메뉴 건너뛰기




Volumn 6, Issue 2, 2014, Pages 112-121

Validation of N-myristoyltransferase as an antimalarial drug target using an integrated chemical biology approach

Author keywords

[No Author keywords available]

Indexed keywords

ACYL COENZYME A; ACYLTRANSFERASE; ANTIMALARIAL AGENT; BIOMIMETIC MATERIAL; CAPRIN1 PROTEIN, HUMAN; CELL CYCLE PROTEIN; ENZYME INHIBITOR; GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE; PROTEIN N MYRISTOYLTRANSFERASE; RECOMBINANT PROTEIN; S TETRADECANOYL COENZYME A; S-TETRADECANOYL-COENZYME A;

EID: 84892956192     PISSN: 17554330     EISSN: 17554349     Source Type: Journal    
DOI: 10.1038/nchem.1830     Document Type: Article
Times cited : (180)

References (51)
  • 1
    • 84856679687 scopus 로고    scopus 로고
    • Global malaria mortality between 1980 and 2010: A systematic analysis
    • Murray, C. J. L. et al. Global malaria mortality between 1980 and 2010: a systematic analysis. Lancet 379, 413-431 (2012).
    • (2012) Lancet , vol.379 , pp. 413-431
    • Murray, C.J.L.1
  • 2
    • 40049109886 scopus 로고    scopus 로고
    • Vivax malaria: Neglected and not benign
    • Price, R. N. et al. Vivax malaria: neglected and not benign. Am. J. Trop. Med. Hyg. 77, 79-87 (2007).
    • (2007) Am. J. Trop. Med. Hyg. , vol.77 , pp. 79-87
    • Price, R.N.1
  • 3
    • 84861461519 scopus 로고    scopus 로고
    • Emergence of artemisinin-resistant malaria on the western border of Thailand: A longitudinal study
    • Phyo, A. P. et al. Emergence of artemisinin-resistant malaria on the western border of Thailand: a longitudinal study. Lancet 379, 1960-1966 (2012).
    • (2012) Lancet , vol.379 , pp. 1960-1966
    • Phyo, A.P.1
  • 6
    • 77950406212 scopus 로고    scopus 로고
    • N-myristoyltransferase inhibitors as new leads to treat sleeping sickness
    • Frearson, J. A. et al. N-myristoyltransferase inhibitors as new leads to treat sleeping sickness. Nature 464, 728-732 (2010).
    • (2010) Nature , vol.464 , pp. 728-732
    • Frearson, J.A.1
  • 7
    • 84891873689 scopus 로고    scopus 로고
    • N-Myristoyltransferase as a potential drug target in malaria and leishmaniasis
    • available on CJO2013.
    • Tate, E.W., Bell, A. S., Rackham, M. D. &Wright, M. H. N-Myristoyltransferase as a potential drug target in malaria and leishmaniasis. Parasitology, available on CJO2013. http://dx.doi.org/doi:10.1017/ S0031182013000450 (2013).
    • (2013) Parasitology
    • Tate, E.W.1    Bell, A.S.2    Rackham, M.D.3    Wright, M.H.4
  • 8
    • 84872411888 scopus 로고    scopus 로고
    • High-throughput profiling of N-myristoylation substrate specificity across species including pathogens
    • Traverso, J. A., Giglione, C. & Meinnel, T. High-throughput profiling of N-myristoylation substrate specificity across species including pathogens. Proteomics 13, 25-36 (2013).
    • (2013) Proteomics , vol.13 , pp. 25-36
    • Traverso, J.A.1    Giglione, C.2    Meinnel, T.3
  • 9
    • 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
    • DOI 10.1111/j.1365-2958.2004.04313.x
    • Moskes, C. et al. 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). (Pubitemid 39457290)
    • (2004) Molecular Microbiology , vol.54 , Issue.3 , pp. 676-691
    • Moskes, C.1    Burghaus, P.A.2    Wernli, B.3    Sauder, U.4    Durrenberger, M.5    Kappes, B.6
  • 11
    • 62949100525 scopus 로고    scopus 로고
    • Fatty acid acylation regulates trafficking of the unusual Plasmodium falciparum calpain to the nucleolus
    • Russo, I., Oksman, A. & Goldberg, D. E. Fatty acid acylation regulates trafficking of the unusual Plasmodium falciparum calpain to the nucleolus. Mol. Microbiol. 72, 229-245 (2009).
