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Analysis of glutathione: implication in redox and detoxification.
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Colorimetric and fluorometric assays of glutathione transferase based on 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole.
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Glutathione transferases and development of new principles to overcome drug resistance.
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Determination of blood total, reduced, and oxidized glutathione in pediatric subjects.
TLDR
A rapid and fully automated HPLC method for determining total, reduced, reduced (GSH), and oxidized glutathione (GSSG) in whole blood is reported, and values for the different forms of blood glutATHione in pediatric subjects are reported.
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Epigenetically silenced miR-34b/c as a novel faecal-based screening marker for colorectal cancer
TLDR
Findings show that aberrant hypermethylation of miR-34b/c could be an ideal class of early screening marker, whereas mi R-148a could serve as a disease progression follow-up marker.
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Structural basis for the binding of the anticancer compound 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-transferases.
TLDR
The crystal structure of 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol (NBDHEX) was identified and tested on several tumor cell lines demonstrating high antiproliferative activity and it is shown here that the Ile(104)Val and IleAla variants display a 4-fold higher affinity for the compound.
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Seven mutations in the human insulin gene linked to permanent neonatal/infancy-onset diabetes mellitus.
TLDR
It is found that mutations in the insulin gene that promote proinsulin misfolding may cause permanent neonatal diabetes mellitus.
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Differential expression of miR-144* as a novel fecal-based diagnostic marker for colorectal cancer
TLDR
It is demonstrated that miRNAs are stable in the fecal microenvironment, and that, among them, miR-144* represents a novel fecal-based diagnostic marker for CRC screening.
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The splice variant LOXIN inhibits LOX-1 receptor function through hetero-oligomerization.
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Actin Glutathionylation Increases in Fibroblasts of Patients with Friedreich's Ataxia
TLDR
It is demonstrated that, in fibroblasts of patients with FRDA, the cellular redox equilibrium is shifted toward more protein-bound glutathione, and actin is glutathionylated, probably as a result of the accumulation of reactive oxygen species, generated by iron overload in the disease.
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