CHARACTERIZING PROTEIN STRUCTURES IN BETA-AMYLOID TREATED NEURONS WITH LIMITED PROTEOLYSIS-MASS SPECTROMETRY
Kuren Anderson-Steward, Ying Hao, Deyaan Guha, Ziyi Li, Benjamin Jin, Andrew Singleton, Andy Qi · 2024
Read CHARACTERIZING PROTEIN STRUCTURES IN BETA-AMYLOID TREATED NEURONS WITH LIMITED PROTEOLYSIS-MASS SPECTROMETRY by Kuren Anderson-Steward, Ying Hao, Deyaan Guha, Ziyi Li, Benjamin Jin, Andrew Singleton, Andy Qi (2024) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-11693127.txt.
Description
Kuren Anderson-Steward and co-authors chart protein shape changes in neurons dosed with beta-amyloid. Classic proteomics counts proteins but cannot see their shapes shift. A limited cutting method paired with mass reads fills that gap at scale. Stem-cell-derived neurons were treated with the amyloid tied to Alzheimer's disease.
The control group held 180 protein profiles the treated group lacked. Cutting sites from the enzyme differed widely between the two groups. Paths tied to neuron projections and cell compartments stood out in the data. Shape shifts, not just counts, mark the amyloid's hit on neurons. The work shows the paired method can catch such shifts across the whole proteome.
Catalog record
| CREATOR | Kuren Anderson-Steward, Ying Hao, Deyaan Guha, Ziyi Li, Benjamin Jin, Andrew Singleton, Andy Qi |
|---|---|
| YEAR | 2024 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 1 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |