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Volumn 408, Issue 2, 2007, Pages 173-180

Molecules incorporating a benzothiazole core scaffold inhibit the N-myristoyltransferase of Plasmodium falciparum

Author keywords

Benzothiazole; Codon optimization; Inhibition; N myristoylation; Plasmodium falciparum; Scintillation proximity assay (SPA)

Indexed keywords

BENZOTHIAZOLE CORES; CODON OPTIMIZATION; PLASMODIUM FALCIPARUM; SCINTILLATION PROXIMITY ASSAY (SPA);

EID: 36749030760     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070692     Document Type: Article
Times cited : (61)

References (49)
  • 1
    • 15044338866 scopus 로고    scopus 로고
    • The global distribution of clinical episodes of Plasmodium falciparum malaria
    • Snow, R. W., Guerra, C. A., Noor, A. M., Myint, H. Y. and Hay, S. I. (2005) The global distribution of clinical episodes of Plasmodium falciparum malaria. Nature 434, 214-217
    • (2005) Nature , vol.434 , pp. 214-217
    • Snow, R.W.1    Guerra, C.A.2    Noor, A.M.3    Myint, H.Y.4    Hay, S.I.5
  • 2
    • 0023666521 scopus 로고
    • Acylation of proteins with myristic acid occurs cotranslationally
    • Wilcox, C., Hu, J. S and Olson, E. N. (1987) Acylation of proteins with myristic acid occurs cotranslationally. Science 238, 1275-1278
    • (1987) Science , vol.238 , pp. 1275-1278
    • Wilcox, C.1    Hu, J.S.2    Olson, E.N.3
  • 3
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh, M. D. (1999) Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1451, 1-16
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 4
    • 0036295384 scopus 로고    scopus 로고
    • N-terminal N-myristoylation of proteins: Refinement of the sequence motif and its taxon-specific differences
    • Maurer-Stroh, S., Eisenhaber, B. and Eisenhaber, F. (2002) N-terminal N-myristoylation of proteins: refinement of the sequence motif and its taxon-specific differences. J. Mol. Biol. 317, 523-540
    • (2002) J. Mol. Biol , vol.317 , pp. 523-540
    • Maurer-Stroh, S.1    Eisenhaber, B.2    Eisenhaber, F.3
  • 5
    • 1642340046 scopus 로고    scopus 로고
    • Myristoylation of viral and bacterial proteins
    • Maurer-Stroh, S. and Eisenhaber, F. (2004) Myristoylation of viral and bacterial proteins. Trends Microbiol. 12, 178-185
    • (2004) Trends Microbiol , vol.12 , pp. 178-185
    • Maurer-Stroh, S.1    Eisenhaber, F.2
  • 6
    • 0025834950 scopus 로고
    • Kinetic and structural evidence for a sequential ordered Bi Bi mechanism of catalysis by Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase
    • Rudnick, D. A., McWherter, C. A., Rocque, W. J., Lennon, P. J., Getman, D. P. and Gordon, J. I. (1991) Kinetic and structural evidence for a sequential ordered Bi Bi mechanism of catalysis by Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase. J. Biol. Chem. 266, 9732-9739
    • (1991) J. Biol. Chem , vol.266 , pp. 9732-9739
    • Rudnick, D.A.1    McWherter, C.A.2    Rocque, W.J.3    Lennon, P.J.4    Getman, D.P.5    Gordon, J.I.6
  • 7
    • 0035967517 scopus 로고    scopus 로고
    • Structures of Saccharomyces cerevisiae N-myristoyltransferase with bound myristoylCoA and peptide provide insights about substrate recognition and catalysis
    • Farazi, T. A., Waksman, G. and Gordon, J. I. (2001) Structures of Saccharomyces cerevisiae N-myristoyltransferase with bound myristoylCoA and peptide provide insights about substrate recognition and catalysis. Biochemistry 40, 6335-6343
    • (2001) Biochemistry , vol.40 , pp. 6335-6343
    • Farazi, T.A.1    Waksman, G.2    Gordon, J.I.3
  • 9
    • 0030612443 scopus 로고    scopus 로고
    • Selective peptidic and peptidomimetic inhibitors of Candida albicans myristoylCoA: Protein N-myristoyltransferase: a new approach to antifungal therapy
