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Gp70 is a cell wall protein required for adhesion, proper interaction with innate immune cells, and virulence.

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Departamento de Biología, División de Ciencias Naturales y Exactas, Campus Guanajuato, Universidad de Guanajuato, Noria Alta s/n, col. Noria Alta, C.P. 36050 Guanajuato, Gto, Mexico.

is one of the leading etiological agents of sporotrichosis, a cutaneous and subcutaneous mycosis worldwide distributed. This organism has been recently associated with epidemic outbreaks in Brazil. Despite the medical relevance of this species, little is known about its virulence factors, and most of the information on this subject is extrapolated from .

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The epithelial-mesenchymal transition (EMT) is a biological process in which epithelial cells change into mesenchymal cells with fibroblast-like characteristics. EMT plays a crucial role in the progression of fibrosis. Classical inducers associated with the maintenance of EMT, such as TGF-β1, have become targets of several anti-EMT therapeutic strategies.

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Article Synopsis
  • The study investigates how high glucose levels in diabetes lead to kidney cell damage through the activation of a signaling pathway involving DJ-1 and PTEN.
  • DJ-1 is found to be upregulated in kidney cells under high glucose conditions, which triggers the Akt/mTORC1 signaling pathway, resulting in cell growth and fibrosis.
  • The research indicates that inhibiting DJ-1 can prevent glucose-induced cell growth and damage, while overexpressing DJ-1 replicates the harmful effects, highlighting its role in renal injury related to diabetes.
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To investigate the role of appetite-related factors, including interleukin 6 (IL-6), irisin, interleukin 7 (IL-7), neuropeptide Y (NPY), and leptin, on appetite perception in males with obesity. Eleven males (BMI 35.3 ± 4.

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Missense mutations in the EPHA1 receptor tyrosine kinase have been identified in Alzheimer's patients. To gain insight into their potential role in disease pathogenesis, we investigated the effects of four of these mutations. We show that the P460L mutation in the second fibronectin type III (FN2) domain drastically reduces EPHA1 cell surface localization while increasing tyrosine phosphorylation of the cell surface-localized receptor.

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