I had my first job this summer working as a paid intern at the Buck Institute for Age Research, where I worked alongside scientists from Nobel-winning labs around the world studying Alzheimer's disease.
Within this large research project, are smaller individual projects. My project was to find out what interactions with other proteins and peptides the lower section of the protein APP (Amyloid Precurser Protein), segment AICD, has when it breaks off from the protein APP.
In neuronal cells, the protein APP (Amyloid Precurser Protein) spans across the membrane, inside and outside of the cell. The protein is cleaved (separated) at two location just outside of the cell. I was studying the protein on the inside* of the cell.
* For a long time scientists believed the cleavage of the other segment of the protein, along with the collection of Aβ in the brain, was connected to Alzheimers. Buck scientists proved that the outside protein was not associated with Alzheimer’s, by creating a line of mice with a genetic mutation at the cleavage location. These mice with the mutation preventing the cleavage of AICD have better memories than normal mice, whereas normal mice who have cleavage at AICD and also above the membrane to produce Aβ have significant
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