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Characterization of a selective inhibitor of the parkinson's disease kinase lrrk2

Academic Article
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Overview

authors

  • Deng, X. M.
  • Dzamko, N.
  • Prescott, A.
  • Davies, P.
  • Liu, Q. S.
  • Yang, Q. K.
  • Lee, Jiing-Dwan
  • Patricelli, Matt
  • Nomanbhoy, T. K.
  • Alessi, D. R.
  • Gray, N. S.

publication date

  • April 2011

journal

  • Nature Chemical Biology  Journal

abstract

  • Mutations in leucine-rich repeat kinase 2 (LRRK2) are strongly associated with late-onset autosomal dominant Parkinson's disease. We employed a new, parallel, compound-centric approach to identify a potent and selective LRRK2 inhibitor, LRRK2-IN-1, and demonstrated that inhibition of LRRK2 induces dephosphorylation of Ser910 and Ser935 and accumulation of LRRK2 within aggregate structures. LRRK2-IN-1 will serve as a versatile tool to pharmacologically interrogate LRRK2 biology and study its role in Parkinson's disease.

subject areas

  • Benzodiazepinones
  • Dose-Response Relationship, Drug
  • Enzyme Activation
  • Enzyme Inhibitors
  • HEK293 Cells
  • Humans
  • Mutation
  • Parkinson Disease
  • Phosphorylation
  • Protein Serine-Threonine Kinases
  • Pyrimidines
  • Serine
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Identity

PubMed Central ID

  • PMC3287420

International Standard Serial Number (ISSN)

  • 1552-4450

Digital Object Identifier (DOI)

  • 10.1038/nchembio.538

PubMed ID

  • 21378983
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Additional Document Info

start page

  • 203

end page

  • 205

volume

  • 7

issue

  • 4

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