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Volumn 9, Issue 10, 2014, Pages

Computational design of protein-based inhibitors of Plasmodium vivax subtilisin-like 1 protease

Author keywords

[No Author keywords available]

Indexed keywords

ANTIMALARIAL AGENT; ECBALLIUM ELATERIUM TRYPSIN INHIBITOR II; SUBTILISIN; SUBTILISIN LIKE 1 PROTEASE; UNCLASSIFIED DRUG; PROTEIN BINDING; PROTOZOAL PROTEIN; SUBTILISIN-LIKE PROTEASE 1, PLASMODIUM FALCIPARUM;

EID: 84908650015     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0109269     Document Type: Article
Times cited : (4)

References (52)
  • 1
    • 80054056017 scopus 로고    scopus 로고
    • Malaria vaccines and the new malaria agenda
    • Greenwood BM, Targett GA (2011) Malaria vaccines and the new malaria agenda. Clin Microbiol Infect 17: 1600-1607.
    • (2011) Clin Microbiol Infect , vol.17 , pp. 1600-1607
    • Greenwood, B.M.1    Targett, G.A.2
  • 3
    • 68049146050 scopus 로고    scopus 로고
    • Artemisinin-resistant malaria in asia
    • Noedl H, Socheat D, Satimai W (2009) Artemisinin-resistant malaria in Asia. N Engl J Med 361: 540-541.
    • (2009) N Engl J Med , vol.361 , pp. 540-541
    • Noedl, H.1    Socheat, D.2    Satimai, W.3
  • 5
    • 67649161040 scopus 로고    scopus 로고
    • Diagnosis and management of the neurological complications of falciparum malaria
    • Mishra SK, Newton CR (2009) Diagnosis and management of the neurological complications of falciparum malaria. Nat Rev Neurol 5: 189-198.
    • (2009) Nat Rev Neurol , vol.5 , pp. 189-198
    • Mishra, S.K.1    Newton, C.R.2
  • 6
    • 36849090615 scopus 로고    scopus 로고
    • Subcellular discharge of a serine protease mediates release of invasive malaria parasites from host erythrocytes
    • Yeoh S, O'Donnell RA, Koussis K, Dluzewski AR, Ansell KH, et al. (2007) Subcellular discharge of a serine protease mediates release of invasive malaria parasites from host erythrocytes. Cell 131: 1072-1083.
    • (2007) Cell , vol.131 , pp. 1072-1083
    • Yeoh, S.1    O'Donnell, R.A.2    Koussis, K.3    Dluzewski, A.R.4    Ansell, K.H.5
  • 7
    • 84887836603 scopus 로고    scopus 로고
    • A key role for plasmodium subtilisin-like SUB1 protease in egress of malaria parasites from host hepatocytes
    • Tawk L, Lacroix C, Gueirard P, Kent R, Gorgette O, et al. (2013) A Key Role for Plasmodium Subtilisin-like SUB1 Protease in Egress of Malaria Parasites from Host Hepatocytes. J Biol Chem 288: 33336-33346.
    • (2013) J Biol Chem , vol.288 , pp. 33336-33346
    • Tawk, L.1    Lacroix, C.2    Gueirard, P.3    Kent, R.4    Gorgette, O.5
  • 8
    • 0042473228 scopus 로고    scopus 로고
    • Structures of phage-display peptides that bind to the malarial surface protein, apical membrane antigen 1, and block erythrocyte invasion
    • Keizer DW, Miles LA, Li F, Nair M, Anders RF, et al. (2003) Structures of phage-display peptides that bind to the malarial surface protein, apical membrane antigen 1, and block erythrocyte invasion. Biochemistry 42: 9915-9923.
    • (2003) Biochemistry , vol.42 , pp. 9915-9923
    • Keizer, D.W.1    Miles, L.A.2    Li, F.3    Nair, M.4    Anders, R.F.5
  • 9
    • 0036682237 scopus 로고    scopus 로고
    • Synthesis and in vitro studies of novel pyrimidinyl peptidomimetics as potential antimalarial therapeutic agents
    • Zhu S, Hudson TH, Kyle DE, Lin AJ (2002) Synthesis and in vitro studies of novel pyrimidinyl peptidomimetics as potential antimalarial therapeutic agents. J Med Chem 45: 3491-3496.
