Results 1 to 10 of about 21,521,606 (315)

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 Raj Singh, Katie M. Reindl
doaj   +6 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   +3 more sources

Functional and Structural Diversity of Insect Glutathione S-transferases in Xenobiotic Adaptation. [PDF]

open access: yesInt J Biol Sci, 2022
As a superfamily of multifunctional enzymes that is mainly associated with xenobiotic adaptation, glutathione S-transferases (GSTs) facilitate insects' survival under chemical stresses in their environment.
Koirala B K S, Moural T, Zhu F.
europepmc   +2 more sources

The role of glutathione S-transferases in human disease pathogenesis and their current inhibitors. [PDF]

open access: yesGenes Dis
Glutathione S-transferases (GSTs) are a family of enzymes detoxifying various harmful compounds by conjugating them with glutathione. While primarily beneficial, dysregulation of GST activity or specific isoforms can contribute to disease pathogenesis ...
Alnasser SM.
europepmc   +2 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   +3 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

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

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

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

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

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