Heat shock protein 90 modulates LRRK2 stability: potential implications for Parkinson's disease treatment

J Neurosci. 2008 Jul 2;28(27):6757-9. doi: 10.1523/JNEUROSCI.1870-08.2008.
No abstract available

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Down-Regulation / drug effects
  • Down-Regulation / genetics
  • Enzyme Inhibitors / pharmacology
  • Enzyme Inhibitors / therapeutic use
  • HSP90 Heat-Shock Proteins / antagonists & inhibitors
  • HSP90 Heat-Shock Proteins / genetics
  • HSP90 Heat-Shock Proteins / metabolism*
  • Humans
  • Leucine-Rich Repeat Serine-Threonine Protein Kinase-2
  • Molecular Chaperones / antagonists & inhibitors
  • Molecular Chaperones / genetics
  • Molecular Chaperones / metabolism
  • Nerve Degeneration / drug therapy
  • Nerve Degeneration / genetics
  • Nerve Degeneration / metabolism*
  • Neurotoxins / antagonists & inhibitors
  • Neurotoxins / metabolism*
  • Parkinson Disease / genetics
  • Parkinson Disease / metabolism*
  • Parkinson Disease / physiopathology
  • Proteasome Endopeptidase Complex / genetics
  • Proteasome Endopeptidase Complex / metabolism
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism*

Substances

  • Enzyme Inhibitors
  • HSP90 Heat-Shock Proteins
  • Molecular Chaperones
  • Neurotoxins
  • LRRK2 protein, human
  • Leucine-Rich Repeat Serine-Threonine Protein Kinase-2
  • Protein Serine-Threonine Kinases
  • Proteasome Endopeptidase Complex