    • (2002) J Med Chem , vol.45 , pp. 3491-3496
    • Zhu, S.1    Hudson, T.H.2    Kyle, D.E.3    Lin, A.J.4
  • 12
    • 3242886171 scopus 로고    scopus 로고
    • Ribosome display: Cell-free protein display technology
    • He M, Taussig MJ (2002) Ribosome display: cell-free protein display technology. Brief Funct Genomic Proteomic 1: 204-212.
    • (2002) Brief Funct Genomic Proteomic , vol.1 , pp. 204-212
    • He, M.1    Taussig, M.J.2
  • 13
    • 0030817279 scopus 로고    scopus 로고
    • Rna-peptide fusions for the in vitro selection of peptides and proteins
    • Roberts RW, Szostak JW (1997) RNA-peptide fusions for the in vitro selection of peptides and proteins. Proc Natl Acad Sci U S A 94: 12297-12302.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 12297-12302
    • Roberts, R.W.1    Szostak, J.W.2
  • 14
    • 79960820617 scopus 로고    scopus 로고
    • Computational reverse-engineering of a spider-venom derived peptide active against plasmodium falciparum sub1
    • Bastianelli G, Bouillon A, Nguyen C, Crublet E, Petres S, et al. (2011) Computational reverse-engineering of a spider-venom derived peptide active against Plasmodium falciparum SUB1. PLoS One 6: e21812.
    • (2011) PLoS One , vol.6 , pp. e21812
    • Bastianelli, G.1    Bouillon, A.2    Nguyen, C.3    Crublet, E.4    Petres, S.5
  • 15
    • 84880063851 scopus 로고    scopus 로고
    • In silico screening on the three-dimensional model of the plasmodium vivax sub1 protease leads to the validation of a novel anti-parasite compound
    • Bouillon A, Giganti D, Benedet C, Gorgette O, Petres S, et al. (2013) In Silico Screening on the Three-dimensional Model of the Plasmodium vivax SUB1 Protease Leads to the Validation of a Novel Anti-parasite Compound. J Biol Chem 288: 18561-18573.
    • (2013) J Biol Chem , vol.288 , pp. 18561-18573
    • Bouillon, A.1    Giganti, D.2    Benedet, C.3    Gorgette, O.4    Petres, S.5
  • 16
    • 0024975550 scopus 로고
    • 1 H 2D NMR and distance geometry study of the folding of ecballium elaterium trypsin inhibitor, a member of the squash inhibitors family
    • Heitz A, Chiche L, Le-Nguyen D, Castro B (1989) 1 H 2D NMR and distance geometry study of the folding of Ecballium elaterium trypsin inhibitor, a member of the squash inhibitors family. Biochemistry 28: 2392-2398.
    • (1989) Biochemistry , vol.28 , pp. 2392-2398
    • Heitz, A.1    Chiche, L.2    Le-Nguyen, D.3    Castro, B.4
  • 17
    • 0035239222 scopus 로고    scopus 로고
    • The cystine knot motif in toxins and implications for drug design
    • Craik DJ, Daly NL, Waine C (2001) The cystine knot motif in toxins and implications for drug design. Toxicon 39: 43-60.
    • (2001) Toxicon , vol.39 , pp. 43-60
    • Craik, D.J.1    Daly, N.L.2    Waine, C.3
  • 18
    • 34248222232 scopus 로고    scopus 로고
    • Potential therapeutic applications of the cyclotides and related cystine knot mini-proteins
    • Craik DJ, Clark RJ, Daly NL (2007) Potential therapeutic applications of the cyclotides and related cystine knot mini-proteins. Expert Opin Investig Drugs 16: 595-604.
    • (2007) Expert Opin Investig Drugs , vol.16 , pp. 595-604
    • Craik, D.J.1    Clark, R.J.2    Daly, N.L.3
  • 19
    • 70349414437 scopus 로고    scopus 로고
    • Biological diversity and therapeutic potential of natural and engineered cystine knot miniproteins
    • Kolmar H (2009) Biological diversity and therapeutic potential of natural and engineered cystine knot miniproteins. Curr Opin Pharmacol 9: 608-614.
    • (2009) Curr Opin Pharmacol , vol.9 , pp. 608-614
    • Kolmar, H.1
  • 20
    • 0024317784 scopus 로고
    • Design and chemical synthesis of a 32 residues chimeric microprotein inhibiting both trypsin and carboxypeptidase A
    • Le-Nguyen D, Mattras H, Coletti-Previero MA, Castro B (1989) Design and chemical synthesis of a 32 residues chimeric microprotein inhibiting both trypsin and carboxypeptidase A. Biochem Biophys Res Commun 162: 1425-1430.