    • (2009) Mol. Microbiol. , vol.72 , pp. 229-245
    • Russo, I.1    Oksman, A.2    Goldberg, D.E.3
  • 12
    • 57849147553 scopus 로고    scopus 로고
    • Myristoylated adenylate kinase-2 of Plasmodium falciparum forms a heterodimer with myristoyltransferase
    • Rahlfs, S. et al. Myristoylated adenylate kinase-2 of Plasmodium falciparum forms a heterodimer with myristoyltransferase. Mol. Biochem. Parasitol. 163, 77-84 (2009).
    • (2009) Mol. Biochem. Parasitol. , vol.163 , pp. 77-84
    • Rahlfs, S.1
  • 13
    • 48049090703 scopus 로고    scopus 로고
    • Plasmodium falciparum possesses two GRASP proteins that are differentially targeted to the Golgi complex via a higher- and lowereukaryote- like mechanism
    • Struck, N. S. et al. Plasmodium falciparum possesses two GRASP proteins that are differentially targeted to the Golgi complex via a higher- and lowereukaryote- like mechanism. J. Cell Sci. 121, 2123-2129 (2008).
    • (2008) J. Cell Sci. , vol.121 , pp. 2123-2129
    • Struck, N.S.1
  • 14
    • 33750266831 scopus 로고    scopus 로고
    • Trafficking and signaling by fatty-acylated and prenylated proteins
    • DOI 10.1038/nchembio834, PII NCHEMBIO834
    • Resh, M. D. Trafficking and signaling by fatty-acylated and prenylated proteins. Nature Chem. Biol. 2, 584-590 (2006). (Pubitemid 44610342)
    • (2006) Nature Chemical Biology , vol.2 , Issue.11 , pp. 584-590
    • Resh, M.D.1
  • 16
    • 84871020221 scopus 로고    scopus 로고
    • A tetracycline-repressible transactivator system to study essential genes in malaria parasites
    • Pino, P. et al. A tetracycline-repressible transactivator system to study essential genes in malaria parasites. Cell Host Microbe 12, 824-834 (2012).
    • (2012) Cell Host Microbe , vol.12 , pp. 824-834
    • Pino, P.1
  • 17
    • 79957577925 scopus 로고    scopus 로고
    • Functional genetics in Apicomplexa: Potentials and limits
    • Limenitakis, J. & Soldati-Favre, D. Functional genetics in Apicomplexa: potentials and limits. FEBS Lett. 585, 1579-1588 (2011).
    • (2011) FEBS Lett. , vol.585 , pp. 1579-1588
    • Limenitakis, J.1    Soldati-Favre, D.2
  • 18
    • 76249116706 scopus 로고    scopus 로고
    • Getting a chemical handle on protein post-translational modification
    • Heal,W. P. & Tate, E.W. Getting a chemical handle on protein post-translational modification. Org. Biomol. Chem. 8, 731-738 (2010).
    • (2010) Org. Biomol. Chem. , vol.8 , pp. 731-738
    • Heal, W.P.1    Tate, E.W.2
  • 19
    • 80054075348 scopus 로고    scopus 로고
    • Exploring protein lipidation with chemical biology
    • Hang, H. C. & Linder, M. E. Exploring protein lipidation with chemical biology. Chem. Rev. 111, 6341-6358 (2011).
    • (2011) Chem. Rev. , vol.111 , pp. 6341-6358
    • Hang, H.C.1    Linder, M.E.2
  • 21
    • 84855880056 scopus 로고    scopus 로고
    • Multifunctional protein labeling via enzymatic N-terminal tagging and elaboration by click chemistry
    • Heal, W. P., Wright, M. H., Thinon, E. & Tate, E. W. Multifunctional protein labeling via enzymatic N-terminal tagging and elaboration by click chemistry. Nature Protoc. 7, 105-117 (2012).
    • (2012) Nature Protoc. , vol.7 , pp. 105-117
    • Heal, W.P.1    Wright, M.H.2    Thinon, E.3    Tate, E.W.4
  • 22
    • 67749086564 scopus 로고    scopus 로고
    • Robust fluorescent detection of protein fatty-acylation with chemical reporters
    • Charron, G. et al. Robust fluorescent detection of protein fatty-acylation with chemical reporters. J. Am. Chem. Soc. 131, 4967-4975 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 4967-4975
    • Charron, G.1
  • 23
    • 67650803380 scopus 로고    scopus 로고
    • Imaging the lipidome: Omega-alkynyl fatty acids for detection and cellular visualization of lipid-modified proteins
    • Hannoush, R. N. & Arenas-Ramirez, N. Imaging the lipidome: omega-alkynyl fatty acids for detection and cellular visualization of lipid-modified proteins. ACS Chem. Biol. 4, 581-587 (2009).
