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Volumn 76, Issue 3, 1996, Pages 631-649

Cellular functions of immunophilins

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CALCINEURIN; CYCLOPHILIN; IMMUNOPHILIN; ISOMERASE; RYANODINE RECEPTOR; TACROLIMUS; TRANSFORMING GROWTH FACTOR BETA RECEPTOR;

EID: 0029816659     PISSN: 00319333     EISSN: None     Source Type: Journal    
DOI: 10.1152/physrev.1996.76.3.631     Document Type: Review
Times cited : (341)

References (159)
  • 1
    • 0027978751 scopus 로고
    • Single channel activity of the ryanodine receptor calcium release channel is modulated by FK-506
    • AHERN, G. P., P. R. JUNANKAR, AND A. F. DULHUNTY. Single channel activity of the ryanodine receptor calcium release channel is modulated by FK-506. FEBS Lett. 352: 369-374, 1994.
    • (1994) FEBS Lett. , vol.352 , pp. 369-374
    • Ahern, G.P.1    Junankar, P.R.2    Dulhunty, A.F.3
  • 2
    • 0027370186 scopus 로고
    • FKBP-rapamycin inhibits a cyclin-dependent kinase activity and a cyclin D1-Cdk association in early G1 of an osteosarcoma cell
    • ALBERS, M., R. WILLIAMS, E. BROWN, A. TANAKA, F. HALL, AND S. SCHREIBER. FKBP-rapamycin inhibits a cyclin-dependent kinase activity and a cyclin D1-Cdk association in early G1 of an osteosarcoma cell. J. Biol. Chem. 268: 22825-22829, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22825-22829
    • Albers, M.1    Williams, R.2    Brown, E.3    Tanaka, A.4    Hall, F.5    Schreiber, S.6
  • 3
    • 0025035782 scopus 로고
    • Substrate specificity of the human rotamase FKBP: A view of FK506 and rapamycin as leucine-(twisted amide)-proline mimics
    • ALBERS, M. W., C. T. WALSH, AND S. L. SCHREIBER. Substrate specificity of the human rotamase FKBP: a view of FK506 and rapamycin as leucine-(twisted amide)-proline mimics. J. Org. Chem. 55: 4984-4986, 1990.
    • (1990) J. Org. Chem. , vol.55 , pp. 4984-4986
    • Albers, M.W.1    Walsh, C.T.2    Schreiber, S.L.3
  • 5
    • 0026527418 scopus 로고
    • s-Cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin
    • ARBER, S., K.-H. KRAUSE, AND P. CARONI. s-Cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin. J. Cell Biol. 116: 113-125, 1992.
    • (1992) J. Cell Biol. , vol.116 , pp. 113-125
    • Arber, S.1    Krause, K.-H.2    Caroni, P.3
  • 10
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • BERRIDGE, M. J. Inositol trisphosphate and calcium signalling. Nature Lond. 361: 315-325, 1993.
    • (1993) Nature Lond. , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 11
    • 0027231287 scopus 로고
    • Ratio of ryanodine to dihydropyridine receptors in cardiac and skeletal muscle and implications for E-C coupling
    • Cell Physiol. 33
    • BERS, D. M., AND V. M. STIFFEL. Ratio of ryanodine to dihydropyridine receptors in cardiac and skeletal muscle and implications for E-C coupling. Am. J. Physiol. 264 (Cell Physiol. 33): C1587-C1593, 1993.
    • (1993) Am. J. Physiol. , vol.264
    • Bers, D.M.1    Stiffel, V.M.2
  • 12
    • 0026432666 scopus 로고
    • 3- and calcium-gated channels from endoplasmic reticulum of cerebellum
    • 3- and calcium-gated channels from endoplasmic reticulum of cerebellum. Nature Lond. 351: 751-754, 1991.
    • (1991) Nature Lond. , vol.351 , pp. 751-754
    • Bezprozvanny, I.1    Watras, J.2    Ehrlich, B.3
  • 14
    • 0008755365 scopus 로고
    • Advances in therapeutic immunosuppression: Biological, molecular actions, and clinical implications
    • BIERER, B. E. Advances in therapeutic immunosuppression: biological, molecular actions, and clinical implications. Curr. Opin. Hematol. 1: 149-159, 1993.
    • (1993) Curr. Opin. Hematol. , vol.1 , pp. 149-159
    • Bierer, B.E.1
  • 15
    • 0025647885 scopus 로고
    • Two distinct signal transmission pathways in T lymphocytes are inhibited by complexes formed between an immunophilin and either FK506 or rapamycin
    • BIERER, B. E., P. S. MATTILIA, R. STANDAERT, L. HERZENBERG, S. BURAKOFF, G. CRABTREE, AND S. SCHREIBER. Two distinct signal transmission pathways in T lymphocytes are inhibited by complexes formed between an immunophilin and either FK506 or rapamycin. Proc. Natl. Acad. Sci. USA 87: 9231-9235, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9231-9235
    • Bierer, B.E.1    Mattilia, P.S.2    Standaert, R.3    Herzenberg, L.4    Burakoff, S.5    Crabtree, G.6    Schreiber, S.7
  • 16
    • 0024245148 scopus 로고
    • Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle
    • BLOCK, B. A., T. IMAGAWA, K. P. CAMPBELL, AND C. FRANZINI-ARMSTRONG. Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle. J. Cell Biol. 107: 2587-2600, 1988.
    • (1988) J. Cell Biol. , vol.107 , pp. 2587-2600
    • Block, B.A.1    Imagawa, T.2    Campbell, K.P.3    Franzini-Armstrong, C.4
  • 17
    • 0027318996 scopus 로고
    • Sequence and functional characterization of a third inositol trisphosphate receptor subtype, IP3R-3, expressed in pancreatic islets, kidney, gastrointestinal tract, and other tissues
    • BLONDEL, O., J. TAKEDA, H. JANSSEN, S. SEINO, AND G. BELL. Sequence and functional characterization of a third inositol trisphosphate receptor subtype, IP3R-3, expressed in pancreatic islets, kidney, gastrointestinal tract, and other tissues. J. Biol. Chem. 268: 11356-11363, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11356-11363
    • Blondel, O.1    Takeda, J.2    Janssen, H.3    Seino, S.4    Bell, G.5
  • 18
    • 0027323876 scopus 로고
    • Identification of the immunophilin capable of mediating inhibition of signal transduction by cyclosporin A and FK506: Roles of calcineurin and cellular location
    • BRAM, R. J., D. T. HUNG, P. K. MARTIN, S. L. SCHREIBER, AND G. R. CRABTREE. Identification of the immunophilin capable of mediating inhibition of signal transduction by cyclosporin A and FK506: roles of calcineurin and cellular location. Mol. Cell. Biol. 13: 4760-4769, 1993.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4760-4769
    • Bram, R.J.1    Hung, D.T.2    Martin, P.K.3    Schreiber, S.L.4    Crabtree, G.R.5
  • 19
    • 0027968586 scopus 로고
    • Developmental and tissue-specific regulation of expression of the cardiac and skeletal muscle calcium channels involved in excitation-contraction coupling
    • BRILLANTES, A.-M. B., S. BREZPROZVANNAYA, AND A. MARKS. Developmental and tissue-specific regulation of expression of the cardiac and skeletal muscle calcium channels involved in excitation-contraction coupling. Circ. Res. 75: 503-510, 1994.
