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Volumn 125, Issue 1-2, 2002, Pages 1-9

Rapamycin insensitivity in Schistosoma mansoni is not due to FKBP12 functionality

Author keywords

Immunophilin FK506 binding protein; Immunosuppressant rapamycin; Schistosoma mansoni

Indexed keywords

DRUG RECEPTOR; RAPAMYCIN; RECEPTOR FKBP12; UNCLASSIFIED DRUG;

EID: 0036860230     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(02)00207-4     Document Type: Article
Times cited : (12)

References (31)
  • 1
    • 0032823635 scopus 로고    scopus 로고
    • Antifungal activities of antineoplastic agents: Saccharomyces cerevisiae as a model system to study drug action
    • Cardenas M.E., Cruz M.C., Del Poeta M., Chung N., Perfect J.R., Heitman J. Antifungal activities of antineoplastic agents: Saccharomyces cerevisiae as a model system to study drug action. Clin. Microbiol. Rev. 12:1999;583-611.
    • (1999) Clin. Microbiol. Rev. , vol.12 , pp. 583-611
    • Cardenas, M.E.1    Cruz, M.C.2    Del Poeta, M.3    Chung, N.4    Perfect, J.R.5    Heitman, J.6
  • 2
    • 0019494962 scopus 로고
    • Antischistosomal effects of cyclosporin A
    • Bueding E., Hawkins J., Cha Y.N. Antischistosomal effects of cyclosporin A. Agents Actions. 11:1981;380-383.
    • (1981) Agents Actions , vol.11 , pp. 380-383
    • Bueding, E.1    Hawkins, J.2    Cha, Y.N.3
  • 3
    • 0030250811 scopus 로고    scopus 로고
    • The antiparasite effects of cyclosporin A: Possible drug targets and clinical applications
    • Bell A., Roberts H.C., Chappell L.H. The antiparasite effects of cyclosporin A: possible drug targets and clinical applications. Gen. Pharmacol. 27:1996;963-971.
    • (1996) Gen. Pharmacol. , vol.27 , pp. 963-971
    • Bell, A.1    Roberts, H.C.2    Chappell, L.H.3
  • 4
    • 0028060031 scopus 로고
    • Roles of peptidyl-prolyl cis-trans isomerase and calcineurin in the mechanisms of antimalarial action of cyclosporin A, FK506, and rapamycin
    • Bell A., Wernli B., Franklin R.M. Roles of peptidyl-prolyl cis-trans isomerase and calcineurin in the mechanisms of antimalarial action of cyclosporin A, FK506, and rapamycin. Biochem. Pharmacol. 48:1994;495-503.
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 495-503
    • Bell, A.1    Wernli, B.2    Franklin, R.M.3
  • 6
    • 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. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell. 66:1991;807-815.
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu, J.1    Farmer J.D., Jr.2    Lane, W.S.3    Friedman, J.4    Weissman, I.5    Schreiber, S.L.6
  • 7
    • 0033869659 scopus 로고    scopus 로고
    • Sequence diversification of the FK506-binding proteins in several different genomes
    • Galat A. Sequence diversification of the FK506-binding proteins in several different genomes. Eur. J. Biochem. 267:2000;4945-4959.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4945-4959
    • Galat, A.1
  • 8
    • 0026738916 scopus 로고
    • FK506 binding protein associated with the calcium release channel (ryanodine receptor)
    • Jayaraman T., Brillantes A.M., Timerman A.P., et al. FK506 binding protein associated with the calcium release channel (ryanodine receptor). J. Biol. Chem. 267:1992;9474-9477.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9474-9477
    • Jayaraman, T.1    Brillantes, A.M.2    Timerman, A.P.3
  • 10
    • 0030576525 scopus 로고    scopus 로고
    • The immunophilin FKBP12 functions as a common inhibitor of the TGF beta family type I receptors
    • Wang T., Li B.Y., Danielson P.D., et al. The immunophilin FKBP12 functions as a common inhibitor of the TGF beta family type I receptors. Cell. 86:1996;435-444.
