메뉴 건너뛰기




Volumn 10, Issue 4, 2005, Pages 355-364

Cell-based assays to detect inhibitors of fungal mRNA capping enzymes and characterization of sinefungin as a cap methyltransferase inhibitor

Author keywords

(guanine 7 ) methyltransferase; Candida; mRNA cap; Sinefungin; Yeast

Indexed keywords

FUNGAL RNA; METHYLTRANSFERASE INHIBITOR; SINEFUNGIN;

EID: 20444415618     PISSN: 10870571     EISSN: None     Source Type: Journal    
DOI: 10.1177/1087057104273333     Document Type: Article
Times cited : (25)

References (53)
  • 1
    • 0031572262 scopus 로고    scopus 로고
    • Viral and cellular enzymes involved in synthesis of mRNA cap structure
    • Bisaillon M, Lemay G: Viral and cellular enzymes involved in synthesis of mRNA cap structure. Virology 1997;236:1-7.
    • (1997) Virology , vol.236 , pp. 1-7
    • Bisaillon, M.1    Lemay, G.2
  • 2
    • 0032077454 scopus 로고    scopus 로고
    • Accelerated mRNA decay in conditional mutants of yeast mRNA capping enzyme
    • Schwer B, Mao X, Shuman S: Accelerated mRNA decay in conditional mutants of yeast mRNA capping enzyme. Nucleic Acids Res 1998;26:2050-2057.
    • (1998) Nucleic Acids Res , vol.26 , pp. 2050-2057
    • Schwer, B.1    Mao, X.2    Shuman, S.3
  • 3
    • 0035201941 scopus 로고    scopus 로고
    • Structure, mechanism, and evolution of the mRNA capping apparatus
    • Shuman S: Structure, mechanism, and evolution of the mRNA capping apparatus. Prog Nucleic Acid Res Mol Biol 2001;66:1-40.
    • (2001) Prog Nucleic Acid Res Mol Biol , vol.66 , pp. 1-40
    • Shuman, S.1
  • 4
    • 0026733001 scopus 로고
    • mRNA capping enzyme: Isolation and characterization of the gene encoding mRNA guanylytransferase subunit from Saccharomyces cerevisiae
    • Shibagaki Y, Itoh N, Yamada H, Nagata S, Mizumoto K: mRNA capping enzyme: isolation and characterization of the gene encoding mRNA guanylytransferase subunit from Saccharomyces cerevisiae. J Biol Chem 1992;267:9521-9528.
    • (1992) J Biol Chem , vol.267 , pp. 9521-9528
    • Shibagaki, Y.1    Itoh, N.2    Yamada, H.3    Nagata, S.4    Mizumoto, K.5
  • 5
    • 0029001790 scopus 로고
    • Yeast mRNA cap methyltransferase is a 50-kilodalton protein encoded by an essential gene
    • Mao X, Schwer B, Shuman S: Yeast mRNA cap methyltransferase is a 50-kilodalton protein encoded by an essential gene. Mol Cell Biol 1995;15:4167-4174.
    • (1995) Mol Cell Biol , vol.15 , pp. 4167-4174
    • Mao, X.1    Schwer, B.2    Shuman, S.3
  • 6
    • 0031561370 scopus 로고    scopus 로고
    • Isolation and characterization of the yeast mRNA capping enzyme beta subunit gene encoding RNA 5′-triphosphatase, which is essential for cell viability
    • Tsukamoto T, Shibagaki Y, Imajoh-Ohmi S, et al: Isolation and characterization of the yeast mRNA capping enzyme beta subunit gene encoding RNA 5′-triphosphatase, which is essential for cell viability. Biochem Biophys Res Commun 1997;239:116-122.
