메뉴 건너뛰기




Volumn 5, Issue 17, 2013, Pages 2019-2035

Corrigendum: A pharmacophore-based virtual screening approach for the discovery of Trypanosoma cruzi GAPDH inhibitors (Future Medicinal Chemistry (2013) 5: 17 (2019-2035) DOI: 10.4155/fmc.13.166);A pharmacophore-based virtual screening approach for the discovery of Trypanosoma cruzi GAPDH inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

1 PYRAZOLYL ETHANONE DERIVATIVE; 1,3 DIOXOISOINDOLINE DERIVATIVE; 4 AMINO THIOPHEN DERIVATIVE; ANTITRYPANOSOMAL AGENT; INDOLEACETIC ACID; TRYPANOSOMA CRUZI GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 84887935819     PISSN: 17568919     EISSN: 17568927     Source Type: Journal    
DOI: 10.4155/fmc.13.213     Document Type: Erratum
Times cited : (25)

References (53)
  • 2
    • 34548636054 scopus 로고    scopus 로고
    • The path to new medicines
    • DOI 10.1038/449164a, PII 449164A
    • Callan B, Gillespie I. The path to new medicines. Nature 449(7159), 164-165 (2007). (Pubitemid 47402354)
    • (2007) Nature , vol.449 , Issue.7159 , pp. 164-165
    • Callan, B.1    Gillespie, I.2
  • 3
    • 84864116400 scopus 로고    scopus 로고
    • The role of academic institutions in the development of drugs for rare and neglected diseases
    • Coles LD, Cloyd JC The role of academic institutions in the development of drugs for rare and neglected diseases. Clin. Pharmacol. Ther. 92(2), 193-202 (2012).
    • (2012) Clin. Pharmacol. Ther. , vol.92 , Issue.2 , pp. 193-202
    • Coles, L.D.1    Cloyd, J.C.2
  • 4
    • 77953094699 scopus 로고    scopus 로고
    • The role of product development partnerships in research and development for neglected diseases
    • Moran M, Guzman J, Ropars A.L., Illmer A. The role of product development partnerships in research and development for neglected diseases. Int. Health 2(2), 114-122 (2010).
    • (2010) Int. Health , vol.2 , Issue.2 , pp. 114-122
    • Moran, M.1    Guzman, J.2    Ropars, A.L.3    Illmer, A.4
  • 5
    • 77950824213 scopus 로고    scopus 로고
    • Chagas disease
    • Rassi A, Marin-Neto JA.Chagas disease. Lancet 375(9723), 1388-1402 (2010).
    • (2010) Lancet , vol.375 , Issue.9723 , pp. 1388-1402
    • Rassi, A.1    Marin-Neto, J.A.2
  • 6
    • 70449566766 scopus 로고    scopus 로고
    • Feasibility, drug safety, and effectiveness of etiological treatment programs for chagas disease in Honduras, guatemala, and bolivia: 10-year experience of médecins sans frontières
    • Yun O, Lima MA, Ellman T et al. Feasibility, drug safety, and effectiveness of etiological treatment programs for Chagas disease in Honduras, Guatemala, and Bolivia: 10-year experience of Médecins Sans Frontières. PLoS Neglect. Trop. Dis. 3(7), e488 (2009).
    • (2009) PLoS Neglect. Trop. Dis. , vol.3 , Issue.7
    • Yun, O.1    Lima, M.A.2    Ellman, T.3
  • 7
    • 0002921521 scopus 로고
    • Nova tripanossomíase humana. Estudos sobre a morfologia e o ciclo evolutivo do Schizotrypanum cruzi n. gen., n. sp., agente etiológico de nova entidade mórbida do homem
    • Chagas C. Nova tripanossomíase humana. Estudos sobre a morfologia e o ciclo evolutivo do Schizotrypanum cruzi n. gen., n. sp., agente etiológico de nova entidade mórbida do homem. Mem. Inst. Oswaldo Cruz. 1(2), 159-218 (1909).
