Zobrazeno 1 - 10
of 1 813
pro vyhledávání: '"S-glutathionylation"'
Autor:
Jacqueline S. Womersley, Clémence Obellianne, Audrey E. Padula, Marcelo F. Lopez, William C. Griffin, Lauren E. Ball, Stefano Berto, Kathleen A. Grant, Danyelle M. Townsend, Joachim D. Uys, Patrick J. Mulholland
Publikováno v:
Biomedicine & Pharmacotherapy, Vol 180, Iss , Pp 117514- (2024)
Alcohol use disorder (AUD) is the most prevalent substance use disorder but there is incomplete knowledge of the underlying molecular etiology. Here, we examined the cytosolic proteome from the nucleus accumbens core (NAcC) of ethanol drinking rhesus
Externí odkaz:
https://doaj.org/article/065fd24f7c074ee98ae105b126d2ddbc
Autor:
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
Publikováno v:
Journal of Pharmaceutical Analysis, Vol 13, Iss 12, Pp 1548-1561 (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). S-glutathionylation is a reversible red
Externí odkaz:
https://doaj.org/article/063c7bc8b2f447eda513b9fc63f26214
Autor:
Xiaolin Sun, Chaorui Guo, Chunyan Huang, Ning Lv, Huili Chen, Haoyan Huang, Yulin Zhao, Shanliang Sun, Di Zhao, Jingwei Tian, Xijing Chen, Yongjie Zhang
Publikováno v:
Redox Biology, Vol 71, Iss , Pp 103116- (2024)
Oxidative stress plays an important role in the pathogenesis of acute lung injury (ALI). As a typical post-translational modification triggered by oxidative stress, protein S-glutathionylation (PSSG) is regulated by redox signaling pathways and plays
Externí odkaz:
https://doaj.org/article/15a23e4295e04d80a5dfcc6924adcc6c
Autor:
Yunfei Zhang, Mei Yan, Yingying Xia, Yingbin Yue, Shuli Wang, Yuhui Hu, Genjian Lai, Quanjiang Wu, Qianyang Liu, Xin Ding, Chunbao Guo
Publikováno v:
Molecular Therapy: Methods & Clinical Development, Vol 32, Iss 1, Pp 101214- (2024)
Inducible nitric oxide synthase (iNOS), regulated by nuclear factor kappa B (NF-κB), is crucial for intestinal inflammation and barrier injury in the progression of necrotizing enterocolitis (NEC). The NF-κB pathway is inhibited by S-glutathionylat
Externí odkaz:
https://doaj.org/article/955a5d3a180e4323a9968faa034bcc22
Publikováno v:
Nutrients, Vol 16, Iss 16, p 2753 (2024)
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. Gluta
Externí odkaz:
https://doaj.org/article/f50d35c0c31b4d3796dea9d337236194
Autor:
Elena Kalinina
Publikováno v:
International Journal of Molecular Sciences, Vol 25, Iss 15, p 8423 (2024)
The most abundant tripeptide—glutathione (GSH)—and the major GSH-related enzymes—glutathione peroxidases (GPxs) and glutathione S-transferases (GSTs)—are highly significant in the regulation of tumor cell viability, initiation of tumor develo
Externí odkaz:
https://doaj.org/article/323a51e2d9364d0c8337b9d85842a9a6
Autor:
Finja Bohle, Jacopo Rossi, Sadia S. Tamanna, Hannah Jansohn, Marlene Schlosser, Frank Reinhardt, Alexa Brox, Stephanie Bethmann, Stanislav Kopriva, Oliver Trentmann, Peter Jahns, Marcel Deponte, Markus Schwarzländer, Paolo Trost, Mirko Zaffagnini, Andreas J. Meyer, Stefanie J. Müller-Schüssele
Publikováno v:
Redox Biology, Vol 69, Iss , Pp 103015- (2024)
Redox status of protein cysteinyl residues is mediated via glutathione (GSH)/glutaredoxin (GRX) and thioredoxin (TRX)-dependent redox cascades. An oxidative challenge can induce post-translational protein modifications on thiols, such as protein S-gl
Externí odkaz:
https://doaj.org/article/d765821352f849e893ab5c37a6b91512
Publikováno v:
Cell Communication and Signaling, Vol 21, Iss 1, Pp 1-23 (2023)
Abstract 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). However, the interact
Externí odkaz:
https://doaj.org/article/366b7d304aa144c49d0f05647c16258f
Autor:
Xiufang Chen, Qian Zhou, Huamin Chen, Juan Bai, Ruike An, Keyi Zhang, Xinyue Zhang, Hui An, Jitai Zhang, Yongyu Wang, Ming Li
Publikováno v:
Antioxidants, Vol 13, Iss 4, p 400 (2024)
Glutathione (GSH), a robust endogenous antioxidant, actively participates in the modulation of the redox status of cysteine residues in proteins. Previous studies have indicated that GSH can prevent β-cell failure and prediabetes caused by chronic o
Externí odkaz:
https://doaj.org/article/60c749b66abf461da3f72ce589b6fec4
Publikováno v:
Redox Biology, Vol 62, Iss , Pp 102676- (2023)
Oxidative stress drives protein S-glutathionylation, which regulates the structure and function of target proteins and is implicated in the pathogenesis of many diseases. Glutaredoxin 1 (Grx1), a cytoplasmic deglutathionylating enzyme, maintains a re
Externí odkaz:
https://doaj.org/article/1d89468080f5494cab95907d6a6ddb97