    • (1997) Biochem Biophys Res Commun , vol.239 , pp. 116-122
    • Tsukamoto, T.1    Shibagaki, Y.2    Imajoh-Ohmi, S.3
  • 7
    • 0032540231 scopus 로고    scopus 로고
    • The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxyl-terminal domain of RNA polymerase II
    • Ho CK, Sriskanda V, McCracken S, Bentley D, Schwer B, Shuman S: The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxyl-terminal domain of RNA polymerase II. J Biol Chem 1998;273:9577-9585.
    • (1998) J Biol Chem , vol.273 , pp. 9577-9585
    • Ho, C.K.1    Sriskanda, V.2    McCracken, S.3    Bentley, D.4    Schwer, B.5    Shuman, S.6
  • 8
    • 0033522898 scopus 로고    scopus 로고
    • Characterization of human, Schizosacchammyces pombe, and Candida albicans mRNA cap methyltransferases and complete replacement of the yeast capping apparatus by mammalian enzymes
    • Saha N, Schwer B, Shuman S: Characterization of human, Schizosacchammyces pombe, and Candida albicans mRNA cap methyltransferases and complete replacement of the yeast capping apparatus by mammalian enzymes. J Biol Chem 1999;274:16553-16562.
    • (1999) J Biol Chem , vol.274 , pp. 16553-16562
    • Saha, N.1    Schwer, B.2    Shuman, S.3
  • 9
    • 0028172876 scopus 로고
    • Covalent catalysis in nucleotidyl transfer reactions: Essential motifs in Saccharomyces cerevisiae RNA capping enzyme are conserved in Schizosaccharomyces pombe and viral capping enzymes and among polynucleotide ligases
    • Shuman S, Liu Y, Schwer B: Covalent catalysis in nucleotidyl transfer reactions: essential motifs in Saccharomyces cerevisiae RNA capping enzyme are conserved in Schizosaccharomyces pombe and viral capping enzymes and among polynucleotide ligases. Proc Natl Acad Sci USA 1994;91:12046-12050.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12046-12050
    • Shuman, S.1    Liu, Y.2    Schwer, B.3
  • 10
    • 19044390412 scopus 로고    scopus 로고
    • RNA triphosphatase is essential in Schizosaccharomyces pombe and Candida albicans
    • Pei Y, Schwer B, Saiz J, Fisher RP, Shuman S: RNA triphosphatase is essential in Schizosaccharomyces pombe and Candida albicans. BMC Microbiol 2001;1:29.
    • (2001) BMC Microbiol , vol.1 , pp. 29
    • Pei, Y.1    Schwer, B.2    Saiz, J.3    Fisher, R.P.4    Shuman, S.5
  • 11
    • 0032508492 scopus 로고    scopus 로고
    • Isolation and characterization of the Candida albicans gene for mRNA 5′-triphosphatase: Association of mRNA 5′-triphosphatase and mRNA 5′-guanylyltransferase activities is essential for the function of mRNA 5′-capping enzyme in vivo
    • Yamada-Okabe T, Mio T, Matsui M, Kashima Y, Arisawa M, Yamada-Okabe H: Isolation and characterization of the Candida albicans gene for mRNA 5′-triphosphatase: association of mRNA 5′-triphosphatase and mRNA 5′-guanylyltransferase activities is essential for the function of mRNA 5′-capping enzyme in vivo. FEBS Lett 1998;435:49-54.
    • (1998) FEBS Lett , vol.435 , pp. 49-54
    • Yamada-Okabe, T.1    Mio, T.2    Matsui, M.3    Kashima, Y.4    Arisawa, M.5    Yamada-Okabe, H.6
  • 12
    • 0029764473 scopus 로고    scopus 로고
    • Isolation of the mRNA-capping enzyme and ferric-reductase-related genes from Candida albicans
    • Yamada-Okabe T, Shimmi O, Doi R, Mizumoto K, Arisawa M, Yamada-Okabe H: Isolation of the mRNA-capping enzyme and ferric-reductase-related genes from Candida albicans. Microbiology 1996;142(Pt 9):2515-2523.