    • (1909) Mem. Inst. Oswaldo Cruz , vol.1 , Issue.2 , pp. 159-218
    • Chagas, C.1
  • 8
    • 34248375271 scopus 로고    scopus 로고
    • An insight on targets and patented drugs for chemotherapy of chagas disease
    • Duschak VG, Couto AS An insight on targets and patented drugs for chemotherapy of Chagas disease. Recent Pat. Antiinfect. Drug Discov. 2(1), 19-51 (2007). (Pubitemid 46729086)
    • (2007) Recent Patents on Anti-Infective Drug Discovery , vol.2 , Issue.1 , pp. 19-51
    • Duschak, V.G.1    Couto, A.S.2
  • 9
    • 77953082627 scopus 로고    scopus 로고
    • Specific chemotherapy of chagas disease: Relevance, current limitations and new approaches
    • Urbina JA. Specific chemotherapy of Chagas disease: relevance, current limitations and new approaches. Acta Trop. 115(1-2), 55-68 (2010).
    • (2010) Acta Trop. , vol.115 , Issue.1-2 , pp. 55-68
    • Urbina, J.A.1
  • 10
    • 73449123081 scopus 로고    scopus 로고
    • Structure-based drug discovery for tropical diseases
    • Guido RVC, Oliva G. Structure-based drug discovery for tropical diseases. Curr. Top. Med. Chem. 9(9), 824-843 (2009).
    • (2009) Curr. Top. Med. Chem , vol.9 , Issue.9 , pp. 824-843
    • Guido, R.V.C.1    Oliva, G.2
  • 12
    • 71549138698 scopus 로고    scopus 로고
    • Genetic validation of aldolase and glyceraldehyde-3-phosphate dehydrogenase as drug targets in trypanosoma brucei
    • Cáceres A.J., Michels PAM, Hannaert V. Genetic validation of aldolase and glyceraldehyde-3-phosphate dehydrogenase as drug targets in Trypanosoma brucei. Mol. Biochem. Parasitol. 169(1), 50-54 (2010).
    • (2010) Mol. Biochem. Parasitol. , vol.169 , Issue.1 , pp. 50-54
    • Cáceres, A.J.1    Michels, P.A.M.2    Hannaert, V.3
  • 13
    • 80054923170 scopus 로고    scopus 로고
    • Modern drug discovery technologies: Opportunities and challenges in lead discovery
    • Guido RVC, Oliva G, Andricopulo AD Modern drug discovery technologies: opportunities and challenges in lead discovery. Comb. Chem. High Throughput Screen 14(10), 830-839 (2011).
    • (2011) Comb. Chem. High Throughput Screen , vol.14 , Issue.10 , pp. 830-839
    • Guido, R.V.C.1    Oliva, G.2    Andricopulo, A.D.3
  • 14
    • 84865370542 scopus 로고    scopus 로고
    • Structure- and ligand-based drug design approaches for neglected tropical diseases
    • Guido RVC, Oliva G, Andricopulo AD Structure- and ligand-based drug design approaches for neglected tropical diseases. Pure Appl. Chem. 84(9), 1857-1866 (2012).
    • (2012) Pure Appl. Chem. , vol.84 , Issue.9 , pp. 1857-1866
    • Guido, R.V.C.1    Oliva, G.2    Andricopulo, A.D.3
  • 15
  • 16
    • 39049094335 scopus 로고    scopus 로고
    • Virtual screening and its integration with modern drug design technologies
    • DOI 10.2174/092986708783330683
    • Guido RVC, Oliva G, Andricopulo AD Virtual screening and its integration with modern drug design technologies. Curr. Med. Chem. 15(1), 37-46 (2008). (Pubitemid 351234626)
    • (2008) Current Medicinal Chemistry , vol.15 , Issue.1 , pp. 37-46
    • Guido, R.V.C.1    Oliva, G.2    Andricopulo, A.D.3
  • 17
    • 77957235318 scopus 로고    scopus 로고
    • Discovery of new inhibitors of schistosoma mansoni PNP by pharmacophore-based virtual screening
    • Postigo MP, Guido RVC, Oliva G et al. Discovery of new inhibitors of Schistosoma mansoni PNP by pharmacophore-based virtual screening. J. Chem. Inf. Model. 50(9), 1693-1705 (2010).