    • (2009) ACS Chem. Biol. , vol.4 , pp. 581-587
    • Hannoush, R.N.1    Arenas-Ramirez, N.2
  • 24
    • 77952737760 scopus 로고    scopus 로고
    • Rapid and selective detection of fatty acylated proteins using omega-alkynyl-fatty acids and click chemistry
    • Yap, M. C. et al. Rapid and selective detection of fatty acylated proteins using omega-alkynyl-fatty acids and click chemistry. J. Lipid Res. 51, 1566-1580 (2010).
    • (2010) J. Lipid Res. , vol.51 , pp. 1566-1580
    • Yap, M.C.1
  • 25
    • 84859790956 scopus 로고    scopus 로고
    • Discovery of Plasmodium vivax N-myristoyltransferase inhibitors: Screening, synthesis, and structural characterization of their binding mode
    • Goncalves, V. et al. Discovery of Plasmodium vivax N-myristoyltransferase inhibitors: screening, synthesis, and structural characterization of their binding mode. J. Med. Chem. 55, 3578-3582 (2012).
    • (2012) J. Med. Chem. , vol.55 , pp. 3578-3582
    • Goncalves, V.1
  • 27
    • 79955036748 scopus 로고    scopus 로고
    • Bioorthogonal chemical tagging of protein cholesterylation in living cells
    • Heal, W. P. et al. Bioorthogonal chemical tagging of protein cholesterylation in living cells. Chem. Commun. 47, 4081-4083 (2011).
    • (2011) Chem. Commun. , vol.47 , pp. 4081-4083
    • Heal, W.P.1
  • 28
    • 57649221595 scopus 로고    scopus 로고
    • The motor complex of Plasmodium falciparum: Phosphorylation by a calcium-dependent protein kinase
    • Green, J. L. et al. The motor complex of Plasmodium falciparum: phosphorylation by a calcium-dependent protein kinase. J. Biol. Chem. 283, 30980-30989 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 30980-30989
    • Green, J.L.1
  • 29
    • 0029869566 scopus 로고    scopus 로고
    • Structural analysis of the glycosyl-phosphatidylinositol membrane anchor of the merozoite surface proteins-1 and -2 of Plasmodium falciparum
    • DOI 10.1016/0166-6851(95)02518-9
    • Gerold, P., Schofield, L., Blackman, M. J., Holder, A. A. & Schwarz, R. T. Structural analysis of the glycosyl-phosphatidylinositol membrane anchor of the merozoite surface proteins-1 and -2 of Plasmodium falciparum. Mol. Biochem. Parasitol. 75, 131-143 (1996). (Pubitemid 26107821)
    • (1996) Molecular and Biochemical Parasitology , vol.75 , Issue.2 , pp. 131-143
    • Gerold, P.1    Schofield, L.2    Blackman, M.J.3    Holder, A.A.4    Schwarz, R.T.5
  • 30
    • 80855140147 scopus 로고    scopus 로고
    • Discovery of GAMA, a Plasmodium falciparum merozoite micronemal protein, as a novel blood-stage vaccine candidate antigen
    • Arumugam, T. U. et al. Discovery of GAMA, a Plasmodium falciparum merozoite micronemal protein, as a novel blood-stage vaccine candidate antigen. Infect. Immun. 79, 4523-4532 (2011).
    • (2011) Infect. Immun. , vol.79 , pp. 4523-4532
    • Arumugam, T.U.1
  • 32
    • 84862573534 scopus 로고    scopus 로고
    • Protein lysine acylation and cysteine succination by intermediates of energy metabolism
    • Lin, H., Su, X. & He, B. Protein lysine acylation and cysteine succination by intermediates of energy metabolism. ACS Chem. Biol. 7, 947-960 (2012).
    • (2012) ACS Chem. Biol. , vol.7 , pp. 947-960
    • Lin, H.1    Su, X.2    He, B.3
  • 33
    • 84866302859 scopus 로고    scopus 로고
    • Dissection of minimal sequence requirements for rhoptry membrane targeting in the malaria parasite
    • Cabrera, A. et al. Dissection of minimal sequence requirements for rhoptry membrane targeting in the malaria parasite. Traffic 13, 1335-1350 (2012).
