Research reveals atomic-level changes in ALS-linked protein

said braka 12:35 AM
The long-term goal of the research is to target

this  with a drug or other therapy to prevent these diseases, said the study's senior author, Nicolas Fawzi of Brown University. "There is currently no therapy or cure for ALS and . We are pursuing new hypotheses and angles to fight these illnesses."
Many proteins connected with these diseases contain "low-complexity" domains or pieces. Compared to a cell's best-understood proteins, which are ordered and static in structure, low-complexity domains are squirmy and disordered. Instead of a rigid shape, these pieces of  are flexible and float inside cells until cued into action.
In non-disease situations, low-complexity domains help proteins perform healthy functions, including assembling into liquid-like droplets, where important cellular processes, such as RNA processing, take place.
When low-complexity domains go awry, as in disease, they transform into inclusions, intractable and accumulating knots or clumps. In certain cancers, low-complexity domains are improperly attached to other proteins that may then incorrectly form droplets in cellular locations, leading to mis-regulated expression of genes, Fawzi said.
"We're trying to understand why they change behavior and aggregate, and how we can disrupt those processes," he said.
In the study, the researchers describe the microscopic physical interactions and chemical changes of proteins associated with several cellular functions, including disease forms, and how still-healthy cells could try to temper it.