Publications by authors named "Bei-Lei Sun"
Article Synopsis
- Current research highlights -nitrosoglutathione reductase (GSNOR) as a key enzyme in regulating protein -nitrosylation and its dysregulation linked to various organ pathologies, making it a target for drug development.
- The study shows that GSNOR is activated by its substrate, -nitrosoglutathione (GSNO), exhibiting positive allosteric effects, validated by kinetic analysis and molecular dynamics.
- Identification of the allosteric binding site for GSNO on GSNOR, involving specific amino acids, opens new avenues for pharmacological intervention to control GSNOR activity in disease contexts.
S-nitrosoglutathione reductase (GSNOR) is a multifunctional enzyme. It can catalyze NADH-dependent reduction of S-nitrosoglutathione (GSNO); as well as NAD-dependent oxidation of hydroxymethylglutathione (HMGSH; an adduct formed by the spontaneous reaction between formaldehyde and glutathione). While initially recognized as the enzyme that is involved in formaldehyde detoxification, increasing amount of evidence has shown that GSNOR also plays a significant role in nitric oxide mediated signaling through its modulation of protein S-nitrosothiol signaling.
View Article and Find Full Text PDFAim: To investigate GATA5, SFRP2, and ITGA4 methylation in plasma DNA as noninvasive biomarkers for colorectal cancer (CRC) or adenomas.
Methods: There were 57 CRC patients, 30 adenomas patients, and 47 control patients enrolled in this study. Methylation-specific polymerase chain reaction was used to determine the promoter methylation status of GATA5, SFRP2, and ITGA4 genes in plasma DNA, and their association with clinical outcome in CRC.
[Raman spectroscopic characteristics of different rank coals and the relation with XRD structural parameters].
Guang Pu Xue Yu Guang Pu Fen Xi
September 2009
The Raman spectroscopic analysis for eleven different rank coals (57.58% to 94.01% of Cdaf, %) indicated that two distinct bands, i.
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