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MyJournals.org - Science - 'IJMS, Vol. 24, Pages 8116: Development of Galectin-3 Targeting Drugs for Therapeutic Applications in Various Diseases' (International Journal of Molecular Sciences)

MyJournals.org - Science - IJMS, Vol. 24, Pages 8116: Development of Galectin-3 Targeting Drugs for Therapeutic Applications in Various Diseases (International Journal of Molecular Sciences) ....

Alectin 3 ,

MyJournals.org - Science - 'IJMS, Vol. 24, Pages 7683: Galectin-3 as a Marker for Increased Thrombogenicity in COVID-19' (International Journal of Molecular Sciences)

MyJournals.org - Science - IJMS, Vol. 24, Pages 7683: Galectin-3 as a Marker for Increased Thrombogenicity in COVID-19 (International Journal of Molecular Sciences) ....

Willebrand Factor , Alectin 3 , Covid 19 ,

"Investigation of the Molecular Details of the Interactions of Selenogl" by Mária Raics, Álex Kálmán Balogh et al.

Human galectin-3 (hGal-3) is involved in a variety of biological processes and is implicated in wide range of diseases. As a result, targeting hGal-3 for clinical applications has become an intense area of research. As a step towards the development of novel hGal-3 inhibitors, we describe a study of the binding of two Se-containing hGal-3 inhibitors, specifically that of di(β-D-galactopyranosyl)selenide (SeDG), in which two galactose rings are linked by one Se atom and a di(β-D-galactopyranosyl)diselenide (DSeDG) analogue with a diseleno bond between the two sugar units. The binding affinities of these derivatives to hGal-3 were determined by15N-1H HSQC NMR spectroscopy and fluorescence anisotropy titrations in solution, indicating a slight decrease in the strength of interaction for SeDG compared to thiodigalactoside (TDG), a well-known inhibitor of hGal-3, while DSeDG displayed a much weaker interaction strength. NMR and FA measurements showed that both seleno derivatives bind to t ....

Fluorescence Anisotropy , Alectin 3 , Molecular Dynamics , Nmr Spectroscopy , X Ray Crystallography ,

"Overcoming microenvironment-mediated chemoprotection through stromal g" by Somayeh S. Tarighat, Fei Fei et al.

Environmentally-mediated drug resistance in B-cell precursor acute lymphoblastic leukemia (BCP-ALL) significantly contributes to relapse. Stromal cells in the bone marrow environment protect leukemia cells by secretion of chemokines as cues for BCP-ALL migration towards, and adhesion to, stroma. Stromal cells and BCP-ALL cells communicate through stromal galectin-3. Here, we investigated the significance of stromal galectin-3 to BCP-ALL cells. We used CRISPR/Cas9 genome editing to ablate galectin-3 in stromal cells and found that galectin-3 is dispensable for steady-state BCP-ALL proliferation and viability. However, efficient leukemia migration and adhesion to stromal cells are significantly dependent on stromal galectin-3. Importantly, the loss of stromal galectin-3 production sensitized BCP-ALL cells to conventional chemotherapy. We therefore tested novel carbohydrate-based small molecule compounds (Cpd14 and Cpd17) with high specificity for galectin-3. Consistent with results obtai ....

B Cell Precursor All , Arbohydrate Based Galectin 3 Inhibitor , Drug Resistance , Alectin 3 ,