Prolyl isomerases in yeast.

@article{ArevaloRodriguez2004ProlylII,
  title={Prolyl isomerases in yeast.},
  author={Miguel Arévalo-Rodríguez and Xiaoyun Wu and Steven D. Hanes and Joseph Heitman},
  journal={Frontiers in bioscience : a journal and virtual library},
  year={2004},
  volume={9},
  pages={
          2420-46
        }
}
Prolyl isomerases are enzymes that catalyze cis-trans isomerization of peptidyl-prolyl bonds and span three structurally unrelated protein families: the cyclophilins, FKBPs, and parvulins. The genome of the budding yeast Saccharomyces cerevisiae encodes eight different cyclophilins (Cpr1 to Cpr8), four FKBPs (Fpr1 to Fpr4), and a single parvulin (Ess1). Remarkably, two of these proteins, cyclophilin A and FKBP12, are conserved from yeast to humans and mediate virtually all of the intracellular… 
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