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Volumn 26, Issue 2, 2012, Pages 132-143

From Drosophila to humans: Reflections on the roles of the prolyl isomerases and chaperones, cyclophilins, in cell function and disease

Author keywords

chaperone; cyclophilin; cyclosporin A (CsA); immunophilin; ninaA; proly isomerase; protein biogenesis

Indexed keywords

CHAPERONE; COLLAGEN TYPE 1; CYCLOPHILIN; CYCLOPHILIN B; CYCLOSPORIN A; FK 506 BINDING PROTEIN; G PROTEIN COUPLED RECEPTOR; IMMUNOPHILIN; LEUCINE; PEPTIDYLPROLYL ISOMERASE; RHODOPSIN; TACROLIMUS; TYROSINE;

EID: 84863863992     PISSN: 01677063     EISSN: 15635260     Source Type: Journal    
DOI: 10.3109/01677063.2011.647143     Document Type: Review
Times cited : (13)

References (91)
  • 2
    • 0027955787 scopus 로고
    • Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins
    • DOI 10.1006/jmbi.1994.1052
    • Abagyan, R., & Totrov, M. (1994). Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins. J Mol Biol, 235, 983-1002 (Pubitemid 24047836)
    • (1994) Journal of Molecular Biology , vol.235 , Issue.3 , pp. 983-1002
    • Abagyan, R.1    Totrov, M.2
  • 3
    • 84986522918 scopus 로고
    • ICM - A new method for protein modeling and design: Applications to docking and structure prediction from the distorted native conformation
    • Abagyan, R., Totrov, M., & Kuznetsov, D. (1994). ICM - A new method for protein modeling and design: Applications to docking and structure prediction from the distorted native conformation. J Comput Chem, 15, 488-506.
    • (1994) J Comput Chem , vol.15 , pp. 488-506
    • Abagyan, R.1    Totrov, M.2    Kuznetsov, D.3
  • 4
    • 0031576355 scopus 로고    scopus 로고
    • Do aligned sequences share the same fold?
    • DOI 10.1006/jmbi.1997.1287
    • Abagyan, R. A., & Batalov, S.(1997). Do aligned sequences share the same fold? J Mol Biol, 273, 355-368. (Pubitemid 27460236)
    • (1997) Journal of Molecular Biology , vol.273 , Issue.1 , pp. 355-368
    • Abagyan, R.A.1    Batalov, S.2
  • 6
    • 1842424727 scopus 로고    scopus 로고
    • 1 Cell Cycle Arrest from Tolerance Induction
    • Allen, A., Zheng, Y., Gardner, L., Safford, M., Horton, M.R., &Powell, J.D. (2004). The novel cyclophilin binding comp ound, sanglifehrin A, disassociates G1 cell cycle arrest from tolerance induction. J Immunol, 172, 4797-4803. (Pubitemid 38456401)
    • (2004) Journal of Immunology , vol.172 , Issue.8 , pp. 4797-4803
    • Allen, A.1    Zheng, Y.2    Gardner, L.3    Safford, M.4    Horton, M.R.5    Powell, J.D.6
  • 7
    • 0242528876 scopus 로고    scopus 로고
    • Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase
    • Arevalo-Rodriguez, M., Cardenas, M.E., Wu, X., Hanes, S.D., & Heitman, J. (2000). Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-Rpd3 histone deacetylase. EMBO J, 19, 3739-3749. (Pubitemid 30462131)
    • (2000) EMBO Journal , vol.19 , Issue.14 , pp. 3739-3749
    • Arevalo-Rodriguez, M.1    Cardenas, M.E.2    Wu, X.3    Hanes, S.D.4    Heitman, J.5
  • 8
    • 0028143610 scopus 로고
    • The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin
    • Baker, E.K., Colley, N.J., & Zuker, C.S. (1994). The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin. EMBO J, 13, 4886-4895. (Pubitemid 24319372)
    • (1994) EMBO Journal , vol.13 , Issue.20 , pp. 4886-4895
    • Baker, E.K.1    Colley, N.J.2    Zuker, C.S.3
  • 11
    • 76149098224 scopus 로고    scopus 로고
    • Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates
    • Bernasconi, R., Galli, C., Calanca, V., Nakajima, T., & Molinari, M. (2010a). Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates. J Cell Biol, 188, 223-235.
