Results 21 to 30 of about 6,975 (121)

High glutathionylation of placental endothelial nitric oxide synthase in preeclampsia

Redox Biology, 2019
Decreased nitric oxide (NO) bioavailability plays a critical role in the pathophysiology of preeclampsia (PE). Recent evidence indicates that S-glutathionylation may occur on the endothelial nitric oxide synthase (eNOS), leading to eNOS uncoupling ...
Paul Guerby, Audrey Swiader, Nathalie Augé, Olivier Parant, Christophe Vayssière, Koji Uchida, Robert Salvayre, Anne Negre-Salvayre   +7 more
doaj   +1 more source

S-glutathionylation proteome profiling reveals a crucial role of a thioredoxin-like protein in interspecies competition and cariogenecity of Streptococcus mutans.

PLoS Pathogens, 2020
S-glutathionylation is an important post-translational modification (PTM) process that targets protein cysteine thiols by the addition of glutathione (GSH).
Zhengyi Li, Chenzi Zhang, Cheng Li, Jiajia Zhou, Xin Xu, Xian Peng, Xuedong Zhou   +6 more
doaj   +1 more source

Positive Regulation of Interleukin-1β Bioactivity by Physiological ROS-Mediated Cysteine S-Glutathionylation

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, Peng Liu, Christie Zhang, Direkrit Chiewchengchol, Fan Zhao, Hongbo Yu, Jingyu Li, Hiroto Kambara, Kate Y. Luo, Arvind Venkataraman, Ziling Zhou, Weidong Zhou, Haiyan Zhu, Li Zhao, Jiro Sakai, Yuanyuan Chen, Ye-Shih Ho, Besnik Bajrami, Bing Xu, Leslie E. Silberstein, Tao Cheng, Yuanfu Xu, Yuehai Ke, Hongbo R. Luo   +23 more
doaj   +1 more source

Temporal changes in glutaredoxin 1 and protein s-glutathionylation in allergic airway inflammation. [PDF]

PLoS ONE, 2015
Asthma is a chronic inflammatory disorder of the airways, involving oxidative stress. Upon oxidative stress, glutathione covalently binds to protein thiols to protect them against irreversible oxidation.
Kanako Maki, Katsura Nagai, Masaru Suzuki, Takashi Inomata, Takayuki Yoshida, Masaharu Nishimura   +5 more
doaj   +1 more source

The redox mechanism for vascular barrier dysfunction associated with metabolic disorders: Glutathionylation of Rac1 in endothelial cells

Redox Biology, 2016
Background: Oxidative stress is implicated in increased vascular permeability associated with metabolic disorders, but the underlying redox mechanism is poorly defined.
Jingyan Han, Robert M. Weisbrod, Di Shao, Yosuke Watanabe, Xiaoyan Yin, Markus M. Bachschmid, Francesca Seta, Yvonne M.W. Janssen-Heininger, Reiko Matsui, Mengwei Zang, Naomi M. Hamburg, Richard A. Cohen   +11 more
doaj   +1 more source

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, Lauren E Ball, Danyelle M Townsend, Peter W Kalivas, Joachim D Uys   +4 more
doaj   +1 more source

New insights into posttranslational modifications of proteins during bull sperm capacitation

Cell Communication and Signaling, 2023
Background Due to the unique nature of spermatozoa, which are transcriptionally and translationally silent, the regulation of capacitation is based on the formation of posttranslational modifications of proteins (PTMs).
Agnieszka Mostek-Majewska, Anna Majewska, Anna Janta, Andrzej Ciereszko   +3 more
doaj   +1 more source

S-Glutathionylation of Protein Disulfide Isomerase Regulates Estrogen Receptor α Stability and Function

International Journal of Cell Biology, 2012
S-Glutathionylation of cysteine residues within target proteins is a posttranslational modification that alters structure and function. We have shown that S-glutathionylation of protein disulfide isomerase (PDI) disrupts protein folding and leads to the ...
Ying Xiong, Yefim Manevich, Kenneth D. Tew, Danyelle M. Townsend   +3 more
doaj   +1 more source

Plasticity in plastid redox networks: evolution of glutathione-dependent redox cascades and glutathionylation sites

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, Finja Bohle, Jacopo Rossi, Paolo Trost, Andreas J. Meyer, Mirko Zaffagnini   +5 more
doaj   +1 more source

GSTpi regulates VE-cadherin stabilization through promoting S-glutathionylation of Src

Redox Biology, 2020
GSTpi is a Phase II metabolic enzyme which is originally considered as an important facilitator of cellular detoxification. Here, we found that GSTpi stabilized VE-cadherin in endothelial cell membrane through inhibiting VE-cadherin phosphorylation and ...
Yang Yang, Xiaoliang Dong, Shuangning Zheng, Jinbing Sun, Juan Ye, Jiao Chen, Yuan Fang, Bing Zhao, Zhimin Yin, Peng Cao, Lan Luo   +10 more
doaj   +1 more source