    • (1996) Microbiology , vol.142 , Issue.PART 9 , pp. 2515-2523
    • Yamada-Okabe, T.1    Shimmi, O.2    Doi, R.3    Mizumoto, K.4    Arisawa, M.5    Yamada-Okabe, H.6
  • 13
    • 3543026832 scopus 로고    scopus 로고
    • Genetic, physical, and functional interactions between the triphosphatase and guanylyltransferase components of the yeast mRNA capping apparatus
    • Ho CK, Schwer B, Shuman S: Genetic, physical, and functional interactions between the triphosphatase and guanylyltransferase components of the yeast mRNA capping apparatus. Mol Cell Biol 1998;18:5189-5198.
    • (1998) Mol Cell Biol , vol.18 , pp. 5189-5198
    • Ho, C.K.1    Schwer, B.2    Shuman, S.3
  • 14
    • 0030660264 scopus 로고    scopus 로고
    • Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II
    • Yue Z, Maldonado E, Pillutla R, Cho H, Reinberg D, Shatkin AJ: Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II. Proc Natl Acad Sci USA 1997;94:12898-12903.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12898-12903
    • Yue, Z.1    Maldonado, E.2    Pillutla, R.3    Cho, H.4    Reinberg, D.5    Shatkin, A.J.6
  • 16
    • 0032545284 scopus 로고    scopus 로고
    • Yeast and viral RNA 5′ triphosphatases comprise a new nucleoside triphosphatase family
    • Ho CK, Pei Y, Shuman S: Yeast and viral RNA 5′ triphosphatases comprise a new nucleoside triphosphatase family. J Biol Chem 1998;273:34151-34156.
    • (1998) J Biol Chem , vol.273 , pp. 34151-34156
    • Ho, C.K.1    Pei, Y.2    Shuman, S.3
  • 17
    • 0033601125 scopus 로고    scopus 로고
    • Structure and mechanism of yeast RNA triphosphatase: An essential component of the mRNA capping apparatus
    • Lima CD, Wang LK, Shuman S: Structure and mechanism of yeast RNA triphosphatase: an essential component of the mRNA capping apparatus. Cell 1999;99:533-543.
    • (1999) Cell , vol.99 , pp. 533-543
    • Lima, C.D.1    Wang, L.K.2    Shuman, S.3
  • 18
    • 0032849895 scopus 로고    scopus 로고
    • Mutational analyses of yeast RNA triphosphatases highlight a common mechanism of metal-dependent NTP hydrolysis and a means of targeting enzymes to pre-mRNAs in vivo by fusion to the guanylyltransferase component of the capping apparatus
    • Pei Y, Ho CK, Schwer B, Shuman S: Mutational analyses of yeast RNA triphosphatases highlight a common mechanism of metal-dependent NTP hydrolysis and a means of targeting enzymes to pre-mRNAs in vivo by fusion to the guanylyltransferase component of the capping apparatus. J Biol Chem 1999;274:28865-28874.
    • (1999) J Biol Chem , vol.274 , pp. 28865-28874
    • Pei, Y.1    Ho, C.K.2    Schwer, B.3    Shuman, S.4
  • 19
    • 0032514620 scopus 로고    scopus 로고
    • Mammalian capping enzyme binds RNA and uses protein tyrosine phosphatase mechanism
    • Wen Y, Yue Z, Shatkin AJ: Mammalian capping enzyme binds RNA and uses protein tyrosine phosphatase mechanism. Proc Natl Acad Sci USA 1998;95:12226-12231.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12226-12231
    • Wen, Y.1    Yue, Z.2    Shatkin, A.J.3
  • 20
    • 0035910568 scopus 로고    scopus 로고
    • Characterization of the mRNA capping apparatus of Candida albicans
    • Schwer B, Lehman K, Saha N, Shuman S: Characterization of the mRNA capping apparatus of Candida albicans. J Biol Chem 2001;276:1857-1864.
