Results 1 to 10 of about 61,356 (195)

Glutathione S-Transferases in Cancer [PDF]

open access: yesAntioxidants, 2021
In humans, the glutathione S-transferases (GST) protein family is composed of seven members that present remarkable structural similarity and some degree of overlapping functionalities.
Rahul R Singh, Katie M Reindl
exaly   +8 more sources

Glutathione S-transferases in pediatric cancer [PDF]

open access: yesFrontiers in Oncology, 2011
The glutathione S-transferases (GSTs) are a family of ubiquitously-expressed polymorphic enzymes important for detoxifying endogenous and exogenous compounds.
Wen eLuo   +3 more
doaj   +4 more sources

Glutathione S-transferases Control astrocyte activation and neuronal health during neuroinflammation [PDF]

open access: yesFrontiers in Molecular Biosciences, 2023
Glutathione S-transferases (GST) are phase II detoxification enzymes of xenobiotic metabolism and readily expressed in the brain. Nevertheless, the current knowledge about their roles in the brain is limited.
Ken Matoba   +5 more
doaj   +2 more sources

The Multifaceted Role of Glutathione S-Transferases in Health and Disease [PDF]

open access: yesBiomolecules, 2023
In humans, the cytosolic glutathione S-transferase (GST) family of proteins is encoded by 16 genes presented in seven different classes. GSTs exhibit remarkable structural similarity with some overlapping functionalities. As a primary function, GSTs play
Aslam M. A. Mazari   +5 more
doaj   +2 more sources

Efficient Adsorption and Extraction of Glutathione S-Transferases with Glutathione-Functionalized Graphene Oxide–Polyhedral Oligomeric Silsesquioxane Composite [PDF]

open access: yesMolecules, 2023
Glutathione S-transferases (GSTs) are important type-II detoxification enzymes that protect DNA and proteins from damage and are often used as protein tags for the expression of fusion proteins.
Jingqi Sun, Limin Jia, Xuwei Chen
doaj   +2 more sources

Characterization of the Glutathione S-Transferases Involved in Styrene Degradation in Gordonia rubripertincta CWB2 [PDF]

open access: yesMicrobiology Spectrum, 2021
The glutathione S-transferases carried on the plasmid for the styrene-specific degradation pathway in the Actinobacterium Gordonia rubripertincta CWB2 were heterologously expressed in Escherichia coli.
Anna C. Lienkamp   +4 more
doaj   +2 more sources

Diversity of Glutathione S-Transferases (GSTs) in Cyanobacteria with Reference to Their Structures, Substrate Recognition and Catalytic Functions [PDF]

open access: yesMicroorganisms, 2020
Glutathione S-Transferases (GSTs) comprise a diverse group of protein superfamily involved in cellular detoxification of various harmful xenobiotics and endobiotics.
Mohandass ShylajaNaciyar   +6 more
doaj   +2 more sources

Arabidopsis Glutathione-S-Transferases GSTF11 and GSTU20 Function in Aliphatic Glucosinolate Biosynthesis [PDF]

open access: yesFrontiers in Plant Science, 2022
Glutathione (GSH) conjugation with intermediates is required for the biosynthesis of glucosinolate (GSL) by serving as a sulfur supply. Glutathione-S-transferases (GSTs) primarily work on GSH conjugation, suggesting their involvement in GSL metabolism ...
Aiqin Zhang   +6 more
doaj   +2 more sources

Association of Androgen-Receptor Gene Mutations with the Copy Number of Androgen-Receptor Silk Protein A Complex and Glutathione-S-Transferases T1 and M1 in Prostate Cancer Patients [PDF]

open access: yesGenetics Research, 2023
Objective. The purpose of our work was to explore the association of mutations in the androgen receptor gene and copy numbers of the androgen-receptor silk protein A complex with glutathione-S-transferases T1 and M1 in prostate cancer patients. Materials
Yan Zhang   +4 more
doaj   +2 more sources

Genetic Polymorphisms of Glutathione S-Transferases T1 (GSTT1) and M1 (GSTM1) in Iranian Mandaeans Population [PDF]

open access: yesIranian Journal of Public Health, 2019
Genetic Polymorphisms of Glutathione S-Transferases T1 (GSTT1) and M1 (GSTM1) in Iranian Mandaeans ...
Fariba BOROUMAND   +2 more
doaj   +2 more sources

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