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Volumn 44, Issue 1, 2000, Pages 143-149

Immunosuppressive and nonimmunosuppressive cyclosporine analogs are toxic to the opportunistic fungal pathogen Cryptococcus neoformans via cyclophilin-dependent inhibition of calcineurin

Author keywords

[No Author keywords available]

Indexed keywords

ANTIFUNGAL AGENT; ANTIINFECTIVE AGENT; CALCINEURIN; CYCLOPHILIN A; CYCLOSPORIN DERIVATIVE; IMMUNOSUPPRESSIVE AGENT; INTERLEUKIN 2; PHOSPHOPROTEIN PHOSPHATASE;

EID: 0033986998     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.44.1.143-149.2000     Document Type: Article
Times cited : (120)

References (63)
  • 1
    • 0026693772 scopus 로고
    • Cyclosporine and its analogue SDZ IMM 125 mediate very similar effects on T-cell activation - A comparative analysis in vitro
    • Baumann, G., E. Andersen, V. Quesniaux, and M. K. Eberle. 1992. Cyclosporine and its analogue SDZ IMM 125 mediate very similar effects on T-cell activation - a comparative analysis in vitro. Transplant. Proc. 24:43-48.
    • (1992) Transplant. Proc. , vol.24 , pp. 43-48
    • Baumann, G.1    Andersen, E.2    Quesniaux, V.3    Eberle, M.K.4
  • 3
    • 0027360244 scopus 로고
    • Correlation of in vitro fluconazole resistance of Candida isolates in relation to therapy and symptoms of individuals seropositive for human immunodeficiency virus type 1
    • Cameron, M. L., W. A. Schell, S. Bruch, J. Bartlett, H. A. Waskin, and J. R. Perfect. 1993. Correlation of in vitro fluconazole resistance of Candida isolates in relation to therapy and symptoms of individuals seropositive for human immunodeficiency virus type 1. Antimicrob. Agents Chemother. 37: 2449-2453.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 2449-2453
    • Cameron, M.L.1    Schell, W.A.2    Bruch, S.3    Bartlett, J.4    Waskin, H.A.5    Perfect, J.R.6
  • 4
    • 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. 1994. Immunophilins interact with calcineurin in the absence of exogenous immunosuppressive ligands. EMBO J. 13:5944-5957.
    • (1994) 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
  • 5
    • 0029101514 scopus 로고
    • Mutations that perturb cyclophilin A ligand binding pocket confer cyclosporin A resistance in Saccharomyces cerevisiae
    • Cardenas, M. E., E. Lim, and J. Heitman. 1995. Mutations that perturb cyclophilin A ligand binding pocket confer cyclosporin A resistance in Saccharomyces cerevisiae. J. Biol. Chem. 270:20997-21002.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20997-21002
    • Cardenas, M.E.1    Lim, E.2    Heitman, J.3
  • 7
    • 0028998848 scopus 로고
    • Targets of immunophilin-immunosuppressant complexes are distinct highly conserved regions of calcineurin A
    • Cardenas, M. E., R. S. Muir, T. Breuder, and J. Heitman. 1995. Targets of immunophilin-immunosuppressant complexes are distinct highly conserved regions of calcineurin A. EMBO J. 14:2772-2783.
    • (1995) EMBO J. , vol.14 , pp. 2772-2783
    • Cardenas, M.E.1    Muir, R.S.2    Breuder, T.3    Heitman, J.4
  • 8
    • 0031789983 scopus 로고    scopus 로고
    • Signaltransduction cascades as targets for therapeutic intervention by natural products
    • Cardenas, M. E., A. Sanfridson, N. S. Cutler, and J. Heitman. 1998. Signaltransduction cascades as targets for therapeutic intervention by natural products. Trends Biotechnol. 16:427-433.
