메뉴 건너뛰기




Volumn 6, Issue 4, 2012, Pages

Selective inhibitors of protozoan protein N-myristoyltransferases as starting points for tropical disease medicinal chemistry programs

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN N MYRISTOYLTRANSFERASE; PROTEIN N MYRISTOYLTRANSFERASE INHIBITOR; ACYLTRANSFERASE; ANTIPROTOZOAL AGENT; ENZYME INHIBITOR; GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE; PROTOZOAL PROTEIN;

EID: 84861212906     PISSN: 19352727     EISSN: 19352735     Source Type: Journal    
DOI: 10.1371/journal.pntd.0001625     Document Type: Article
Times cited : (78)

References (47)
  • 1
    • 77954235856 scopus 로고    scopus 로고
    • TDR: For Research on Diseases of Poverty
    • TDR: For Research on Diseases of Poverty. http://apps.who.int/tdr/.
  • 2
    • 84861211738 scopus 로고    scopus 로고
    • TDR: Leishmaniasis
    • TDR: Leishmaniasis. http://www.who.int/tdr/diseases/leish/diseaseinfo.htm.
  • 4
    • 0034780949 scopus 로고    scopus 로고
    • Drug resistance in Indian visceral leishmaniasis
    • Sundar S, (2001) Drug resistance in Indian visceral leishmaniasis. Trop Med Int Health 6: 849-854.
    • (2001) Trop Med Int Health , vol.6 , pp. 849-854
    • Sundar, S.1
  • 6
    • 84860727658 scopus 로고    scopus 로고
    • World Malaria Report
    • WHO,
    • WHO (2011) World Malaria Report. http://www.who.int/entity/malaria/world_malaria_report_2011/en/index.html.
    • (2011)
  • 9
    • 0035884456 scopus 로고    scopus 로고
    • Chloroquine-resistant malaria
    • Wellems TE, Plowe CV, (2001) Chloroquine-resistant malaria. J Infect Dis 184: 770-776.
    • (2001) J Infect Dis , vol.184 , pp. 770-776
    • Wellems, T.E.1    Plowe, C.V.2
  • 10
    • 0003989708 scopus 로고    scopus 로고
    • Drug Resistance in Malaria
    • WHO/CDS/DRS4: WHO
    • Bloland PB, (2001) Drug Resistance in Malaria. WHO/CDS/DRS4: WHO.
    • (2001)
    • Bloland, P.B.1
  • 13
    • 0033182170 scopus 로고    scopus 로고
    • Delaying antimalarial drug resistance with combination chemotherapy
    • White NJ, (1999) Delaying antimalarial drug resistance with combination chemotherapy. Parassitologia 41: 301-308.
    • (1999) Parassitologia , vol.41 , pp. 301-308
    • White, N.J.1
  • 14
  • 15
    • 36148945171 scopus 로고    scopus 로고
    • Genomics, systems biology and drug development for infectious diseases
    • Sakata T, Winzeler EA, (2007) Genomics, systems biology and drug development for infectious diseases. Mol Biosyst 3: 841-848.
    • (2007) Mol Biosyst , vol.3 , pp. 841-848
    • Sakata, T.1    Winzeler, E.A.2
  • 16
    • 58049219752 scopus 로고    scopus 로고
    • Identification and characterization of small molecule inhibitors of Plasmodium falciparum dihydroorotate dehydrogenase
    • Patel V, Booker M, Kramer M, Ross L, Celatka CA, et al. (2008) Identification and characterization of small molecule inhibitors of Plasmodium falciparum dihydroorotate dehydrogenase. J Biol Chem 283: 35078-35085.
    • (2008) J Biol Chem , vol.283 , pp. 35078-35085
    • Patel, V.1    Booker, M.2    Kramer, M.3    Ross, L.4    Celatka, C.A.5
  • 17
    • 79955825448 scopus 로고    scopus 로고
    • Drug to genome to drug: discovery of new antiplasmodial compounds
    • Beghyn TB, Charton J, Leroux F, Laconde G, Bourin A, et al. (2011) Drug to genome to drug: discovery of new antiplasmodial compounds. J Med Chem 54: 3222-3240.