    • (1994) Circ. Res. , vol.75 , pp. 503-510
    • Brillantes, A.-M.B.1    Brezprozvannaya, S.2    Marks, A.3
  • 26
    • 0028043643 scopus 로고
    • Activation of 70-kDa S6 kinase, induced by the cytokines interleukin-3 and erythropoietin and inhibited by rapamycin, is not an absolute requirement for cell proliferation
    • CALVO, V., M. WOOD, C. GJERTSON, T. VIK, AND B. E. BIERER, Activation of 70-kDa S6 kinase, induced by the cytokines interleukin-3 and erythropoietin and inhibited by rapamycin, is not an absolute requirement for cell proliferation. Eur. J. Immunol. 24: 2664-2671, 1994.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 2664-2671
    • Calvo, V.1    Wood, M.2    Gjertson, C.3    Vik, T.4    Bierer, B.E.5
  • 27
    • 0028843879 scopus 로고
    • Calcineurin associated with the inositol 1,4,5,-trisphosphate receptor-FKBP12 complex modulates calcium influx
    • CAMERON, A., J. P. STEINER, A. J. ROSKAMS, S. M. ALI, AND S. H. SNYDER. Calcineurin associated with the inositol 1,4,5,-trisphosphate receptor-FKBP12 complex modulates calcium influx. Cell 83: 463-472, 1995.
    • (1995) Cell , vol.83 , pp. 463-472
    • Cameron, A.1    Steiner, J.P.2    Roskams, A.J.3    Ali, S.M.4    Snyder, S.H.5
  • 28
    • 0028918776 scopus 로고
    • Immunophilin FK506 binding protein associated with inositol 1,4,5-trisphosphate receptor modulates calcium influx
    • CAMERON, A. M., J. P. STEINER, D. M. SABATINI, A. I. KAPLIN, L. D. WALENSKY, AND S. H. SNYDER. Immunophilin FK506 binding protein associated with inositol 1,4,5-trisphosphate receptor modulates calcium influx. Proc. Natl. Acad. Sci. USA 92: 1784-1788, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1784-1788
    • Cameron, A.M.1    Steiner, J.P.2    Sabatini, D.M.3    Kaplin, A.I.4    Walensky, L.D.5    Snyder, S.H.6
  • 29
    • 0028597938 scopus 로고
    • Immunophilins interact with calcineurin in the absence of exogenous immunosuppressive ligands
    • CARDENAS, M. E., C. HEMENWAY, R. S. MUIR, R. YE, D. FIORENTINO, AND J. HEITMAN. Immunophilins interact with calcineurin in the absence of exogenous immunosuppressive ligands. EMBO J. 13: 5944-5957, 1995.
    • (1995) EMBO J. , vol.13 , pp. 5944-5957
    • Cardenas, M.E.1    Hemenway, C.2    Muir, R.S.3    Ye, R.4    Fiorentino, D.5    Heitman, J.6
  • 30
    • 0026093412 scopus 로고
    • Excitation-contraction coupling in vertebrate skeletal muscle: A tale of two calcium channels
    • CATTERALL, W. A. Excitation-contraction coupling in vertebrate skeletal muscle: a tale of two calcium channels. Cell 64: 871-874, 1991.
    • (1991) Cell , vol.64 , pp. 871-874
    • Catterall, W.A.1
  • 31
    • 0025246299 scopus 로고
    • Isolation and characterization of the inositol trisphosphate receptor from smooth muscle
    • CHADWICK, C. C., A. SAITO, AND S. FLEISCHER. Isolation and characterization of the inositol trisphosphate receptor from smooth muscle. Proc. Natl. Acad. Sci. USA 87: 2132-2136, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2132-2136
    • Chadwick, C.C.1    Saito, A.2    Fleischer, S.3
  • 32
  • 33
    • 0025301950 scopus 로고
    • Ryanodine as a probe for the functional state of the skeletal muscle sarcoplasmic reticulum calcium release channel
    • CHU, A., M. DIAZ-MUNOZ, M. HAWKES, K. BRUSH, AND S. HAMILTON. Ryanodine as a probe for the functional state of the skeletal muscle sarcoplasmic reticulum calcium release channel. Mol. Pharmacol. 37: 735-741, 1990.
    • (1990) Mol. Pharmacol. , vol.37 , pp. 735-741
    • Chu, A.1    Diaz-Munoz, M.2    Hawkes, M.3    Brush, K.4    Hamilton, S.5
  • 34
    • 0026659046 scopus 로고
    • Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling the 70 kd S6 protein kinases
    • CHUNG, J., C. J. KUO, G. R. CRABTREE, AND J. BLENIS. Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling the 70 kd S6 protein kinases. Cell 69: 1227-1236, 1992.
    • (1992) Cell , vol.69 , pp. 1227-1236
    • Chung, J.1    Kuo, C.J.2    Crabtree, G.R.3    Blenis, J.4
  • 35
    • 0026667614 scopus 로고
    • Planar bilayer recording of ryanodine receptors of sarcoplasmic reticulum
    • CORONADO, R., S. KAWANO, C. LEE, C. VALDIVIA, AND H. VALDIVIA. Planar bilayer recording of ryanodine receptors of sarcoplasmic reticulum. Methods Enzymol. 207: 699-707, 1992.
    • (1992) Methods Enzymol. , vol.207 , pp. 699-707
    • Coronado, R.1    Kawano, S.2    Lee, C.3    Valdivia, C.4    Valdivia, H.5
  • 36
    • 0025857174 scopus 로고
    • Inositol 1,4,5-trisphosphate receptors: Distinct neuronal and nonneuronal forms derived by alternative splicing differ in phosphorylation
    • DANOFF, S., C. FERRIS, C. DONATH, G. FISCHER, S. MUNEMITSU, A. ULLRICH, S. SNYDER, AND C. ROSS. Inositol 1,4,5-trisphosphate receptors: distinct neuronal and nonneuronal forms derived by alternative splicing differ in phosphorylation. Proc. Natl. Acad. Sci. USA 88: 2951-2955, 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2951-2955
    • Danoff, S.1    Ferris, C.2    Donath, C.3    Fischer, G.4    Munemitsu, S.5    Ullrich, A.6    Snyder, S.7    Ross, C.8
  • 37
  • 38
    • 0028210361 scopus 로고
    • Relationship between multiple biologic effects of rapamycin and the inhibition of pp70S6 protein kinase activity
    • DUMONT, F. J., A. ALTMEYER, C. KASTNER, P. A. FISCHER, K. P. LEMIN, J. CHUNG, J. BLENIS, AND M. J. STARUCH. Relationship between multiple biologic effects of rapamycin and the inhibition of pp70S6 protein kinase activity. J. Immunol. 152: 992-1003, 1994.
    • (1994) J. Immunol. , vol.152 , pp. 992-1003
    • Dumont, F.J.1    Altmeyer, A.2    Kastner, C.3    Fischer, P.A.4    Lemin, K.P.5    Chung, J.6    Blenis, J.7    Staruch, M.J.8
  • 39
    • 0025099697 scopus 로고
    • Distinct mechanisms of suppression of murine T-cell activation by the related macrolides FK-506 and rapamycin
    • DUMONT, F. J., M. J. STARUCH, S. L. KOOPRAK, M. R. MELINO, AND N. H. SIGAL. Distinct mechanisms of suppression of murine T-cell activation by the related macrolides FK-506 and rapamycin. J. Immun. 144: 251-258, 1990.
    • (1990) J. Immun. , vol.144 , pp. 251-258
    • Dumont, F.J.1    Staruch, M.J.2    Kooprak, S.L.3    Melino, M.R.4    Sigal, N.H.5
  • 40
    • 0024432233 scopus 로고
    • Purified inositol 1,4,5-trisphosphate receptor mediates calcium flux in reconstituted lipid vesicles
    • FERRIS, C. D., R. L. HUGANIR, S. SUPATTAPONE, AND S. H. SNYDER. Purified inositol 1,4,5-trisphosphate receptor mediates calcium flux in reconstituted lipid vesicles. Nature Lond. 342: 87-89, 1989.
    • (1989) Nature Lond. , vol.342 , pp. 87-89
    • Ferris, C.D.1    Huganir, R.L.2    Supattapone, S.3    Snyder, S.H.4
  • 41
    • 0024959449 scopus 로고
    • Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
    • FISCHER, G., B. WITTMAN-LIEBOLD, K. LANG, T. KIEFHABER, AND F. X. SCHMID. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature Lond. 337: 476-478, 1989.