    • (1998) Trends Biotechnol. , vol.16 , pp. 427-433
    • Cardenas, M.E.1    Sanfridson, A.2    Cutler, N.S.3    Heitman, J.4
  • 9
    • 0029559927 scopus 로고
    • Molecular mechanisms of immunosuppression by cyclosporine, FK506, and rapamycin
    • Cardenas, M. E., D. Zhu, and J. Heitman. 1995. Molecular mechanisms of immunosuppression by cyclosporine, FK506, and rapamycin. Curr. Opin. Nephrol. Hypertens. 4:472-477.
    • (1995) Curr. Opin. Nephrol. Hypertens. , vol.4 , pp. 472-477
    • Cardenas, M.E.1    Zhu, D.2    Heitman, J.3
  • 11
    • 0026643141 scopus 로고
    • Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation
    • Clipstone, N. A., and G. R. Crabtree. 1992. Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation. Nature 357:695-697.
    • (1992) Nature , vol.357 , pp. 695-697
    • Clipstone, N.A.1    Crabtree, G.R.2
  • 14
    • 0025913953 scopus 로고
    • Yeast has homologs (CNA1 and CNA2 gene products) of mammalian calcineurin, a calmodulin-regulated phosphoprotein phosphatase
    • Cyert, M. S., R. Kunisawa, D. Kaim, and J. Thorner. 1991. Yeast has homologs (CNA1 and CNA2 gene products) of mammalian calcineurin, a calmodulin-regulated phosphoprotein phosphatase. Proc. Natl. Acad. Sci. USA 88:7376-7380.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7376-7380
    • Cyert, M.S.1    Kunisawa, R.2    Kaim, D.3    Thorner, J.4
  • 15
    • 0026637095 scopus 로고
    • 2+/calmodulin-dependent phosphoprotein phosphatases is required for adaptation to pheromone
    • 2+/calmodulin-dependent phosphoprotein phosphatases is required for adaptation to pheromone. Mol. Cell. Biol. 12:3460-3469.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3460-3469
    • Cyert, M.S.1    Thorner, J.2
  • 17
    • 0000404916 scopus 로고    scopus 로고
    • Peptidyl-prolyl isomerases (PPIases)
    • S. Tooze (ed.). Oxford University Press, Oxford, United Kingdom
    • Dolinski, K., and J. Heitman. 1997. Peptidyl-prolyl isomerases (PPIases), p. 359-369. In S. Tooze (ed.), Guidebook to molecular chaperones and protein folding catalysts. Oxford University Press, Oxford, United Kingdom.
    • (1997) Guidebook to Molecular Chaperones and Protein Folding Catalysts , pp. 359-369
    • Dolinski, K.1    Heitman, J.2
  • 18
    • 0025871394 scopus 로고
    • Nuclear association of a T-cell transcription factor blocked by FK-506 and cyclosporin A
    • Flanagan, W. M., B. Corthésy, R. J. Bram, and G. R. Crabtree. 1991 Nuclear association of a T-cell transcription factor blocked by FK-506 and cyclosporin A. Nature 352:803-807.
    • (1991) Nature , vol.352 , pp. 803-807
    • Flanagan, W.M.1    Corthésy, B.2    Bram, R.J.3    Crabtree, G.R.4
  • 19
    • 0026619467 scopus 로고
    • Calcineurin mediates inhibition by FK506 and cyclosporin of recovery from α-factor arrest in yeast
    • Foor, F., S. A. Parent, N. Morin, A. M. Dahl, N. Ramadan, G. Chrebet, K. A. Bostian, and J. B. Nielsen. 1992. Calcineurin mediates inhibition by FK506 and cyclosporin of recovery from α-factor arrest in yeast. Nature 360:682-684.