    • (1989) Biochem Biophys Res Commun , vol.162 , pp. 1425-1430
    • Le-Nguyen, D.1    Mattras, H.2    Coletti-Previero, M.A.3    Castro, B.4
  • 21
    • 0032824531 scopus 로고    scopus 로고
    • The cystine knot of a squash-type protease inhibitor as a structural scaffold for escherichia coli cell surface display of conformationally constrained peptides
    • Christmann A, Walter K, Wentzel A, Kratzner R, Kolmar H (1999) The cystine knot of a squash-type protease inhibitor as a structural scaffold for Escherichia coli cell surface display of conformationally constrained peptides. Protein Eng 12: 797-806.
    • (1999) Protein Eng , vol.12 , pp. 797-806
    • Christmann, A.1    Walter, K.2    Wentzel, A.3    Kratzner, R.4    Kolmar, H.5
  • 22
    • 0043092182 scopus 로고    scopus 로고
    • Design and characterization of a hybrid miniprotein that specifically inhibits porcine pancreatic elastase
    • Hilpert K, Wessner H, Schneider-Mergener J, Welfle K, Misselwitz R, et al. (2003) Design and characterization of a hybrid miniprotein that specifically inhibits porcine pancreatic elastase. J Biol Chem 278: 24986-24993.
    • (2003) J Biol Chem , vol.278 , pp. 24986-24993
    • Hilpert, K.1    Wessner, H.2    Schneider-Mergener, J.3    Welfle, K.4    Misselwitz, R.5
  • 23
    • 33646933038 scopus 로고    scopus 로고
    • Inhibition of platelet aggregation by grafting RGD and KGD sequences on the structural scaffold of small disulfide-rich proteins
    • Reiss S, Sieber M, Oberle V, Wentzel A, Spangenberg P, et al. (2006) Inhibition of platelet aggregation by grafting RGD and KGD sequences on the structural scaffold of small disulfide-rich proteins. Platelets 17: 153-157.
    • (2006) Platelets , vol.17 , pp. 153-157
    • Reiss, S.1    Sieber, M.2    Oberle, V.3    Wentzel, A.4    Spangenberg, P.5
  • 24
    • 18544368988 scopus 로고    scopus 로고
    • New binding specificities derived from min-23, a small cystine-stabilized peptidic scaffold
    • Souriau C, Chiche L, Irving R, Hudson P (2005) New binding specificities derived from Min-23, a small cystine-stabilized peptidic scaffold. Biochemistry 44: 7143-7155.
    • (2005) Biochemistry , vol.44 , pp. 7143-7155
    • Souriau, C.1    Chiche, L.2    Irving, R.3    Hudson, P.4
  • 25
    • 0033597789 scopus 로고    scopus 로고
    • Sequence requirements of the GPNG beta-turn of the ecballium elaterium trypsin inhibitor II explored by combinatorial library screening
    • Wentzel A, Christmann A, Kratzner R, Kolmar H (1999) Sequence requirements of the GPNG beta-turn of the Ecballium elaterium trypsin inhibitor II explored by combinatorial library screening. J Biol Chem 274: 21037-21043.
    • (1999) J Biol Chem , vol.274 , pp. 21037-21043
    • Wentzel, A.1    Christmann, A.2    Kratzner, R.3    Kolmar, H.4
  • 26
    • 35148855712 scopus 로고    scopus 로고
    • Computational design of antibodyaffinity improvement beyond in vivo maturation
    • Lippow SM, Wittrup KD, Tidor B (2007) Computational design of antibodyaffinity improvement beyond in vivo maturation. Nat Biotechnol 25: 1171-1176.
    • (2007) Nat Biotechnol , vol.25 , pp. 1171-1176
    • Lippow, S.M.1    Wittrup, K.D.2    Tidor, B.3
  • 28
    • 0009130599 scopus 로고    scopus 로고
    • A structural explanation for the twilight zone of protein sequence homology
    • Chung SY, Subbiah S (1996) A structural explanation for the twilight zone of protein sequence homology. Structure 4: 1123-1127.
