@misc{Nuc_Katarzyna_Structure_2002,
 author={Nuc, Katarzyna and Słomski, Ryszard},
 volume={58},
 number={3},
 copyright={Creative Commons Attribution BY-SA 4.0 license},
 journal={Biotechnologia, vol.58, 3 (2002)-.},
 howpublished={online},
 year={2002},
 publisher={Committee on Biotechnology PAS},
 publisher={Institute of Bioorganic Chemistry PAS},
 language={pol},
 abstract={Cyclophilins (CyPs) constitute a large class of highly conserved, ubiquitousPPlases (EC 5.2.1.8) that together with FK560 binding proteins (FKBP) and parvulinsbelong to a superfamily of immunophilins. These three classes of proteins areeasily distinguishable by their selective interactions with immunosuppressivedrugs. Cyclophilins are targets for cyclosporin A (CsA), parvulins bind juglone(5-hydroxy-l.4-naphthoquinone) and FKBP, they are inhibited either by FK560drug or by rapamycin. Despite the lack of structural similarity, all these proteinshave been shown to act as peptidylprolyl cis-trans isomerases. In all cases, binding of the drug inhibits their PPIase activity. Distinct isoforms of cyclophilinshave been localized in the cytoplasm, nucleus, mitochondria, chloroplasts andendoplasmic reticulum.},
 type={Text},
 title={Structure and Function of Cyclophilins},
 URL={http://rcin.org.pl/Content/137917/PDF/POZN271_173026_biotechnologia-2002-no3-nuc.pdf},
 keywords={biotechnology},
}