    • (1992) Nature , vol.360 , pp. 682-684
    • Foor, F.1    Parent, S.A.2    Morin, N.3    Dahl, A.M.4    Ramadan, N.5    Chrebet, G.6    Bostian, K.A.7    Nielsen, J.B.8
  • 21
    • 0024453536 scopus 로고
    • Yeast cyclophilin: Isolation and characterization of the protein, cDNA and gene
    • Haendler, B., R. Keller, P. C. Hiestand, H. P. Kocher, G. Wegmann, and N. R. Movva. 1989. Yeast cyclophilin: isolation and characterization of the protein, cDNA and gene. Gene 83:39-46.
    • (1989) Gene , vol.83 , pp. 39-46
    • Haendler, B.1    Keller, R.2    Hiestand, P.C.3    Kocher, H.P.4    Wegmann, G.5    Movva, N.R.6
  • 23
    • 0026857926 scopus 로고
    • Proline isomerases at the crossroads of protein folding, signal transduction, and immunosuppression
    • Heitman, J., N. R. Movva, and M. N. Hall. 1992. Proline isomerases at the crossroads of protein folding, signal transduction, and immunosuppression. New Biol. 4:448-460.
    • (1992) New Biol. , vol.4 , pp. 448-460
    • Heitman, J.1    Movva, N.R.2    Hall, M.N.3
  • 24
    • 0025776523 scopus 로고
    • Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast
    • Heitman, J., N. R. Movva, and M. N. Hall. 1991. Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast. Science 253:905-909.
    • (1991) Science , vol.253 , pp. 905-909
    • Heitman, J.1    Movva, N.R.2    Hall, M.N.3
  • 25
    • 0026012156 scopus 로고
    • FK506-binding protein proline rotamase is a target for the immunosuppressive agent FK506 in Saccharomyces cerevisiae
    • Heitman, J., N. R. Movva, P. C. Hiestand, and M. N. Hall. 1991. FK506-binding protein proline rotamase is a target for the immunosuppressive agent FK506 in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 88:1948-1952.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1948-1952
    • Heitman, J.1    Movva, N.R.2    Hiestand, P.C.3    Hall, M.N.4
  • 27
    • 0032602932 scopus 로고    scopus 로고
    • Calcineurin structure, function, and inhibition
    • Hemenway, C. S., and J. Heitman. 1999. Calcineurin structure, function, and inhibition. Cell Biochem. Biophys. 30:115-151.
    • (1999) Cell Biochem. Biophys. , vol.30 , pp. 115-151
    • Hemenway, C.S.1    Heitman, J.2
  • 28
    • 0028234434 scopus 로고
    • The antimicrobial activities of cyclosporine, FK506, and rapamycin
    • High, K. P. 1994. The antimicrobial activities of cyclosporine, FK506, and rapamycin. Transplantation 57:1689-1700.
    • (1994) Transplantation , vol.57 , pp. 1689-1700
    • High, K.P.1
  • 29
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 31
    • 0025858482 scopus 로고
    • Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy
    • Kallen, J., C. Spitzfaden, M. G. M. Zurini, G. Wider, H. Widmer, K. Wuthrich, and M. D. Walkinshaw. 1991. Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy. Nature 353:276-279.
    • (1991) Nature , vol.353 , 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
  • 32
    • 0027483416 scopus 로고
    • Crystal structure of cyclophilin A complexed with substrate ala-pro suggests a solvent-assisted mechanism of cis-trans isomerization
    • Ke, H., D. Mayrose, and W. Cao. 1993. Crystal structure of cyclophilin A complexed with substrate ala-pro suggests a solvent-assisted mechanism of cis-trans isomerization. Proc. Natl. Acad. Sci. USA 90:3324-3328.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3324-3328
    • Ke, H.1    Mayrose, D.2    Cao, W.3
  • 33
    • 0026042453 scopus 로고
    • Crystal structure of recombinant human T-cell cyclophilin A at 2.5 A resolution
    • Ke, H., L. D. Zydowsky, J. Liu, and C. T. Walsh. 1991. Crystal structure of recombinant human T-cell cyclophilin A at 2.5 A resolution. Proc. Natl. Acad. Sci. USA 88:9483-9487.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9483-9487
    • Ke, H.1    Zydowsky, L.D.2    Liu, J.3    Walsh, C.T.4
  • 34
    • 0021013645 scopus 로고
    • Cyclosporin A inhibits Coccidioides immitis in vitro and in vivo
    • Kirkland, T. N., and J. Fierer. 1983. Cyclosporin A inhibits Coccidioides immitis in vitro and in vivo. Antimicrob. Agents Chemother. 24:921-924.