    • (2010) J. Chem. Inf. Model. , vol.50 , Issue.9 , pp. 1693-1705
    • Postigo, M.P.1    Guido, R.V.C.2    Oliva, G.3
  • 18
    • 64949178452 scopus 로고    scopus 로고
    • Kinetic and crystallographic studies on glyceraldehyde-3-phosphate dehydrogenase from trypanosoma cruzi in complex with iodoacetate
    • Guido RVC, Balliano TL, Andricopulo A.D., Oliva G. Kinetic and crystallographic studies on glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi in complex with iodoacetate. Lett. Drug Des. Discov. 6(3), 210-214 (2009).
    • (2009) Lett. Drug Des. Discov. , vol.6 , Issue.3 , pp. 210-214
    • Guido, R.V.C.1    Balliano, T.L.2    Andricopulo, A.D.3    Oliva, G.4
  • 19
    • 77958067493 scopus 로고    scopus 로고
    • Structural insights into the molecular basis responsible for the effects of immobilization on the kinetic parameters of glyceraldehyde-3-phosphate dehydrogenase from trypanosoma cruzi and human
    • Guido RVC, Cardoso CL, Moraes MC de, Andricopulo AD, Cass QB, Oliva G. Structural insights into the molecular basis responsible for the effects of immobilization on the kinetic parameters of glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi and human. J. Braz. Chem. Soc. 21(10), 1845-1853 (2010).
    • (2010) J. Braz. Chem. Soc. , vol.21 , Issue.10 , pp. 1845-1853
    • Guido, R.V.C.1    Cardoso, C.L.2    De Moraes, M.C.3    Andricopulo, A.D.4    Cass, Q.B.5    Oliva, G.6
  • 20
    • 44449109653 scopus 로고    scopus 로고
    • Structural basis for selective inhibition of trypanosomatid glyceraldehyde-3-phosphate dehydrogenase: Molecular docking and 3D QSAR studies
    • DOI 10.1021/ci700453j
    • Guido RVC, Oliva G, Montanari C.A., Andricopulo AD Structural basis for selective inhibition of trypanosomatid glyceraldehyde-3-phosphate dehydrogenase: molecular docking and 3D QSAR studies. J. Chem. Inf. Model. 48(4), 918-929 (2008). (Pubitemid 351757757)
    • (2008) Journal of Chemical Information and Modeling , vol.48 , Issue.4 , pp. 918-929
    • Guido, R.V.C.1    Oliva, G.2    Montanari, C.A.3    Andricopulo, A.D.4
  • 21
    • 0032513293 scopus 로고    scopus 로고
    • Trypanosoma cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase: Structure, catalytic mechanism and targeted inhibitor design
    • DOI 10.1016/S0014-5793(98)00154-9, PII S0014579398001549
    • Souza DH, Garratt RC, Araújo AP et al. Trypanosoma cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase: structure, catalytic mechanism and targeted inhibitor design. FEBS Lett. 424(3), 131-135 (1998). (Pubitemid 28135298)
    • (1998) FEBS Letters , vol.424 , Issue.3 , pp. 131-135
    • Souza, D.H.F.1    Garratt, R.C.2    Araujo, A.P.U.3    Guimaraes, B.G.4    Jesus, W.D.P.5    Michels, P.A.M.6    Hannaert, V.7    Oliva, G.8
  • 22
  • 23
    • 0038131064 scopus 로고    scopus 로고
    • Evidence for the two phosphate binding sites of an analogue of the thioacyl intermediate for the trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase-catalyzed reaction, from its crystal structure
    • DOI 10.1021/bi0206107
    • Castilho MS, Pavão F, Oliva G., Ladame S, Willson M, Périé J. Evidence for the two phosphate binding sites of an analogue of the thioacyl intermediate for the Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase-catalyzed reaction, from its crystal structure. Biochemistry 42(23), 7143-7151 (2003). (Pubitemid 36706497)
