References
- Benneta, P. C., L. G. Singaretnamb, W.-Q. Zhao, A. Lawenb, and K. T. Ng. 1998. Peptidyl-prolyl-cisltrans-isomerase activity may be necessary for memory formation. FEBS Lett. 431: 386-390 https://doi.org/10.1016/S0014-5793(98)00795-9
- Colly, N. J., E. K. Baker, M. A. Stamnes, and C. S. Zuker. 1991. The cyclophilin homolog nina A is required in the secretory pathway. Cell 67: 255-263 https://doi.org/10.1016/0092-8674(91)90177-Z
- Dennis, E. B. 1968. The Biology of Euglena. Academic Press. Burlington. U.S.A
- Fisher, G. 1994. Peptidyl-prolyl cisltrans isomerases and their effectors. Angew. Chem. Int. Ed. Engl. 33: 1415-1436 https://doi.org/10.1002/anie.199414151
- Fischer, G., B. Wittmann-Lieborld, K. Lang, T. Kiefgaber, and F. K. Schmid. 1989. Cyclophilins and peptidyl-prolyl cisltrans isomerase are probably identical proteins. Nature 34: 953-955
- Fischer, G., H. Bang, E. Berger, and A. Schelenberger. 1984. Conformational specificity of chymotrypsin toward proline-containing substrates. Biochim. Biophys. Acta 791: 87-97 https://doi.org/10.1016/0167-4838(84)90285-1
- Fischer, G. and F. X. Schmid. 1990. The mechanism of protein folding: Implications of in vitro refolding models for de novo protein folding and translocation in the cell. Biochemistry 29: 2205-2216 https://doi.org/10.1021/bi00461a001
- Fischer, G., T. Tradler, and T. Zarnt. 1998. The mode of action of peptidyl proly cis/trans isomerases in vivo: Binding vs. catalysis. FEEs Lett. 429: 17-20 https://doi.org/10.1016/S0014-5793(98)00505-5
- Franziska, P. 2000. Three-step purification of a fragment of the large immunophilin. J. Chromatogr. 737: 71- 76 https://doi.org/10.1016/S0378-4347(99)00413-2
- Friedman, J. and I. Weissman. 1991. Two cytoplasmic candidates for immunophilin action are revealed by affinity for a new cyclophilin; One in the presence and one the absence of CsA. Cell 66: 799-806 https://doi.org/10.1016/0092-8674(91)90123-G
- Furutani, M., T. Iida, S. Yamano, K. Kamino, and T. Maruyama. 1998. Biochemical and genetic characterization of an FK506-sensitive peptydyl prolyl cis-trans isomerase from a Thermophilic archaeom, Methanococcus thermolithotrophicus. J. Bacteriol. 80: 388-394
- Galat, A. and S. M. Metcalfe. 1995. Peptidyl proline cis/trans isomerase. Prog. Biophys. Molec. Biol. 63: 67 -118 https://doi.org/10.1016/0079-6107(94)00009-X
- Harrison, R. K. and R. L. Stein. 1990. Substrate specificites of the peptidyl-prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: Evidence for the existence of a family of distinct enzymes. Biochemistry 29: 3813-3816 https://doi.org/10.1021/bi00468a001
- Iida, T., T. Iwabuchi, A. Ideno, S. Suzuki, and T. Maruyama. 2000. FK506-binding protein-type peptidyl-prolyl cis-trans isomerase from a halophilic archaeum, Halobacterium cutirubrum k. Gene 256: 319-326 https://doi.org/10.1016/S0378-1119(00)00378-4
- Jorg, H. and G. Fischer. 1993. Immunophi\ins: Structure-function relationship and possible role in microbial pathogencity. Molec. Microbiol. 10: 445-456 https://doi.org/10.1111/j.1365-2958.1993.tb00917.x
- Kim, S. J. and C. Lee. 1996. Kinetic studies of peptidyl-prolyl cis-trans isomerase from Porcine spleen. J. Biochem. Mol. 29: 519-524
- Kim, W. S., S. Davis, G. Wong, and A. L. Demain. 2003. Nutritional studies on the growth ofthe rapamycin-producing Streptomyces hygroscopicus. J. Microbiol. Biotechnol. 13: 560-563
- Kofron, J. L., P. Kuzmic, V. Kischore, B. E. Colon, and D. H. Rich. 1991. Determination of kinetic constants for peptidyl-prolyl cis-trans isomerases by an improved spectrophotometric assay. Biochemistry 30: 6127-6134 https://doi.org/10.1021/bi00239a007