    • (2001) J Biol Chem , vol.276 , pp. 1857-1864
    • Schwer, B.1    Lehman, K.2    Saha, N.3    Shuman, S.4
  • 21
    • 0015887305 scopus 로고
    • A9145, a new adenine-containing antifungal antibiotic: II. Biological activity
    • Gordee RS, Butler TF: A9145, a new adenine-containing antifungal antibiotic: II. Biological activity. J Antibiot (Tokyo) 1973;26:466-470.
    • (1973) J Antibiot (Tokyo) , vol.26 , pp. 466-470
    • Gordee, R.S.1    Butler, T.F.2
  • 22
    • 0015890607 scopus 로고
    • A9145, a new adenine-containing antifungal antibiotic: I. Discovery and isolation
    • Hamil RL, Hoehn MM: A9145, a new adenine-containing antifungal antibiotic: I. Discovery and isolation. J Antibiot (Tokyo) 1973;26:463-465.
    • (1973) J Antibiot (Tokyo) , vol.26 , pp. 463-465
    • Hamil, R.L.1    Hoehn, M.M.2
  • 23
    • 0017899194 scopus 로고
    • Sinefungin, a potent inhibitor of virion mRNA(guanine-7-)- methyltransferase, mRNA(nucleoside-2′-)-methyltransferase, and viral multiplication
    • Pugh CS, Borchardt RT, Stone HO: Sinefungin, a potent inhibitor of virion mRNA(guanine-7-)-methyltransferase, mRNA(nucleoside-2′-)- methyltransferase, and viral multiplication. J Biol Chem 1978;253:4075-4077.
    • (1978) J Biol Chem , vol.253 , pp. 4075-4077
    • Pugh, C.S.1    Borchardt, R.T.2    Stone, H.O.3
  • 24
    • 0020471023 scopus 로고
    • Effects of S-adenosylhomocysteine analogues on vaccinia viral messenger ribonucleic acid synthesis and methylation
    • Pugh CS, Borchardt RT: Effects of S-adenosylhomocysteine analogues on vaccinia viral messenger ribonucleic acid synthesis and methylation. Biochemistry 1982;21:1535-1541.
    • (1982) Biochemistry , vol.21 , pp. 1535-1541
    • Pugh, C.S.1    Borchardt, R.T.2
  • 25
    • 0026661825 scopus 로고
    • Trypanosoma brucei spliced-leader RNA methylations are required for trans splicing in vivo
    • McNally KP, Agabian N: Trypanosoma brucei spliced-leader RNA methylations are required for trans splicing in vivo. Mol Cell Biol 1992;12:4844-4851.
    • (1992) Mol Cell Biol , vol.12 , pp. 4844-4851
    • McNally, K.P.1    Agabian, N.2
  • 26
    • 0026703547 scopus 로고
    • A simple and efficient procedure for transformation of yeasts
    • Elble R: A simple and efficient procedure for transformation of yeasts. Biotechniques 1992;13:18-20.
    • (1992) Biotechniques , vol.13 , pp. 18-20
    • Elble, R.1
  • 27
    • 0030798070 scopus 로고    scopus 로고
    • A set of vectors with a tetracycline-regulatable promoter system for modulated gene expression in Saccharomyces cerevisiae
    • Gari E, Piedrafita L, Aldea M, Herrero E: A set of vectors with a tetracycline-regulatable promoter system for modulated gene expression in Saccharomyces cerevisiae. Yeast 1997;13:837-848.
    • (1997) Yeast , vol.13 , pp. 837-848
    • Gari, E.1    Piedrafita, L.2    Aldea, M.3    Herrero, E.4
  • 28
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz RD, Sugino A: New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 1988;74:527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 29
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • Zhang JH, Chung TD, Oldenburg KR: A simple statistical parameter for use in evaluation and validation of high throughput screening assays. J Biomol Screen 1999;4:67-73.