    • (2003) Biochemistry , vol.42 , Issue.23 , pp. 7143-7151
    • Castilho, M.S.1    Pavao, F.2    Oliva, G.3    Ladame, S.4    Willson, M.5    Perie, J.6
  • 25
    • 0032548073 scopus 로고    scopus 로고
    • Selective tight binding inhibitors of trypanosomal glyceraldehyde-3- phosphate dehydrogenase via structure-based drug design
    • DOI 10.1021/jm9802620
    • Aronov AM, Verlinde CL, Hol W.G., Gelb MH Selective tight binding inhibitors of trypanosomal glyceraldehyde-3-phosphate dehydrogenase via structure-based drug design. J. Med. Chem. 41(24), 4790-4799 (1998). (Pubitemid 28530455)
    • (1998) Journal of Medicinal Chemistry , vol.41 , Issue.24 , pp. 4790-4799
    • Aronov, A.M.1    Verlinde, C.L.M.J.2    Hol, W.G.J.3    Gelb, M.H.4
  • 27
    • 0035931561 scopus 로고    scopus 로고
    • + analogue is a nanomolar inhibitor of trypanosomal glyceraldehyde-3-phosphate dehydrogenase
    • DOI 10.1016/S0960-894X(00)00608-9, PII S0960894X00006089
    • + analogue is a nanomolar inhibitor of trypanosomal glyceraldehyde-3-phosphate dehydrogenase. Bioorg. Med. Chem. Lett. 11(2), 95-98 (2001). (Pubitemid 32101441)
    • (2001) Bioorganic and Medicinal Chemistry Letters , vol.11 , Issue.2 , pp. 95-98
    • Kennedy, K.J.1    Bressi, J.C.2    Gelb, M.H.3
  • 28
    • 0038336897 scopus 로고    scopus 로고
    • Application and limitations of x-ray crystallographic data in structure-based ligand and drug design
    • DOI 10.1002/anie.200200539
    • Davis AM, Teague SJ, Kleywegt GJ Application and limitations of x-ray crystallographic data in structure-based ligand and drug design. Angew. Chem. Int. Ed. Engl. 42(24), 2718-2736 (2003). (Pubitemid 36813974)
    • (2003) Angewandte Chemie - International Edition , vol.42 , Issue.24 , pp. 2718-2736
    • Davis, A.M.1    Teague, S.J.2    Kleywegt, G.J.3
  • 30
    • 0344442882 scopus 로고    scopus 로고
    • Crystal structure of Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase complexed with an analogue of 1,3-bisphospho-D-glyceric acid: Selective inhibition by structure-based design
    • DOI 10.1046/j.1432-1033.2003.03857.x
    • Ladame S, Castilho MS, Silva CHTP et al. Crystal structure of Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase complexed with an analogue of 1,3-bisphospho-D-glyceric acid. Eur. J. Biochem. 270(22), 4574-4586 (2003). (Pubitemid 37452534)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.22 , pp. 4574-4586
    • Ladame, S.1    Castilho, M.S.2    Silva, C.H.T.P.3    Denier, C.4    Hannaert, V.5    Perie, J.6    Oliva, G.7    Willson, M.8
  • 32
    • 84952944528 scopus 로고    scopus 로고
    • 'Hot spot' analysis of protein-binding sites as a prerequisite for structure-based virtual screening and lead optimization
    • Langer T, Hoffmann RD (Eds). Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany
    • Brenk R, Klebe G. 'Hot Spot' Analysis of Protein-binding Sites as a Prerequisite for Structure-based Virtual Screening and Lead Optimization In: Pharmacophores and Pharmacophore Searches (Volume 32) Langer T, Hoffmann RD (Eds). Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany (2006).
