Covalent modification of the interleukin-5 receptor by isothiazolones leads to inhibition of the binding of interleukin-5.

@article{Devos1994CovalentMO,
  title={Covalent modification of the interleukin-5 receptor by isothiazolones leads to inhibition of the binding of interleukin-5.},
  author={Rene Devos and Yves Guisez and Geert Plaetinck and Sigrid Cornelis and Jan Tavernier and Jos{\'e} van der Heyden and Louise H Foley and Julie E Scheffler},
  journal={European journal of biochemistry},
  year={1994},
  volume={225 2},
  pages={635-40}
}
Using a fusion protein of the human interleukin-5-receptor alpha chain (hIL5R alpha) and the human IgG C gamma 3 chain (hIL5R alpha-h gamma 3), we have developed a solid-phase assay for high-flux screening of a collection of synthetic compounds. We report on the identification of isothiazolone derivatives as potent inhibitors of binding of interleukin-5 (IL5) to the hIL5R alpha, as measured in a solid-phase assay (soluble hIL5R alpha or hIL5R alpha-h gamma 3) or on COS-1 cells expressing the… CONTINUE READING