Publications by authors named "M Barreca"

The prevalence of malignant cells in clinical specimens, or tumour purity, is affected by both intrinsic biological factors and extrinsic sampling bias. Molecular characterization of large clinical cohorts is typically performed on bulk samples; data analysis and interpretation can be biased by tumour purity variability. Transcription-based strategies to estimate tumour purity have been proposed, but no breast cancer specific method is available yet.

View Article and Find Full Text PDF
Article Synopsis
  • * Researchers developed a compound, derivative 33, from a quinolone library that showed anti-ovarian cancer activity and worked well alongside cisplatin in resistant cancer cells.
  • * Derivative 33 binds to TRBP, influencing miRNA maturation, and has a stronger effect against ovarian cancer cells compared to the previously known modulator, enoxacin, suggesting it could lead to new treatments.
View Article and Find Full Text PDF

Citrus wastewater from industries is a source of bioactive compounds whose recovery could be a useful approach to convert processing waste into potential resources to be exploited in food, pharmaceutical, and chemical companies. Citrus wastewater, obtained from the industrial processing of Citrus sinensis, was freeze-dried and qualitative/quantitative evaluated using HPLC/MS Q-TOF analysis. Antiproliferative activity was investigated on MDA-MB-231 (triple-negative breast cancer cell line), MCF-7 (breast cancer cell line), and its multidrug-resistant variant MCF-7R.

View Article and Find Full Text PDF
Article Synopsis
  • * The study explored the effects of a natural compound combination (escin-bromelain-ginkgo biloba-sage miltiorrhiza, or EBGS) on inhibiting platelet adhesion to damaged blood vessels, a crucial step in thrombus formation.
  • * Results indicated that EBGS pretreatment reduces platelet adhesion by inhibiting adhesion molecules and inflammatory cytokines, suggesting its potential as a preventive therapy against thrombus formation.
View Article and Find Full Text PDF

The correction of protein folding is fundamental for cellular functionality and its failure can lead to severe diseases. In this context, molecular chaperones are crucial players involved in the tricky process of assisting in protein folding, stabilization, and degradation. Chaperones, such as heat shock proteins (HSP) 90, 70, and 60, operate within complex systems, interacting with co-chaperones both to prevent protein misfolding and direct to the correct folding.

View Article and Find Full Text PDF