    • (1996) Cell , vol.86 , pp. 435-444
    • Wang, T.1    Li, B.Y.2    Danielson, P.D.3
  • 11
    • 0029133116 scopus 로고
    • X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex
    • Griffith J.P., Kim J.L., Kim E.E., et al. X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex. Cell. 82:1995;507-522.
    • (1995) Cell , vol.82 , pp. 507-522
    • Griffith, J.P.1    Kim, J.L.2    Kim, E.E.3
  • 12
    • 0025776523 scopus 로고
    • Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast
    • Heitman J., Movva N.R., Hall M.N. Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast. Science. 253:1991;905-909.
    • (1991) Science , vol.253 , pp. 905-909
    • Heitman, J.1    Movva, N.R.2    Hall, M.N.3
  • 13
    • 0028239893 scopus 로고
    • RAFT1: A mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs
    • Sabatini D.M., Erdjument-Bromage H., Lui M., Tempst P., Snyder S.H. RAFT1: a mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs. Cell. 78:1994;35-43.
    • (1994) Cell , vol.78 , pp. 35-43
    • Sabatini, D.M.1    Erdjument-Bromage, H.2    Lui, M.3    Tempst, P.4    Snyder, S.H.5
  • 14
    • 0026643141 scopus 로고
    • Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation
    • Clipstone N.A., Crabtree G.R. Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation. Nature. 357:1992;695-697.
    • (1992) Nature , vol.357 , pp. 695-697
    • Clipstone, N.A.1    Crabtree, G.R.2
  • 15
    • 0031008864 scopus 로고    scopus 로고
    • Calcineurin is required for virulence of Cryptococcus neoformans
    • Odom A., Muir S., Lim E., Toffaletti D.L., Perfect J., Heitman J. Calcineurin is required for virulence of Cryptococcus neoformans. EMBO J. 16:1997;2576-2589.
    • (1997) EMBO J. , vol.16 , pp. 2576-2589
    • Odom, A.1    Muir, S.2    Lim, E.3    Toffaletti, D.L.4    Perfect, J.5    Heitman, J.6
  • 16
    • 0027385382 scopus 로고
    • Protein phosphatase type 2B (calcineurin)-mediated, FK506-sensitive regulation of intracellular ions in yeast is an important determinant for adaptation to high salt stress conditions
    • Nakamura T., Liu Y., Hirata D., et al. Protein phosphatase type 2B (calcineurin)-mediated, FK506-sensitive regulation of intracellular ions in yeast is an important determinant for adaptation to high salt stress conditions. EMBO J. 12:1993;4063-4071.
    • (1993) EMBO J. , vol.12 , pp. 4063-4071
    • Nakamura, T.1    Liu, Y.2    Hirata, D.3
  • 17
    • 0033662883 scopus 로고    scopus 로고
    • Praziquantel: Is there real resistance and are there alternatives?
    • Cioli D. Praziquantel: is there real resistance and are there alternatives? Curr. Opin. Infect. Dis. 13:2000;659-663.
    • (2000) Curr. Opin. Infect. Dis. , vol.13 , pp. 659-663
    • Cioli, D.1
  • 18
    • 0029598801 scopus 로고
    • Characterization of a Schistosoma mansoni cDNA encoding a B-like cyclophilin and its expression in Escherichia coli
    • Klinkert M.Q., Bugli F., Engels B., Carrasquillo E., Valle C., Cioli D. Characterization of a Schistosoma mansoni cDNA encoding a B-like cyclophilin and its expression in Escherichia coli. Mol. Biochem. Parasitol. 75:1995;99-111.
    • (1995) Mol. Biochem. Parasitol. , vol.75 , pp. 99-111
    • Klinkert, M.Q.1    Bugli, F.2    Engels, B.3    Carrasquillo, E.4    Valle, C.5    Cioli, D.6
  • 19
    • 0031754226 scopus 로고    scopus 로고
    • Cyclosporins: Lack of correlation between antischistosomal properties and inhibition of cyclophilin isomerase activity