    • (2011) J Med Chem , vol.54 , pp. 3222-3240
    • Beghyn, T.B.1    Charton, J.2    Leroux, F.3    Laconde, G.4    Bourin, A.5
  • 18
    • 79955867106 scopus 로고    scopus 로고
    • Trypanosoma brucei Glycogen Synthase Kinase-3, A Target for Anti-Trypanosomal Drug Development: A Public-Private Partnership to Identify Novel Leads
    • Oduor RO, Ojo KK, Williams GP, Bertelli F, Mills J, et al. (2011) Trypanosoma brucei Glycogen Synthase Kinase-3, A Target for Anti-Trypanosomal Drug Development: A Public-Private Partnership to Identify Novel Leads. PLoS Negl Trop Dis 5: e1017.
    • (2011) PLoS Negl Trop Dis , vol.5
    • Oduor, R.O.1    Ojo, K.K.2    Williams, G.P.3    Bertelli, F.4    Mills, J.5
  • 19
    • 0345073644 scopus 로고    scopus 로고
    • Protein farnesyl and N-myristoyl transferases: piggy-back medicinal chemistry targets for the development of antitrypanosomatid and antimalarial therapeutics
    • Gelb MH, Van Voorhis WC, Buckner FS, Yokoyama K, Eastman R, et al. (2003) Protein farnesyl and N-myristoyl transferases: piggy-back medicinal chemistry targets for the development of antitrypanosomatid and antimalarial therapeutics. Molecular and Biochemical Parasitology 126: 155-163.
    • (2003) Molecular and Biochemical Parasitology , vol.126 , pp. 155-163
    • Gelb, M.H.1    Van Voorhis, W.C.2    Buckner, F.S.3    Yokoyama, K.4    Eastman, R.5
  • 20
    • 0037697840 scopus 로고    scopus 로고
    • N-Myristoyltransferase inhibitors as potential antifungal drugs
    • Ohtsuka T, Aoki I, (2003) N-Myristoyltransferase inhibitors as potential antifungal drugs. Drugs of the Future 28: 143-152.
    • (2003) Drugs of the Future , vol.28 , pp. 143-152
    • Ohtsuka, T.1    Aoki, I.2
  • 21
    • 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, et al. (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
  • 22
    • 77950406212 scopus 로고    scopus 로고
    • N-myristoyltransferase inhibitors as new leads to treat sleeping sickness
    • Frearson JA, Brand S, McElroy SP, Cleghorn LAT, Smid O, et al. (2010) N-myristoyltransferase inhibitors as new leads to treat sleeping sickness. Nature 464: 728-732.
    • (2010) Nature , vol.464 , pp. 728-732
    • Frearson, J.A.1    Brand, S.2    McElroy, S.P.3    Cleghorn, L.A.T.4    Smid, O.5
  • 24
    • 33744806630 scopus 로고    scopus 로고
    • Characterization and selective inhibition of myristoyl-CoA:protein N-myristoyltransferase from Trypanosoma brucei and Leishmania major
    • Panethymitaki C, Bowyer PW, Price HP, Leatherbarrow RJ, Brown KA, et al. (2006) Characterization and selective inhibition of myristoyl-CoA:protein N-myristoyltransferase 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
  • 25
    • 71549117083 scopus 로고    scopus 로고
    • Myristoyl-CoA:protein N-myristoyltransferase depletion in trypanosomes causes avirulence and endocytic defects
    • Price HP, Guther ML, Ferguson MA, Smith DF, (2010) Myristoyl-CoA:protein N-myristoyltransferase depletion in trypanosomes causes avirulence and endocytic defects. Mol Biochem Parasitol 169: 55-58.