    • (2010) J Cell Biol , vol.188 , pp. 223-235
    • Bernasconi, R.1    Galli, C.2    Calanca, V.3    Nakajima, T.4    Molinari, M.5
  • 12
    • 77958543957 scopus 로고    scopus 로고
    • Cyclosporine A-sensitive, cyclophilin B-dependent endoplasmic reticulum-associated degradation
    • Bernasconi, R., Solda, T., Galli, C., Pertel, T., Luban, J., &Molinari, M. (2010b). Cyclosporine A-sensitive, cyclophilin B-dependent endoplasmic reticulum-associated degradation. PLoS ONE, 5, e13008
    • (2010) PLoS ONE , vol.5
    • Bernasconi, R.1    Solda, T.2    Galli, C.3    Pertel, T.4    Luban, J.5    Molinari, M.6
  • 13
    • 0030936121 scopus 로고    scopus 로고
    • Presence of cyclophilin A in synovial fluids of patients with rheumatoid arthritis
    • DOI 10.1084/jem.185.5.975
    • Billich, A., Winkler, G., Aschauer, H., Rot, A., & Peichl, P. (1997). Presence of cyclophilin A in synovial fluids of patients with rheumatoid arthritis. J Exp Med, 185, 975-980. (Pubitemid 27119882)
    • (1997) Journal of Experimental Medicine , vol.185 , Issue.5 , pp. 975-980
    • Billich, A.1    Winkler, G.2    Aschauer, H.3    Rot, A.4    Peichl, P.5
  • 14
    • 0027291282 scopus 로고
    • Spectral tuning of rhodopsin and metarhodopsin in vivo
    • DOI 10.1016/0896-6273(93)90268-V
    • Britt, S.G., Feiler, R., Kirschfeld, K., & Zuker, C.S. (1993). Spectral tuning of rhodopsin and metarhodopsin in vivo. Neuron, 11, 29-39. (Pubitemid 23222531)
    • (1993) Neuron , vol.11 , Issue.1 , pp. 29-39
    • Britt, S.G.1    Feiler, R.2    Kirschfeld, K.3    Zuker, C.S.4
  • 16
    • 18644384463 scopus 로고    scopus 로고
    • Cyclophilin A-deficient mice are resistant to immunosuppression by cyclosporine
    • Colgan, J., Asmal, M., Yu, B., & Luban, J. (2005). Cyclophilin A-deficient mice are resistant to immunosuppression by cyclosporine. J Immunol, 174, 6030-6038. (Pubitemid 40663790)
    • (2005) Journal of Immunology , vol.174 , Issue.10 , pp. 6030-6038
    • Colgan, J.1    Asmal, M.2    Yu, B.3    Luban, J.4
  • 17
    • 0025995535 scopus 로고
    • The cyclophilin homolog ninaA is required in the secretory pathway
    • Colley, N.J., Baker, E.K., Stamnes, M.A., & Zuker, C.S. (1991). The cyclophilin homolog ninaA is required in the secretory pathway. Cell, 67, 255-263. (Pubitemid 121001441)
    • (1991) Cell , vol.67 , Issue.2 , pp. 255-263
    • Colley, N.J.1    Baker, E.K.2    Stamnes, M.A.3    Zuker, C.S.4
  • 19
    • 0043074679 scopus 로고    scopus 로고
    • High binding capacity of cyclophilin B to chondrocyte heparan sulfate proteoglycans and its release from the cell surface by matrix metalloproteinases: Possible role as a proinflammatory mediator in arthritis
    • DOI 10.1002/art.11099
    • De Ceuninck, F., Allain, F., Caliez, A., Spik, G., & Vanhoutte, P.M. (2003). High binding capacity of cyclo philin B to chondrocyte heparan sulfate proteoglycans and its release from the cell surface by matrix metall oproteinases: Possible role as a proinflammatory mediator in arthritis. Arthritis Rheum, 48, 2197-2206. (Pubitemid 36959200)
    • (2003) Arthritis and Rheumatism , vol.48 , Issue.8 , pp. 2197-2206
    • De Ceuninck, F.1    Allain, F.2    Caliez, A.3    Spik, G.4    Vanhoutte, P.M.5
  • 23
    • 0029112610 scopus 로고
    • Retina-specifically expressed novel subtypes of bovine cyclophilin
    • Ferreira, P.A., Hom, J.T., & Pak, W.L. (1995). Retina-specifically expressed novel subtypes of bovine cyclophilin. J Biol Chem, 270, 23179-23188.
    • (1995) J Biol Chem , vol.270 , pp. 23179-23188
    • Ferreira, P.A.1    Hom, J.T.2    Pak, W.L.3
  • 24
    • 0029859847 scopus 로고    scopus 로고
    • Cyclophilin-related protein RanBP2 acts as chaperone for red/green opsin
    • DOI 10.1038/383637a0
    • Ferreira, P.A., Nakayama, T.A., Pak, W.L., & Travis, G.H. (1996). Cyclophilin-related protein RanBP2 acts as chaper one for red/green opsin. Nature, 383, 637-640. (Pubitemid 26347588)
    • (1996) Nature , vol.383 , Issue.6601 , pp. 637-640
    • Ferreira, P.A.1    Nakayama, T.A.2    Pak, W.L.3    Travis, G.H.4
  • 26
    • 0021668676 scopus 로고
    • NACHWEIS EINER ENZYMKATALYSE FUR DIE CIS-TRANS-ISOMERISIERUNG DER PEPTIDBINDUNG IN PROLINHALTIGEN PEPTIDEN
    • Fischer, G., Bang, H., & Mech, C. (1984). Determination of enzymatic catalysis for the cis-trans -isomerization of peptide binding in proline-containing peptides. Biomed Biochim Acta, 43, 1101-1111. (Pubitemid 15221717)
    • (1984) Biomedica Biochimica Acta , vol.43 , Issue.10 , pp. 1101-1111
    • Fischer, G.1    Bang, H.2    Mech, C.3
  • 27
    • 0024959449 scopus 로고
    • Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
    • 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, 476-478.