    • Sikorski, J. A., Devadas, B., Zupec, M. E., Freeman, S. K., Brown, D. L., Lu, H. F., Nagarajan, S., Mehta, P. P., Wade, A. C., Kishore, N. S. et al. (1997) Selective peptidic and peptidomimetic inhibitors of Candida albicans myristoylCoA: protein N-myristoyltransferase: a new approach to antifungal therapy. Biopolymers 43, 43-71
    • (1997) Biopolymers , vol.43 , pp. 43-71
    • Sikorski, J.A.1    Devadas, B.2    Zupec, M.E.3    Freeman, S.K.4    Brown, D.L.5    Lu, H.F.6    Nagarajan, S.7    Mehta, P.P.8    Wade, A.C.9    Kishore, N.S.10
  • 10
    • 0036051790 scopus 로고    scopus 로고
    • Antifungals targeted to protein modification: Focus on protein N-myristoyltransferase
    • Georgopapadakou, N. H. (2002) Antifungals targeted to protein modification: focus on protein N-myristoyltransferase. Expert Opin. Investig. Drugs 11, 1117-1125
    • (2002) Expert Opin. Investig. Drugs , vol.11 , pp. 1117-1125
    • Georgopapadakou, N.H.1
  • 11
  • 12
    • 0036781702 scopus 로고    scopus 로고
    • Myristoyl-CoA:protein N-myristoyltransferase: A novel molecular approach for cancer therapy
    • Selvakumar, P., Pasha, M. K., Ashakumary, L., Dimmock, J. R. and Sharma, R. K. (2002) Myristoyl-CoA:protein N-myristoyltransferase: a novel molecular approach for cancer therapy. Int. J. Mol. Med. 10, 493-500
    • (2002) Int. J. Mol. Med , vol.10 , pp. 493-500
    • Selvakumar, P.1    Pasha, M.K.2    Ashakumary, L.3    Dimmock, J.R.4    Sharma, R.K.5
  • 13
    • 24144464240 scopus 로고    scopus 로고
    • Two N-myristoyltransferase isozymes play unique roles in protein myristoylation, proliferation, and apoptosis
    • Ducker, C. E., Upson, J. J., French, K. J. and Smith, C. D. (2005) Two N-myristoyltransferase isozymes play unique roles in protein myristoylation, proliferation, and apoptosis. Mol. Cancer Res. 3, 463-476
    • (2005) Mol. Cancer Res , vol.3 , pp. 463-476
    • Ducker, C.E.1    Upson, J.J.2    French, K.J.3    Smith, C.D.4
  • 15
    • 33645230781 scopus 로고    scopus 로고
    • N-myristoyltransferase 2 expression in human colon cancer: Cross-talk between the calpain and caspase system
    • Selvakumar, P., Smith-Windsor, E., Bonham, K. and Sharma, R. K. (2006) N-myristoyltransferase 2 expression in human colon cancer: cross-talk between the calpain and caspase system. FEBS Lett. 580, 2021-2026
    • (2006) FEBS Lett , vol.580 , pp. 2021-2026
    • Selvakumar, P.1    Smith-Windsor, E.2    Bonham, K.3    Sharma, R.K.4
  • 16
    • 0028053746 scopus 로고
    • Targeted gene replacement demonstrates that myristoyl-CoA:protein N-myristoyltransferase is essential for viability of Cryptococcus neoformans
    • Lodge, J. K., Jackson-Machelski, E., Toffaletti, D. L., Perfect, J. R. and Gordon, J. I. (1994) Targeted gene replacement demonstrates that myristoyl-CoA:protein N-myristoyltransferase is essential for viability of Cryptococcus neoformans. Proc. Natl. Acad. Sci. U.S.A. 91, 12008-12012
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , pp. 12008-12012
    • Lodge, J.K.1    Jackson-Machelski, E.2    Toffaletti, D.L.3    Perfect, J.R.4    Gordon, J.I.5
  • 17
    • 0029070249 scopus 로고
    • Genetic studies reveal that myristoylCoA:protein N-myristoyltransferase is an essential enzyme in Candida albicans
    • Weinberg, R. A., McWherter, C. A., Freeman, S. K., Wood, D. C., Gordon, J. I. and Lee, S. C. (1995) Genetic studies reveal that myristoylCoA:protein N-myristoyltransferase is an essential enzyme in Candida albicans. Mol. Microbiol. 16, 241-250
    • (1995) Mol. Microbiol , vol.16 , pp. 241-250
    • Weinberg, R.A.1    McWherter, C.A.2    Freeman, S.K.3    Wood, D.C.4    Gordon, J.I.5    Lee, S.C.6