    • (1996) Structure , vol.4 , pp. 1123-1127
    • Chung, S.Y.1    Subbiah, S.2
  • 29
    • 17844410707 scopus 로고    scopus 로고
    • The many faces of proteaseprotein inhibitor interaction
    • Otlewski J, Jelen F, Zakrzewska M, Oleksy A (2005) The many faces of proteaseprotein inhibitor interaction. EMBO J 24: 1303-1310.
    • (2005) EMBO J , vol.24 , pp. 1303-1310
    • Otlewski, J.1    Jelen, F.2    Zakrzewska, M.3    Oleksy, A.4
  • 30
    • 76249085850 scopus 로고    scopus 로고
    • How to obtain statistically converged mm/gbsa results
    • Genheden S, Ryde U (2010) How to obtain statistically converged MM/GBSA results. J Comput Chem 31: 837-846.
    • (2010) J Comput Chem , vol.31 , pp. 837-846
    • Genheden, S.1    Ryde, U.2
  • 31
    • 0037478705 scopus 로고    scopus 로고
    • Optimization of protease-inhibitor interactions by randomizing adventitious contacts
    • Komiyama T, VanderLugt B, Fugere M, Day R, Kaufman RJ, et al. (2003) Optimization of protease-inhibitor interactions by randomizing adventitious contacts. Proc Natl Acad Sci U S A 100: 8205-8210.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 8205-8210
    • Komiyama, T.1    VanderLugt, B.2    Fugere, M.3    Day, R.4    Kaufman, R.J.5
  • 32
    • 62649150175 scopus 로고    scopus 로고
    • A multifunctional serine protease primes the malaria parasite for red blood cell invasion
    • Koussis K, Withers-Martinez C, Yeoh S, Child M, Hackett F, et al. (2009) A multifunctional serine protease primes the malaria parasite for red blood cell invasion. Embo J 28: 725-735.
    • (2009) Embo J , vol.28 , pp. 725-735
    • Koussis, K.1    Withers-Martinez, C.2    Yeoh, S.3    Child, M.4    Hackett, F.5
  • 33
    • 79952307062 scopus 로고    scopus 로고
    • Global identification of multiple substrates for plasmodium falciparum SUB1, an essential malarial processing protease
    • Silmon de Monerri NC, Flynn HR, Campos MG, Hackett F, Koussis K, et al. (2011) Global identification of multiple substrates for Plasmodium falciparum SUB1, an essential malarial processing protease. Infect Immun 79: 1086-1097.
    • (2011) Infect Immun , vol.79 , pp. 1086-1097
    • Silmon De Monerri, N.C.1    Flynn, H.R.2    Campos, M.G.3    Hackett, F.4    Koussis, K.5
  • 37
    • 1942423619 scopus 로고    scopus 로고
    • MMTSB tool set: Enhanced sampling and multiscale modeling methods for applications in structural biology
    • rd (2004) MMTSB Tool Set: enhanced sampling and multiscale modeling methods for applications in structural biology. J Mol Graph Model 22: 377-395.
    • (2004) J Mol Graph Model , vol.22 , pp. 377-395
    • Feig, M.1    Karanicolas, J.2    Brooks, C.L.3
  • 39
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple amber force fields and development of improved protein backbone parameters
    • Hornak V, Abel R, Okur A, Strockbine B, Roitberg A, et al. (2006) Comparison of multiple Amber force fields and development of improved protein backbone parameters. Proteins 65: 712-725.
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5
  • 40
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • Jorgensen WL, Chandrasekhar J, Madura JD (1983) Comparison of simple potential functions for simulating liquid water. J Chem Phys 79: 926.
    • (1983) J Chem Phys , vol.79 , pp. 926
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Madura, J.D.3
  • 41
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert J, Ciccotti G, Berendsen H (1977) Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J Comput Phys 23: 327-341.
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.1    Ciccotti, G.2    Berendsen, H.3
  • 42
    • 33846823909 scopus 로고
    • Particle mesh ewald-an nlog(n) method for ewald sums in large systems
    • Darden T, York D, Pederson L (1993) Particle mesh ewald-an nlog(n) method for ewald sums in large systems. J Chem Phys 98: 10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pederson, L.3
  • 44
    • 0034193510 scopus 로고    scopus 로고
    • Protein docking using spherical polar fourier correlations
    • Ritchie DW, Kemp GJ (2000) Protein docking using spherical polar Fourier correlations. Proteins 39: 178-194.