    • (1983) Antimicrob. Agents Chemother. , vol.24 , pp. 921-924
    • Kirkland, T.N.1    Fierer, J.2
  • 35
    • 0002427193 scopus 로고
    • Cryptococcosis
    • Lea & Febiger, Malvern, Pa.
    • Kwon-Chung, K. J., and J. E. Bennett. 1992. Cryptococcosis, p. 397-446. In Medical mycology. Lea & Febiger, Malvern, Pa.
    • (1992) Medical Mycology , pp. 397-446
    • Kwon-Chung, K.J.1    Bennett, J.E.2
  • 37
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
    • Liu, J., J. D. Farmer, W. S. Lane, J. Friedman, I. Weissman, and S. L. Schreiber. 1991. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 66:807-815.
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu, J.1    Farmer, J.D.2    Lane, W.S.3    Friedman, J.4    Weissman, I.5    Schreiber, S.L.6
  • 38
    • 0003144621 scopus 로고
    • The MLR in the mouse
    • L. Lefkovits and B. Pernis (ed.). Academic Press, New York, N.Y.
    • Meo, T. 1979. The MLR in the mouse, p. 227-239. In L. Lefkovits and B. Pernis (ed.), Immunological methods. Academic Press, New York, N.Y.
    • (1979) Immunological Methods , pp. 227-239
    • Meo, T.1
  • 39
    • 0027772159 scopus 로고
    • X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 A resolution
    • Mikol, V., J. Kallen, G. Pflugl, and M. D. Walkinshaw. 1993. X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 A resolution. J. Mol. Biol. 234:1119-1130.
    • (1993) J. Mol. Biol. , vol.234 , pp. 1119-1130
    • Mikol, V.1    Kallen, J.2    Pflugl, G.3    Walkinshaw, M.D.4
  • 40
    • 0028786641 scopus 로고
    • Cryptococcosis in the era of AIDS - 100 years after the discovery of Cryptococcus neoformans
    • Mitchell, T. G., and J. R. Perfect. 1995. Cryptococcosis in the era of AIDS - 100 years after the discovery of Cryptococcus neoformans. Clin. Microbiol. Rev. 8:515-548.
    • (1995) Clin. Microbiol. Rev. , vol.8 , pp. 515-548
    • Mitchell, T.G.1    Perfect, J.R.2
  • 41
    • 0023882309 scopus 로고
    • Cyclosporin A inhibits the growth of Cryptococcus neoformans in a murine model
    • Mody, C. H., G. B. Toews, and M. F. Lipscomb. 1988. Cyclosporin A inhibits the growth of Cryptococcus neoformans in a murine model. Infect. Immun. 56:7-12.
    • (1988) Infect. Immun. , vol.56 , pp. 7-12
    • Mody, C.H.1    Toews, G.B.2    Lipscomb, M.F.3
  • 42
    • 0024493070 scopus 로고
    • Treatment of murine cryptococcosis with cyclosporin-A in normal and athymic mice
    • Mody, C. H., G. B. Toews, and M. F. Lipscomb. 1989. Treatment of murine cryptococcosis with cyclosporin-A in normal and athymic mice. Am. Rev. Respir. Dis. 139:8-13.
    • (1989) Am. Rev. Respir. Dis. , vol.139 , pp. 8-13
    • Mody, C.H.1    Toews, G.B.2    Lipscomb, M.F.3
  • 43
    • 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., V. Liu, D. Hirata, H. Namba, S.-I. Harada, T. Hirokawa, and T. Miyakawa. 1993. 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: 4063-4071.