    • (1999) J Biomol Screen , vol.4 , pp. 67-73
    • Zhang, J.H.1    Chung, T.D.2    Oldenburg, K.R.3
  • 31
    • 0035883736 scopus 로고    scopus 로고
    • AdoMet-dependent methylation, DNA methyltransferases and base flipping
    • Cheng X, Roberts RJ: AdoMet-dependent methylation, DNA methyltransferases and base flipping. Nucleic Acids Res 2001;29:3784-3795.
    • (2001) Nucleic Acids Res , vol.29 , pp. 3784-3795
    • Cheng, X.1    Roberts, R.J.2
  • 33
    • 0028841409 scopus 로고
    • Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes
    • Malone T, Blumenthal RM, Cheng X: Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes. J Mol Biol 1995;253:618-632.
    • (1995) J Mol Biol , vol.253 , pp. 618-632
    • Malone, T.1    Blumenthal, R.M.2    Cheng, X.3
  • 34
    • 0002401076 scopus 로고    scopus 로고
    • mRNA:guanine-N7 cap methyltransferases: Identification of novel members of the family, evolutionary analysis, homology modeling, and analysis of sequence-structure-function relationships
    • Bujnicki JM, Feder M, Radlinska M, Rychlewski L: mRNA:guanine-N7 cap methyltransferases: identification of novel members of the family, evolutionary analysis, homology modeling, and analysis of sequence-structure-function relationships. BMC Bioinformatics 2001;2:2.
    • (2001) BMC Bioinformatics , vol.2 , pp. 2
    • Bujnicki, J.M.1    Feder, M.2    Radlinska, M.3    Rychlewski, L.4
  • 35
    • 0034696755 scopus 로고    scopus 로고
    • Mechanisms for auto-inhibition and forced product release in glycine N-methyltransferase: Crystal structures of wild-type, mutant R175K and S-adenosylhomocysteine-bound R175K enzymes
    • Huang Y, Komoto J, Konishi K, et al: Mechanisms for auto-inhibition and forced product release in glycine N-methyltransferase: crystal structures of wild-type, mutant R175K and S-adenosylhomocysteine-bound R175K enzymes. J Mol Biol 2000;298:149-162.
    • (2000) J Mol Biol , vol.298 , pp. 149-162
    • Huang, Y.1    Komoto, J.2    Konishi, K.3
  • 36
    • 0030060410 scopus 로고    scopus 로고
    • Mutational analysis of the Saccharomyces cerevisiae ABD1 gene: Cap methyltransferase activity is essential for cell growth
    • Mao X, Schwer B, Shuman S: Mutational analysis of the Saccharomyces cerevisiae ABD1 gene: cap methyltransferase activity is essential for cell growth. Mol Cell Biol 1996;16:475-480.
    • (1996) Mol Cell Biol , vol.16 , pp. 475-480
    • Mao, X.1    Schwer, B.2    Shuman, S.3
  • 37
    • 0000643270 scopus 로고    scopus 로고
    • Structure-function analysis of the mRNA cap methyltransferase of Saccharomyces cerevisiae
    • Wang SP, Shuman S: Structure-function analysis of the mRNA cap methyltransferase of Saccharomyces cerevisiae. J Biol Chem 1997;272:14683-14689.
    • (1997) J Biol Chem , vol.272 , pp. 14683-14689
    • Wang, S.P.1    Shuman, S.2
  • 38
    • 0032741669 scopus 로고    scopus 로고
    • The Candida albicans gene for mRNA 5-cap methyltransferase: Identification of additional residues essential for catalysis
    • Yamada-Okabe T, Mio T, Kashima Y, Matsui M, Arisawa M, Yamada-Okabe H: The Candida albicans gene for mRNA 5-cap methyltransferase: identification of additional residues essential for catalysis. Microbiology 1999;145(Pt 11):3023-3033.