    • (1989) Nature Lond. , vol.337 , pp. 476-478
    • Fischer, G.1    Wittman-Liebold, B.2    Lang, K.3    Kiefhaber, T.4    Schmid, F.X.5
  • 42
    • 0027742843 scopus 로고
    • A mechanism for rotamase catalysis by the FK506 binding protein (FKBP)
    • FISCHER, S., S. MICHNICK, AND M. KARPLUS. A mechanism for rotamase catalysis by the FK506 binding protein (FKBP). Biochemistry 32: 13830-13837, 1993.
    • (1993) Biochemistry , vol.32 , pp. 13830-13837
    • Fischer, S.1    Michnick, S.2    Karplus, M.3
  • 43
    • 0025871394 scopus 로고
    • Nuclear association of a T-cell transcription factor blocked by FK-506 and cyclosporin A
    • FLANAGAN, W., B. CORTHESY, R. BRAM, AND G. CRABTREE. Nuclear association of a T-cell transcription factor blocked by FK-506 and cyclosporin A. Nature Lond. 352: 803-807, 1991.
    • (1991) Nature Lond. , vol.352 , pp. 803-807
    • Flanagan, W.1    Corthesy, B.2    Bram, R.3    Crabtree, G.4
  • 44
    • 0024534815 scopus 로고
    • Biochemistry and biophysics of excitation-contraction coupling
    • FLEISCHER, S., AND M. INUI. Biochemistry and biophysics of excitation-contraction coupling. Annu. Rev. Biophys. Biophys. Chem. 18: 333-364, 1989.
    • (1989) Annu. Rev. Biophys. Biophys. Chem. , vol.18 , pp. 333-364
    • Fleischer, S.1    Inui, M.2
  • 45
    • 0027940713 scopus 로고
    • Specific incorporation of cyclophilin A into HIV-1 virions
    • FRANKE, E. K., H. E. YUAN, AND J. LUBAN. Specific incorporation of cyclophilin A into HIV-1 virions [see comments]. Nature Lond. 372: 359-362, 1994.
    • (1994) Nature Lond. , vol.372 , pp. 359-362
    • Franke, E.K.1    Yuan, H.E.2    Luban, J.3
  • 46
    • 0020578983 scopus 로고
    • Junctional feet and membrane particles in the triad of a fast twitch muscle fiber
    • FRANZINI-ARMSTRONG, C., AND G. NUNZI. Junctional feet and membrane particles in the triad of a fast twitch muscle fiber. J. Muscle Res. Cell. Motil. 4: 233-252, 1983.
    • (1983) J. Muscle Res. Cell. Motil. , vol.4 , pp. 233-252
    • Franzini-Armstrong, C.1    Nunzi, G.2
  • 47
    • 0026499641 scopus 로고
    • Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase
    • FRESKGARD, P.-O., N. BERGENHEM, B.-H. JONSSON, M. SVENSSON, AND U. CARLSSON. Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase. Science Wash. DC 258: 466-468, 1992.
    • (1992) Science Wash. DC , vol.258 , pp. 466-468
    • Freskgard, P.-O.1    Bergenhem, N.2    Jonsson, B.-H.3    Svensson, M.4    Carlsson, U.5
  • 48
    • 0027210009 scopus 로고
    • Cloning and characterization of a cyclophilin C-associated protein: A candidate natural cellular ligand for cyclophilin C
    • FRIEDMAN, J., M. TRAHEY, AND I. WEISSMAN. Cloning and characterization of a cyclophilin C-associated protein: a candidate natural cellular ligand for cyclophilin C. Proc. Natl. Acad. Sci. USA 90: 6815-6819, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6815-6819
    • Friedman, J.1    Trahey, M.2    Weissman, I.3
  • 49
    • 0025831980 scopus 로고
    • Two cytoplasmic candidates for immunophilin action are revealed by affinity for a new cyclophilin: One in the presence and one the absence of CsA
    • FRIEDMAN, J., AND I. WEISSMAN. 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, 1991.
    • (1991) Cell , vol.66 , pp. 799-806
    • Friedman, J.1    Weissman, I.2
  • 50
    • 0028813436 scopus 로고
    • The complex of FK506-binding protein 12 and FK506 inhibits calcineurin phosphatase activity and IgE activation-induced cytokine transcripts, but not exocytosis, in mouse mast cells
    • FRUMAN, D. A., B. E. BIERER, J. E. BENES, S. J. BURAKOFF, K. F. AUSTEN, AND H. R. KATZ. The complex of FK506-binding protein 12 and FK506 inhibits calcineurin phosphatase activity and IgE activation-induced cytokine transcripts, but not exocytosis, in mouse mast cells. J. Immunol. 154: 1846-1851, 1995.
    • (1995) J. Immunol. , vol.154 , pp. 1846-1851
    • Fruman, D.A.1    Bierer, B.E.2    Benes, J.E.3    Burakoff, S.J.4    Austen, K.F.5    Katz, H.R.6
  • 51
    • 0028276439 scopus 로고
    • Immunophilins in protein folding and immunosuppression
    • FRUMAN, D. A., S. J. BURAKOFF, AND B. E. BIERER. Immunophilins in protein folding and immunosuppression (Review). FASEB J. 8: 391-400, 1894.
    • (1894) FASEB J. , vol.8 , pp. 391-400
    • Fruman, D.A.1    Burakoff, S.J.2    Bierer, B.E.3
  • 52
    • 0026503434 scopus 로고
    • Calcineurin phosphatase activity in T lymphocytes is inhibited by FK 506 and cyclosporin A
    • FRUMAN, D. A., C. B. KLEE, B. E. BIERER, AND S. J. BURAKOFF. Calcineurin phosphatase activity in T lymphocytes is inhibited by FK 506 and cyclosporin A. Proc. Natl. Acad. Sci. USA 89: 3686-3690, 1992.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3686-3690
    • Fruman, D.A.1    Klee, C.B.2    Bierer, B.E.3    Burakoff, S.J.4
  • 53
    • 0028923877 scopus 로고
    • FK506 binding protein 12 mediates sensitivity to both FK506 and rapamycin in murine mast cells
    • FRUMAN, D. A., M. A. WOOD, C. K. GJERTSON, H. R. KATZ, S. J. BURAKOFF, AND B. E. BIERER. FK506 binding protein 12 mediates sensitivity to both FK506 and rapamycin in murine mast cells. Eur. J. Immunol. 25: 563-571, 1995.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 563-571
    • Fruman, D.A.1    Wood, M.A.2    Gjertson, C.K.3    Katz, H.R.4    Burakoff, S.J.5    Bierer, B.E.6
  • 54
    • 0024432232 scopus 로고
    • Primary structure and functional expression of the inositol 1,4,5-trisphosphate-binding protein P400
    • FURUICHI, T., S. YOSHIKAWA, A. MIYAWAKI, K. WADA, N. MAEDA, AND K. MIKOSHIBA. Primary structure and functional expression of the inositol 1,4,5-trisphosphate-binding protein P400. Nature Lond. 342: 32-38, 1989.
    • (1989) Nature Lond. , vol.342 , pp. 32-38
    • Furuichi, T.1    Yoshikawa, S.2    Miyawaki, A.3    Wada, K.4    Maeda, N.5    Mikoshiba, K.6
  • 55
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • GETHING, M.-J., AND J. SAMBROOK. Protein folding in the cell. Nature Lond. 355: 33-45, 1992.
    • (1992) Nature Lond. , vol.355 , pp. 33-45
    • Gething, M.-J.1    Sambrook, J.2
  • 57
    • 2642611675 scopus 로고
    • FK-506 influences adaptive behavior of the SR ryanodine receptor
    • GYORKE, S., C. DETTBARN, AND P. PALADE. FK-506 influences adaptive behavior of the SR ryanodine receptor (Abstract). Biophys. J. 66: A225, 1994.
