Publications by authors named "S Petrella"

Article Synopsis
  • Cathepsins are important cysteine proteases involved in various cellular processes and play a significant role in pancreatic cancer progression.
  • Recent studies have focused on developing cathepsin inhibitors, particularly targeting cathepsin S, to improve cancer treatment effectiveness.
  • A new series of inhibitors based on fluorinated cinnamate compounds have shown strong potential against pancreatic cancer cell lines, demonstrating considerable antiproliferative effects.
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Article Synopsis
  • * Researchers synthesized triazole-containing compounds that showed strong antibacterial effects, especially one named BDM71403, which was found to be more effective than the reference drug, gepotidacin.
  • * Detailed structural studies using cryo-electron microscopy revealed how BDM71403 interacts with DNA gyrase and DNA, providing insights for future antibiotic development to combat resistant bacteria.
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Cells are continuously facing the risk of taking up foreign DNA that can compromise genomic integrity. Therefore, bacteria are in a constant arms race with mobile genetic elements such as phages, transposons and plasmids. They have developed several active strategies against invading DNA molecules that can be seen as a bacterial 'innate immune system'.

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Polo-like kinase 1 (PLK1) is the principle member of the well conserved serine/threonine kinase family. PLK1 has a key role in the progression of mitosis and recent evidence suggest its important involvement in regulating the G2/M checkpoint, in DNA damage and replication stress response, and in cell death pathways. PLK1 expression is tightly spatially and temporally regulated to ensure its nuclear activation at the late S-phase, until the peak of expression at the G2/M-phase.

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Eukaryotic topoisomerases I (TOP1) are ubiquitous enzymes removing DNA torsional stress. However, there is little data concerning the three-dimensional structure of TOP1 in the absence of DNA, nor how the DNA molecule can enter/exit its closed conformation. Here, we solved the structure of thermostable archaeal Caldiarchaeum subterraneum CsTOP1 in an apo-form.

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