    • (2000) Proteins , vol.39 , pp. 178-194
    • Ritchie, D.W.1    Kemp, G.J.2
  • 45
    • 0043245780 scopus 로고    scopus 로고
    • Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the ras-raf and ras-ralgds complexes
    • Gohlke H, Kiel C, Case DA (2003) Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes. J Mol Biol 330: 891-913.
    • (2003) J Mol Biol , vol.330 , pp. 891-913
    • Gohlke, H.1    Kiel, C.2    Case, D.A.3
  • 46
    • 14244273182 scopus 로고    scopus 로고
    • Theory and applications of the generalized born solvation model in macromolecular simulations
    • Tsui V, Case DA (2000) Theory and applications of the generalized Born solvation model in macromolecular simulations. Biopolymers 56: 275-291.
    • (2000) Biopolymers , vol.56 , pp. 275-291
    • Tsui, V.1    Case, D.A.2
  • 47
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman GL (1959) Tissue sulfhydryl groups. Arch Biochem Biophys 82: 70-77.
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 48
    • 0034614404 scopus 로고    scopus 로고
    • Maturation and specificity of plasmodium falciparum subtilisin-like protease-1, a malaria merozoite subtilisinlike serine protease
    • Sajid M, Withers-Martinez C, Blackman MJ (2000) Maturation and specificity of Plasmodium falciparum subtilisin-like protease-1, a malaria merozoite subtilisinlike serine protease. J Biol Chem 275: 631-641.
    • (2000) J Biol Chem , vol.275 , pp. 631-641
    • Sajid, M.1    Withers-Martinez, C.2    Blackman, M.J.3
  • 49
    • 0026632573 scopus 로고
    • Intramolecular mapping of plasmodium falciparum p126 proteolytic fragments by n-terminal amino acid sequencing
    • Debrabant A, Maes P, Delplace P, Dubremetz JF, Tartar A, et al. (1992) Intramolecular mapping of Plasmodium falciparum P126 proteolytic fragments by N-terminal amino acid sequencing. Molecular and Biochemical Parasitology 53: 89-96.
    • (1992) Molecular and Biochemical Parasitology , vol.53 , pp. 89-96
    • Debrabant, A.1    Maes, P.2    Delplace, P.3    Dubremetz, J.F.4    Tartar, A.5
  • 50
    • 0028114015 scopus 로고
    • Nterminal amino acid sequence of the plasmodium falciparum merozoite surface protein-1 polypeptides
    • Stafford WH, Blackman MJ, Harris A, Shai S, Grainger M, et al. (1994) Nterminal amino acid sequence of the Plasmodium falciparum merozoite surface protein-1 polypeptides. Mol Biochem Parasitol 66: 157-160.
    • (1994) Mol Biochem Parasitol , vol.66 , pp. 157-160
    • Stafford, W.H.1    Blackman, M.J.2    Harris, A.3    Shai, S.4    Grainger, M.5
  • 51
    • 0024590266 scopus 로고
    • The nterminal amino acid sequences of the plasmodium falciparum (FCBI) merozoite surface antigen of 42 and 36 kilodaltons, both derived from the 185-195 kilodalton precursor
    • Heidrich HG, Miettinin-Bauman A, Eckerskorn C, Lottspeich F (1989) The Nterminal amino acid sequences of the Plasmodium falciparum (FCBI) merozoite surface antigen of 42 and 36 kilodaltons, both derived from the 185-195 kilodalton precursor Molecular and Biochemical Parasitology 34: 147-154.
    • (1989) Molecular and Biochemical Parasitology , vol.34 , pp. 147-154
    • Heidrich, H.G.1    Miettinin-Bauman, A.2    Eckerskorn, C.3    Lottspeich, F.4
  • 52
    • 0029081160 scopus 로고
    • Processing of the plasmodium chabaudi chabaudi AS merozoite surface protein 1 in vivo and in vitro
    • O'Dea KP, McKean PG, Harris A, Brown KN (1995) Processing of the Plasmodium chabaudi chabaudi AS merozoite surface protein 1 in vivo and in vitro. Molecular and Biochemical Parasitology 72: 111-119.
    • (1995) Molecular and Biochemical Parasitology , vol.72 , pp. 111-119
    • O'Dea, K.P.1    McKean, P.G.2    Harris, A.3    Brown, K.N.4


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