    • (1989) Nature , vol.337 , pp. 476-478
    • Fischer, G.1    Wittmann-Liebold, B.2    Lang, K.3    Kiefhaber, T.4    Schmid, F.X.5
  • 28
    • 0025831980 scopus 로고
    • 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
    • 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, 799-806. (Pubitemid 121001713)
    • (1991) Cell , vol.66 , Issue.4 , pp. 799-806
    • Friedman, J.1    Weissman, I.2
  • 29
    • 0028241135 scopus 로고
    • Cyclophilin-B is an abundant protein whose conformation is similar to cyclophilin-A
    • DOI 10.1016/0014-5793(94)00501-X
    • Galat, A., & Bouet, F. (1994). Cyclophilin-B is an abundant protein whose conformation is similar to cyclophilin-A. FEBS Lett, 347, 31-36. (Pubitemid 24205025)
    • (1994) FEBS Letters , vol.347 , Issue.1 , pp. 31-36
    • Galat, A.1
  • 30
    • 77957357258 scopus 로고    scopus 로고
    • Molecular aspects of cyclophilins mediating therapeutic actions of their ligands
    • Galat, A., & Bua, J. (2010). Molecular aspects of cyclophilins mediating therapeutic actions of their ligands. Cell Mol Life Sci, 67, 3467-3488.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 3467-3488
    • Galat, A.1    Bua, J.2
  • 31
    • 24144473671 scopus 로고    scopus 로고
    • Pro23His human retinitis pigmentosa
    • DOI 10.1093/hmg/ddi258
    • Galy, A., Roux, M.J., Sahel, J.A., Leveillard, T., & Giangrande, A. (2005). Rhodopsin maturation defects induce photoreceptor death by apoptosis: A fly model for Rhodopsin Pro23His human retinitis pigmentosa. Hum Mol Genet, 14, 2547-2557. (Pubitemid 41236067)
    • (2005) Human Molecular Genetics , vol.14 , Issue.17 , pp. 2547-2557
    • Galy, A.1    Roux, M.J.2    Sahel, J.A.3    Leveillard, T.4    Giangrande, A.5
  • 32
    • 0018744071 scopus 로고
    • Photoconvertible pigment states and excitation in Calliphora; the induction and properties of the prolonged depolarising afterpotential
    • DOI 10.1007/BF00535444
    • Hamdorf, K., & Razmjoo, S. (1979). Photoconvertible pigment states and excitation in Calliphora; the induction and properties of the prolonged depolarizing afterpotential. Biophys Struct Mech, 5, 137-161. (Pubitemid 9209931)
    • (1979) Biophysics of Structure and Mechanism , vol.5 , Issue.2-3 , pp. 137-161
    • Hamdorf, K.1    Razmjoo, S.2
  • 33
    • 0021159379 scopus 로고
    • Cyclophilin: A specific cytosolic binding protein for cyclosporin A
    • Handschumacher, R.E., Harding, M.W., Rice, J., Drugge, R.J., &Speicher, D.W. (1984). Cyclophilin: A specific cytosolic binding protein for cyclosporin A. Science, 226, 544-547. (Pubitemid 14018525)
    • (1984) Science , vol.226 , Issue.4674 , pp. 544-547
    • Handschumacher, R.E.1    Harding, M.W.2    Rice, J.3
  • 34
    • 0024472603 scopus 로고
    • A receptor for the immunosupressant FK506 is a cis-trans peptidyl-prolyl isomerase
    • DOI 10.1038/341758a0
    • Harding, M.W., Galat, A., Uehling, D.E., & Schreiber, S.L. (1989). A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase. Nature, 341, 758-760. (Pubitemid 19260893)
    • (1989) Nature , vol.341 , Issue.6244 , pp. 758-760
    • Harding, M.W.1    Galat, A.2    Uehling, D.E.3    Schreiber, S.L.4
  • 36
    • 33750947173 scopus 로고    scopus 로고
    • Retinitis pigmentosa
    • DOI 10.1016/S0140-6736(06)69740-7, PII S0140673606697407
    • Hartong, D.T., Berson, E.L., & Dryja, T.P. (2006). Retinitis pigmentosa. Lancet, 368, 1795-1809. (Pubitemid 44739028)
    • (2006) Lancet , vol.368 , Issue.9549 , pp. 1795-1809
    • Hartong, D.T.1    Berson, E.L.2    Dryja, T.P.3
  • 37
    • 57649134970 scopus 로고    scopus 로고
    • The rough endoplasmic reticulum-resident FK506-binding protein FKBP65 is a molecular chaperone that interacts with collagens
    • Ishikawa, Y., Vranka, J., Wirz, J., Nagata, K., & Bachinger, H.P. (2008). The rough endoplasmic reticulum-resident FK506-binding protein FKBP65 is a molecular chaperone that interacts with collagens. J Biol Chem, 283, 31584-31590.
