Getting site-specific with actomyosin inhibitors

Laura K. Gunther, Christopher Yengo

Research output: Contribution to journalArticle

Abstract

Actin and myosin play important roles in many devastating diseases and thus are attractive targets for small-molecule therapy. In this issue of JBC, Guhathakurta et al. have developed a high-throughput screening assay to find small molecules that interfere with the actomyosin interaction. They utilized time-resolved FRET (TR-FRET) and a unique donor–acceptor pair (filamentous actin and a peptide that binds near the myosin-binding site on actin) to find novel molecules that interfere with the actomyosin ATPase and alter the structure of actin filaments. These findings demonstrate the power and potential of high-throughput TR-FRET in monitoring molecular interactions.

Original languageEnglish (US)
Pages (from-to)12299-12300
Number of pages2
JournalJournal of Biological Chemistry
Volume293
Issue number31
DOIs
StatePublished - Jan 1 2018

Fingerprint

Actomyosin
Myosins
Actins
High-Throughput Screening Assays
Molecules
Throughput
Actin Cytoskeleton
Molecular interactions
Binding Sites
Assays
Screening
Peptides
Monitoring
Therapeutics

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Gunther, Laura K. ; Yengo, Christopher. / Getting site-specific with actomyosin inhibitors. In: Journal of Biological Chemistry. 2018 ; Vol. 293, No. 31. pp. 12299-12300.
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Getting site-specific with actomyosin inhibitors. / Gunther, Laura K.; Yengo, Christopher.

In: Journal of Biological Chemistry, Vol. 293, No. 31, 01.01.2018, p. 12299-12300.

Research output: Contribution to journalArticle

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