In vitro combination effects of plant-derived quercetin with synthetic bicalutamide on prostate cancer and normal cell lines: in silico comparison.

Prostate cancer is the second most frequent and the fifth greatest cause of death in men. Although diet has been connected to the prevalence of cancer in addition to other factors, the relation between cancer and prevention is weak. Treatment options are at risk due to cell resistance.

Amalgamation of quercetin with anastrozole and capecitabine: A novel combination to treat breast and colon cancers - An study.

Context: Globally, cancer stands as the principle cause of mortality and immediate attention on its treatment options is required. Natural compounds stay at first priority in encountering novel therapeutics without adverse effects.

Aim: The aim of the study is to extract flavonol quercetin from leafy vegetables of Anethum graveolens L.

New tetrameric forms of the rotavirus NSP4 with antiparallel helices.

Rotavirus nonstructural protein 4, the first viral enterotoxin to be identified, is a multidomain, multifunctional glycoprotein. Earlier, we reported a Ca-bound coiled-coil tetrameric structure of the diarrhea-inducing region of NSP4 from the rotavirus strains SA11 and I321 and a Ca-free pentameric structure from the rotavirus strain ST3, all with a parallel arrangement of α-helices. pH was found to determine the oligomeric state: a basic pH favoured a tetramer, whereas an acidic pH favoured a pentamer.

Conformational Differences Unfold a Wide Range of Enterotoxigenic Abilities Exhibited by rNSP4 Peptides from Different Rotavirus Strains.

NSP4 has been recognized as the rotavirus-encoded enterotoxin. However, a few studies failed to support its diarrheagenic activity. As recombinant NSP4 (rNSP4) peptides of different lengths were used in the limited number of studies, a comparison of relative diarrheagenic potential of NSP4 from different strains could not be possible.

The flexible C terminus of the rotavirus non-structural protein NSP4 is an important determinant of its biological properties.

The rotavirus non-structural protein NSP4 functions as the viral enterotoxin and intracellular receptor for the double-layered particles (DLP). The full-length protein cannot be expressed and/or purified to homogeneity from bacterial or insect cells. However, a bacterially expressed and purified mutant lacking the N-terminal 72 aa (DeltaN72) was recently obtained from strains Hg18 and SA11 exhibiting approximately 17-20-, 150-200- and 13166-15800-fold lower DD50 (50% diarrhoea-inducing dose) values in suckling mice compared with that reported for the partially pure, full-length protein, a C-terminal M175I mutant and a synthetic peptide comprising aa 114-135, respectively, suggesting the requirement for a unique conformation for optimal functions of the purified protein.