SEARCH

SEARCH BY CITATION

References

  • Altschuh, D., Vix, O., Rees, B., & Thierry, J.-C. (1992). A conformation of cyclosporin A in aqueous environment revealed by the X-ray structure of cyclosporin-Fab complex. Science 256, 9294.
  • Bierer, B., Schreiber, S.L., & Burakoff, S.J. (1991). The effect of the immunosuppressant FK-506 on alternate pathways of T cell activation. Eur. J. Immunol. 21, 439445.
  • Blumenthal, D.K., Takio, K., Hansen, R.S., & Krebs, E.G. (1986). Dephosphorylation of cAMP-dependent protein kinase regulatory subunit (type II) by calmodulin-dependent protein phosphatase. J. Biol. Chem. 261, 81408145.
  • Emmel, E.A., Verweij, C.L., Durand, D.B., Higgins, K.M., Lacy, E., & Crabtree, G.R. (1989). Cyclosporin A specifically inhibits function of nuclear proteins involved in T cell activation. Science 246, 16171620.
  • Fesik, S.W., Gampe, R.T. Jr., Eaton, H.L., Gemmecker, G., Olejniczak, E.T., Neri, P., Holzman, T.F., Egan, D.A., Edalji, R., Simmer, R., Helfrich, R., Hochlowski, J., & Jackson, M. (1991). NMR studies of [U-13C]cyclosporin A bound to cyclophilin: Bound conformation and portions of cyclosporin involved in binding. Biochemistry 30, 65746583.
  • Fischer, G., Wittmann-Liebold, B., Lang, K., Kiefhaber, T., & Schmid, F.X. (1989). Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature 337, 476478.
  • Flanagan, W.M., Corthésy, B., Bram, R.J., & Crabtree, G.R. (1991). Nuclear association of a T-cell transcription factor blocked by FK-506 and cyclosporin A. Nature 352, 803807.
  • Friedman, J. & Weissman, I. (1991). Two cytoplasmic candidates for immunophilin action are revealed by affinity for a new cyclophilin: One in the presence and one in the absence of CsA. Cell 66, 799806.
  • Handschumacher, R.E., Harding, M.W., Rice, J., & Drugge, R.J. (1984). Cyclophilin: A specific cytosolic binding protein for cyclosporin A. Science 226, 544547.
  • Harding, M.W., Galat, A., Uehling, D.E., & Schreiber, S.L. (1989). A receptor for the immunosuppressant FK506 is a cis-trans peptidylprolyl isomerase. Nature 341, 758760.
  • Harrison, R.K., Caldwell, C.G., Rosegay, A., Melillo, D., & Stein, R.L. (1990). Confirmation of the secondary deuterium isotope effect for the peptidyl prolyl cis-trans isomerase activity of cyclophilin by a competitive, double-label technique. J. Am. Chem. Soc. 112, 70637064.
  • Harrison, R.K. & Stein, R.L. (1990). Mechanistic studies of peptidyl prolyl cis-trans isomerase: Evidence for catalysis by distortion. Biochemistry 29, 16841689.
  • Hayano, T., Takahashi, N., Kato, S., Maki, N., & Suzuki, M. (1991). Two distinct forms of peptidyl-prolyl-cis-trans-isomerase are expressed separately in periplasmic and cytoplasmic compartments of Escherichia coli cells. Biochemistry 30, 30413048.
  • Kallen, J., Spitzfaden, C., Zurini, M.G.M., Wider, G., Widmer, H., Wüthrich, K., & Walkinshaw, M.D. (1991). Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy. Nature 353, 276279.
  • Kallen, J., Spitzfaden, C., Zurini, M.G.M., Wider, H., Wüthrich, K., & Walkinshaw, M.D. (1992). Catalysis steps. Nature 356, 24.
  • Ke, H., Zydowsky, L.D., Liu, J., & Walsh, C.T. (1991). Crystal structure of recombinant human T-cell cyclophilin A at 2.5 Å resolution. Proc. Natl. Acad. Sci. USA 88, 94839487.
  • Kessler, H., Köck, M., Wein, T., & Gehrke, M. (1990). Reinvestigation of the conformation of cyclosporin A in chloroform. Helv. Chim. Acta 73, 18181832.