    • (1993) EMBO J. , vol.12 , pp. 4063-4071
    • Nakamura, T.1    Liu, V.2    Hirata, D.3    Namba, H.4    Harada, S.-I.5    Hirokawa, T.6    Miyakawa, T.7
  • 46
    • 0026632557 scopus 로고
    • FK-506- and CsA-sensitive activation of the interleukin-2 promoter by calcineurin
    • O'Keefe, S. J., J. I. Tamura, R. L. Kincaid, M. J. Tocci, and E. A. O'Neill. 1992. FK-506- and CsA-sensitive activation of the interleukin-2 promoter by calcineurin. Nature 357:692-694.
    • (1992) Nature , vol.357 , pp. 692-694
    • O'Keefe, S.J.1    Tamura, J.I.2    Kincaid, R.L.3    Tocci, M.J.4    O'Neill, E.A.5
  • 47
    • 0031008864 scopus 로고    scopus 로고
    • Calcineurin is required for virulence of Cryptococcus neoformans
    • Odom, A., S. Muir, E. Lim, D. L. Toffaletti, J. Perfect, and J. Heitman. 1997. Calcineurin is required for virulence of Cryptococcus neoformans. EMBO J. 16:2576-2589.
    • (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
  • 48
    • 0031028176 scopus 로고    scopus 로고
    • The immunosuppressant FK506 and its nonimmunosuppressive analog L-685,818 are toxic to Cryptococcus neoformans by inhibition of a common target protein
    • Odom, A., M. D. Poeta, J. Perfect, and J. Heitman. 1997. The immunosuppressant FK506 and its nonimmunosuppressive analog L-685,818 are toxic to Cryptococcus neoformans by inhibition of a common target protein. Antimicrob. Agents Chemother. 41:156-161.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 156-161
    • Odom, A.1    Poeta, M.D.2    Perfect, J.3    Heitman, J.4
  • 49
    • 0027987183 scopus 로고
    • Increased fluconazole resistance of Cryptococcus neoformans isolated from a patient with AIDS and recurrent meningitis
    • Paugam, A., J. Dupouy-Camet, P. Blanche, J. P. Gangneux, C. Tourte-Schaefer, and D. Sicard. 1994. Increased fluconazole resistance of Cryptococcus neoformans isolated from a patient with AIDS and recurrent meningitis. Clin. Infect. Dis. 19:975-976.
    • (1994) Clin. Infect. Dis. , vol.19 , pp. 975-976
    • Paugam, A.1    Dupouy-Camet, J.2    Blanche, P.3    Gangneux, J.P.4    Tourte-Schaefer, C.5    Sicard, D.6
  • 50
    • 0021929967 scopus 로고
    • Effects of cyclosporine in experimental cryptococcal meningitis
    • Perfect, J. R., and D. T. Durack. 1985. Effects of cyclosporine in experimental cryptococcal meningitis. Infect. Immun. 50:22-26.
    • (1985) Infect. Immun. , vol.50 , pp. 22-26
    • Perfect, J.R.1    Durack, D.T.2
  • 53
    • 0027256737 scopus 로고
    • Prolyl isomerase - Enzymatic catalysis of slow protein-folding reactions
    • Schmid, F. X. 1993. Prolyl isomerase - enzymatic catalysis of slow protein-folding reactions. Annu. Rev. Biophys. Biomol. Struct. 22:123-143.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 123-143
    • Schmid, F.X.1
  • 54
    • 0027964239 scopus 로고
    • Human cyclophilin C: Primary structure, tissue distribution, and determination of binding specificity for cyclosporins
    • Schneider, H., N. Charara, R. Schmitz, S. Wehrli, V. Mikol, M. G. M. Zurini, V. F. J. Quesniaux, and N. R. Movva. 1994. Human cyclophilin C: primary structure, tissue distribution, and determination of binding specificity for cyclosporins. Biochemistry 33:8218-8224.