    • (1994) Biophys. J. , vol.66
    • Gyorke, S.1    Dettbarn, C.2    Palade, P.3
  • 59
    • 0026471048 scopus 로고
    • Primary structure and distribution of a novel ryanodine receptor/calcium release channel from rabbit brain
    • HAKAMATA, Y., J. NAKAI, H. TAKESHIMA, AND K. IMOTO. Primary structure and distribution of a novel ryanodine receptor/calcium release channel from rabbit brain. FEBS Lett. 312: 229-235, 1992.
    • (1992) FEBS Lett. , vol.312 , pp. 229-235
    • Hakamata, Y.1    Nakai, J.2    Takeshima, H.3    Imoto, K.4
  • 60
    • 0024472603 scopus 로고
    • A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
    • HARDING, M. W., A. GALAT, D. E. UEHLING, AND S. L. SCHREIBER. A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase. Nature Lond. 341: 758-760, 1989.
    • (1989) Nature Lond. , vol.341 , pp. 758-760
    • Harding, M.W.1    Galat, A.2    Uehling, D.E.3    Schreiber, S.L.4
  • 61
    • 0028853108 scopus 로고
    • The human type 1 inositol 1,4,5-trisphosphate receptor from T lymphocytes: Structure, localization and phosphorylation
    • HARNICK, D. H., T. JAYARAMAN, L. GO, Y. MA, P. MULIERI, AND A. R. MARKS. The human type 1 inositol 1,4,5-trisphosphate receptor from T lymphocytes: structure, localization and phosphorylation. J. Biol. Chem. 270: 2833-2840, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2833-2840
    • Harnick, D.H.1    Jayaraman, T.2    Go, L.3    Ma, Y.4    Mulieri, P.5    Marks, A.R.6
  • 62
    • 0025373627 scopus 로고
    • Substrate specificities 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
    • HARRISON, R. K., AND R. L. STEIN. Substrate specificities 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, 1990.
    • (1990) Biochemistry , vol.29 , pp. 3813-3816
    • Harrison, R.K.1    Stein, R.L.2
  • 66
    • 0025776523 scopus 로고
    • Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast
    • HEITMAN, J., N. R. MOVVA, AND M. N. HALL. Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast. Science Wash. DC 253: 905-909, 1991.
    • (1991) Science Wash. DC , vol.253 , pp. 905-909
    • Heitman, J.1    Movva, N.R.2    Hall, M.N.3
  • 68
    • 0026647856 scopus 로고
    • cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein
    • HUNG, D. T., AND S. L. SCHREIBER. cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein. Biochem. Biophys. Res. Commun. 184: 733-738, 1992.
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 733-738
    • Hung, D.T.1    Schreiber, S.L.2
  • 69
    • 0027491776 scopus 로고
    • The T-cell transcription factor NFATp is a substrate for calcineurin and interacts with Fos and Jun
    • JAIN, J., P. MCCAFFREY, Z. MINER, T. KERPPOLA, J. LAMBERT, G. VERDINE, T. CURRAN, AND A. RAO. The T-cell transcription factor NFATp is a substrate for calcineurin and interacts with Fos and Jun. Nature Lond. 365: 352-355, 1993.
    • (1993) Nature Lond. , vol.365 , pp. 352-355
    • Jain, J.1    Mccaffrey, P.2    Miner, Z.3    Kerppola, T.4    Lambert, J.5    Verdine, G.6    Curran, T.7    Rao, A.8
  • 71
    • 0027440164 scopus 로고
    • Rapamycin-FKBP blocks proliferation, induces differentiation and inhibits cdc2 kinase activity in a myogenic cell line
    • JAYARAMAN, T., AND A. R. MARKS. Rapamycin-FKBP blocks proliferation, induces differentiation and inhibits cdc2 kinase activity in a myogenic cell line. J. Biol. Chem. 268: 25385-25388, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25385-25388
    • Jayaraman, T.1    Marks, A.R.2
  • 74
    • 0027296619 scopus 로고
    • The 25-kDa FK506-binding protein is localized in the nucleus and associates with casein kinase II and nucleolin
    • JIN, Y.-J., AND S. J. BURAKOFF. The 25-kDa FK506-binding protein is localized in the nucleus and associates with casein kinase II and nucleolin. Proc. Natl. Acad. Sci. USA 90: 7769-7773, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7769-7773
    • Jin, Y.-J.1    Burakoff, S.J.2
  • 75
    • 0026764829 scopus 로고
    • Molecular cloning of a 25-kDa high affinity rapamycin binding protein, FKBP25
    • JIN, Y.-J., S. J. BURAKOFF, AND B. E. BIERER. Molecular cloning of a 25-kDa high affinity rapamycin binding protein, FKBP25. J. Biol. Chem. 267: 10942-10945, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10942-10945
    • Jin, Y.-J.1    Burakoff, S.J.2    Bierer, B.E.3
  • 76
    • 0027321984 scopus 로고
    • The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin
    • KERN, D., T. DRAKENBERG, M. WIKSTROM, S. FORSEN, H. BANG, AND G. FISCHER. The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin. FEBS Lett. 323: 198-202, 1993.
    • (1993) FEBS Lett. , vol.323 , pp. 198-202
    • Kern, D.1    Drakenberg, T.2    Wikstrom, M.3    Forsen, S.4    Bang, H.5    Fischer, G.6
  • 77
    • 0028278089 scopus 로고
    • Reassessment of the putative chaperone function of prolyl-cis/trans-isomerases
    • KERN, G., D. KERN, F. X. SCHMID, AND G. FISCHER. Reassessment of the putative chaperone function of prolyl-cis/trans-isomerases. FEBS Lett. 348: 145-148, 1994.
    • (1994) FEBS Lett. , vol.348 , pp. 145-148
    • Kern, G.1    Kern, D.2    Schmid, F.X.3    Fischer, G.4
  • 78
    • 0027217548 scopus 로고
    • Cyclophilin-40, a protein with homology to the p59 component of the steroid receptor complex
    • KIEFFER, L. J., T. W. SENG, W. LI, D. G. OSTERMAN, R. E. HANDSCHUMACHER, AND R. M. BAYNEY. Cyclophilin-40, a protein with homology to the p59 component of the steroid receptor complex. J. Biol. Chem. 268: 12303-12310, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12303-12310
    • Kieffer, L.J.1    Seng, T.W.2    Li, W.3    Osterman, D.G.4    Handschumacher, R.E.5    Bayney, R.M.6
  • 79
    • 0029587585 scopus 로고
    • Expressed ryanodine receptor can substitute for the inositol 1,4,5-trisphosphate receptor during progesterone induced maturation in
    • KOBRINSKY, E., K. ONDRIAS, AND A. R. MARKS. Expressed ryanodine receptor can substitute for the inositol 1,4,5-trisphosphate receptor during progesterone induced maturation in Xenopus oocytes. Dev. Biol. 172: 531-540, 1995.
    • (1995) Xenopus Oocytes. Dev. Biol. , vol.172 , pp. 531-540
    • Kobrinsky, E.1    Ondrias, K.2    Marks, A.R.3
  • 83
    • 0023903046 scopus 로고
    • Purification and reconstitution of the calcium release channel from skeletal muscle
    • LAI, F. A., H. P. ERICKSON, E. ROUSSEAU, Q. L. LIU, AND G. MEISSNER. Purification and reconstitution of the calcium release channel from skeletal muscle. Nature Lond. 331: 315-319, 1988.
    • (1988) Nature Lond. , vol.331 , pp. 315-319
    • Lai, F.A.1    Erickson, H.P.2    Rousseau, E.3    Liu, Q.L.4    Meissner, G.5
  • 84
    • 0029098342 scopus 로고
    • Isolation of a cDNA encoding a novel human FK506-binding protein homolog containing leucine zipper and tetratricopeptide repeat motifs
    • LAM, E., M. MARTIN, AND G. WIEDERRECHT. Isolation of a cDNA encoding a novel human FK506-binding protein homolog containing leucine zipper and tetratricopeptide repeat motifs. Gene 160: 297-302, 1995.