    • (1999) Microbiology , vol.145 , Issue.PART 11 , pp. 3023-3033
    • Yamada-Okabe, T.1    Mio, T.2    Kashima, Y.3    Matsui, M.4    Arisawa, M.5    Yamada-Okabe, H.6
  • 39
    • 0034192193 scopus 로고    scopus 로고
    • Characterization of Candida albicans RNA triphosphatase and mutational analysis of its active site
    • Pei Y, Lehman K, Tian L, Shuman S: Characterization of Candida albicans RNA triphosphatase and mutational analysis of its active site. Nucleic Acids Res 2000;28:1885-1892.
    • (2000) Nucleic Acids Res , vol.28 , pp. 1885-1892
    • Pei, Y.1    Lehman, K.2    Tian, L.3    Shuman, S.4
  • 40
    • 0033895727 scopus 로고    scopus 로고
    • Structure-function analysis of yeast mRNA cap methyltransferase and high-copy suppression of conditional mutants by AdoMet synthase and the ubiquitin conjugating enzyme Cdc34p
    • Schwer B, Saha N, Mao X, Chen HW, Shuman S: Structure-function analysis of yeast mRNA cap methyltransferase and high-copy suppression of conditional mutants by AdoMet synthase and the ubiquitin conjugating enzyme Cdc34p. Genetics 2000;155:1561-1576.
    • (2000) Genetics , vol.155 , pp. 1561-1576
    • Schwer, B.1    Saha, N.2    Mao, X.3    Chen, H.W.4    Shuman, S.5
  • 41
    • 0033808667 scopus 로고    scopus 로고
    • A single-transformation gene function test in diploid Candida albicans
    • Enloe B, Diamond A, Mitchell AP: A single-transformation gene function test in diploid Candida albicans. J Bacteriol 2000;182:5730-5736.
    • (2000) J Bacteriol , vol.182 , pp. 5730-5736
    • Enloe, B.1    Diamond, A.2    Mitchell, A.P.3
  • 42
    • 0038369972 scopus 로고    scopus 로고
    • Deletion of individual mRNA capping genes is unexpectedly not lethal to Candida albicans and results in modified mRNA cap structures
    • Dunyak DS, Everdeen DS, Albanese JG, Quinn CL: Deletion of individual mRNA capping genes is unexpectedly not lethal to Candida albicans and results in modified mRNA cap structures. Eukaryot Cell 2002;1:1010-1020.
    • (2002) Eukaryot Cell , vol.1 , pp. 1010-1020
    • Dunyak, D.S.1    Everdeen, D.S.2    Albanese, J.G.3    Quinn, C.L.4
  • 43
    • 0033028595 scopus 로고    scopus 로고
    • Rapid hypothesis testing with Candida albicans through gene disruption with short homology regions
    • Wilson RB, Davis D, Mitchell AP: Rapid hypothesis testing with Candida albicans through gene disruption with short homology regions. J Bacteriol 1999;181:1868-1874.
    • (1999) J Bacteriol , vol.181 , pp. 1868-1874
    • Wilson, R.B.1    Davis, D.2    Mitchell, A.P.3
  • 44
    • 0021187208 scopus 로고
    • Cell cycle effects in yeast cells of the antifungal agent sinefungin
    • Li AW, Singer RA, Johnston GC: Cell cycle effects in yeast cells of the antifungal agent sinefungin. FEMS Microbiol Lett 1984;23:243-247.
    • (1984) FEMS Microbiol Lett , vol.23 , pp. 243-247
    • Li, A.W.1    Singer, R.A.2    Johnston, G.C.3
  • 45
    • 0021734006 scopus 로고
    • Mating ability during chemically induced G1 arrest of cells of the yeast Sacchammyces cerevisiae
    • Bedard DP, Li AW, Singer RA, Johnston GC: Mating ability during chemically induced G1 arrest of cells of the yeast Sacchammyces cerevisiae. J Bacteriol 1984;160:1196-1198.
