Publications by authors named "C R Carluccio"

In the last years, it has been proved that some viruses are able to re-structure chromatin organization and alter the epigenomic landscape of the host genome. In addition, they are able to affect the physical mechanisms shaping chromatin 3D structure, with a consequent impact on gene activity. Here, we investigate with polymer physics genome re-organization of the host genome upon SARS-CoV-2 viral infection and how it can impact structural variability within the population of single-cell chromatin configurations.

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The spatial organization of chromatin within the eukaryotic nucleus is critical in regulating key cellular functions, such as gene expression, and its disruption can lead to disease. Advances in experimental techniques, such as Hi-C and microscopy, have significantly enhanced our understanding of chromatin's intricate and dynamic architecture, revealing complex patterns of interaction at multiple scales. Along with experimental methods, physics-based computational models, including polymer phase separation and loop-extrusion mechanisms, have been developed to explain chromatin structure in a principled manner.

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Lipopolysaccharides (LPS) decorating the cell surface of Gram-negative bacteria exhibit nuanced functionalities linked to their precise structural composition. However, despite their critical role in health and disease, information on the structure and function of LPS from members of the human gut microbiota is still limited. Here, we deciphered the complete structure of the LPS isolated from the human gut bacterium Bacteroides eggerthii 1_2_48FAA.

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Article Synopsis
  • Mycoplasma pneumoniae and Mycoplasma genitalium are bacteria that infect the human respiratory and urogenital tracts by attaching to host cells through cytoadhesins.
  • These cytoadhesins bind specifically to sialylated glycans on host surfaces, making them critical for infection.
  • Researchers are exploring ways to design inhibitors that block these interactions, which could lead to new treatments for infections caused by these pathogens.
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Article Synopsis
  • Protein-glycan interactions are essential for various biological processes, including cell recognition and immune response, making their understanding important for both health and disease.
  • Computational techniques are crucial for visualizing and analyzing these interactions at the molecular level, particularly using all-atom molecular dynamics simulations.
  • This review discusses key computational tools for studying glycans and proteins, detailing their methodologies, applications, and case studies that illustrate their effectiveness in exploring binding kinetics and molecular interactions.
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