    • (1995) Gene , vol.160 , pp. 297-302
    • Lam, E.1    Martin, M.2    Wiederrecht, G.3
  • 86
    • 0026781440 scopus 로고
    • p59 an hsp 90-binding protein: Cloning and sequencing of its cDNA and preparation of a peptide-directed polyclonal antibody
    • LEBEAU, M.-C., N. MASSOL, J. HERRICK, L. E. FABER, J.-M. RENOIR, C. RADANYI, AND E.-E. BAULIEU. p59 an hsp 90-binding protein: cloning and sequencing of its cDNA and preparation of a peptide-directed polyclonal antibody. J. Biol. Chem. 267: 4281-4284, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4281-4284
    • Lebeau, M.-C.1    Massol, N.2    Herrick, J.3    Faber, L.E.4    Renoir, J.-M.5    Radanyi, C.6    Baulieu, E.-E.7
  • 87
    • 0027444278 scopus 로고
    • Anti-ryanodine receptor antibody binding sites in aortic and endocardial endothelium
    • LESH, R. E., A. R. MARKS, A. SOMLYO, S. FLEISCHER, AND A. SOMLYO. Anti-ryanodine receptor antibody binding sites in aortic and endocardial endothelium. Circ. Res. 72: 481-488, 1993.
    • (1993) Circ. Res. , vol.72 , pp. 481-488
    • Lesh, R.E.1    Marks, A.R.2    Somlyo, A.3    Fleischer, S.4    Somlyo, A.5
  • 88
    • 0025869897 scopus 로고
    • Functional characterization of the ryanodine receptor from sheep cardiac muscle sarcoplasmic reticulum
    • LINDSAY, A., AND A. WILLIAMS. Functional characterization of the ryanodine receptor from sheep cardiac muscle sarcoplasmic reticulum. Biochim. Biophys. Acta 1064: 89-102, 1991.
    • (1991) Biochim. Biophys. Acta , vol.1064 , pp. 89-102
    • Lindsay, A.1    Williams, A.2
  • 89
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
    • LIU, J., J. FARMER, W. LANE, J. FRIEDMAN, I. WEISSMAN, AND S. SCHREIBER. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 66: 807-815, 1991.
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu, J.1    Farmer, J.2    Lane, W.3    Friedman, J.4    Weissman, I.5    Schreiber, S.6
  • 90
    • 0025916166 scopus 로고
    • Cyclosporin A inhibits an initial step in folding of transferrin within the endoplasmic reticulum
    • LODISH, H. F., AND N. KONG. Cyclosporin A inhibits an initial step in folding of transferrin within the endoplasmic reticulum. J. Biol. Chem. 266: 14835-14838, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14835-14838
    • Lodish, H.F.1    Kong, N.2
  • 91
    • 0028158402 scopus 로고
    • Light-regulated, tissue-specific immunophilins in a higher plant
    • LUAN, S., M. W. ALBERS, AND S. L. SCHREIBER. Light-regulated, tissue-specific immunophilins in a higher plant. Proc. Natl. Acad. Sci. USA 91: 984-988, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 984-988
    • Luan, S.1    Albers, M.W.2    Schreiber, S.L.3
  • 92
    • 0028096222 scopus 로고
    • Primary structure, ligand binding, and localization of the human type 3 inositol 1,4,5-trisphosphate receptor expressed in intestinal epithelium
    • MARANTO, A. Primary structure, ligand binding, and localization of the human type 3 inositol 1,4,5-trisphosphate receptor expressed in intestinal epithelium. J. Biol. Chem. 269: 1222-1230, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1222-1230
    • Maranto, A.1
  • 93
    • 0025327389 scopus 로고
    • Surface topography analysis of the ryanodine receptor/junctional channel complex based on proteolysis sensitivity mapping
    • MARKS, A. R., S. FLEISCHER, AND P. TEMPST. Surface topography analysis of the ryanodine receptor/junctional channel complex based on proteolysis sensitivity mapping. J. Biol. Chem. 265: 13143-13149, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13143-13149
    • Marks, A.R.1    Fleischer, S.2    Tempst, P.3
  • 94
    • 0025613843 scopus 로고
    • Smooth muscle and brain inositol 1,4,5-trisphosphate receptors are structurally and functionally similar
    • MARKS, A. R., P. TEMPST, C. C. CHADWICK, L. RIVIERE, S. FLEISCHER, AND B. NADAL-GINARD. Smooth muscle and brain inositol 1,4,5-trisphosphate receptors are structurally and functionally similar. J. Biol. Chem. 265: 20719-20722, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20719-20722
    • Marks, A.R.1    Tempst, P.2    Chadwick, C.C.3    Riviere, L.4    Fleischer, S.5    Nadal-Ginard, B.6
  • 95
    • 0024372718 scopus 로고
    • Molecular cloning and characterization of the ryanodine receptor/junctional channel complex cDNA from skeletal muscle sarcoplasmic reticulum
    • MARKS, A. R., P. TEMPST, K. S. HWANG, M. B. TAUBMAN, M. INUI, C. CHADWICK, S. FLEISCHER, AND B. NADAL-GINARD. Molecular cloning and characterization of the ryanodine receptor/junctional channel complex cDNA from skeletal muscle sarcoplasmic reticulum. Proc. Natl. Acad. Sc. USA 86: 8683-8687, 1989.
    • (1989) Proc. Natl. Acad. Sc. USA , vol.86 , pp. 8683-8687
    • Marks, A.R.1    Tempst, P.2    Hwang, K.S.3    Taubman, M.B.4    Inui, M.5    Chadwick, C.6    Fleischer, S.7    Nadal-Ginard, B.8
  • 96
    • 0028876806 scopus 로고
    • Rapamycin-FKBP inhibits cell cycle regulators of proliferation in vascular smooth muscle cells
    • MARX, S. O., T. JAYARAMAN, L. O. GO, AND A. R. MARKS. Rapamycin-FKBP inhibits cell cycle regulators of proliferation in vascular smooth muscle cells. Circ. Res. 76: 412-417, 1995.
    • (1995) Circ. Res. , vol.76 , pp. 412-417
    • Marx, S.O.1    Jayaraman, T.2    Go, L.O.3    Marks, A.R.4
  • 97
    • 0026730719 scopus 로고
    • Rabbit FKBP59-heat shock protein binding immunophilin (HBI) is a calmodulin binding protein
    • MASSOL, N., M. C. LEBEAU, J. M. RENOIR, L. E. FABER, AND E. E. BAULIEU. Rabbit FKBP59-heat shock protein binding immunophilin (HBI) is a calmodulin binding protein. Biochem. Biophys. Res. Commun. 187: 1330-1333, 1993.
    • (1993) Biochem. Biophys. Res. Commun. , vol.187 , pp. 1330-1333
    • Massol, N.1    Lebeau, M.C.2    Renoir, J.M.3    Faber, L.E.4    Baulieu, E.E.5
  • 99
    • 4243843915 scopus 로고
    • The effects of FK-506 on cardiac Ca transients and contraction
    • MCCALL, E., L. LI, AND D. M. BERS. The effects of FK-506 on cardiac Ca transients and contraction (Abstract). Biophys. J. 68: A176, 1995.
    • (1995) Biophys. J. , vol.68
    • Mccall, E.1    Li, L.2    Bers, D.M.3
  • 101
    • 0026561902 scopus 로고
    • Cortical localization of a calcium release channel in sea urchin eggs
    • MCPHERSON, S., P. MCPHERSON, L. MATHEWS, K. CAMPBELL, AND F. LONGO. Cortical localization of a calcium release channel in sea urchin eggs. J. Cell Biol. 116: 1111-1121, 1992.