- Lang, K., F. X. Schmid, and G. Fischer. 1987. Catalysis of protein folding by prolyl isomerase. Nature 329: 268-270 https://doi.org/10.1038/329268a0
- Lodish, H. F. and N. Kong. 1991. Cyclosporin A inhibits an initial step in folding of transferrin within the endoplasmic reticulum. J. Biol. Chem. 266: 14835-14838
- Masse, K., S. Bhamra, C. E. Haldin, and E. A. Jones. 2004. Cloning and characterisation of the immunophilin X-CypA. Gene Express. Patterns 5: 51-60 https://doi.org/10.1016/j.modgep.2004.06.007
- Moss, M. L., R. E. Palmer, B. E. Dunlap, W. Henzel, J. I. Kofron, W. S. Mellon, C. A. Rowyer, and D. H. Rich. 1992. Identification of actin and HSP 70 as cyclosporin A binding proteins by photoaffinity labeling and fluorescence displacement assays. J. Biol. Chem 267: 22054-22059
- Peterson, M. R., D. H. Hall, M. Berriman, J. A. Nunes, G. A. Leonard, A. H. Fairlamb, and W. N. Hunter. 2000. The three-dimensional structure of a Plasmodium falciparum cyclophilin in complex with the potent anti-malarial cyclosporin A. J. Mol. Biol. 298: 123-133 https://doi.org/10.1006/jmbi.2000.3633
- Philip, S. S. and A. V. Michael. 1996. Purification and characterization of cytosolic and microsomal cyclophilins from maize. Biochem. J. 315: 965-969 https://doi.org/10.1042/bj3150965
- Price, E. R., L. D. Zydowsky, M. Jin, C. M. Boker, F. D. Mckeon, and C. T. Walsh, 1991. Human cyclophilin B; A second cyclophilin gene encodes a peptidyl-prolyl isomerase with signal sequence. Proc. Natl. Acad. Sci. 88: 1903-1907
- Rahfeld, J. U., K. P. Rucknagel, G. Schelbert, B. Ludwig, J. Hacker, K. Mann, and G. Fisher. 1994. Confirmation of the existence of a third family among peptidyl-prolyl cis/trans isomerases: Amino acid sequence and recombinant production of parvulin. FEBS Lett. 352: 180-184 https://doi.org/10.1016/0014-5793(94)00932-5
- Rainer, Z., U. Keller, C. Lee, and K. Hoffman. 1992. A seventeen kilodaltons peptidyl-prolyl cis/trans isomerase of the cyclosporin-producer Tolpocladium inflatum is sensitive to cycloporin A. J. Antibiot. 45: 265-268 https://doi.org/10.7164/antibiotics.45.265
- Saul, F. A., J.-P. Arie, B. Vulliezle-Ie Normand, R. Kahn, J.-M. Betton, and G. A. Bentley. 2004. Structural and functional studies of Fkbp A from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. J. Mol. Biol. 335: 595-608 https://doi.org/10.1016/j.jmb.2003.10.056
- Schreiber, S. L. 1991. Chemistry and biology of the immunophilins and their immunosuppressive ligands. Science 251: 283-287 https://doi.org/10.1126/science.1702904
- Schreiber, S. L. and G. R. Crabtree. 1992. The machanism of action of cyclosporin A and FK506. lmmunol. Today 13: 136-142 https://doi.org/10.1016/0167-5699(92)90111-J
- Steinmann, B., P. Burckner, and A. Superti-Furga. 1991. Cyclosporin A slows collagen triple-helix formation in vivo: Indirect evidence for a physiologic role of peptidyl-prolyl cis-trans isomerase. J. Biol. Chem. 266: 1299-1303
- Such ira, B., M. Mattias, and B. F. Robert. 1994. The charactrization of a cyclophilin-type peptidyl-prolyl cis-trans isomerase from the endoplasmic-reticulum lumen. Biochem. J. 300: 871-875 https://doi.org/10.1042/bj3000871
- Tropschug, M., I. B. Barthelmess, and W. Neupert. 1989. Sensitivity to cyclosporin A is mediated by cyclophilin in Neurospora crassa and Saccharomyces cerevisiae. Nature 342: 953-955 https://doi.org/10.1038/342953a0
- Walsh, C. T, L. D. Zydowsky, and F. D. Mckeon. 1992. Cyclosporin A, the cyclophilin class of peptidyl-prolyl isomerases and blockade of T cell signal transduction. J. Biol. Chem. 267: 13115-13118