    • (2008) J Biol Chem , vol.283 , pp. 31584-31590
    • Ishikawa, Y.1    Vranka, J.2    Wirz, J.3    Nagata, K.4    Bachinger, H.P.5
  • 38
    • 62649087890 scopus 로고    scopus 로고
    • Molecular determinants of a native-state prolyl isomerization
    • Jakob, R.P., & Schmid, F.X. (2009). Molecular determinants of a native-state prolyl isomerization. J Mol Biol, 387, 1017-1031.
    • (2009) J Mol Biol , vol.387 , pp. 1017-1031
    • Jakob, R.P.1    Schmid, F.X.2
  • 39
    • 0025858482 scopus 로고
    • Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy
    • Kallen, J., Spitzfaden, C., Zurini, M.G., Wider, G., Widmer, H., Wuthrich, 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, 276-279. (Pubitemid 21896773)
    • (1991) Nature , vol.353 , Issue.6341 , pp. 276-279
    • Kallen, J.1    Spitzfaden, C.2    Zurini, M.G.M.3    Wider, G.4    Widmer, H.5    Wuthrich, K.6    Walkinshaw, M.D.7
  • 40
    • 0026532431 scopus 로고
    • The X-ray structure of a tetrapeptide bound to the active site of human cyclophilin A
    • Kallen, J., & Walkinshaw, M.D. (1992). The X-ray structure of a tetrapeptide bound to the active site of human cyclophilin A. FEBS Lett, 300, 286-290.
    • (1992) FEBS Lett , vol.300 , pp. 286-290
    • Kallen, J.1    Walkinshaw, M.D.2
  • 42
    • 0019845444 scopus 로고
    • Mutation that selectively affects rhodopsin concentration in the peripheral photoreceptors of Drosophila melanogaster
    • Larrivee, D.C., Conrad, S.K., Stephenson, R.S., & Pak, W.L. (1981). Mutation that selectively affects rhodopsin concentration in the peripheral photoreceptors of Drosophila melanogaster. J Gen Physiol, 78, 521-545. (Pubitemid 12247661)
    • (1981) Journal of General Physiology , vol.78 , Issue.5 , pp. 521-545
    • Larrivee, D.C.1    Conrad, S.K.2    Stephenson, R.S.3    Pak, W.L.4
  • 43
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
    • Liu, J., Farmer, J.D., Jr., Lane, W.S., Friedman, J., Weissman, I., & Schreiber, S.L. (1991). Calcineurin is a common target of cyclophilin- cyclosporin A and FKBP-FK506 complexes. Cell, 66, 807-815. (Pubitemid 121001714)
    • (1991) Cell , vol.66 , Issue.4 , pp. 807-815
    • Liu, J.1    Farmer Jr., J.O.2    Lane, W.S.3    Friedman, J.4    Weissman, I.5    Schreiber, S.L.6
  • 44
    • 0029916122 scopus 로고    scopus 로고
    • A human peptidyl-prolyl isomerase essential for regulation of mitosis
    • DOI 10.1038/380544a0
    • Lu, K.P., Hanes, S.D., & Hunter, T. (1996). A human peptidylprolyl isomerase essential for regulation of mitosis. Nature, 380, 544-547. (Pubitemid 26111332)
    • (1996) Nature , vol.380 , Issue.6574 , pp. 544-547
    • Lu, K.P.1    Hanes, S.D.2    Hunter, T.3
  • 45
  • 46
    • 40549104452 scopus 로고    scopus 로고
    • The calcineurin/NFAT signaling pathway: A novel therapeutic target in leukemia and solid tumors
    • Medyouf, H., & Ghysdael, J. (2008). The calcineurin/NFAT signaling pathway: a novel therapeutic target in leukemia and solid tumors. Cell Cycle, 7, 297-303. (Pubitemid 351366491)
    • (2008) Cell Cycle , vol.7 , Issue.3 , pp. 297-303
    • Medyouf, H.1    Ghysdael, J.2
  • 48
    • 0002648001 scopus 로고
    • Photopigment-dependent adaptation in invertebrates: Implications for vertebrates
    • H. Stieve (Ed.), Berlin: Dahlem Konferenzen, Springer
    • Minke, B. (1986). Photopigment-dependent adaptation in invertebrates: implications for vertebrates. In H. Stieve (Ed.), The Molecular Mechanisms of Photoreception (pp. 241-265). Berlin: Dahlem Konferenzen, Springer.
