Results 31 to 40 of about 6,811 (158)

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

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: From Molecular Mechanisms to Health Outcomes [PDF]

Antioxidants & Redox Signaling, 2011
Redox homeostasis governs a number of critical cellular processes. In turn, imbalances in pathways that control oxidative and reductive conditions have been linked to a number of human disease pathologies, particularly those associated with aging.
Ying, Xiong, Joachim D, Uys, Kenneth D, Tew, Danyelle M, Townsend   +3 more
openaire   +2 more sources

S-glutathionylation: relevance in diabetes and potential role as a biomarker [PDF]

bchm, 2013
Abstract Glutathione is considered the main regulator of redox balance in the cellular milieu due to its capacity for detoxifying deleterious molecules. The oxidative stress induced as a result of a variety of stimuli promotes protein oxidation, usually at cysteine residues, leading to changes in their activity.
Sánchez Gómez, Francisco Javier, Espinosa-Díez, Cristina, Dubey, Megha, Dikshit, Madhu, Lamas Peláez, Santiago   +4 more
openaire   +3 more sources

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

Regulation of antigen 85C activity by reversible S‐glutathionylation [PDF]

IUBMB Life, 2018
AbstractMycobacterium tuberculosis is the causative agent of many strains of tuberculosis, as it is composed of an impenetrable, complex cell wall. The proteins active in the synthesis of the cell wall are mycolyl transferase antigens 85A, 85B, and 85C, encoded by genes fbpA, fbpB, and fbpC. Antigen 85C contains one cysteine residue.
Alysia Mandato, Yuh‐Cherng Chai
openaire   +2 more sources