Results 51 to 60 of about 6,885 (176)

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., Janssen Heininger, Y.M., Reynaert, N.L.   +2 more
openaire   +2 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

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

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, Tanganyika eWilder, R. John Solaro   +2 more
doaj   +1 more source

Structural and functional fine mapping of cysteines in mammalian glutaredoxin reveal their differential oxidation susceptibility

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, Mona Sharafi, Robert Hondal, Maximilian MacPherson, Sheryl White, Ying-Wai Lam, Clarissa Gold, Allison M. Manuel, Albert van der Vliet, Severin T. Schneebeli, Vikas Anathy, Jianing Li, Yvonne M. W. Janssen-Heininger   +12 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

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, Yan Xia, Qinhui Liu, Xiandan Jing, Qin Tang, Jinhang Zhang, Qingyi Jia, Zijing Zhang, Jiahui Li, Jiahao Chen, Yimin Xiong, Yanping Li, Jinhan He   +12 more
doaj   +1 more source

Evaluation of protein S-glutathionylation patterns.

, 2013
Evaluation of protein S-glutathionylation patterns was performed by 2D-immunoblotting with anti-GSH antibody: A) control cells. B) H-RasV12 expressing cells.
Carla Emiliani (184188), Lorena Urbanelli (293124), Francesca Magherini (293125), Giovanni Principato (293128), Alessandra Modesti (293127), Alessandro Magini (184184), Armanda Pugnaloni (293126), Francesco Piva (72402), Luisa Ercolani (293123), Tatiana Armeni (293122)   +9 more
core   +1 more source

Nitrosative Stress-Induced S-Glutathionylation of Protein Disulfide Isomerase [PDF]

, 2011
Oxidative and nitrosative stress result in the accumulation of reactive oxygen and nitrogen species (ROS/RNS) which trigger redox-mediated signaling cascades through posttranslational modifications on cysteine residues, including S-nitrosylation (P-SNO) and S-glutathionylation (P-SSG). Protein disulfide isomerase (PDI) is the most abundant chaperone in
Joachim D, Uys, Ying, Xiong, Danyelle M, Townsend   +2 more
openaire   +2 more sources

Dataset related to the article "Impact of oxidative stress and protein S-Glutathionylation in aortic valve sclerosis patients with overt atherosclerosis

, 2020
This record contains raw data related to the article "Impact of oxidative stress and protein S-Glutathionylation in aortic valve sclerosis patients with overt atherosclerosis" Abstract: Aortic valve sclerosis (AVSc) is characterized by non-uniform ...
Moschetta, D, Myasoedova, VA, Perucci, GL, Poggio, P, Cavalca, V, Songia, P, Cavallotti, L, Porro, B, Valerio, V   +8 more
core   +2 more sources

Membrane skeletal protein S-glutathionylation and hemolysis in human red blood cells.

, 2006
In this work, protein-glutathione mixed disulfide formation in human red blood cells (RBCs) was evaluated in vitro by using the thiol-specific reagent diamide. We investigated what mechanism could lead to S-glutathionylation of membrane skeletal proteins,
D. Giustarini, A. Milzani, Rossi, Ranieri, Dalle Donne, I., I. Dalle Donne, Giustarini, D., Milzani, A., R. Rossi   +7 more
core   +1 more source