    • (1986) The Molecular Mechanisms of Photoreception , pp. 241-265
    • Minke, B.1
  • 49
    • 76749168158 scopus 로고    scopus 로고
    • Chaperone activity of Cyp18 through hydrophobic condensation that enables rescue of transient misfolded molten globule intermediates
    • Moparthi, S.B., Fristedt, R., Mishra, R., Almstedt, K., Karlsson, M., Hammarstrom, P., & Carlsson, U. (2010). Chaperone activity of Cyp18 through hydrophobic condensation that enables rescue of transient misfolded molten globule intermediates. Biochemistry, 49, 1137-1145.
    • (2010) Biochemistry , vol.49 , pp. 1137-1145
    • Moparthi, S.B.1    Fristedt, R.2    Mishra, R.3    Almstedt, K.4    Karlsson, M.5    Hammarstrom, P.6    Carlsson, U.7
  • 50
    • 59949105375 scopus 로고    scopus 로고
    • A non-essential role for Arg 55 in cyclophilin18 for catalysis of proline isomerization during protein folding
    • Moparthi, S.B., Hammarstrom, P., & Carlsson, U. (2009). A non-essential role for Arg 55 in cyclophilin18 for catalysis of proline isomerization during protein folding. Prot Sci, 18, 475-479.
    • (2009) Prot Sci , vol.18 , pp. 475-479
    • Moparthi, S.B.1    Hammarstrom, P.2    Carlsson, U.3
  • 51
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • Needleman, S.B., & Wunsch, C.D. (1970). A general method applicable to the search for similarities in the amino acid sequence of two proteins. J Mol Biol, 48, 443-453.
    • (1970) J Mol Biol , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 53
    • 0026707686 scopus 로고
    • Genetic dissection of cyclophilin function. Saturation mutagenesis of the Drosophila cyclophilin homolog ninaA
    • Ondek, B., Hardy, R.W., Baker, E.K., Stamnes, M.A., Shieh, B.H., & Zuker, C.S. (1992). Genetic dissection of cyclophilin function. Saturation mutagenesis of the Drosophila cyclophilin homolog ninaA. J Biol Chem, 267, 16460-16466.
    • (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
  • 54
    • 0034774703 scopus 로고    scopus 로고
    • Chaperone-like activity of peptidyl-prolyl cis-trans isomerase during creatine kinase refolding
    • DOI 10.1110/ps.23301
    • Ou, W.B., Luo, W., Park, Y.D., & Zhou, H.M. (2001). Chaperone-like activity of peptidyl-prolyl cis-trans isomerase during creatine kinase refolding. Prot Sci, 10, 2346-2353. (Pubitemid 32988650)
    • (2001) Protein Science , vol.10 , Issue.11 , pp. 2346-2353
    • Ou, W.-B.1    Luo, W.2    Park, Y.-D.3    Zhou, H.-M.4
  • 55
    • 0002079492 scopus 로고
    • Study of photoreceptor function using Drosophila mutants
    • X. Breakfield (Ed.), New York: Elsevier
    • Pak, W.L. (1979). Study of photoreceptor function using Drosophila mutants. In X. Breakfield (Ed.), Neurogenetics: Genetic Approaches to the Nervous System (pp. 67-99). New York: Elsevier.
    • (1979) Neurogenetics: Genetic Approaches to the Nervous System , pp. 67-99
    • Pak, W.L.1
  • 56
    • 0028868905 scopus 로고
    • Drosophila in vision research. The Friedenwald Lecture
    • Pak, W.L. (1995). Drosophila in vision research. The Friedenwald Lecture. Invest Ophthalmol Vis Sci, 36, 2340-2357.
    • (1995) Invest Ophthalmol Vis Sci , vol.36 , pp. 2340-2357
    • Pak, W.L.1
  • 57
    • 0030988450 scopus 로고    scopus 로고
    • A new rhodopsin in R8 photoreceptors of Drosophila: Evidence for coordinate expression with Rh3 in R7 cells
    • Papatsenko, D., Sheng, G., & Desplan, C. (1997). A new rhodopsin in R8 photoreceptors of Drosophila: Evidence for coordinate expression with Rh3 in R7 cells. Development, 124, 1665-1673. (Pubitemid 27248334)
    • (1997) Development , vol.124 , Issue.9 , pp. 1665-1673
    • Papatsenko, D.1    Sheng, G.2    Desplan, C.3
  • 58
    • 0027473625 scopus 로고
    • X-ray structure of a decameric cyclophilin-cyclosporin crystal complex
    • DOI 10.1038/361091a0
    • Pflugl, G., Kallen, J., Schirmer, T., Jansonius, J.N., Zurini, M.G., & Walkinshaw, M.D. (1993). X-ray structure of a decameric cyclophilin-cyclosporin crystal complex. Nature, 361, 91-94. (Pubitemid 23020782)
    • (1993) Nature , vol.361 , Issue.6407 , pp. 91-94
    • Pflugl, G.1    Kallen, J.2    Schirmer, T.3    Jansonius, J.N.4    Zurini, M.G.M.5    Walkinshaw, M.D.6
  • 61
    • 79953087965 scopus 로고    scopus 로고
    • Mutations in PPIB (cyclophilin B) delay type I procollagen chain association and result in perinatal lethal to moderate osteogenesis imperfecta phenotypes
    • Pyott, S.M., Schwarze, U., Christiansen, H.E., Pepin, M.G., Leistritz, D.F., Dineen, R., Harris, C., Burton, B.K., Angle, B., Kim, K., et al. (2011). Mutations in PPIB (cyclophilin B) delay type I procollagen chain association and result in perinatal lethal to moderate osteogenesis imperfecta phenotypes. Hum Mol Gen, 20, 1595-1609.