    • (2006) Pharmacophores and Pharmacophore Searches , vol.32
    • Brenk, R.1    Klebe, G.2
  • 33
    • 0036510961 scopus 로고    scopus 로고
    • Identification and mapping of small-molecule binding sites in proteins: Computational tools for structure-based drug design
    • DOI 10.1016/S0014-827X(02)01211-9, PII S0014827X02012119
    • Sotriffer C, Klebe G. Identification and mapping of small-molecule binding sites in proteins: computational tools for structure-based drug design. Farmaco 57(3), 243-251 (2002). (Pubitemid 38365952)
    • (2002) Farmaco , vol.57 , Issue.3 , pp. 243-251
    • Sotriffer, C.1    Klebe, G.2
  • 34
    • 0034645763 scopus 로고    scopus 로고
    • Knowledge-based scoring function to predict protein-ligand interactions
    • DOI 10.1006/jmbi.1999.3371
    • Gohlke H, Hendlich M, Klebe G. Knowledge-based scoring function to predict protein-ligand interactions. J. Mol. Biol. 2(2), 337-356 (2000). (Pubitemid 30045364)
    • (2000) Journal of Molecular Biology , vol.295 , Issue.2 , pp. 337-356
    • Gohlke, H.1    Hendlich, M.2    Klebe, G.3
  • 35
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • DOI 10.1021/jm00145a002
    • Goodford PJ. A computational procedure for determining energetically favorable binding sites on biologically important macromolecules. J. Med. Chem. 28(7), 849-857 (1985). (Pubitemid 15012490)
    • (1985) Journal of Medicinal Chemistry , vol.28 , Issue.7 , pp. 849-857
    • Goodford, P.J.1
  • 37
    • 0030599010 scopus 로고    scopus 로고
    • A fast flexible docking method using an incremental construction algorithm
    • DOI 10.1006/jmbi.1996.0477
    • Rarey M, Kramer B, Lengauer T., Klebe G. A fast flexible docking method using an incremental construction algorithm. J. Mol. Biol. 261(3), 470-489 (1996). (Pubitemid 26335901)
    • (1996) Journal of Molecular Biology , vol.261 , Issue.3 , pp. 470-489
    • Rarey, M.1    Kramer, B.2    Lengauer, T.3    Klebe, G.4
  • 38
    • 52949103672 scopus 로고    scopus 로고
    • Anacardic acid derivatives as inhibitors of glyceraldehyde-3-phosphate dehydrogenase from trypanosoma cruzi
    • Pereira JM, Severino R P, Vieira PC et al. Anacardic acid derivatives as inhibitors of glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi. Bioorg. Med. Chem. 16(19), 8889-8888 (2008).
    • (2008) Bioorg. Med. Chem. , vol.16 , Issue.19 , pp. 8889-8888
    • Pereira, J.M.1    Severino, R.P.2    Vieira, P.C.3
  • 43
    • 62149091122 scopus 로고    scopus 로고
    • Discovery of novel trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase inhibitors
    • Freitas R.F., Prokopczyk IM, Zottis A et al. Discovery of novel Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase inhibitors. Bioorg. Med. Chem. 17(6), 2476-2482 (2009).
    • (2009) Bioorg. Med. Chem. , vol.17 , Issue.6 , pp. 2476-2482
    • Freitas, R.F.1    Prokopczyk, I.M.2    Zottis, A.3
  • 44
    • 0034461768 scopus 로고    scopus 로고
    • Drug-like properties and the causes of poor solubility and poor permeability
    • DOI 10.1016/S1056-8719(00)00107-6, PII S1056871900001076
    • Lipinski CA. Drug-like properties and the causes of poor solubility and poor permeability. J. Pharmacol. Toxicol. Methods. 44(1), 235-249 (2000). (Pubitemid 32239479)
    • (2000) Journal of Pharmacological and Toxicological Methods , vol.44 , Issue.1 , pp. 235-249
    • Lipinski, C.A.1
  • 45
    • 0030914681 scopus 로고    scopus 로고
    • Polar molecular surface properties predict the intestinal absorption of drugs in humans
    • DOI 10.1023/A:1012188625088
    • Palm K, Stenberg P, Luthman K., Artursson P. Polar molecular surface properties predict the intestinal absorption of drugs in humans. Pharm Res. 14(5), 568-571 (1997). (Pubitemid 27220272)
    • (1997) Pharmaceutical Research , vol.14 , Issue.5 , pp. 568-571
    • Palm, K.1    Stenberg, P.2    Luthman, K.3    Artursson, P.4
  • 46
    • 1942453243 scopus 로고    scopus 로고
    • Ligand efficiency: A useful metric for lead selection
    • DOI 10.1016/S1359-6446(04)03069-7, PII S1359644604030697
    • Hopkins AL, Groom CR, Alex A. Ligand efficiency: a useful metric for lead selection. Drug Discov. Today. 9(10), 430-431 (2004). (Pubitemid 38510559)
    • (2004) Drug Discovery Today , vol.9 , Issue.10 , pp. 430-431
    • Hopkins, A.L.1    Groom, C.R.2    Alex, A.3
  • 47
    • 0035438391 scopus 로고    scopus 로고
    • Is there a difference between leads and drugs? A historical perspective
    • Oprea TI, Davis AM, Teague S.J., Leeson PD Is there a difference between leads and drugs? A historical perspective. J. Chem. Inf. Comput. Sci. 41(5), 1308-1315 (2001).