    • Khattab A., Pica-Mattoccia L., Klinkert M.Q., Wenger R., Cioli D. Cyclosporins: lack of correlation between antischistosomal properties and inhibition of cyclophilin isomerase activity. Exp. Parasitol. 90:1998;103-109.
    • (1998) Exp. Parasitol. , vol.90 , pp. 103-109
    • Khattab, A.1    Pica-Mattoccia, L.2    Klinkert, M.Q.3    Wenger, R.4    Cioli, D.5
  • 20
    • 0032932001 scopus 로고    scopus 로고
    • Assay of Schistosoma mansoni calcineurin phosphatase activity and assessment of its role in parasite survival
    • Khattab A., Pica-Mattoccia L., Wenger R., Cioli D., Klinkert M.Q. Assay of Schistosoma mansoni calcineurin phosphatase activity and assessment of its role in parasite survival. Mol. Biochem. Parasitol. 99:1999;269-273.
    • (1999) Mol. Biochem. Parasitol. , vol.99 , pp. 269-273
    • Khattab, A.1    Pica-Mattoccia, L.2    Wenger, R.3    Cioli, D.4    Klinkert, M.Q.5
  • 21
    • 0033746145 scopus 로고    scopus 로고
    • Molecular cloning of Schistosoma mansoni calcineurin subunits and immunolocalization to the excretory system
    • Mecozzi B., Rossi A., Lazzaretti P., et al. Molecular cloning of Schistosoma mansoni calcineurin subunits and immunolocalization to the excretory system. Mol. Biochem. Parasitol. 110:2000;333-343.
    • (2000) Mol. Biochem. Parasitol. , vol.110 , pp. 333-343
    • Mecozzi, B.1    Rossi, A.2    Lazzaretti, P.3
  • 23
    • 0025868143 scopus 로고
    • Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay
    • Kofron J.L., Kuzmic P., Kishore V., Colon-Bonilla E., Rich D.H. Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay. Biochemistry. 30:1991;6127-6134.
    • (1991) Biochemistry , vol.30 , pp. 6127-6134
    • Kofron, J.L.1    Kuzmic, P.2    Kishore, V.3    Colon-Bonilla, E.4    Rich, D.H.5
  • 24
    • 0029871347 scopus 로고    scopus 로고
    • PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae
    • Wach A. PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae. Yeast. 12:1996;259-265.
    • (1996) Yeast , vol.12 , pp. 259-265
    • Wach, A.1
  • 27
    • 0029064085 scopus 로고
    • Schistosoma mansoni: Characterization of p50, an immunophilin
    • Osman A., Kiang D., Lo Verde P.T., Karim A.M. Schistosoma mansoni: characterization of p50, an immunophilin. Exp. Parasitol. 80:1995;550-559.
    • (1995) Exp. Parasitol. , vol.80 , pp. 550-559
    • Osman, A.1    Kiang, D.2    Lo Verde, P.T.3    Karim, A.M.4
  • 29
    • 0029842109 scopus 로고    scopus 로고
    • Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP
    • Choi J., Chen J., Schreiber S.L., Clardy J. Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP. Science. 273:1996;239-242.
    • (1996) Science , vol.273 , pp. 239-242
    • Choi, J.1    Chen, J.2    Schreiber, S.L.3    Clardy, J.4
  • 30
    • 0029079643 scopus 로고
    • FK506 binding protein mutational analysis. Defining the surface residue contributions to stability of the calcineurin co-complex
    • Futer O., DeCenzo M.T., Aldape R.A., Livingston D.J. FK506 binding protein mutational analysis. Defining the surface residue contributions to stability of the calcineurin co-complex. J. Biol. Chem. 270:1995;18935-18940.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18935-18940
    • Futer, O.1    DeCenzo, M.T.2    Aldape, R.A.3    Livingston, D.J.4
  • 31
    • 0028825698 scopus 로고
    • TOR mutations confer rapamycin resistance by preventing interaction with FKBP12-rapamycin
    • Lorenz M.C., Heitman J. TOR mutations confer rapamycin resistance by preventing interaction with FKBP12-rapamycin. J. Biol. Chem. 270:1995;27531-27537.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27531-27537
    • Lorenz, M.C.1    Heitman, J.2


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