    • (2011) Hum Mol Gen , vol.20 , pp. 1595-1609
    • Pyott, S.M.1    Schwarze, U.2    Christiansen, H.E.3    Pepin, M.G.4    Leistritz, D.F.5    Dineen, R.6    Harris, C.7    Burton, B.K.8    Angle, B.9    Kim, K.10
  • 62
    • 0028918401 scopus 로고
    • A proficient enzyme
    • Radzicka, A., & Wolfenden, R. (1995). A proficient enzyme. Science, 267, 90-93.
    • (1995) Science , vol.267 , pp. 90-93
    • Radzicka, A.1    Wolfenden, R.2
  • 63
    • 0008233581 scopus 로고    scopus 로고
    • Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent
    • Ranganathan, R., Lu, K.P., Hunter, T., & Noel, J.P. (1997). Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell, 89, 875-886. (Pubitemid 27513514)
    • (1997) Cell , vol.89 , Issue.6 , pp. 875-886
    • Ranganathan, R.1    Lu, K.P.2    Hunter, T.3    Noel, J.P.4
  • 64
    • 0030973579 scopus 로고    scopus 로고
    • Transcription factors of the NFAT family: Regulation and function
    • DOI 10.1146/annurev.immunol.15.1.707
    • Rao, A., Luo, C., & Hogan, P.G. (1997). Transcription factors of the NFAT family: Regulation and function. Annu Rev Immunol, 15, 707-747. (Pubitemid 27169297)
    • (1997) Annual Review of Immunology , vol.15 , pp. 707-747
    • Rao, A.1    Luo, C.2    Hogan, P.G.3
  • 65
    • 0037823485 scopus 로고    scopus 로고
    • Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide
    • DOI 10.1016/S0022-2836(03)00684-3
    • Reidt, U., Wahl, M.C., Fasshauer, D., Horowitz, D.S., Luhrmann, R., & Ficner, R. (2003). Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide. J Mol Biol, 331, 45-56. (Pubitemid 36870776)
    • (2003) Journal of Molecular Biology , vol.331 , Issue.1 , pp. 45-56
    • Reidt, U.1    Wahl, M.C.2    Fasshauer, D.3    Horowitz, D.S.4    Luhrmann, R.5    Ficner, R.6
  • 66
    • 0037007447 scopus 로고    scopus 로고
    • Local structural changes caused by peptidyl-prolyl cis/trans isomerization in the native state of proteins
    • DOI 10.1016/S0301-4622(02)00013-3, PII S0301462202000133
    • Reimer, U., & Fischer, G. (2002). Local structural changes caused by peptidyl-prolyl cis / trans isomerization in the native state of proteins. Biophys Chem, 96, 203-212. (Pubitemid 34548233)
    • (2002) Biophysical Chemistry , vol.96 , Issue.2-3 , pp. 203-212
    • Reimer, U.1    Fischer, G.2
  • 67
    • 67349235964 scopus 로고    scopus 로고
    • Cyclophilin A enhances vascular oxidative stress and the development of angiotensin II-induced aortic aneurysms
    • Satoh, K., Nigro, P., Matoba, T., O'Dell, M.R., Cui, Z., Shi, X., Mohan, A., Yan, C., Abe, J., Illig, K.A., et al. (2009). Cyclophilin A enhances vascular oxidative stress and the development of angiotensin II-induced aortic aneurysms. Nat Med, 15, 649-656.
