% Bibliography for hypothesis h-8ffdaff434
% Title: CHIP-mediated ubiquitination selectively targets oligomeric pathologic conformers for proteasomal degradation
% Generated: 2026-06-08T13:29:16Z

@article{pmid35760815,
  title = {Hsp multichaperone complex buffers pathologically modified Tau.},
  journal = {Nat Commun},
  year = {2022},
  pmid = {35760815},
}

@article{pmid36195875,
  title = {Treadmill exercise promotes E3 ubiquitin ligase to remove amyloid β and P-tau and improve cognitive ability in APP/PS1 transgenic mice.},
  journal = {J Neuroinflammation},
  year = {2022},
  pmid = {36195875},
}

@article{pmid20478262,
  title = {Tau protein degradation is catalyzed by the ATP/ubiquitin-independent 20S proteasome under normal cell conditions.},
  journal = {Arch Biochem Biophys},
  year = {2010},
  pmid = {20478262},
}

@article{pmid14962978,
  title = {CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation.},
  journal = {Hum Mol Genet},
  year = {2004},
  pmid = {14962978},
}