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High-throughput screening for small molecule modulators of motor protein Kinesin

Academic Article
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Overview

authors

  • Kadakkuzha, B. M.
  • Spicer, Timothy
  • Chase, P.
  • Richman, J. B.
  • Hodder, Peter
  • Puthanveettil, Sathyanarayanan

publication date

  • October 2014

journal

  • Assay and Drug Development Technologies  Journal

abstract

  • The kinesin superfamily of motor proteins are involved in the active transport of a large number of cargos such as organelles, proteins, and RNAs from the neuronal cell body to distal neuronal processes. Previously, we have shown that kinesin-mediated axonal transport of proteins and RNAs are important for long-term memory storage. Identification of small molecules that can activate or inhibit kinesins is of specific interest due to the significance of kinesin-mediated functions in neuronal health and plasticity. Here, we describe a high-throughput screening assay designed to specifically identify compounds that inhibit or activate adenosine triphosphatase activity of the kinesin 5B of humans. The luminescence-based assay that we developed is highly reproducible and robust. Using this approach, we screened a pharmacologically characterized compound collection and have identified small molecules with either activator or inhibitor-like activity. To further characterize screening hits, we also developed an orthogonal assay based on absorbance and a counter screen assay based on luminescence. Development of such assays is important to help identify small molecules that can be used in potential drug development efforts targeted at modulating the function of kinesin.

subject areas

  • Adenosine Triphosphatases
  • Adenosine Triphosphate
  • Dose-Response Relationship, Drug
  • Enzyme-Linked Immunosorbent Assay
  • High-Throughput Screening Assays
  • Humans
  • Indicators and Reagents
  • Kinesin
  • Luminescence
  • Reproducibility of Results
  • Small Molecule Libraries
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Identity

International Standard Serial Number (ISSN)

  • 1540-658X

Digital Object Identifier (DOI)

  • 10.1089/adt.2014.579

PubMed ID

  • 25383721
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Additional Document Info

start page

  • 470

end page

  • 480

volume

  • 12

issue

  • 8

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