    • (2009) Nat Med , vol.15 , pp. 649-656
    • Satoh, K.1    Nigro, P.2    Matoba, T.3    O'Dell, M.R.4    Cui, Z.5    Shi, X.6    Mohan, A.7    Yan, C.8    Abe, J.9    Illig, K.A.10
  • 68
    • 0033137131 scopus 로고    scopus 로고
    • Prediction of the binding energy for small molecules, peptides and proteins
    • DOI 10.1002/(SICI)1099-1352(199905/06)12:3<177::AID-JMR451>3.0. CO;2-Z
    • Schapira, M., Totrov, M., & Abagyan, R. (1999). Prediction of the binding energy for small molecules, peptides and proteins. J Mol Recognit, 12, 177-190. (Pubitemid 29266968)
    • (1999) Journal of Molecular Recognition , vol.12 , Issue.3 , pp. 177-190
    • Schapira, M.1    Totrov, M.2    Abagyan, R.3
  • 69
    • 84862178030 scopus 로고    scopus 로고
    • Peptide bond cis / trans isomerases: A biocatalysis pers pective of conformational dynamics in proteins
    • Schiene-Fischer, C., Aumuller, T., & Fischer, G. (2011). Peptide bond cis / trans isomerases: A biocatalysis pers pective of conformational dynamics in proteins. Top Curr Chem, 1-33
    • (2011) Top Curr Chem , pp. 1-33
    • Schiene-Fischer, C.1    Aumuller, T.2    Fischer, G.3
  • 70
  • 71
    • 0026030568 scopus 로고
    • Chemistry and biology of the immunophilins and their immunosuppressive ligands
    • Schreiber, S.L. (1991). Chemistry and biology of the immunophilins and their immunosuppressive ligands. Science, 251, 283-287.
    • (1991) Science , vol.251 , pp. 283-287
    • Schreiber, S.L.1
  • 72
    • 0026625939 scopus 로고
    • Immunophilin-sensitive protein phosphatase action in cell signaling pathways
    • Schreiber, S.L. (1992). Immunophilin-sensitive protein phosphatase action in cell signaling pathways. Cell, 70, 365-368.
    • (1992) Cell , vol.70 , pp. 365-368
    • Schreiber, S.L.1
  • 73
    • 0026554163 scopus 로고
    • Identification of cyclophilin as a proinflammatory secretory product of lipopolysaccharide-activated macrophages
    • Sherry, B., Yarlett, N., Strupp, A., & Cerami, A. (1992). Identification of cyclophilin as a proinflammatory secretory product of lipopolysaccharide-activated macrophages. Proc Natl Acad Sci USA, 89, 3511-3515.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3511-3515
    • Sherry, B.1    Yarlett, N.2    Strupp, A.3    Cerami, A.4
  • 74
    • 0024959573 scopus 로고
    • The ninaA gene required for visual transduction in Drosophila encodes a homologue of cyclosporin A-binding protein
    • Shieh, B.H., Stamnes, M.A., Seavello, S., Harris, G.L., & Zuker, C.S. (1989). The ninaA gene required for visual transduction in Drosophila encodes a homologue of cyclosporin A-binding protein. Nature, 338, 67-70.
    • (1989) Nature , vol.338 , pp. 67-70
    • Shieh, B.H.1    Stamnes, M.A.2    Seavello, S.3    Harris, G.L.4    Zuker, C.S.5
  • 76
    • 0029132706 scopus 로고
    • Hsp47 and cyclophilin B traverse the endoplasmic reticulum with procollagen into pre-Golgi intermediate vesicles. A role for Hsp47 and cyclophilin B in the export of procollagen from the endoplasmic reticulum
    • Smith, T., Ferreira, L.R., Hebert, C., Norris, K., & Sauk, J.J. (1995). Hsp47 and cyclophilin B traverse the endoplasmic reticulum with procollagen into pre-Golgi intermediate vesicles. A role for Hsp47 and cyclophilin B in the export of procollagen from the endoplasmic reticulum. J Biol Chem, 270, 18323-18328.
    • (1995) J Biol Chem , vol.270 , pp. 18323-18328
    • Smith, T.1    Ferreira, L.R.2    Hebert, C.3    Norris, K.4    Sauk, J.J.5
  • 77
    • 0032142911 scopus 로고    scopus 로고
    • Immunophilins in the nervous system
    • Snyder, S.H., Lai, M.M., & Burnett, P.E. (1998). Immunophilins in the nervous system. Neuron, 21, 283-294. (Pubitemid 28399689)
    • (1998) Neuron , vol.21 , Issue.2 , pp. 283-294
    • Snyder, S.H.1    Lai, M.M.2    Burnett, P.E.3
  • 78
    • 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.A., Shieh, B.H., Chuman, L., Harris, G.L., & Zuker, C.S. (1991). 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) Cell , vol.65 , pp. 219-227
    • Stamnes, M.A.1    Shieh, B.H.2    Chuman, L.3    Harris, G.L.4    Zuker, C.S.5
  • 79
    • 0020862852 scopus 로고
    • Drosophila mutants with reduced rhodopsin content
    • D. J. Cosens & D. Vince-Price (Eds.), Cambridge, UK: Cambridge University Press
    • Stephenson, R.S., O'Tousa, J., Scavarda, N.J., Randall, L.L., &Pak, W.L. (1983). Drosophila mutants with reduced rhodopsin content. In D. J. Cosens & D. Vince-Price (Eds.), The Biology of Photoreception (pp. 477-501). Cambridge, UK: Cambridge University Press.
