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Volumn 5, Issue , 2015, Pages

Structure-based discovery of the first non-covalent inhibitors of Leishmania major tryparedoxin peroxidase by high throughput docking

Author keywords

[No Author keywords available]

Indexed keywords

ANTIPROTOZOAL AGENT; ENZYME INHIBITOR; PEROXIDASE; PROTEIN BINDING; PROTOZOAL PROTEIN; TRYPAREDOXIN PEROXIDASE;

EID: 84929000082     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep09705     Document Type: Article
Times cited : (65)

References (35)
  • 1
    • 84928995251 scopus 로고    scopus 로고
    • Updated: february 2015
    • Leishmaniasis. Fact sheet Nu375 Available at: http://www.who.int/leishmaniasis/ en/. (Updated: february 2015)
    • Leishmaniasis. Fact Sheet Nu375
  • 2
    • 0142043920 scopus 로고    scopus 로고
    • Current treatment approaches to leishmaniasis
    • Berman, J. Current treatment approaches to leishmaniasis. Curr. Opin. Infect. Dis. 16, 397-401 (2003)
    • (2003) Curr. Opin. Infect. Dis , vol.16 , pp. 397-401
    • Berman, J.1
  • 3
    • 84886497242 scopus 로고    scopus 로고
    • Structural insights into the enzymes of the trypanothione pathway: Targets for antileishmaniasis drugs
    • Colotti, G. et al. Structural insights into the enzymes of the trypanothione pathway: targets for antileishmaniasis drugs. Future Med. Chem. 5, 1861-1875 (2013)
    • (2013) Future Med. Chem , vol.5 , pp. 1861-1875
    • Colotti, G.1
  • 4
    • 78751591332 scopus 로고    scopus 로고
    • Polyamine metabolism in Leishmania: From arginine to trypanothione
    • Colotti, G. & Ilari, A. Polyamine metabolism in Leishmania: from arginine to trypanothione. Amino Acids 40, 269-85 (2011)
    • (2011) Amino Acids , vol.40 , pp. 269-285
    • Colotti, G.1    Ilari, A.2
  • 5
    • 0026793462 scopus 로고
    • Metabolism and functions of trypanothione in the kinetoplastida
    • Fairlamb, A. H. & Cerami, A. Metabolism and functions of trypanothione in the kinetoplastida. Annu. Rev. Microbial. 46, 695-729 (1992)
    • (1992) Annu. Rev. Microbial , vol.46 , pp. 695-729
    • Fairlamb, A.H.1    Cerami, A.2
  • 6
    • 61349124238 scopus 로고    scopus 로고
    • The cytosolic tryparedoxin of Leishmania infantum is essential for parasite survival
    • Romao, S., Castro, H., Sousa, C., Carvalho, S. & Tomas, A. M. The cytosolic tryparedoxin of Leishmania infantum is essential for parasite survival. Int. J. Parasitol. 39, 703-711 (2009)
    • (2009) Int. J. Parasitol , vol.39 , pp. 703-711
    • Romao, S.1    Castro, H.2    Sousa, C.3    Carvalho, S.4    Tomas, A.M.5
  • 7
    • 0037518119 scopus 로고    scopus 로고
    • Role of peroxidoxins in Leishmania chagasi survival Evidence of an enzymatic defense against nitrosative stress
    • Barr, S. D. & Gedamu, L. Role of peroxidoxins in Leishmania chagasi survival. Evidence of an enzymatic defense against nitrosative stress. J. Biol. Chem. 278, 10816-10823 (2003)
    • (2003) J. Biol. Chem , vol.278 , pp. 10816-10823
    • Barr, S.D.1    Gedamu, L.2
  • 8
    • 15444362698 scopus 로고    scopus 로고
    • Crystal structure of the tryparedoxin peroxidase from the human parasite Trypanosoma cruzi
    • Pineyro, M. D. et al. Crystal structure of the tryparedoxin peroxidase from the human parasite Trypanosoma cruzi. J. Struct. Biol. 150, 11-22 (2005)
    • (2005) J. Struct. Biol , vol.150 , pp. 11-22
    • Pineyro, M.D.1
  • 9
    • 0034697984 scopus 로고    scopus 로고
    • The structure of reduced tryparedoxin peroxidase reveals a decamer and insight into reactivity of 2Cys-peroxiredoxins
    • Alphey, M. S., Bond, C. S., Tetaud, E., Fairlamb, A. H. & Hunter, W. N. The structure of reduced tryparedoxin peroxidase reveals a decamer and insight into reactivity of 2Cys-peroxiredoxins. J. Mol. Biol. 300, 903-916 (2000)
    • (2000) J. Mol. Biol , vol.300 , pp. 903-916
    • Alphey, M.S.1    Bond, C.S.2    Tetaud, E.3    Fairlamb, A.H.4    Hunter, W.N.5
  • 10
    • 38749122130 scopus 로고    scopus 로고
    • Structural survey of the peroxiredoxins
