Abstract
Neurodegenerative diseases severely affect millions of people around the world and are responsible for detrimental symptoms like dementia. Alzheimer's and Parkinson's diseases are the most common neurodegenerative diseases and both share a common leading cause - aggregation or misfolding of specific proteins. Therapeutic protein disaggregases like bacterial ClpB and yeast Hsp104 can couple energy from ATP binding and hydrolysis to drive mechanical work, such as unfolding protein aggregates or misfolded proteins. Unfortunately, little is known about how ClpB and Hsp104 carry out their disaggregase function.
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