Results 91 to 100 of about 8,996 (206)

Protein S-glutathionylation levels in control dogs and in dogs infused with sodium nitrite.

, 2015
Compared with controls, there was an increase in protein S-glutathionylation in dogs that had been infused with sodium nitrite prior to occlusion (NaNO2-PO group), as determined via Western immunoblot with an anti-glutathionylation antibody.
Attila Kiss (619090), József Kaszaki (618316), Mária Kovács (729488), György Seprényi (729491), Mark J. Kohr (649470), Elizabeth Murphy (649471), Ágnes Végh (729492), Márton Gönczi (729489), Gottfried Miskolczi (729490)   +8 more
core   +1 more source

Activation of Nrf2 at Critical Windows of Development Alters Tissue-Specific Protein S-Glutathionylation in the Zebrafish (Danio rerio) Embryo

Antioxidants
Activation of Nrf2—the master regulator of antioxidative response—at different stages of embryonic development has been shown to result in changes in gene expression, but the tissue-specific and downstream effects of Nrf2 activation during development ...
Emily S. Marques, Emily G. Severance, Paige Arsenault, Sarah M. Zahn, Alicia R. Timme-Laragy   +4 more
doaj   +1 more source

Detection of ROS Induced Proteomic Signatures by Mass Spectrometry

Frontiers in Physiology, 2017
Reversible and irreversible post-translational modifications (PTMs) induced by endogenously generated reactive oxygen species (ROS) in regulatory enzymes and proteins plays an essential role in cellular signaling.
Brian McDonagh
doaj   +1 more source

Dietary glycine supplementation enhances growth, feed utilization, and antioxidant capacity of large yellow croaker Larimichthys crocea

Journal of the World Aquaculture Society, Volume 57, Issue 5, October 2026.
Abstract Glycine is a dispensable and functional amino acid that promotes fish growth, however, the optimal glycine content in fish diets is not known. This study assessed the effect of dietary glycine content on growth, feed utilization, and antioxidant capacity of large yellow croaker (LYC) Larimichthys crocea.
Mingtao Lei, Jieliang Fan, Pingding Liu, Peng Li, Yan Wang   +4 more
wiley   +1 more source

S-Glutathionylation Enhances Human Cystathionine β-Synthase Activity Under Oxidative Stress Conditions [PDF]

, 2014
Aims: Cystathionine β-synthase (CBS) catalyzes the first and rate-limiting step in the two-step trans-sulfuration pathway that converts homocysteine to cysteine.
Banerjee, Ruma, Adamec, Jiri, Niu, Wei-Ning, Yadav, Pramod Kumar   +3 more
core   +1 more source

Glutathionylspermidine in the Modification of Protein SH Groups: The Enzymology and Its Application to Study Protein Glutathionylation

Molecules, 2015
Cysteine is very susceptible to reactive oxygen species. In response; posttranslational thiol modifications such as reversible disulfide bond formation have arisen as protective mechanisms against undesired in vivo cysteine oxidation.
Jason Ching-Yao Lin, Bing-Yu Chiang, Chi-Chi Chou, Tzu-Chieh Chen, Yi-Ju Chen, Yu-Ju Chen, Chun-Hung Lin   +6 more
doaj   +1 more source

A cross‐species post‐translational modification profiling of histones by LC‐MS/MS revealed conserved oxidative modifications in plants

New Phytologist, Volume 252, Issue 2, Page 538-545, October 2026.
Conservation of post‐translational modifications (PTMs) in histones across six plant species.
Sau‐Shan Cheng, Wai‐Ching Sin, Yuen‐Yi Chau, Hon‐Ming Lam   +3 more
wiley   +1 more source

Redox regulation of the proteasome via S-glutathionylation

Redox Biology, 2014
The proteasome is a multimeric and multicatalytic intracellular protease responsible for the degradation of proteins involved in cell cycle control, various signaling processes, antigen presentation, and control of protein synthesis. The central catalytic complex of the proteasome is called the 20S core particle.
Marilene Demasi, Luis E.S. Netto, Gustavo M. Silva, Adrian Hand, Cristiano L.P. de Oliveira, Renata N. Bicev, Fabio Gozzo, Mario H. Barros, Janaina M.M. Leme, Erina Ohara   +9 more
openaire   +3 more sources

Integrated redox sensor and effector functions for tetrahydrobiopterin- and glutathionylation-dependent endothelial nitric-oxide synthase uncoupling.

, 2016
Endothelial nitric-oxide synthase (eNOS) is a critical regulator of vascular homeostasis by generation of NO that is dependent on the cofactor tetrahydrobiopterin (BH4). When BH4 availability is limiting, eNOS becomes "uncoupled," resulting in superoxide

core   +1 more source

Glutathionylation of beta-actin via a cysteinyl sulfenic acid intermediary-4

, 2011
Copyright information:Taken from "Glutathionylation of beta-actin via a cysteinyl sulfenic acid intermediary"http://www.biomedcentral.com/1471-2091/8/26BMC Biochemistry 2007;8():26-26.Published online 10 Dec 2007PMCID:PMC2228301.del for glutathionylation
Magnus Johansson (85854), Mathias Lundberg (85855)   +1 more
core   +1 more source