    • (2010) Mol Biochem Parasitol , vol.169 , pp. 55-58
    • Price, H.P.1    Guther, M.L.2    Ferguson, M.A.3    Smith, D.F.4
  • 26
    • 0037470198 scopus 로고    scopus 로고
    • Myristoyl-CoA:protein N-myristoyltransferase, an essential enzyme and potential drug target in kinetoplastid parasites
    • Price HP, Menon MR, Panethymitaki C, Goulding D, McKean PG, et al. (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
  • 27
    • 36749030760 scopus 로고    scopus 로고
    • Molecules incorporating a benzothiazole core scaffold inhibit the N-myristoyltransferase of Plasmodium falciparum
    • Bowyer PW, Gunaratne RS, Grainger M, Withers-Martinez C, Wickramsinghe SR, et al. (2007) Molecules incorporating a benzothiazole core scaffold inhibit the N-myristoyltransferase of Plasmodium falciparum. Biochem J 408: 173-180.
    • (2007) Biochem J , vol.408 , pp. 173-180
    • Bowyer, P.W.1    Gunaratne, R.S.2    Grainger, M.3    Withers-Martinez, C.4    Wickramsinghe, S.R.5
  • 28
    • 0034212670 scopus 로고    scopus 로고
    • Characterization of N-myristoyltransferase from Plasmodium falciparum
    • Gunaratne RS, Sajid M, Ling IT, Tripathi R, Pachebat JA, et al. (2000) Characterization of N-myristoyltransferase from Plasmodium falciparum. Biochem J 348 Pt 2: 459-463.
    • (2000) Biochem J , vol.348 , Issue.Pt 2 , pp. 459-463
    • Gunaratne, R.S.1    Sajid, M.2    Ling, I.T.3    Tripathi, R.4    Pachebat, J.A.5
  • 31
    • 0036775770 scopus 로고    scopus 로고
    • Crystal Structures of Candida albicans N-Myristoyltransferase with Two Distinct Inhibitors
    • Sogabe S, Masubuchi M, Sakata K, Fukami TA, Morikami K, et al. (2002) Crystal Structures of Candida albicans N-Myristoyltransferase with Two Distinct Inhibitors. Chemistry & Biology 9: 1119-1128.
    • (2002) Chemistry & Biology , vol.9 , pp. 1119-1128
    • Sogabe, S.1    Masubuchi, M.2    Sakata, K.3    Fukami, T.A.4    Morikami, K.5
  • 32
    • 0030923009 scopus 로고    scopus 로고
    • Scanning Alanine Mutagenesis and De-peptidization of a Candida albicans Myristoyl-CoA:ProteinN-Myristoyltransferase Octapeptide Substrate Reveals Three Elements Critical for Molecular Recognition
    • McWherter CA, Rocque WJ, Zupec ME, Freeman SK, Brown DL, et al. (1997) Scanning Alanine Mutagenesis and De-peptidization of a Candida albicans Myristoyl-CoA:ProteinN-Myristoyltransferase Octapeptide Substrate Reveals Three Elements Critical for Molecular Recognition. Journal of Biological Chemistry 272: 11874-11880.
    • (1997) Journal of Biological Chemistry , 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
  • 33
    • 0031788774 scopus 로고    scopus 로고
    • Structure of N-myristoyltransferase with bound myristoylCoA and peptide substrate analogs
    • Bhatnagar RS, Futterer K, Farazi TA, Korolev S, Murray CL, et al. (1998) Structure of N-myristoyltransferase with bound myristoylCoA and peptide substrate analogs. Nat Struct Biol 5: 1091-1097.
    • (1998) Nat Struct Biol , vol.5 , pp. 1091-1097
    • Bhatnagar, R.S.1    Futterer, K.2    Farazi, T.A.3    Korolev, S.4    Murray, C.L.5
  • 34
    • 0032510384 scopus 로고    scopus 로고
    • Novel biologically active nonpeptidic inhibitors of myristoylCoA:protein N-myristoyltransferase
    • Devadas B, Freeman SK, McWherter CA, Kishore NS, Lodge JK, et al. (1998) Novel biologically active nonpeptidic inhibitors of myristoylCoA:protein N-myristoyltransferase. J Med Chem 41: 996-1000.
    • (1998) J Med Chem , vol.41 , pp. 996-1000
    • Devadas, B.1    Freeman, S.K.2    McWherter, C.A.3    Kishore, N.S.4    Lodge, J.K.5
  • 35
    • 0037794723 scopus 로고    scopus 로고
    • Discovery of fungicidal N-myristoyl transferase inhibitors
    • San Diego, CA, United States
    • Bell AS, (2001) Discovery of fungicidal N-myristoyl transferase inhibitors. 221st ACS National Meeting. San Diego, CA, United States.
