Publications by authors named "Ryan Oliverio"
HspA1A is a cytosolic molecular chaperone essential for cellular homeostasis. HspA1A also localizes at the plasma membrane (PM) of tumor and stressed cells. However, it is currently unknown how this cytosolic protein translocates to the PM.
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- This report examines how natural single nucleotide polymorphisms (SNPs) impact the function of the HSPA1A gene, which is crucial for stress response in humans.
- All mutant proteins can still hydrolyze ATP, but three mutants do so at a significantly lower rate than the wild-type, while some show increased reaction entropies.
- Mutations also influence the ability of HSPA1A to refold proteins and prevent apoptosis, with some leading to increased cell death compared to the wild-type, suggesting alterations in the protein's chaperone activities.
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- Evolutionary mechanisms influence how mutations and genes develop in populations, particularly through their functional effects.
- This study focuses on the Hsp70 genes HSPA1A and HSPA1B, which are crucial for the cellular stress response and linked to various diseases, revealing that these genes evolved through duplications in the lineage of placental mammals.
- The research found that purifying selection maintained the stability of these genes while gene conversion kept their sequences highly conserved, resulting in mostly synonymous mutations and specific regions lacking mutations, ultimately highlighting the balance between evolution and conservation in stress response mechanisms.
Toll-like receptor 2 (TLR2) plays an important role in recognition by the innate immune system of Gram-positive bacteria. As Gram-positive bacteria cause mastitis, we examined variations in the region of the TLR2 gene that codes for the extracellular domain. Samples of forty goats from a single dairy herd were collected, half with low SCC (≤200,000 cells/mL), and half with higher SCC.
View Article and Find Full Text PDFCharacterization of the binding between a 70-kDa heat shock protein, HspA1A, and phosphoinositides.
Biochem Biophys Res Commun
March 2016
HspA1A, a seventy-kilodalton heat shock protein, binds to specific anionic lipids and this interaction regulates important physiological phenomena like apoptosis, tumor growth, and lysosomal rescue. However, whether HspA1A binds to phosphoinositides has yet to be established and quantified. Therefore, in this study, we determined the binding affinity of HspA1A to several phosphoinositides and characterized five aspects of their molecular interaction.
View Article and Find Full Text PDFThe Cyt1Aa protein of Bacillus thuringiensis subsp. israelensis is known to synergize mosquitocidal proteins of B. thuringiensis and Bacillus sphaericus strains.
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