    • (1992) J. Cell Biol. , vol.116 , pp. 1111-1121
    • Mcpherson, S.1    Mcpherson, P.2    Mathews, L.3    Campbell, K.4    Longo, F.5
  • 102
    • 9444248871 scopus 로고
    • Association of the ryanodine receptor and the FK-506 binding protein
    • MEHRAN, R., A. BRILLANTES, T. JAYARAMAN, E. KOBRINKSY, AND A. MARKS. Association of the ryanodine receptor and the FK-506 binding protein (Abstract). Circulation 88, Suppl. I:I-624, 1993.
    • (1993) Circulation , vol.88 , Issue.1 SUPPL.
    • Mehran, R.1    Brillantes, A.2    Jayaraman, T.3    Kobrinksy, E.4    Marks, A.5
  • 105
    • 0025826966 scopus 로고
    • Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin
    • MICHNICK, S. W., M. K. ROSEN, T. J. WANDLESS, M. KARPLUS, AND S. L. SCHREIBER. Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin. Science Wash. DC 252: 836-839, 1991.
    • (1991) Science Wash. DC , vol.252 , pp. 836-839
    • Michnick, S.W.1    Rosen, M.K.2    Wandless, T.J.3    Karplus, M.4    Schreiber, S.L.5
  • 106
    • 0024449839 scopus 로고
    • Putative receptor for inositol 1,4,5-trisphosphate similar to ryanodine receptor
    • MIGNERY, G., T. SUDHOF, K. TAKEI, AND P. CAMILLI. Putative receptor for inositol 1,4,5-trisphosphate similar to ryanodine receptor. Nature Lond. 342: 192-195, 1989.
    • (1989) Nature Lond. , vol.342 , pp. 192-195
    • Mignery, G.1    Sudhof, T.2    Takei, K.3    Camilli, P.4
  • 107
    • 0025332712 scopus 로고
    • Structure and expression of the rat inositol-1,4,5-trisphosphate receptor
    • MIGNERY, G. A., C. L. NEWTON, B. T. ARCHER, AND T. C. SUDHOF. Structure and expression of the rat inositol-1,4,5-trisphosphate receptor. J. Biol. Chem. 265: 12679-12685, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12679-12685
    • Mignery, G.A.1    Newton, C.L.2    Archer, B.T.3    Sudhof, T.C.4
  • 108
    • 0025048773 scopus 로고
    • The ligand binding site and transduction mechanism in the inositol 1,4,5-trisphosphate receptor
    • MIGNERY, G. A., AND T. C. SUDHOF. The ligand binding site and transduction mechanism in the inositol 1,4,5-trisphosphate receptor. EMBO J. 9: 3893-3898, 1990.
    • (1990) EMBO J. , vol.9 , pp. 3893-3898
    • Mignery, G.A.1    Sudhof, T.C.2
  • 110
    • 0027500251 scopus 로고
    • Inositol 1,4,5-trisphosphate receptor expression in cardiac myocytes
    • MOSCHELLA, M. C., AND A. R. MARKS. Inositol 1,4,5-trisphosphate receptor expression in cardiac myocytes. J. Cell Biol. 120: 1137-1146, 1993.
    • (1993) J. Cell Biol. , vol.120 , pp. 1137-1146
    • Moschella, M.C.1    Marks, A.R.2
  • 111
    • 0025605192 scopus 로고
    • Purification and characterization of the inositol 1,4,5-trisphosphate receptor protein from rat vas deferens
    • MOUREY, R. J., A. VERMA, S. SUPATTAPONE, AND S. H. SNYDER. Purification and characterization of the inositol 1,4,5-trisphosphate receptor protein from rat vas deferens. Biochem. J. 272: 383-389, 1990.
    • (1990) Biochem. J. , vol.272 , pp. 383-389
    • Mourey, R.J.1    Verma, A.2    Supattapone, S.3    Snyder, S.H.4
  • 112
    • 0025835204 scopus 로고
    • The subtypes of the mouse inositol 1,4,5-trisphosphate receptor are expressed in a tissue-specific and developmentally specific manner
    • NAKAGAWA, T., H. OKANO, T. FURUICHI, J. ARUGA, AND K. MIKOSHIBA. The subtypes of the mouse inositol 1,4,5-trisphosphate receptor are expressed in a tissue-specific and developmentally specific manner. Proc. Natl. Acad. Sci. USA 88: 6244-6248, 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6244-6248
    • Nakagawa, T.1    Okano, H.2    Furuichi, T.3    Aruga, J.4    Mikoshiba, K.5
  • 113
    • 0025123804 scopus 로고
    • Primary structure and functional expression from cDNA of the cardiac ryanodine receptor/calcium release channel
    • NAKAI, J., T. IMAGAWA, Y. HAKAMATA, M. SHIGEKAWA, H. TAKESHIMA, AND S. NUMA. Primary structure and functional expression from cDNA of the cardiac ryanodine receptor/calcium release channel. FEBS Lett. 271: 169-177, 1990.
    • (1990) FEBS Lett. , vol.271 , pp. 169-177
    • Nakai, J.1    Imagawa, T.2    Hakamata, Y.3    Shigekawa, M.4    Takeshima, H.5    Numa, S.6
  • 115
    • 0027267916 scopus 로고
    • Localization of the FK506-binding protein, FKBP 13, to the lumen of the endoplasmic reticulum
    • NIGAM, S. K., Y. J. JIN, M. J. JIN, K. T. BUSH, B. E. BIERER, AND S. J. BURAKOFF. Localization of the FK506-binding protein, FKBP 13, to the lumen of the endoplasmic reticulum. Biochem. J. 294: 511-515, 1993.
    • (1993) Biochem. J. , vol.294 , pp. 511-515
    • Nigam, S.K.1    Jin, Y.J.2    Jin, M.J.3    Bush, K.T.4    Bierer, B.E.5    Burakoff, S.J.6
  • 116
    • 0026707686 scopus 로고
    • Genetic dissection of cyclophilin function. Saturation mutagenesis of the Drosophila cyclophilin homolog ninaA
    • ONDEK, B., R. W. HARDY, E. K. BAKER, M. A. STAMNES, B. H. SHIEH, AND C. S. ZUKER. Genetic dissection of cyclophilin function. Saturation mutagenesis of the Drosophila cyclophilin homolog ninaA. J. Biol. Chem. 267: 16460-16466, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16460-16466
    • Ondek, B.1    Hardy, R.W.2    Baker, E.K.3    Stamnes, M.A.4    Shieh, B.H.5    Zuker, C.S.6
  • 117
    • 9444257704 scopus 로고
    • A role for FKBP in coupled gating of the recombinant ryanodine receptor/calcium release channel
    • ONDRIAS, K., AND A. R. MARKS. A role for FKBP in coupled gating of the recombinant ryanodine receptor/calcium release channel (Abstract). Circulation 92, Suppl. I: I-235, 1995.
    • (1995) Circulation , vol.92 , Issue.1 SUPPL.
    • Ondrias, K.1    Marks, A.R.2
  • 119
    • 0028123018 scopus 로고
    • Streptomyces chrysomallus FKBP-33 is a novel immunophilin consisting of two FK506 binding domains: Its gene is transcriptionally coupled to the FKBP12 gene
    • PAHL, A., AND U. KELLER. Streptomyces chrysomallus FKBP-33 is a novel immunophilin consisting of two FK506 binding domains: its gene is transcriptionally coupled to the FKBP12 gene. EMBO J. 13: 3472-3480, 1994.