    • (1984) J Bacteriol , vol.160 , pp. 1196-1198
    • Bedard, D.P.1    Li, A.W.2    Singer, R.A.3    Johnston, G.C.4
  • 46
    • 0019464724 scopus 로고
    • Inhibition of sterol transmethylation by S-adenosylhomocysteine analogs
    • McCammon MT, Parks LW: Inhibition of sterol transmethylation by S-adenosylhomocysteine analogs. J Bacteriol 1981;145:106-112.
    • (1981) J Bacteriol , vol.145 , pp. 106-112
    • McCammon, M.T.1    Parks, L.W.2
  • 47
    • 0022258156 scopus 로고
    • Effects of sinefungin on rRNA production and methylation in the yeast Sacchammyces cerevisiae
    • Li AW, Singer RA, Johnston GC: Effects of sinefungin on rRNA production and methylation in the yeast Sacchammyces cerevisiae. Arch Biochem Biophys 1985;240:613-620.
    • (1985) Arch Biochem Biophys , vol.240 , pp. 613-620
    • Li, A.W.1    Singer, R.A.2    Johnston, G.C.3
  • 48
    • 0027522990 scopus 로고
    • Curative and preventive anticryptosporidium activities of sinefungin in an immunosuppressed adult rat model
    • Brasseur P, Lemeteil D, Ballet JJ: Curative and preventive anticryptosporidium activities of sinefungin in an immunosuppressed adult rat model. Antimicrob Agents Chemother 1993;37:889-892.
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 889-892
    • Brasseur, P.1    Lemeteil, D.2    Ballet, J.J.3
  • 49
    • 0028293768 scopus 로고
    • Putative anticryptosporidial agents tested with an immunodeficient mouse model
    • Leitch GJ, He Q: Putative anticryptosporidial agents tested with an immunodeficient mouse model. Antimicrob Agents Chemother 1994;38:865-867.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 865-867
    • Leitch, G.J.1    He, Q.2
  • 50
    • 0027439757 scopus 로고
    • Assessment of candidate anticryptosporidial agents in an immunosuppressed rat model
    • Lemeteil D, Roussel F, Favennec L, Ballet JJ, Brausseur P: Assessment of candidate anticryptosporidial agents in an immunosuppressed rat model. J Infect Dis 1993;167;766-768.
    • (1993) J Infect Dis , vol.167 , pp. 766-768
    • Lemeteil, D.1    Roussel, F.2    Favennec, L.3    Ballet, J.J.4    Brausseur, P.5
  • 51
    • 0024579387 scopus 로고
    • Efficacy of experimental trypanocidal compounds against a multiple drug-resistant Trypanosoma brucei brucei stock in mice
    • Zweygarth E, Rottcher D: Efficacy of experimental trypanocidal compounds against a multiple drug-resistant Trypanosoma brucei brucei stock in mice. Parasitol Res 1989;75:178-182.
    • (1989) Parasitol Res , vol.75 , pp. 178-182
    • Zweygarth, E.1    Rottcher, D.2
  • 52
    • 0023266641 scopus 로고
    • Molecular target of the antileishmanial action of sinefungin
    • Nolan LL: Molecular target of the antileishmanial action of sinefungin. Antimicrob Agents Chemother 1987;31:1542-1548.
    • (1987) Antimicrob Agents Chemother , vol.31 , pp. 1542-1548
    • Nolan, L.L.1
  • 53
    • 0022478231 scopus 로고
    • Evaluation of sinefungin for the treatment of Trypanosoma (Nannomonas) congolense infections in goats
    • Zweygarth F, Schillinger D, Kaufmann W, Rottcher D: Evaluation of sinefungin for the treatment of Trypanosoma (Nannomonas) congolense infections in goats. Trop Med Parasitol 1986;37:255-257.
    • (1986) Trop Med Parasitol , vol.37 , pp. 255-257
    • Zweygarth, F.1    Schillinger, D.2    Kaufmann, W.3    Rottcher, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.