    • (2012) Traffic , vol.13 , pp. 1335-1350
    • Cabrera, A.1
  • 34
    • 84868534561 scopus 로고    scopus 로고
    • N-Myristoylation of the Rpt2 subunit regulates intracellular localization of the yeast 26S proteasome
    • Kimura, A., Kato, Y. & Hirano, H. N-Myristoylation of the Rpt2 subunit regulates intracellular localization of the yeast 26S proteasome. Biochemistry 51, 8856-8866 (2012).
    • (2012) Biochemistry , vol.51 , pp. 8856-8866
    • Kimura, A.1    Kato, Y.2    Hirano, H.3
  • 35
    • 84871609304 scopus 로고    scopus 로고
    • Validation of the proteasome as a therapeutic target in Plasmodium using an epoxyketone inhibitor with parasite-specific toxicity
    • Li, H. et al. Validation of the proteasome as a therapeutic target in Plasmodium using an epoxyketone inhibitor with parasite-specific toxicity. Chem. Biol. 19, 1535-1545 (2012).
    • (2012) Chem. Biol. , vol.19 , pp. 1535-1545
    • Li, H.1
  • 36
    • 84863818803 scopus 로고    scopus 로고
    • Exploring the Plasmodium falciparum cyclic-adenosine monophosphate (cAMP)-dependent protein kinase (PfPKA) as a therapeutic target
    • Haste, N. M. et al. Exploring the Plasmodium falciparum cyclic-adenosine monophosphate (cAMP)-dependent protein kinase (PfPKA) as a therapeutic target. Microbes Infect. 14, 838-850 (2012).
    • (2012) Microbes Infect. , vol.14 , pp. 838-850
    • Haste, N.M.1
  • 37
    • 84861796619 scopus 로고    scopus 로고
    • Construction of a Plasmodium falciparum Rab-interactome identifies CK1 and PKA as Rab-effector kinases in malaria parasites
    • Rached, F. B. et al. Construction of a Plasmodium falciparum Rab-interactome identifies CK1 and PKA as Rab-effector kinases in malaria parasites. Biol. Cell 104, 34-47 (2012).
    • (2012) Biol. Cell , vol.104 , pp. 34-47
    • Rached, F.B.1
  • 38
    • 2342611064 scopus 로고    scopus 로고
    • Calcium and a calcium-dependent protein kinase regulate gamete formation and mosquito transmission in a malaria parasite
    • DOI 10.1016/S0092-8674(04)00449-0, PII S0092867404004490
    • Billker, O. et al. Calcium and a calcium-dependent protein kinase regulate gamete formation and mosquito transmission in a malaria parasite. Cell 117, 503-514 (2004). (Pubitemid 38610235)
    • (2004) Cell , vol.117 , Issue.4 , pp. 503-514
    • Billker, O.1    Dechamps, S.2    Tewari, R.3    Wenig, G.4    Franke-Fayard, B.5    Brinkmann, V.6
  • 39
    • 84978538778 scopus 로고    scopus 로고
    • Unique apicomplexan IMC sub-compartment proteins are early markers for apical polarity in the malaria parasite
    • Poulin, B. et al. Unique apicomplexan IMC sub-compartment proteins are early markers for apical polarity in the malaria parasite. Biol. Open 2, 1160-1170 (2013).
    • (2013) Biol. Open , vol.2 , pp. 1160-1170
    • Poulin, B.1
  • 40
    • 84872315887 scopus 로고    scopus 로고
    • Discovery of novel and ligand-efficient inhibitors of Plasmodium falciparum and Plasmodium vivax N-myristoyltransferase
    • Rackham, M. D. et al. Discovery of novel and ligand-efficient inhibitors of Plasmodium falciparum and Plasmodium vivax N-myristoyltransferase. J. Med. Chem. 56, 371-375 (2013).
    • (2013) J. Med. Chem. , vol.56 , pp. 371-375
    • Rackham, M.D.1
  • 41
    • 84855848964 scopus 로고    scopus 로고
    • Discovery of a novel class of orally active trypanocidal Nmyristoyltransferase inhibitors
    • Brand, S. et al. Discovery of a novel class of orally active trypanocidal Nmyristoyltransferase inhibitors. J. Med. Chem. 55, 140-152 (2011).