    • (1994) Biochemistry , vol.33 , pp. 8218-8224
    • Schneider, H.1    Charara, N.2    Schmitz, R.3    Wehrli, S.4    Mikol, V.5    Zurini, M.G.M.6    Quesniaux, V.F.J.7    Movva, N.R.8
  • 55
    • 0026575932 scopus 로고
    • The mechanism of action of cyclosporin A and FK506
    • Schreiber, S. L., and G. R. Crabtree. 1992. The mechanism of action of cyclosporin A and FK506. Immunol. Today 13:136-142.
    • (1992) Immunol. Today , vol.13 , pp. 136-142
    • Schreiber, S.L.1    Crabtree, G.R.2
  • 57
    • 0015609711 scopus 로고
    • In vitro stimulation of murine spleen cells using a microculture system and a multiple automated sample harvester
    • Strong, D. M., A. A. Ahmed, G. B. Thurman, and K. W. Sell. 1973. In vitro stimulation of murine spleen cells using a microculture system and a multiple automated sample harvester. J. Immunol. Methods 2:279-291.
    • (1973) J. Immunol. Methods , vol.2 , pp. 279-291
    • Strong, D.M.1    Ahmed, A.A.2    Thurman, G.B.3    Sell, K.W.4
  • 59
    • 0027467293 scopus 로고
    • Gene transfer in Cryptococcus neoformans by use of biolistic delivery of DNA
    • Toffaletti, D. L., T. H. Rude, S. A. Johnston, D. T. Durack, and J. R. Perfect. 1993. Gene transfer in Cryptococcus neoformans by use of biolistic delivery of DNA. J. Bacteriol. 175:1405-1411.
    • (1993) J. Bacteriol. , vol.175 , pp. 1405-1411
    • Toffaletti, D.L.1    Rude, T.H.2    Johnston, S.A.3    Durack, D.T.4    Perfect, J.R.5
  • 60
    • 0024844391 scopus 로고
    • Sensitivity to cyclosporin A is mediated by cyclophilin in Neurospora crassa and Saccharomyces cerevisiae
    • Tropschug, M., I. B. Barthelmess, and W. Neupert. 1989. Sensitivity to cyclosporin A is mediated by cyclophilin in Neurospora crassa and Saccharomyces cerevisiae. Nature 342:953-955.
    • (1989) Nature , vol.342 , pp. 953-955
    • Tropschug, M.1    Barthelmess, I.B.2    Neupert, W.3
  • 61
    • 0000334044 scopus 로고    scopus 로고
    • Antifungal drug resistance in Candida albicans
    • White, T. C. 1998. Antifungal drug resistance in Candida albicans. ASM News 63:427-433.
    • (1998) ASM News , vol.63 , pp. 427-433
    • White, T.C.1
  • 62
    • 0031969879 scopus 로고    scopus 로고
    • Clinical, cellular, and molecular factors that contribute to antifungal drug resistance
    • White, T. C., K. A. Marr, and R. A. Bowden. 1998. Clinical, cellular, and molecular factors that contribute to antifungal drug resistance. Clin. Microbiol. Rev. 11:382-402.
    • (1998) Clin. Microbiol. Rev. , vol.11 , pp. 382-402
    • White, T.C.1    Marr, K.A.2    Bowden, R.A.3
  • 63
    • 0020457545 scopus 로고
    • The filamentous phage (Ff) as vectors for recombinant DNA - A review
    • Zinder, N. D., and J. D. Boeke. 1982. The filamentous phage (Ff) as vectors for recombinant DNA - a review. Gene 19:1-10.
    • (1982) Gene , vol.19 , pp. 1-10
    • Zinder, N.D.1    Boeke, J.D.2


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