  • 18
    • 0037470198 scopus 로고    scopus 로고
    • Myristoyl-CoA:protein N-myristoyltransferase, an essential enzyme and potential drug target in kinetoplastid parasites
    • Price, H. P., Menon, M. R., Panethymitaki, C., Goulding, D., McKean, P. G. and Smith, D. F. (2003) Myristoyl-CoA:protein N-myristoyltransferase, an essential enzyme and potential drug target in kinetoplastid parasites. J. Biol. Chem. 278, 7206-7214
    • (2003) J. Biol. Chem , vol.278 , pp. 7206-7214
    • Price, H.P.1    Menon, M.R.2    Panethymitaki, C.3    Goulding, D.4    McKean, P.G.5    Smith, D.F.6
  • 19
    • 0027529190 scopus 로고
    • Comparison of the acyl chain specificities of human myristoyl-CoA synthetase and human myristoyl-CoA:protein N- myristoyltransferase
    • Kishore, N. S., Wood, D. C., Mehta, P. P., Wade, A. C., Lu, T., Gokel, G. W. and Gordon, J. I. (1993) Comparison of the acyl chain specificities of human myristoyl-CoA synthetase and human myristoyl-CoA:protein N- myristoyltransferase. J. Biol. Chem. 268, 4889-4902
    • (1993) J. Biol. Chem , vol.268 , pp. 4889-4902
    • Kishore, N.S.1    Wood, D.C.2    Mehta, P.P.3    Wade, A.C.4    Lu, T.5    Gokel, G.W.6    Gordon, J.I.7
  • 20
    • 0032697710 scopus 로고    scopus 로고
    • Myristic acid analogs are inhibitors of Junin virus replication
    • Cordo, S. M., Candurra, N. A. and Damonte, E. B. (1999) Myristic acid analogs are inhibitors of Junin virus replication Microbes Infect. 1, 609-614
    • (1999) Microbes Infect , vol.1 , pp. 609-614
    • Cordo, S.M.1    Candurra, N.A.2    Damonte, E.B.3
  • 22
    • 14844322778 scopus 로고    scopus 로고
    • Synthesis of potent and selective inhibitors of Candida albicans N-myristoyltransferase based on the benzothiazole structure
    • Yamazaki, K., Kaneko, Y., Suwa, K., Ebara, S., Nakazawa, K. and Yasuno, K. (2005) Synthesis of potent and selective inhibitors of Candida albicans N-myristoyltransferase based on the benzothiazole structure. Bioorg. Med. Chem. 13, 2509-2522
    • (2005) Bioorg. Med. Chem , vol.13 , pp. 2509-2522
    • Yamazaki, K.1    Kaneko, Y.2    Suwa, K.3    Ebara, S.4    Nakazawa, K.5    Yasuno, K.6
  • 24
    • 0026544934 scopus 로고
    • Mutations of human myristoyl-CoA:protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae
    • Duronio, R. J., Reed, S. I. and Gordon, J. I. (1992) Mutations of human myristoyl-CoA:protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 89, 4129-4133
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 4129-4133
    • Duronio, R.J.1    Reed, S.I.2    Gordon, J.I.3
  • 25
    • 0032549571 scopus 로고    scopus 로고
    • A second mammalian N-myristoyltransferase
    • Giang, D. K. and Cravatt, B. F. (1998) A second mammalian N-myristoyltransferase. J. Biol. Chem. 273, 6595-6598
    • (1998) J. Biol. Chem , vol.273 , pp. 6595-6598
    • Giang, D.K.1    Cravatt, B.F.2
  • 26
  • 27
    • 33744806630 scopus 로고    scopus 로고
    • Characterisation and selective inhibition of myristoyl CoA:protein N-myristoyl transferase from Trypanosoma brucei and Leishmania major
    • Panethymitaki, C., Bowyer, P. W., Price, H. P., Leatherbarrow, R. J., Brown, K. A. and Smith, D. F. (2006) Characterisation and selective inhibition of myristoyl CoA:protein N-myristoyl transferase from Trypanosoma brucei and Leishmania major. Biochem. J. 396, 277-285
    • (2006) Biochem. J , vol.396 , pp. 277-285
    • Panethymitaki, C.1    Bowyer, P.W.2    Price, H.P.3    Leatherbarrow, R.J.4    Brown, K.A.5    Smith, D.F.6
  • 31
    • 7644221040 scopus 로고    scopus 로고
    • Export of Plasmodium falciparum calcium-dependent protein kinase 1 to the parasitophorous vacuole is dependent on three N-terminal membrane anchor motifs
