Results 41 to 50 of about 24,013,578 (179)
Redox Biology, 2022 Heat shock protein 90 (Hsp90) is a ubiquitous chaperone to interact with numerous proteins to regulate multiple cellular processes, especially during cell proliferation and cell cycle progression.
Yu-Yin Shih +6 more
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Post-translational S-glutathionylation of cofilin increases actin cycling during cocaine seeking.
PLoS ONE, 2019 Neuronal defense against oxidative damage is mediated primarily by the glutathione redox system. Traditionally considered a mechanism to protect proteins from irreversible oxidation, mounting evidence supports a role for protein S-glutathionylation in ...
Anna Kruyer +4 more
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S-Glutathionylation and Redox Protein Signaling in Drug Addiction [PDF]
, 2016 Drug addiction is a chronic relapsing disorder that comes at a high cost to individuals and society. Therefore understanding the mechanisms by which drugs exert their effects is of prime importance. Drugs of abuse increase the production of reactive oxygen and nitrogen species resulting in oxidative stress.
Jacqueline S, Womersley, Joachim D, Uys
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BMC Plant Biology, 2021 Background Flexibility of plant metabolism is supported by redox regulation of enzymes via posttranslational modification of cysteine residues, especially in plastids.
Stefanie J. Müller-Schüssele +5 more
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Frontiers 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
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Protocols for the Detection of S-Glutathionylated and S-Nitrosylated Proteins In Situ [PDF]
, 2010 The oxidation of protein cysteine residues represents significant posttranslational modifications that impact a wide variety of signal transduction cascades and diverse biological processes. Oxidation of cysteines occurs through reactions with reactive oxygen as well as nitrogen species.
Aesif, S.W. +2 more
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Nature Communications, 2023 Protein-S-glutathionylation is a post-translational modification involving the conjugation of glutathione to protein thiols, which can modulate the activity and structure of key cellular proteins.
Elizabeth M. Corteselli +12 more
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Molecular mechanisms and potential clinical significance of S-glutathionylation
, 2008 Protein S-glutathionylation, the reversible binding of glutathione to protein thiols (PSH), is involved in protein redox regulation, storage of glutathione, and protection of PSH from irreversible oxidation.
DALLE DONNE I +5 more
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Glutaredoxin-1 alleviates acetaminophen-induced liver injury by decreasing its toxic metabolites
Journal 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
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Cell Reports, 2017 Reactive oxygen species (ROS)-induced cysteine S-glutathionylation is an important posttranslational modification (PTM) that controls a wide range of intracellular protein activities.
Xue Zhang +23 more
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