Publications by authors named "Gemma Bruno"
Liver fibrosis, characterized by scar tissue accumulation due to liver injury, poses significant barriers to liver-targeted gene therapy. Current clinical trials exclude patients with fibrosis, as intact liver architecture is considered essential for efficient and safe adeno-associated viral vector (AAV)-mediated gene delivery. Here, we show that liver fibrosis reduces the efficiency of hepatocyte transduction by AAV8 vectors across three mouse models with diverse fibrotic patterns.
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- Lysosomes, once thought to be only for degradation, are now recognized for their roles in nutrient sensing, signaling, and metabolism, highlighting their multifunctional significance in cells.
- Recent advancements in research techniques have improved our understanding of lysosome morphology, positioning, motility, and function, facilitating deeper insights into these organelles.
- This review aims to enhance research quality on lysosomes by discussing methods, identifying key characteristics, and encouraging further discoveries in cell biology.
Article Synopsis
- Urea cycle disorders (UCD) are genetic conditions that hinder the body’s ability to remove waste nitrogen, leading to serious health issues.
- Research identified Beclin-1 as a promising target for treatment, and the peptide Tat-Beclin-1 (TB-1) was tested for its effectiveness in common UCD types.
- TB-1 showed beneficial effects in animal models, reducing harmful substances, enhancing survival rates on high-protein diets, and improving liver health in both types of UCD.
Autophagy is a cytosolic quality control process that recognizes substrates through receptor-mediated mechanisms. Procollagens, the most abundant gene products in Metazoa, are synthesized in the endoplasmic reticulum (ER), and a fraction that fails to attain the native structure is cleared by autophagy. However, how autophagy selectively recognizes misfolded procollagens in the ER lumen is still unknown.
View Article and Find Full Text PDFDerivatives of the thiirancarboxylic acid building-block containing a peptide bond were synthesised and screened against the model cysteine protease papain. The most active of the series showed a second-order rate constant of inactivation comparable to that of the parent compound. The insertion of a peptide moiety seems to compensate the lack of a free carboxylate interacting with the histidinium ion at the enzyme's active site.
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