    • Moskes, C., Burghaus, P. A., Wernli, B., Sauder, U., Durrenberger, M. and Kappes, B. (2004) Export of Plasmodium falciparum calcium-dependent protein kinase 1 to the parasitophorous vacuole is dependent on three N-terminal membrane anchor motifs. Mol. Microbiol. 54, 676-691
    • (2004) Mol. Microbiol , vol.54 , pp. 676-691
    • Moskes, C.1    Burghaus, P.A.2    Wernli, B.3    Sauder, U.4    Durrenberger, M.5    Kappes, B.6
  • 33
    • 0032030138 scopus 로고    scopus 로고
    • Codon optimization of the gene encoding a domain from human type 1 neurofibromin protein results in a threefold improvement in expression level in Escherichia coli
    • Hale, R. S. and Thompson, G. (1998) Codon optimization of the gene encoding a domain from human type 1 neurofibromin protein results in a threefold improvement in expression level in Escherichia coli. Protein Expression Purif. 12, 185-188
    • (1998) Protein Expression Purif , vol.12 , pp. 185-188
    • Hale, R.S.1    Thompson, G.2
  • 35
    • 0025232814 scopus 로고
    • Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids
    • Fields, G. B. and Noble, R. L. (1990) Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int. J. Pept. Protein Res. 35, 161-214
    • (1990) Int. J. Pept. Protein Res , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 36
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager, W. and Jensen, J. B. (1976) Human malaria parasites in continuous culture. Science 193, 673-675
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 37
    • 0018249537 scopus 로고
    • Separation of viable schizont-infected red cells of Plasmodium falciparum from human blood
    • Pasvol, G., Wilson, R. J., Smalley, M. E. and Brown, J. (1978) Separation of viable schizont-infected red cells of Plasmodium falciparum from human blood. Ann. Trop. Med. Parasitol. 72, 87-88
    • (1978) Ann. Trop. Med. Parasitol , vol.72 , pp. 87-88
    • Pasvol, G.1    Wilson, R.J.2    Smalley, M.E.3    Brown, J.4
  • 38
    • 0036073678 scopus 로고    scopus 로고
    • High-level expression of the malaria blood-stage vaccine candidate Plasmodium falciparum apical membrane antigen 1 and induction of antibodies that inhibit erythrocyte invasion
    • Kocken, C. H., Withers-Martinez, C., Dubbeld, M. A., van der Wel, A., Hackett, F., Valderrama, A., Blackman, M. J. and Thomas, A. W. (2002) High-level expression of the malaria blood-stage vaccine candidate Plasmodium falciparum apical membrane antigen 1 and induction of antibodies that inhibit erythrocyte invasion. Infect. Immun. 70, 4471-4476
    • (2002) Infect. Immun , vol.70 , pp. 4471-4476
    • Kocken, C.H.1    Withers-Martinez, C.2    Dubbeld, M.A.3    van der Wel, A.4    Hackett, F.5    Valderrama, A.6    Blackman, M.J.7    Thomas, A.W.8
  • 40
    • 0035190397 scopus 로고    scopus 로고
    • Codon optimization of gene fragments encoding Plasmodium falciparum merzoite proteins enhances DNA vaccine protein expression and immunogenicity in mice
    • Narum, D. L., Kumar, S., Rogers, W. O., Fuhrmann, S. R., Liang, H., Oakley, M., Taye, A., Sim, B. K. and Hoffman, S. L. (2001) Codon optimization of gene fragments encoding Plasmodium falciparum merzoite proteins enhances DNA vaccine protein expression and immunogenicity in mice. Infect. Immun. 69, 7250-7253
    • (2001) Infect. Immun , vol.69 , pp. 7250-7253
    • Narum, D.L.1    Kumar, S.2    Rogers, W.O.3    Fuhrmann, S.R.4    Liang, H.5    Oakley, M.6    Taye, A.7    Sim, B.K.8    Hoffman, S.L.9
  • 43
    • 33845482665 scopus 로고    scopus 로고
    • Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms
