Chávez Gutiérrez Lab

Our research is based on the premise that getting a better mechanistic understanding of the function of the molecules involved in familial Alzheimer’s disease (FAD) will offer critical insights into the molecular basis of the disease and open new research avenues leading to innovative and safe strategies to tackle the disease in the clinic.

Genetics has shown that mutations in functionally related genes (Presenilins (PSEN) and Amyloid Precursor Protein (APP)) cause Alzheimer’s disease (AD) with early onset. PSEN is the catalytic subunit of the γ-secretase intramembrane proteases, which sequentially cleave APP to generate Aβ peptides. Alzheimer’s disease-causing mutations consistently lead to production of longer amyloidogenic Aβ peptides and this points at the shift in Aβ length as fundamental to the disease pathogenic mechanism. The mutant-induced changes in Aβ profiles as well as the Aβ-mediated neurotoxicity mechanism are poorly defined. 

We are interested in generating a quantitative understanding of the molecular mechanisms underlying Alzheimer’s disease pathogenicity. Our research is based on the premise that getting a better mechanistic understanding of the function of the molecules involved in familial Alzheimer’s disease (FAD) will offer critical insights into the molecular basis of the disease and open new research avenues leading to innovative and safe strategies to tackle the disease in the clinic.