    • Karplus, P. A.&Hall, A. Structural survey of the peroxiredoxins. Subcell. Biochem. 44, 41-60 (2007)
    • (2007) Subcell. Biochem , vol.44 , pp. 41-60
    • Karplus, P.A.1    Hall, A.2
  • 11
    • 84865996192 scopus 로고    scopus 로고
    • The crystal structures of the tryparedoxin-tryparedoxin peroxidase couple unveil the structural determinants of Leishmania detoxification pathway
    • Fiorillo, A., Colotti, G., Boffi, A., Baiocco, P.&Ilari, A. The crystal structures of the tryparedoxin-tryparedoxin peroxidase couple unveil the structural determinants of Leishmania detoxification pathway. PLoS Negl. Trop. Dis. 6, e1781 (2012)
    • (2012) PLoS Negl. Trop. Dis , vol.6 , pp. e1781
    • Fiorillo, A.1    Colotti, G.2    Boffi, A.3    Baiocco, P.4    Ilari, A.5
  • 12
    • 84055178426 scopus 로고    scopus 로고
    • Structural insights into the peroxidase activity and nactivation of human peroxiredoxin 4
    • Wang, X., Wang, I., Wang, X., Sun, F. &Wang, C. C. Structural insights into the peroxidase activity and nactivation of human peroxiredoxin 4. Biochem J. 441, 113-8 (2012)
    • (2012) Biochem J. , vol.441 , pp. 113-118
    • Wang, X.1    Wang, I.2    Wang, X.3    Sun, F.4    Wang, C.C.5
  • 13
    • 0028854034 scopus 로고
    • Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation
    • Jones, G.,Willett, P. & Glen, R. C.Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation. J. Mol. Biol. 245, 43-53 (1995)
    • (1995) J. Mol. Biol , vol.245 , pp. 43-53
    • Jones, G.1    Willett, P.2    Glen, R.C.3
  • 14
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones, G., Willett, P., Glen, R. C., Leach, A. R. & Taylor, R. Development and validation of a genetic algorithm for flexible docking. J. Mol. Biol. 267, 727-748 (1997)
    • (1997) J. Mol. Biol , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 15
    • 0035416126 scopus 로고    scopus 로고
    • High-throughput docking for lead generation
    • Abagyan, R. & Totrov, M. High-throughput docking for lead generation. Curr. Opin. Chem. Biol. 5, 375-382 (2001)
    • (2001) Curr. Opin. Chem. Biol , vol.5 , pp. 375-382
    • Abagyan, R.1    Totrov, M.2
  • 16
    • 33845917628 scopus 로고    scopus 로고
    • Reactions of yeast thioredoxin peroxidases i and II with hydrogen peroxide and peroxynitrite: Rate constants by competitive kinetics
    • Ogusucu, R., Rettori, D., Munhoz, D. C., Netto, L. E. & Augusto, O. Reactions of yeast thioredoxin peroxidases I and II with hydrogen peroxide and peroxynitrite: rate constants by competitive kinetics. Free Radic. Biol. Med. 42, 326-334 (2007)
    • (2007) Free Radic. Biol. Med , vol.42 , pp. 326-334
    • Ogusucu, R.1    Rettori, D.2    Munhoz, D.C.3    Netto, L.E.4    Augusto, O.5
  • 17
    • 84902481986 scopus 로고    scopus 로고
    • Disease-Modifying Anti-Alzheimers Drugs: Inhibitors of Human Cholinesterases Interfering with beta-Amyloid Aggregation
    • Brogi, S. et al. Disease-Modifying Anti-Alzheimers Drugs: Inhibitors of Human Cholinesterases Interfering with beta-Amyloid Aggregation. CNS Neurosci. Ther. 20, 624-632 (2014)
    • (2014) CNS Neurosci. Ther , vol.20 , pp. 624-632
    • Brogi, S.1
  • 18
    • 84870986351 scopus 로고    scopus 로고
    • Mimicking the Intramolecular Hydrogen Bond: Synthesis, Biological Evaluation, and Molecular Modeling of Benzoxazines and Quinazolines as Potential Antimalarial Agents
    • Gemma, S. et al. Mimicking the Intramolecular Hydrogen Bond: Synthesis, Biological Evaluation, and Molecular Modeling of Benzoxazines and Quinazolines as Potential Antimalarial Agents. J. Med. Chem. 55, 10387-10404 (2012)
    • (2012) J. Med. Chem , vol.55 , pp. 10387-10404
    • Gemma, S.1
  • 19
    • 84903957340 scopus 로고    scopus 로고
    • Rational design of the first difluorostatone-based PfSUB1 inhibitors
    • Giovani, S. et al. Rational design of the first difluorostatone-based PfSUB1 inhibitors. Bioorg. Med. Chem. Lett. 24, 3582-3586 (2014)
    • (2014) Bioorg. Med. Chem. Lett , vol.24 , pp. 3582-3586
    • Giovani, S.1
  • 22
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A. & Teplyakov, A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30, 1022-1025 (1997)