    • (2001) J. Chem. Inf. Comput. Sci. , vol.41 , Issue.5 , pp. 1308-1315
    • Oprea, T.I.1    Davis, A.M.2    Teague, S.J.3    Leeson, P.D.4
  • 48
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • DOI 10.1006/jmbi.1996.0897
    • Jones G, Willet P, Glen RC et al. Development and validation of a genetic algorithm for flexible docking. J. Mol. Biol. 267(3), 727-748 (1997). (Pubitemid 27170693)
    • (1997) Journal of Molecular Biology , vol.267 , Issue.3 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 49
    • 33748667774 scopus 로고    scopus 로고
    • Consensus scoring for protein-ligand interactions
    • DOI 10.1016/j.drudis.2006.03.009, PII S1359644606000523
    • Feher M. Consensus scoring for protein-ligand interactions. Drug Discov. Today. 11(9-10), 421-428 (2006). (Pubitemid 44382521)
    • (2006) Drug Discovery Today , vol.11 , Issue.9-10 , pp. 421-428
    • Feher, M.1
  • 50
    • 77953127571 scopus 로고    scopus 로고
    • Virtual screening: Scope and limitation
    • Alvarez J, Shoichet B (Eds). CRC Press, FL, USA
    • Klebe G. Virtual Screening: Scope And Limitation. In: Virtual Screening in Drug Discovery (Volume 1). Alvarez J, Shoichet B (Eds). CRC Press, FL, USA, 3-24 (2005).
    • (2005) Virtual Screening in Drug Discovery , vol.1 , pp. 3-24
    • Klebe, G.1
  • 51
    • 0029310576 scopus 로고
    • Glycosomal glyceraldehyde-3-phosphate dehydrogenase of trypanosoma brucei and trypanosoma cruzi: Expression in escherichia coli, purification, and characterization of the enzymes
    • Hannaert V, Opperdoes FR, Michels PA Glycosomal glyceraldehyde-3- phosphate dehydrogenase of Trypanosoma brucei and Trypanosoma cruzi: expression in Escherichia coli, purification, and characterization of the enzymes. Protein Expr. Purif. 6(3), 244-250 (1995).
    • (1995) Protein Expr. Purif. , vol.6 , Issue.3 , pp. 244-250
    • Hannaert, V.1    Opperdoes, F.R.2    Michels, P.A.3
  • 52
    • 0043122944 scopus 로고    scopus 로고
    • ExPASy: The proteomics server for in-depth protein knowledge and analysis
    • DOI 10.1093/nar/gkg563
    • Gasteiger E, Gattiker A, Hoogland C., Ivanyi I, Appel RD, Bairoch A. ExPASy: the proteomics server for in-depth protein knowledge and ana lysis. Nucleic Acids Res. 31(13), 3784-3788 (2003). (Pubitemid 37442246)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3784-3788
    • Gasteiger, E.1    Gattiker, A.2    Hoogland, C.3    Ivanyi, I.4    Appel, R.D.5    Bairoch, A.6
  • 53
    • 84886384310 scopus 로고    scopus 로고
    • ClustalW2. www.ebi.ac.uk/Tools/msa/clustalw2
    • ClustalW2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.