    • (1994) EMBO J. , vol.13 , pp. 3472-3480
    • Pahl, A.1    Keller, U.2
  • 120
    • 0027173977 scopus 로고
    • The FKB2 gene of Saccharomyces cerevisiae, encoding the immunosuppressant-binding protein FKBP-13, is regulated in response to accumulation of unfolded proteins in the endoplasmic reticulum
    • PARTALEDIS, J. A., AND V. BERLIN. The FKB2 gene of Saccharomyces cerevisiae, encoding the immunosuppressant-binding protein FKBP-13, is regulated in response to accumulation of unfolded proteins in the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 90: 5450-5454, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5450-5454
    • Partaledis, J.A.1    Berlin, V.2
  • 121
    • 0026495863 scopus 로고
    • Expression and characterization of human FKBP52, an immunophilin that associates with the 90 kDa heat shock protein and is a component of steroid receptor complexes
    • PEATTIE, D. A., M. W. HADING, M. A. FLEMING, M. T. DECENZO, J. A. LIPPKE, D. J. LIVINGSTON, AND M. BENASUTTI. Expression and characterization of human FKBP52, an immunophilin that associates with the 90 kDa heat shock protein and is a component of steroid receptor complexes. Proc. Natl. Acad. Sci. USA 89: 10974-10978, 1992.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10974-10978
    • Peattie, D.A.1    Hading, M.W.2    Fleming, M.A.3    Decenzo, M.T.4    Lippke, J.A.5    Livingston, D.J.6    Benasutti, M.7
  • 122
    • 0028928112 scopus 로고
    • Calcium regulation of calcineurin phosphatase activity by its B subunit and calmodulin. Role of the autoinhibitory domain
    • PERRINO, B. A., L. Y. NG, AND T. R. SODERLING. Calcium regulation of calcineurin phosphatase activity by its B subunit and calmodulin. Role of the autoinhibitory domain. J. Biol. Chem. 270: 340-346, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 340-346
    • Perrino, B.A.1    Ng, L.Y.2    Soderling, T.R.3
  • 123
    • 0026759874 scopus 로고
    • Rapamycin-induced inhibition of the 70-kilodalton S6 protein kinase
    • PRICE, D. J., J. R. GROVE, V. CALVO, J. AVRUCH, AND B. E. BIERER. Rapamycin-induced inhibition of the 70-kilodalton S6 protein kinase. Science Wash. DC 257: 973-977, 1992.
    • (1992) Science Wash. DC , vol.257 , pp. 973-977
    • Price, D.J.1    Grove, J.R.2    Calvo, V.3    Avruch, J.4    Bierer, B.E.5
  • 124
    • 0026013566 scopus 로고
    • Human cyclophilin B: A second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence
    • PRICE, E. R., L. D. ZYDOWSKY, M. JIN, C. H. BAKER, F. D. MCKEON, AND C. T. WALSH. Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence. Proc. Natl. Acad. Sci. USA 88: 1903-1907, 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1903-1907
    • Price, E.R.1    Zydowsky, L.D.2    Jin, M.3    Baker, C.H.4    Mckeon, F.D.5    Walsh, C.T.6
  • 125
    • 0027788244 scopus 로고
    • Immunological identification of a 50 kDa Mr FK506-binding immunophilin as a component of the non-DNA binding, hsp90 and hsp70 containing, heterooligomeric form of the chick oviduct progesterone receptor
    • RENOIR, J. M., A. PAHL, U. KELLER, AND E. E. BAULIEU. Immunological identification of a 50 kDa Mr FK506-binding immunophilin as a component of the non-DNA binding, hsp90 and hsp70 containing, heterooligomeric form of the chick oviduct progesterone receptor. C. R. Acad. Sci. Ser. III Sci. Vie 316: 1410-1416, 1993.
    • (1993) C. R. Acad. Sci. Ser. III Sci. Vie , vol.316 , pp. 1410-1416
    • Renoir, J.M.1    Pahl, A.2    Keller, U.3    Baulieu, E.E.4
  • 126
    • 0028070767 scopus 로고
    • slyD, a host gene required for phi X174 lysis, is related to the FK506-binding protein family of peptidyl-prolyl cis-trans-isomerases
    • ROOF, W. D., S. M. HORNE, K. D. YOUNG, AND R. YOUNG. slyD, a host gene required for phi X174 lysis, is related to the FK506-binding protein family of peptidyl-prolyl cis-trans-isomerases. J. Biol. Chem. 269: 2902-2910, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2902-2910
    • Roof, W.D.1    Horne, S.M.2    Young, K.D.3    Young, R.4
  • 127
    • 0026575583 scopus 로고
    • Natural products as probes of cellular function: Studies of immunophilins
    • ROSEN, M. K., AND S. L. SCHREIBER. Natural products as probes of cellular function: studies of immunophilins. Angewandie Chemie 31: 384-400, 1992.
    • (1992) Angewandie Chemie , vol.31 , pp. 384-400
    • Rosen, M.K.1    Schreiber, S.L.2
  • 128
    • 0025302066 scopus 로고
    • Inhibition of FKBP rotamase activity by immunosuppressant FK506: Twisted amide surrogate
    • ROSEN, M. K., R. F. STANDAERT, A. GALAT, M. NAKATSUKA, AND S. L. SCHREIBER. Inhibition of FKBP rotamase activity by immunosuppressant FK506: twisted amide surrogate. Science Wash. DC 248: 863-866, 1990.
    • (1990) Science Wash. DC , vol.248 , pp. 863-866
    • Rosen, M.K.1    Standaert, R.F.2    Galat, A.3    Nakatsuka, M.4    Schreiber, S.L.5
  • 129
    • 0024311618 scopus 로고
    • Inositol 1,4,5-trisphosphate receptor localized to endoplasmic reticulum in cerebellar Purkinje neurons
    • ROSS, C. A., J. MELDOLESI, T. A. MILNER, T. SALOH, S. SUPATTAPONE, AND S. H. SNYDER. Inositol 1,4,5-trisphosphate receptor localized to endoplasmic reticulum in cerebellar Purkinje neurons. Nature Lond. 339: 468-470, 1989.
    • (1989) Nature Lond. , vol.339 , pp. 468-470
    • Ross, C.A.1    Meldolesi, J.2    Milner, T.A.3    Saloh, T.4    Supattapone, S.5    Snyder, S.H.6
  • 130
    • 0028239893 scopus 로고
    • RAFT1: A mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs
    • SABATINI, D., H. ERDJUMENT-BROMAGE, M. LUI, P. TEMPST, AND S. SNYDER. RAFT1: a mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs. Cell 78: 35-43, 1994.
    • (1994) Cell , vol.78 , pp. 35-43
    • Sabatini, D.1    Erdjument-Bromage, H.2    Lui, M.3    Tempst, P.4    Snyder, S.5
  • 132
    • 0026030568 scopus 로고
    • Chemistry and biology of the immunophilins and their immunosuppressive ligands
    • SCHREIBER, S. Chemistry and biology of the immunophilins and their immunosuppressive ligands. Science Wash. DC 251: 283-287, 1991.
    • (1991) Science Wash. DC , vol.251 , pp. 283-287
    • Schreiber, S.1
  • 134
    • 0024442393 scopus 로고
    • A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin
    • SIEKIERKA, J. J., S. H. Y. HUNG, M. POE, C. S. LIN, AND N. H. SIGAL. A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin. Nature Lond. 341: 755-757, 1989.
    • (1989) Nature Lond. , vol.341 , pp. 755-757
    • Siekierka, J.J.1    Hung, S.H.Y.2    Poe, M.3    Lin, C.S.4    Sigal, N.H.5
  • 135
    • 0025635897 scopus 로고
    • The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase
    • SIEKIERKA, J. J., G. WIEDERRECHT, H. GREULICH, D. BOULTON, S. Y. HUNG, J. CRYAN, P. J. HODGES, AND N. H. SIGAL. The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase. J. Biol. Chem. 265: 21011-21015, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21011-21015
    • Siekierka, J.J.1    Wiederrecht, G.2    Greulich, H.3    Boulton, D.4    Hung, S.Y.5    Cryan, J.6    Hodges, P.J.7    Sigal, N.H.8
  • 136
    • 0026748870 scopus 로고
    • Cyclosporin A, FK-506, and rapamycin: Pharmacolgical probes of lymphocyte signal transduction
    • SIGAL, N. H., AND F. J. DUMONT. Cyclosporin A, FK-506, and rapamycin: pharmacolgical probes of lymphocyte signal transduction. Annu. Rev. Immunol. 10: 519-560, 1992.
