All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae.

@article{Dolinski1997AllCA,
  title={All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae.},
  author={K J Dolinski and S. Muir and Maria Elena Cardenas and Joseph Heitman},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1997},
  volume={94 24},
  pages={13093-8}
}
The cyclophilins and FK506 binding proteins (FKBPs) bind to cyclosporin A, FK506, and rapamycin and mediate their immunosuppressive and toxic effects, but the physiological functions of these proteins are largely unknown. Cyclophilins and FKBPs are ubiquitous and highly conserved enzymes that catalyze peptidyl-prolyl isomerization, a rate-limiting step… CONTINUE READING