    • (2011) J. Med. Chem. , vol.55 , pp. 140-152
    • Brand, S.1
  • 42
    • 33746616420 scopus 로고    scopus 로고
    • In-depth analysis of the membrane and cytosolic proteome of red blood cells
    • DOI 10.1182/blood-2005-11-007799
    • Pasini, E. M. et al. In-depth analysis of the membrane and cytosolic proteome of red blood cells. Blood 108, 791-801 (2006). (Pubitemid 44154609)
    • (2006) Blood , vol.108 , Issue.3 , pp. 791-801
    • Pasini, E.M.1    Kirkegaard, M.2    Mortensen, P.3    Lutz, H.U.4    Thomas, A.W.5    Mann, M.6
  • 43
    • 34347218266 scopus 로고    scopus 로고
    • Labeling, detection and identification of newly synthesized proteomes with bioorthogonal non-canonical amino-acid tagging
    • DOI 10.1038/nprot.2007.52, PII NPROT.2007.52
    • Dieterich, D. C. et al. Labeling, detection and identification of newly synthesized proteomes with bioorthogonal non-canonical amino-acid tagging. Nature Protoc. 2, 532-540 (2007). (Pubitemid 47040017)
    • (2007) Nature Protocols , vol.2 , Issue.3 , pp. 532-540
    • Dieterich, D.C.1    Lee, J.J.2    Link, A.J.3    Graumann, J.4    Tirrell, D.A.5    Schuman, E.M.6
  • 44
    • 84859152006 scopus 로고    scopus 로고
    • Subcellular location, phosphorylation and assembly into the motor complex of GAP45 during Plasmodium falciparum schizont development
    • Ridzuan, M. A. et al. Subcellular location, phosphorylation and assembly into the motor complex of GAP45 during Plasmodium falciparum schizont development. PLoS ONE 7, e33845 (2012).
    • (2012) PLoS ONE , vol.7
    • Ridzuan, M.A.1
  • 45
    • 77958088822 scopus 로고    scopus 로고
    • Functional dissection of the apicomplexan glideosome molecular architecture
    • Frenal, K. et al. Functional dissection of the apicomplexan glideosome molecular architecture. Cell Host Microbe 8, 343-357 (2010).
    • (2010) Cell Host Microbe , vol.8 , pp. 343-357
    • Frenal, K.1
  • 46
    • 84861212906 scopus 로고    scopus 로고
    • Selective inhibitors of protozoan protein N-myristoyltransferases as starting points for tropical disease medicinal chemistry programs
    • Bell, A. S. et al. Selective inhibitors of protozoan protein N-myristoyltransferases as starting points for tropical disease medicinal chemistry programs. PLoS Negl. Trop. Dis. 6, e1625 (2012).
    • (2012) PLoS Negl. Trop. Dis. , vol.6
    • Bell, A.S.1
  • 48
    • 42149152335 scopus 로고    scopus 로고
    • Concentration and purification by magnetic separation of the erythrocytic stages of all human Plasmodium species
    • Ribaut, C. et al. Concentration and purification by magnetic separation of the erythrocytic stages of all human Plasmodium species. Malar. J. 7, 45 (2008).
    • (2008) Malar. J. , vol.7 , pp. 45
    • Ribaut, C.1
  • 49
    • 0018704491 scopus 로고
    • Synchronization of Plasmodium falciparum erythrocytic stages in culture
    • DOI 10.2307/3280287
    • Lambros, C. & Vanderberg, J. P. Synchronization of Plasmodium falciparum erythrocytic stages in culture. J. Parasitol. 65, 418-420 (1979). (Pubitemid 10222999)
    • (1979) Journal of Parasitology , vol.65 , Issue.3 , pp. 418-420
    • Lambros, C.1    Vanderberg, J.P.2
  • 50
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wisniewski, J. R., Zougman, A., Nagaraj, N. & Mann, M. Universal sample preparation method for proteome analysis. Nature Methods 6, 359-362 (2009).
    • (2009) Nature Methods , vol.6 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 51
    • 84855879725 scopus 로고    scopus 로고
    • A fluorescence-based assay for N-myristoyltransferase activity
    • Goncalves, V. et al. A fluorescence-based assay for N- myristoyltransferase activity. Anal. Biochem. 421, 342-344 (2012).
    • (2012) Anal. Biochem. , vol.421 , pp. 342-344
    • Goncalves, V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.