    • (1983) The Biology of Photoreception , pp. 477-501
    • Stephenson, R.S.1    O'Tousa, J.2    Scavarda, N.J.3    Randall, L.L.4    Pak, W.L.5
  • 80
    • 0024959451 scopus 로고
    • Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
    • Takahashi, N., Hayano, T., & Suzuki, M. (1989). Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin. Nature, 337, 473-475.
    • (1989) Nature , vol.337 , pp. 473-475
    • Takahashi, N.1    Hayano, T.2    Suzuki, M.3
  • 83
    • 18144392678 scopus 로고    scopus 로고
    • ZD6474 suppresses oncogenic RET isoforms in a Drosophila model for type 2 multiple endocrine neoplasia syndromes and papillary thyroid carcinoma
    • DOI 10.1158/0008-5472.CAN-04-4561
    • Vidal, M., Wells, S., Ryan, A., & Cagan, R. (2005). ZD6474 suppresses oncogenic RET isoforms in a Drosophila model for type 2 multiple endocrine neoplasia syndromes and papillary thyroid carcinoma. Cancer Res, 65, 3538-3541. (Pubitemid 40616327)
    • (2005) Cancer Research , vol.65 , Issue.9 , pp. 3538-3541
    • Vidal, M.1    Wells, S.2    Ryan, A.3    Cagan, R.4
  • 84
    • 77951174390 scopus 로고    scopus 로고
    • A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR
    • Wang, X., Zhang, S., Zhang, J., Huang, X., Xu, C., Wang, W., Liu, Z., Wu, J., & Shi, Y. (2010). A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR. J Biol Chem, 285, 4951-4963.
    • (2010) J Biol Chem , vol.285 , pp. 4951-4963
    • Wang, X.1    Zhang, S.2    Zhang, J.3    Huang, X.4    Xu, C.5    Wang, W.6    Liu, Z.7    Wu, J.8    Shi, Y.9
  • 85
    • 39749094958 scopus 로고    scopus 로고
    • Human CyP33 binds specifically to mRNA and binding stimulates PPIase activity of hCyP33
    • Wang, Y., Han, R., Zhang, W., Yuan, Y., Zhang, X., Long, Y., &Mi, H. (2008). Human CyP33 binds specifically to mRNA and binding stimulates PPIase activity of hCyP33. FEBS Lett, 582, 835-839.
    • (2008) FEBS Lett , vol.582 , pp. 835-839
    • Wang, Y.1    Han, R.2    Zhang, W.3    Yuan, Y.4    Zhang, X.5    Long, Y.6    Mi, H.7
  • 87
    • 0029070074 scopus 로고
    • Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region
    • Wu, J., Matunis, M.J., Kraemer, D., Blobel, G., & Coutavas, E. (1995). Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region. J Biol Chem, 270, 14209-14213.
    • (1995) J Biol Chem , vol.270 , pp. 14209-14213
    • Wu, J.1    Matunis, M.J.2    Kraemer, D.3    Blobel, G.4    Coutavas, E.5
  • 88
    • 33744904998 scopus 로고    scopus 로고
    • Solution structure of human peptidyl prolyl isomerase-like protein 1 and insights into its interaction with SKIP
    • DOI 10.1074/jbc.M511155200
    • Xu, C., Zhang, J., Huang, X., Sun, J., Xu, Y., Tang, Y., Wu, J., Shi, Y., Huang, Q., & Zhang, Q. (2006). Solution structure of human peptidyl prolyl isomerase-like protein 1 and insights into its interaction with SKIP. J Biol Chem, 281, 15900-15908. (Pubitemid 43848482)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.23 , pp. 15900-15908
    • Xu, C.1    Zhang, J.2    Huang, X.3    Sun, J.4    Xu, Y.5    Tang, Y.6    Wu, J.7    Shi, Y.8    Huang, Q.9    Zhang, Q.10
  • 89
    • 50849113464 scopus 로고    scopus 로고
    • Cyclophilin A up-regulates MMP-9 expression and adhesion of monocytes/macrophages via CD147 signalling pathway in rheumatoid arthritis
    • Yang, Y., Lu, N., Zhou, J., Chen, Z.N., & Zhu, P. (2008). Cyclophilin A up-regulates MMP-9 expression and adhesion of monocytes/macrophages via CD147 signalling pathway in rheumatoid arthritis. Rheumatology, 47, 1299-1310.
    • (2008) Rheumatology , vol.47 , pp. 1299-1310
    • Yang, Y.1    Lu, N.2    Zhou, J.3    Chen, Z.N.4    Zhu, P.5
  • 91
    • 0030051943 scopus 로고    scopus 로고
    • The biology of vision of Drosophila
    • Zuker, C.S. (1996). The biology of vision of Drosophila . Proc Natl Acad Sci USA, 93, 571-576.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 571-576
    • Zuker, C.S.1


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