    • (1992) Annu. Rev. Immunol. , vol.10 , pp. 519-560
    • Sigal, N.H.1    Dumont, F.J.2
  • 137
    • 0027219348 scopus 로고
    • Two FKBP-related proteins are associated with progesterone receptor complexes
    • SMITH, D. F., B. A. BAGGENSTOSS, T. N. MARION, AND R. A. RIMERMAN. Two FKBP-related proteins are associated with progesterone receptor complexes. J. Biol. Chem. 268: 18365-18371, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18365-18371
    • Smith, D.F.1    Baggenstoss, B.A.2    Marion, T.N.3    Rimerman, R.A.4
  • 138
    • 0023029513 scopus 로고
    • Single channel measurements of the calcium release channel from skeletal muscle sarcoplasmic reticulum
    • SMITH, J. S., R. CORONADO, AND G. MEISSNER. Single channel measurements of the calcium release channel from skeletal muscle sarcoplasmic reticulum. J. Gen. Physiol. 88: 573-588, 1986.
    • (1986) J. Gen. Physiol. , vol.88 , pp. 573-588
    • Smith, J.S.1    Coronado, R.2    Meissner, G.3
  • 139
    • 0025907054 scopus 로고
    • The cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins
    • STAMNES, M., B.-H. SHIEH, L. CHUMAN, G. HARRIS, AND C. ZUKER. The cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins. Cell 65: 219-227, 1991.
    • (1991) Cell , vol.65 , pp. 219-227
    • Stamnes, M.1    Shieh, B.-H.2    Chuman, L.3    Harris, G.4    Zuker, C.5
  • 140
    • 0025061678 scopus 로고
    • Molecular cloning and overexpression of the human FK506-binding protein FKBP
    • STANDAERT, R. F., A. GALAT, G. VERDINE, AND S. L. SCHREIBER. Molecular cloning and overexpression of the human FK506-binding protein FKBP. Nature Lond. 346: 671-674, 1990.
    • (1990) Nature Lond. , vol.346 , pp. 671-674
    • Standaert, R.F.1    Galat, A.2    Verdine, G.3    Schreiber, S.L.4
  • 141
    • 0025968746 scopus 로고
    • Cyclosporin A slows collagen triple-helix formation in vivo: Indirect evidence for a physiologic role of peptidyl-prolyl cis-trans isomerase
    • STEINMANN, B., P. BRUCKNER, AND A. SUPERTI-FURGA. 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, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1299-1303
    • Steinmann, B.1    Bruckner, P.2    Superti-Furga, A.3
  • 143
    • 0027455419 scopus 로고
    • Phosphorylation of serine 2843 in ryanodine receptor-calcium release channel of skeletal muscle by cAMP-, cGMP- and CaM-dependent protein kinase
    • SUKO, J., I. MAURER-FOGY, B. PLANK, O. BERTEL, W. WYSKOVSKY, M. HOHENEGGER, AND G. HELLMANN. Phosphorylation of serine 2843 in ryanodine receptor-calcium release channel of skeletal muscle by cAMP-, cGMP- and CaM-dependent protein kinase. Biochim. Biophys. Acta 1175: 193-206, 1993.
    • (1993) Biochim. Biophys. Acta , vol.1175 , pp. 193-206
    • Suko, J.1    Maurer-Fogy, I.2    Plank, B.3    Bertel, O.4    Wyskovsky, W.5    Hohenegger, M.6    Hellmann, G.7
  • 144
    • 0023858663 scopus 로고
    • Solubilization, purification, and characterization of an inositol trisphosphate receptor
    • SUPATTAPONE, S., P. F. WORLEY, J. M. BARABAN, AND S. SNYDER. Solubilization, purification, and characterization of an inositol trisphosphate receptor. J. Biol. Chem. 263: 1530-1534, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1530-1534
    • Supattapone, S.1    Worley, P.F.2    Baraban, J.M.3    Snyder, S.4
  • 148
  • 149
    • 0027500789 scopus 로고
    • The calcium release channel of sarcoplasmic reticulum is modulated by FK-506 binding protein
    • TIMERMAN, A. P., E. OGUNBUNMI, E. FREUND, G. WIEDERRECHT, A. MARKS, AND S. FLEISCHER, The calcium release channel of sarcoplasmic reticulum is modulated by FK-506 binding protein. J. Biol. Chem. 268: 22992-22999, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22992-22999
    • Timerman, A.P.1    Ogunbunmi, E.2    Freund, E.3    Wiederrecht, G.4    Marks, A.5    Fleischer, S.6
  • 150
    • 0028836746 scopus 로고
    • Characterization of an exchange reaction between soluble FKBP-12 and the FKBP-ryanodine receptor complex. Modulation by FKBP mutants deficient in peptidyl-prolyl isomerase activity
    • TIMERMAN, A. P., G. WIEDERRECHT, A. MARCY, AND S. FLEISCHER. Characterization of an exchange reaction between soluble FKBP-12 and the FKBP-ryanodine receptor complex. Modulation by FKBP mutants deficient in peptidyl-prolyl isomerase activity. J. Biol. Chem. 270: 2451-2459, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2451-2459
    • Timerman, A.P.1    Wiederrecht, G.2    Marcy, A.3    Fleischer, S.4
  • 151
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • VAN DUYNE, G. D., R. F. STANDAERT, P. A. KARPLUS, S. L. SCHREIBER, AND J. CLARDY. Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J. Mol. Biol. 229: 105-124, 1993.
    • (1993) J. Mol. Biol. , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 152
    • 0026629246 scopus 로고
    • Cyclosporin A, the cyclophilin class of petidylprolyl isomerases, and blockade of T cell signal transduction
    • WALSH, C. T., L. D. ZYDOWSKY, AND F. D. MCKEON. Cyclosporin A, the cyclophilin class of petidylprolyl isomerases, and blockade of T cell signal transduction. J. Biol. Chem. 267: 13115-13118, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13115-13118
    • Walsh, C.T.1    Zydowsky, L.D.2    Mckeon, F.D.3
  • 153
    • 0028108801 scopus 로고
    • Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12
    • WANG, T., P. K. DONAHOE, AND A. S. ZERVOS. Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12. Science Wash. DC 265: 674-676, 1994.
    • (1994) Science Wash. DC , vol.265 , pp. 674-676
    • Wang, T.1    Donahoe, P.K.2    Zervos, A.S.3
  • 154
    • 0026580708 scopus 로고
    • Ion conduction and discrimination in the sarcoplasmic reticulum ryanodine receptor/calcium-release channel
    • WILLIAMS, A. Ion conduction and discrimination in the sarcoplasmic reticulum ryanodine receptor/calcium-release channel. J. Muscle Res. Cell. Motil. 13: 7-26, 1992.
    • (1992) J. Muscle Res. Cell. Motil. , vol.13 , pp. 7-26
    • Williams, A.1
  • 155
    • 0025772161 scopus 로고
    • Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity
    • WITCHER, D., R. KOVACS, H. SCHULMAN, D. CEFALI, AND L. JONES. Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity. J. Biol. Chem. 266: 11144-11152, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11144-11152
    • Witcher, D.1    Kovacs, R.2    Schulman, H.3    Cefali, D.4    Jones, L.5
  • 157
    • 0027934203 scopus 로고
    • An Escherichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif
    • WULFING, C., J. LOMBARDERO, AND A. PLUCKTHUN. An Escherichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif. J. Biol. Chem. 269: 2895-2901, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2895-2901
    • Wulfing, C.1    Lombardero, J.2    Pluckthun, A.3


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