  • Kofron, J.L., Kuzmič, P., Kishore, V., Colon-Bonilla, E., & Rich, D.H. (1991). Determination of kinetic constants for peptidyl-prolyl cis-trans isomerases by an improved spectrophotometric assay. Biochemistry 30, 61276134.
  • Kofron, J.L., Kuzmič, P., Kishore, V., Gemmecker, G., Fesik, S.W., & Rich, D.H. (1992). Lithium chloride perturbation of cis-trans peptide bond equilibria: Effect on conformational equilibria in cyclosporin A and on time-dependent inhibition of cyclophilin. J. Am. Chem. Soc. 114, 26702675.
  • Kunkel, T.A. (1985). Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82, 488492.
  • Liu, J., Albers, M.W., Chen, C.-M., Schreiber, S.L., & Walsh, C.T. (1990). Cloning, expression, and purification of human cyclophilin in Escherichia coli and assessment of the catalytic role of cysteines by site-directed mutagenesis. Proc. Natl. Acad. Sci. USA 87, 23042308.
  • Liu, J., Chen, C.-M., & Walsh, C.T. (1991a). Human and Escherichia coli cyclophilins: Sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue. Biochemistry 30, 23062310.
  • Liu, J., Farmer, J.D. Jr., Lane, W.S., Friedman, J., Weissman, I., & Schreiber, S.L. (1991b). Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 66, 807815.
  • Liu, J. & Walsh, C.T. (1990). Peptidyl-prolyl cis-trans, isomerase from Escherichia coli: A periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A. Proc. Natl. Acad. Sci. USA 87, 40284032.
  • Neri, P., Meadows, R., Gemmecker, G., Olejniczak, E., Nettesheim, D., Logan, T., Simmer, R., Helfrich, R., Holzman, T., Severin, J., & Fesik, S. (1991). 1H, 13C and 15N backbone assignments of cyclophilin when bound to cyclosporin A (CsA) and preliminary structural characterization of the CsA binding site. FEBS Lett. 294, 8188.
  • Park, S.T., Aldape, R.A., Futer, O., DeCenzo, M.T., & Livingston, D.J. (1992). PPIase catalysis by human FK506-binding protein proceeds through a conformational twist mechanism. J. Biol. Chem. 267, 33163324.
  • Schonbrunner, E.R., Mayer, S., Tropschug, M., Fischer, G., Takahashi, N., & Schmid, F.X. (1991). Catalysis of protein folding by cyclophilins from different species. J. Biol. Chem. 266, 36303635.
  • Siekierka, J.J., Hung, S.H.Y., Poe, M., Lin, C.S., & Sigal, N.H. (1989). A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin. Nature 341, 755757.
  • Stein, R.L. (1992). Catalysis steps. Nature 356, 2324.
  • Swanson, S.K.-H., Born, T., Zydowsky, L.D., Cho, H., Chang, H.Y., Walsh, C.T., & Rusnak, F. (1992). Cyclosporin-mediated inhibition of bovine calcineurin by cyclophilin A and B. Proc. Natl. Acad. Sci. USA 89, 37413745.
  • Takahashi, N., Hayano, T., & Suzuki, M. (1989). Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin. Nature 337, 473475.
  • Tanaka, H., Kuroda, A., Marusawa, H.H., Hatanaka, H., Kino, T., Goto, T., Hashimoto, M., & Taga, T. (1987). Structure of FK506: A novel immunosuppressant isolated from Streptomyces. J. Am. Chem. Soc. 109, 50315033.
  • Tropschug, M., Barthelmess, I.B., & Neupert, W. (1989). Sensitivity to cyclosporin A is mediated by cyclophilin in Neurospora crassa and Saccharomyces cerevisiae. Nature 342, 953955.
  • Van Duyne, G.D., Standaert, R.F., Karplus, P.A., Schreiber, S.L., & Clardy, J. (1991). Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex. Science 252, 839842.
  • Weber, C., Wider, G., von Freyberg, B., Traber, R., Braun, W., Widmer, H., & Wüthrich, K. (1991). The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution. Biochemistry 30, 65636574.
  • Williams, J.W. & Morrison, J.F. (1979). The kinetics of reversible tight-binding inhibition. Methods Enzymol. 63, 437450.