    • (2001) 221st ACS National Meeting
    • Bell, A.S.1
  • 36
    • 84861211739 scopus 로고    scopus 로고
    • Maximizing the coverage and flexibility of a diverse representative subset for screening variable number of compounds to suit target knowledge
    • Washington, DC
    • Yeap SK, Walley RJ, Mason JS, (2005) Maximizing the coverage and flexibility of a diverse representative subset for screening variable number of compounds to suit target knowledge. 230th ACS National Meeting,. Washington, DC.
    • (2005) 230th ACS National Meeting
    • Yeap, S.K.1    Walley, R.J.2    Mason, J.S.3
  • 37
    • 0032549571 scopus 로고    scopus 로고
    • A second mammalian N-myristoyltransferase
    • Giang DK, Cravatt BF, (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
  • 38
    • 21444459919 scopus 로고    scopus 로고
    • N-myristoyltransferase 1 is essential in early mouse development
    • Yang SH, Shrivastav A, Kosinski C, Sharma RK, Chen MH, et al. (2005) N-myristoyltransferase 1 is essential in early mouse development. J Biol Chem 280: 18990-18995.
    • (2005) J Biol Chem , vol.280 , pp. 18990-18995
    • Yang, S.H.1    Shrivastav, A.2    Kosinski, C.3    Sharma, R.K.4    Chen, M.H.5
  • 40
    • 77950344649 scopus 로고    scopus 로고
    • N-Myristoyltransferase from Leishmania donovani: Structural and Functional Characterisation of a Potential Drug Target for Visceral Leishmaniasis
    • Brannigan JA, Smith BA, Yu Z, Brzozowski AM, Hodgkinson MR, et al. (2010) N-Myristoyltransferase from Leishmania donovani: Structural and Functional Characterisation of a Potential Drug Target for Visceral Leishmaniasis. Journal of Molecular Biology 396: 985-999.
    • (2010) Journal of Molecular Biology , vol.396 , pp. 985-999
    • Brannigan, J.A.1    Smith, B.A.2    Yu, Z.3    Brzozowski, A.M.4    Hodgkinson, M.R.5
  • 41
    • 0034895593 scopus 로고    scopus 로고
    • CAP5.5, a life-cycle-regulated, cytoskeleton-associated protein is a member of a novel family of calpain-related proteins in Trypanosoma brucei
    • Hertz-Fowler C, Ersfeld K, Gull K, (2001) CAP5.5, a life-cycle-regulated, cytoskeleton-associated protein is a member of a novel family of calpain-related proteins in Trypanosoma brucei. Mol Biochem Parasitol 116: 25-34.
    • (2001) Mol Biochem Parasitol , vol.116 , pp. 25-34
    • Hertz-Fowler, C.1    Ersfeld, K.2    Gull, K.3
  • 42
    • 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, (1999) A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays. J Biomol Screen 4: 67-73.
    • (1999) J Biomol Screen , vol.4 , pp. 67-73
    • Zhang, J.H.1    Chung, T.D.2    Oldenburg, K.R.3
  • 43
    • 4544350863 scopus 로고    scopus 로고
    • Enrichment of extremely noisy high-throughput screening data using a naive Bayes classifier
    • Glick M, Klon AE, Acklin P, Davies JW, (2004) Enrichment of extremely noisy high-throughput screening data using a naive Bayes classifier. J Biomol Screen 9: 32-36.
    • (2004) J Biomol Screen , vol.9 , pp. 32-36
    • Glick, M.1    Klon, A.E.2    Acklin, P.3    Davies, J.W.4
  • 46
    • 1942453243 scopus 로고    scopus 로고
    • Ligand efficiency: a useful metric for lead selection
    • Hopkins AL, Groom CR, Alex A, (2004) Ligand efficiency: a useful metric for lead selection. Drug Discov Today 9: 430-431.
    • (2004) Drug Discov Today , vol.9 , pp. 430-431
    • Hopkins, A.L.1    Groom, C.R.2    Alex, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.