Results 41 to 50 of about 6,811 (158)

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

S-glutathionylation activates STIM1 and alters mitochondrial homeostasis [PDF]

Journal of Cell Biology, 2010
Oxidant stress influences many cellular processes, including cell growth, differentiation, and cell death. A well-recognized link between these processes and oxidant stress is via alterations in Ca2+ signaling. However, precisely how oxidants influence Ca2+ signaling remains unclear. Oxidant stress led to a phenotypic shift in Ca2+ mobilization from an
Hawkins, Brian J, Irrinki, Krishna M, Mallilankaraman, Karthik, Lien, Yu-Chin, Wang, Youjun, Bhanumathy, Cunnigaiper D, Subbiah, Ramasamy, Ritchie, Michael F, Soboloff, Jonathan, Baba, Yoshihiro, Kurosaki, Tomohiro, Joseph, Suresh K, Gill, Donald L, Madesh, Muniswamy   +13 more
openaire   +3 more sources

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

S-Glutathionylation at Cys328 and Cys542 Impairs STAT3 Phosphorylation

ACS Chemical Biology, 2014
STAT3 is a latent transcription factor that promotes cell survival and proliferation and is often constitutively active in cancers. Although many reports provide evidence that STAT3 is a direct target of oxidative stress, its redox regulation is poorly understood.
BUTTURINI, Elena, DARRA, Elena, Chiavegato, Giulia, CELLINI, Barbara, Flora Cozzolino, Maria Monti, Piero Pucci, DELL'ORCO, Daniele, MARIOTTO, Sofia Giovanna   +8 more
openaire   +3 more sources

Fluorescein-labeled glutathione to study protein S-glutathionylation [PDF]

Analytical Biochemistry, 2010
Numerous studies of S-glutathionylation of cysteine thiols indicate that this protein modification plays a key role in redox regulation of proteins. To facilitate the study of protein S-glutathionylation, we developed a synthesis and purification to produce milligram quantities of fluorescein-labeled glutathione.
Lisa M, Landino, Carolyn M, Brown, Carolyn A, Edson, Laura J, Gilbert, Nathan, Grega-Larson, Anna Jean, Wirth, Kelly C, Lane   +6 more
openaire   +2 more sources

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

The roles of S-nitrosylation and S-glutathionylation in Alzheimer's disease. [PDF]

Methods Enzymol, 2019
Alzheimer's disease (AD) is a debilitating dementia with complex pathophysiological alterations including modifications to endogenous cysteine. S-nitrosylation (SNO) is a well-studied posttranslational modification (PTM) in the context of AD while S-glutathionylation (PSSG) remains less studied. Excess reactive oxygen and reactive nitrogen species (ROS/
Dyer RR, Ford KI, Robinson RAS.
europepmc   +4 more sources

The Role of S-Glutathionylation in Health and Disease: A Bird's Eye View. [PDF]

Nutrients
Protein glutathionylation is a reversible post-translational modification that involves the attachment of glutathione to cysteine residues. It plays a role in the regulation of several cellular processes and protection against oxidative damage. Glutathionylation (GS-ylation) modulates protein function, inhibits or enhances enzymatic activity, maintains
Federici L, Masulli M, De Laurenzi V, Allocati N.   +3 more
europepmc   +3 more sources

Metal‐dependent regulated cell death: Molecular architecture and translational frontiers

iMeta, EarlyView.
Intracellular metal dyshomeostasis orchestrates distinct regulated cell death programs, including iron‐driven ferroptosis, copper‐mediated cuproptosis, calcicoptosis, newly designated zincoptosis, mnoptosis, and coptosis. This review systematically delineates their molecular architectures—spanning from Sorafenib‐induced lipid peroxidation and ...
Haoliang Hu, Zhe Chen, Yaqi Li, Jiayi Peng, Jiangang Cao, Hong Zhou, Mengqi Wang, Yuejia Du, Hailin Wu, Huiqin Zhao, Shifang Huang, Dianmei Yu, Meiqing Liu, Olga V. Shevchenko, Natalia Yu. Matveeva, Yiyuan Yang, Kerui Huang, Deguan Lv, Junxia Min, Linxi Chen, Fudi Wang   +20 more
wiley   +1 more source

In Vivo Tagging and Characterization of S‐Glutathionylated Proteins by a Chemoenzymatic Method [PDF]

Angewandte Chemie, 2012
Glutathione (GSH), a sulfhydryl-containing tripeptide present in most organisms at millimolar levels, plays a crucial role in redox homeostasis.1 Reactive cysteine residues are vulnerable to reactive oxygen or nitrogen species and thus depend heavily on GSH to avoid irreversible oxidation.[1a], [2] Reversible conjugation of GSH to proteins through the ...
Chiang, Bing-Yu, Chou, Chi-Chi, Hsieh, Fu-Tan, Gao, Shijay, Lin, Jason Ching-Yao, Lin, Sheng-Huang, Chen, Tze-Chieh, Khoo, Kay-Hooi, Lin, Chun-Hung   +8 more
openaire   +4 more sources