yesFrontiers in Physiology, 2013
Our previous studies demonstrated a relation between glutathionylation of cardiac myosin binding protein C and diastolic dysfunction in a hypertensive mouse model stressed by treatment with salt, deoxycorticosterone acetate, and unilateral nephrectomy.
Bindiya G Patel   +2 more
doaj   +1 more source

Dicarbonyl Stress and S-Glutathionylation in Cerebrovascular Diseases: A Focus on Cerebral Cavernous Malformations

open access: yesAntioxidants, 2020
Dicarbonyl stress is a dysfunctional state consisting in the abnormal accumulation of reactive α-oxaldehydes leading to increased protein modification.
Cinzia Antognelli   +4 more
doaj   +1 more source

Glutaredoxin-1 alleviates acetaminophen-induced liver injury by decreasing its toxic metabolites

open access: yesJournal of Pharmaceutical Analysis, 2023
Excessive N-acetyl-p-benzoquinone imine (NAPQI) formation is a starting event that triggers oxidative stress and subsequent hepatocyte necrosis in acetaminophen (APAP) overdose caused acute liver failure (ALF).
Ying Xu   +12 more
doaj   +1 more source

OTUD6A‐Mediated Deubiquitination of PRDX1 Protects Against Oral Ulcer by Restoring Mitochondrial Function

open access: yesAdvanced Science, EarlyView.
In human oral keratinocytes, OTUD6A promoted cell migration by deubiquitinating and stabilizing PRDX1. Conversely, OTUD6A deficiency reduced PRDX1 stability, triggering mitochondrial dysfunction and aggravating OU progression. ABSTRACT Oral ulcers (OU), as the most highly prevalent and recurrent oral mucosal lesion, have an unclear pathogenesis that ...
Xiaoyu Sun   +15 more
wiley   +1 more source

Identification of DUOX1-dependent redox signaling through protein S-glutathionylation in airway epithelial cells

open access: yesRedox Biology, 2014
The NADPH oxidase homolog dual oxidase 1 (DUOX1) plays an important role in innate airway epithelial responses to infection or injury, but the precise molecular mechanisms are incompletely understood and the cellular redox-sensitive targets for DUOX1 ...
Milena Hristova   +7 more
doaj   +1 more source

HSV infection induces production of ROS, which potentiate signaling from pattern recognition receptors: role for S-glutathionylation of TRAF3 and 6. [PDF]

open access: yesPLoS Pathogens, 2011
The innate immune response constitutes the first line of defense against infections. Pattern recognition receptors recognize pathogen structures and trigger intracellular signaling pathways leading to cytokine and chemokine expression.
Regina Gonzalez-Dosal   +7 more
doaj   +1 more source

Glutaredoxins Rapidly Reduce Glutathione Hydroper‐ and Polysulfides

open access: yesAngewandte Chemie International Edition, EarlyView.
Glutaredoxins (Grx) rapidly reduce glutathione polysulfides (GSSnSG) to glutathione hydroper/polysulfides (GSSnH) or GSSnH to hydrogen (poly)sulfides (H2Sn). Reduction of glutathionylated glutaredoxins by reduced glutathione (GSH) yields glutathione disulfide (GSSG).
Philipp Reinert   +6 more
wiley   +1 more source

Cellular Compartmentalization, Glutathione Transport and Its Relevance in Some Pathologies

open access: yesAntioxidants, 2023
Reduced glutathione (GSH) is the most abundant non-protein endogenous thiol. It is a ubiquitous molecule produced in most organs, but its synthesis is predominantly in the liver, the tissue in charge of storing and distributing it. GSH is involved in the
Héctor Vázquez-Meza   +4 more
doaj   +1 more source

Ion Activation Methods for Top‐Down Proteomics

open access: yesMass Spectrometry Reviews, EarlyView.
ABSTRACT Mass spectrometry (MS) has emerged as a premier method used to characterize the sequences of proteins. Top‐down proteomics aims to capture the multiple sources of structural diversity reflected in proteins, such as those that arise from alternative RNA splicing events or the addition of post‐translational modifications. Tandem MS (i.e., MS/MS)
Jada N. Walker, Jennifer S. Brodbelt
wiley   +1 more source

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