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Identification of the immunophilins capable of mediating inhibition of signal transduction by cyclosporin A and FK506: roles of calcineurin binding and cellular location.

Bram RJ, Hung DT, Martin PK, Schreiber SL, Crabtree GR. Identification of the immunophilins capable of mediating inhibition of signal transduction by cyclosporin A and FK506: roles of calcineurin binding and cellular location. Mol Cell Biol. 1993;13(8):4760-9.

Effects of cyclosporin A and FK506 on Fc epsilon receptor type I-initiated increases in cytokine mRNA in mouse bone marrow-derived progenitor mast cells: resistance to FK506 is associated with a deficiency in FK506-binding protein FKBP12.

Kaye RE, Fruman DA, Bierer BE, et al. Effects of cyclosporin A and FK506 on Fc epsilon receptor type I-initiated increases in cytokine mRNA in mouse bone marrow-derived progenitor mast cells: resistance to FK506 is associated with a deficiency in FK506-binding protein FKBP12. Proc Natl Acad Sci U S A. 1992;89(18):8542-6.

Protein phosphatase 2A interacts with the 70-kDa S6 kinase and is activated by inhibition of FKBP12-rapamycinassociated protein.

Peterson RT, Desai BN, Hardwick JS, Schreiber SL. Protein phosphatase 2A interacts with the 70-kDa S6 kinase and is activated by inhibition of FKBP12-rapamycinassociated protein. Proc Natl Acad Sci U S A. 1999;96(8):4438-42.

Alpha 4 associates with protein phosphatases 2A, 4, and 6.

Chen J, Peterson RT, Schreiber SL. Alpha 4 associates with protein phosphatases 2A, 4, and 6. Biochem Biophys Res Commun. 1998;247(3):827-32. doi:10.1006/bbrc.1998.8792

Immunophilin-sensitive protein phosphatase action in cell signaling pathways.

Schreiber SL. Immunophilin-sensitive protein phosphatase action in cell signaling pathways. Cell. 1992;70(3):365-8.

pCyP B: a chloroplast-localized, heat shock-responsive cyclophilin from fava bean.

Luan S, Lane WS, Schreiber SL. pCyP B: a chloroplast-localized, heat shock-responsive cyclophilin from fava bean. Plant Cell. 1994;6(6):885-92. doi:10.1105/tpc.6.6.885

Structure-based design of a cyclophilin-calcineurin bridging ligand.

Alberg DG, Schreiber SL. Structure-based design of a cyclophilin-calcineurin bridging ligand. Science. 1993;262(5131):248-50.

Immunosuppressants implicate protein phosphatase regulation of K+ channels in guard cells.

Luan S, Li W, Rusnak F, Assmann SM, Schreiber SL. Immunosuppressants implicate protein phosphatase regulation of K+ channels in guard cells. Proc Natl Acad Sci U S A. 1993;90(6):2202-6.

Inhibition of T cell signaling by immunophilin-ligand complexes correlates with loss of calcineurin phosphatase activity.

Liu J, Albers MW, Wandless TJ, et al. Inhibition of T cell signaling by immunophilin-ligand complexes correlates with loss of calcineurin phosphatase activity. Biochemistry. 1992;31(16):3896-901.

Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes.

Liu J, Farmer JD, Lane WS, Friedman J, Weissman I, Schreiber SL. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell. 1991;66(4):807-15.