Article
Fragments of HdhQ150 mutant huntingtin form a soluble oligomer pool that declines with aggregate deposition upon aging.
PloS one - 1 Jan 2012
Marcellin David, Abramowski Dorothee, Young Douglas, Richter Jens, Weiss Andreas, Marcel Audrey, Maassen Julia, Kauffmann Muriel, Bibel Miriam, Shimshek Derya R, Faull Richard L M, Bates Gillian P, Kuhn Rainer R, Van der Putten P Herman, Schmid Peter, Lotz Gregor P
Abstract excerpt
Cleavage of the full-length mutant huntingtin (mhtt) protein into smaller, soluble aggregation-prone mhtt fragments appears to be a key process in the neuropathophysiology of Huntington's Disease (HD). Recent quantification studies using TR-FRET-based immunoassays showed decreasing levels of soluble mhtt correlating with an increased load of aggregated mhtt in the aging HdhQ150 mouse brain. To better characterize...
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