    • (1997) J. Appl. Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 24
  • 25
    • 0000243829 scopus 로고
    • Procheck - A Program to Check the Stereochemical Quality of Protein Structures
    • Laskowski, R. A., Macarthur, M. W., Moss, D. S. & Thornton, J. M. Procheck - a Program to Check the Stereochemical Quality of Protein Structures. J. Appl. Cryst. 26, 283-291 (1993)
    • (1993) J. Appl. Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 26
    • 79953242071 scopus 로고    scopus 로고
    • Horseradish peroxidase compound i as a tool to investigate reactive protein-cysteine residues: From quantification to kinetics
    • Toledo, J. C. Jr. et al. Horseradish peroxidase compound I as a tool to investigate reactive protein-cysteine residues: from quantification to kinetics. Free Radic. Biol. Med. 50, 1032-1038 (2011)
    • (2011) Free Radic. Biol. Med , vol.50 , pp. 1032-1038
    • Toledo, J.C.1
  • 27
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all atom force field on conformational energetics and properties of organic liquids
    • Jorgensen, W. L., Maxwell, D. S. & TiradoRives, J. Development and testing of the OPLS all atom force field on conformational energetics and properties of organic liquids J. Am. Chem. Soc. 118, 11225-11236 (1996)
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tiradorives, J.3
  • 29
    • 0000504254 scopus 로고
    • AMultiple-Time-step molecular- dynamics algorithm for macromolecules
    • Humphreys, D. D., Friesner, R. A.&Berne, B. J. AMultiple-Time-Step Molecular- Dynamics Algorithm for Macromolecules. J. Phys. Chem. 98, 6885-6892 (1994)
    • (1994) J. Phys. Chem , vol.98 , pp. 6885-6892
    • Humphreys, D.D.1    Friesner, R.A.2    Berne, B.J.3
  • 30
    • 0001538909 scopus 로고
    • Canonical dynamics - Equilibrium phase-space Distributions
    • Hoover, W. G. Canonical Dynamics - Equilibrium Phase-Space Distributions. Physical Rev. A 31, 1695-1697 (1985)
    • (1985) Physical Rev A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 31
    • 36449003554 scopus 로고
    • Constant-pressure molecular- dynamics algorithms
    • Martyna, G. J., Tobias, D. J. & Klein, M. L. Constant-Pressure Molecular- Dynamics Algorithms. J. Chem. Phys. 101, 4177-4189 (1994)
    • (1994) J. Chem. Phys , vol.101 , pp. 4177-4189
    • Martyna, G.J.1    Tobias, D.J.2    Klein, M.L.3
  • 32
    • 33645961739 scopus 로고
    • A smooth particle mesh ewald method
    • Essmann, U. et al. A Smooth Particle Mesh Ewald Method. J. Chem. Phys. 103, 8577-8593 (1995)
    • (1995) J. Chem. Phys , vol.103 , pp. 8577-8593
    • Essmann, U.1
  • 33
    • 33746872935 scopus 로고    scopus 로고
    • Accurate prediction of the relative potencies of members of a series of kinase inhibitors using molecular docking and MMGBSA scoring
    • Lyne, P. D., Lamb, M. L. & Saeh, J. C. Accurate prediction of the relative potencies of members of a series of kinase inhibitors using molecular docking and MMGBSA scoring. J. Med. Chem. 49, 4805-4808 (2006)
    • (2006) J. Med. Chem , vol.49 , pp. 4805-4808
    • Lyne, P.D.1    Lamb, M.L.2    Saeh, J.C.3
  • 34
    • 84913554344 scopus 로고    scopus 로고
    • Targeting dopamine D3 and serotonin 5-HT1A and 5-HT2A receptors for developing effective antipsychotics: Synthesis, biological characterization, and behavioral studies
    • Brindisi, M. et al. Targeting dopamine D3 and serotonin 5-HT1A and 5-HT2A receptors for developing effective antipsychotics: synthesis, biological characterization, and behavioral studies. J. Med. Chem. 57, 9578-9597 (2014)
    • (2014) J. Med. Chem , vol.57 , pp. 9578-9597
    • Brindisi, M.1
  • 35
    • 84923320337 scopus 로고    scopus 로고
    • Synthetic spirocyclic endoperoxides: New antimalarial Scaffolds
    • Brindisi, M. et al. Synthetic Spirocyclic Endoperoxides: New Antimalarial Scaffolds. Med. Chem. Commun. 6, 357-362 (2015)
    • (2015) Med. Chem. Commun , vol.6 , pp. 357-362
    • Brindisi, M.1


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