    • Vedadi, M., Lew, J., Artz, J., Amani, M., Zhao, Y., Dong, A., Wasney, G. A., Gao, M., Hills, T., Brokx, S. et al. (2007) Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms. Mol. Biochem. Parasitol. 151, 100-110
    • (2007) Mol. Biochem. Parasitol , vol.151 , pp. 100-110
    • Vedadi, M.1    Lew, J.2    Artz, J.3    Amani, M.4    Zhao, Y.5    Dong, A.6    Wasney, G.A.7    Gao, M.8    Hills, T.9    Brokx, S.10
  • 44
    • 0023818374 scopus 로고
    • N-myristoylation of p60src. Identification of a myristoyl-CoA:glycylpeptide N-myristoyltransferase in rat tissues
    • Glover, C. J., Goddard, C. and Felsted, R. L. (1988) N-myristoylation of p60src. Identification of a myristoyl-CoA:glycylpeptide N-myristoyltransferase in rat tissues. Biochem. J. 250, 485-491
    • (1988) Biochem. J , vol.250 , pp. 485-491
    • Glover, C.J.1    Goddard, C.2    Felsted, R.L.3
  • 45
    • 0026410483 scopus 로고
    • N-myristoyl transferase assay using phosphocellulose paper binding
    • King, M. J. and Sharma, R. K. (1991) N-myristoyl transferase assay using phosphocellulose paper binding. Anal. Biochem. 199, 149-153
    • (1991) Anal. Biochem , vol.199 , pp. 149-153
    • King, M.J.1    Sharma, R.K.2
  • 46
    • 0030923009 scopus 로고    scopus 로고
    • Scanning alanine mutagenesis and de-peptidization of a Candida albicans myristoyl-CoA:protein N-myristoyltransferase octapeptide substrate reveals three elements critical for molecular recognition
    • McWherter, C. A., Rocque, W. J., Zupec, M. E., Freeman, S. K., Brown, D. L., Devadas, B., Getman, D. P., Sikorski, J. A. and Gordon, J. I. (1997) Scanning alanine mutagenesis and de-peptidization of a Candida albicans myristoyl-CoA:protein N-myristoyltransferase octapeptide substrate reveals three elements critical for molecular recognition. J. Biol. Chem. 272, 11874-11880
    • (1997) J. Biol. Chem , vol.272 , pp. 11874-11880
    • McWherter, C.A.1    Rocque, W.J.2    Zupec, M.E.3    Freeman, S.K.4    Brown, D.L.5    Devadas, B.6    Getman, D.P.7    Sikorski, J.A.8    Gordon, J.I.9
  • 47
    • 0027276545 scopus 로고
    • A comparative analysis of the kinetic mechanism and peptide substrate specificity of human and Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase
    • Rocque, W. J., McWherter, C. A., Wood, D. C. and Gordon, J. I. (1993) A comparative analysis of the kinetic mechanism and peptide substrate specificity of human and Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase. J. Biol. Chem. 268, 9964-9971
    • (1993) J. Biol. Chem , vol.268 , pp. 9964-9971
    • Rocque, W.J.1    McWherter, C.A.2    Wood, D.C.3    Gordon, J.I.4
  • 48
    • 0023109534 scopus 로고
    • Amino-terminal processing of proteins by N-myristoylation. Substrate specificity of N-myristoyl transferase
    • Towler, D. A., Eubanks, S. R., Towery, D. S., Adams, S. P. and Glaser, L. (1987) Amino-terminal processing of proteins by N-myristoylation. Substrate specificity of N-myristoyl transferase. J. Biol. Chem. 262, 1030-1036
    • (1987) J. Biol. Chem , vol.262 , pp. 1030-1036
    • Towler, D.A.1    Eubanks, S.R.2    Towery, D.S.3    Adams, S.P.4    Glaser, L.5
  • 49
    • 33646359916 scopus 로고    scopus 로고
    • Peptide-based inhibitors of N-myristoyl transferase generated from a lipid/combinatorial peptide chimera library
    • Tate, E. W., Bowyer, P. W., Brown, K. A., Smith, D. F., Holder, A. A. and Leatherbarrow, R. J. (2006) Peptide-based inhibitors of N-myristoyl transferase generated from a lipid/combinatorial peptide chimera library. Signal Transduction 6, 160-166
    • (2006) Signal Transduction , vol.6 , pp. 160-166
    • Tate, E.W.1    Bowyer, P.W.2    Brown, K.A.3    Smith, D.F.4    Holder, A.A.5    Leatherbarrow, R.J.6


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