A Novel Fc-FGF21 With Improved Resistance to Proteolysis, Increased Affinity Toward β-Klotho, and Enhanced Efficacy in Mice and Cynomolgus Monkeys.

@article{Stanislaus2017ANF,
  title={A Novel Fc-FGF21 With Improved Resistance to Proteolysis, Increased Affinity Toward β-Klotho, and Enhanced Efficacy in Mice and Cynomolgus Monkeys.},
  author={Shanaka Stanislaus and Randy Hecht and Junming Yie and Todd Hager and Michael P. Hall and Christopher S Spahr and Wei Wang and Jennifer V Weiszmann and Yang Li and Liying Deng and Dwight Winters and S. E. Smith and Lei Zhou and Yuesheng Li and Murielle M V{\'e}niant and Jing Xu},
  journal={Endocrinology},
  year={2017},
  volume={158 5},
  pages={1314-1327}
}
Fibroblast growth factor (FGF) 21 is a natural hormone that modulates glucose, lipid, and energy metabolism. Previously, we engineered an Fc fusion FGF21 variant with two mutations, Fc-FGF21(RG), to extend the half-life and reduce aggregation and in vivo degradation of FGF21. We now describe a new variant developed to reduce the extreme C-terminal degradation and improve the binding affinity to β-Klotho. We demonstrate, by introducing one additional mutation located at the C terminus of FGF21… CONTINUE READING
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