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Volumn 10, Issue 4, 2006, Pages 433-456

What is hidden behind peptide bond restriction and α-carbon asymmetry of conserved antigens? Peptide bond isosters and chirally transformed pseudopeptides as novel elements for synthetic vaccines and therapeutic agents against malaria

Author keywords

Homochirality; Molecular orbital system; Peptide bond surrogates; Peptide based vaccine; Plasmodium falciparum

Indexed keywords

AMINO ACIDS; ANTIGENS; BINDING ENERGY; CARBON; DISEASES; IMMUNE SYSTEM; MOLECULAR ORBITALS; PEPTIDES; STEREOCHEMISTRY; VACCINES;

EID: 33645986520     PISSN: 13852728     EISSN: None     Source Type: Journal    
DOI: 10.2174/138527206776055358     Document Type: Review
Times cited : (4)

References (83)
  • 1
    • 0010664470 scopus 로고
    • Cosmic asymmetry: The meaning of life
    • MacDermontt, A. Cosmic asymmetry: the meaning of life, Chemistry in Britain, 1994, 30, 487.
    • (1994) Chemistry in Britain , vol.30 , pp. 487
    • MacDermontt, A.1
  • 2
    • 0026279962 scopus 로고
    • The origin and amplification of biomolecular chirality
    • Bonner, W.A. The origin and amplification of biomolecular chirality. Orig. Life Evol. Biosph., 1991, 21(2), 59-111.
    • (1991) Orig. Life Evol. Biosph. , vol.21 , Issue.2 , pp. 59-111
    • Bonner, W.A.1
  • 3
    • 0035826726 scopus 로고    scopus 로고
    • Selective adsorption of L- and D-amino acids on calcite: Implications for biochemical homochirality
    • Hazen, R.M., Filley, T.R., Goodfriend, G.A. Selective adsorption of L- and D-amino acids on calcite: Implications for biochemical homochirality. Proc. Natl. Acad. Sci. USA. 2001, 98(10), 5487-90.
    • (2001) Proc. Natl. Acad. Sci. USA. , vol.98 , Issue.10 , pp. 5487-5490
    • Hazen, R.M.1    Filley, T.R.2    Goodfriend, G.A.3
  • 4
    • 0030621130 scopus 로고    scopus 로고
    • Enantiomeric excess in meteoritic amino acids
    • Croning, J.R. and Pizzarello, S. Enantiomeric excess in meteoritic amino acids. Science 1997, 275, 951-955.
    • (1997) Science , vol.275 , pp. 951-955
    • Croning, J.R.1    Pizzarello, S.2
  • 5
    • 33744883979 scopus 로고
    • Weak neutral currents and the origin of biomolecular chirality
    • Kondepudi, D.K. and Nelson, G.W. Weak neutral currents and the origin of biomolecular chirality. Nature 1985, 314, 438-441.
    • (1985) Nature , vol.314 , pp. 438-441
    • Kondepudi, D.K.1    Nelson, G.W.2
  • 6
    • 0031930506 scopus 로고    scopus 로고
    • Homochiral imperative of molecular evolution
    • Siegel, J.S. Homochiral imperative of molecular evolution. Chirality 1998, 10, 24-27.
    • (1998) Chirality , vol.10 , pp. 24-27
    • Siegel, J.S.1
  • 8
    • 0029559848 scopus 로고
    • Asymmetric autocatalysis and amplification of enantiomeric excess of a chiral molecule
    • Soai, K., Shibata, T., Morioka, H. and Choji, K. Asymmetric autocatalysis and amplification of enantiomeric excess of a chiral molecule. Nature 1995, 378, 767-768.
    • (1995) Nature , vol.378 , pp. 767-768
    • Soai, K.1    Shibata, T.2    Morioka, H.3    Choji, K.4
  • 10
    • 0030611061 scopus 로고    scopus 로고
    • Pyranosyl-RNA: Chiroselective self-assembly of base sequences by ligative oligomerization of tetranucleotide-2′,3′-cyclophosphates
    • Bolli, M., Micura, R. and Eschenmoser, A. Pyranosyl-RNA: chiroselective self-assembly of base sequences by ligative oligomerization of tetranucleotide-2′,3′-cyclophosphates. Chem. Biol. 1997, 4, 309-320.
    • (1997) Chem. Biol. , vol.4 , pp. 309-320
    • Bolli, M.1    Micura, R.2    Eschenmoser, A.3
  • 11
    • 0000881952 scopus 로고
    • Chiral symmetry breaking in sodium chlorate crystallization
    • Kondepudi, D.K., Kaufman, R.J. and Singh, N. Chiral symmetry breaking in sodium chlorate crystallization. Science 1990, 250, 975-977.
    • (1990) Science , vol.250 , pp. 975-977
    • Kondepudi, D.K.1    Kaufman, R.J.2    Singh, N.3
  • 12
    • 0004966011 scopus 로고    scopus 로고
    • Crystal structures and cation sites of the rock-forming minerals
    • Allen and Unwin, Boston
    • Smyth, J.R. and Bish, D.L. Crystal structures and cation sites of the rock-forming minerals. Allen and Unwin, Boston, 1998.
    • (1998)
    • Smyth, J.R.1    Bish, D.L.2
  • 13
    • 0030789592 scopus 로고    scopus 로고
    • Template-directed synthesis using the heterogeneous templates produced by montmorillonite catalysis. A possible bridge between the prebiotic and RNA worlds
    • Ertem, G., Ferris, J.P. Template-directed synthesis using the heterogeneous templates produced by montmorillonite catalysis. A possible bridge between the prebiotic and RNA worlds. J. Am. Chem. Soc. 1997, 119, 7197-7201.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 7197-7201
    • Ertem, G.1    Ferris, J.P.2
  • 16
    • 0027624836 scopus 로고
    • Modifications in the amide bond and conformational constraints in pseudopeptide analogues
    • Marraud, G., Dupont, V., Grand, V. et al. (1993) Modifications in the amide bond and conformational constraints in pseudopeptide analogues. Biopolymers 33, 1135-1148.
    • (1993) Biopolymers , vol.33 , pp. 1135-1148
    • Marraud, G.1    Dupont, V.2    Grand, V.3
  • 18
    • 14544300624 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors: A review on pharmacophore mapping and (Q)SARs results
    • Kontogiorgis, C.A., Papaioannou, P., Hadjipavlou-Litina, D.J. Matrix metalloproteinase inhibitors: a review on pharmacophore mapping and (Q)SARs results. Curr. Med. Chem. 2005, 12(3), 339-355.
    • (2005) Curr. Med. Chem. , vol.12 , Issue.3 , pp. 339-355
    • Kontogiorgis, C.A.1    Papaioannou, P.2    Hadjipavlou-Litina, D.J.3
  • 19
    • 0002295690 scopus 로고
    • Pathogenesis of the coagulation defect developing during pathological plasma proteolytic ("fibrinolytic") states. I. the significance of fibrinogen proteolysis and circulating fibrinogen breakdown products
    • Fletcher, A.P., Alkjaersig, N. and Sherry, S. Pathogenesis of the coagulation defect developing during pathological plasma proteolytic ("fibrinolytic") states. I. the significance of fibrinogen proteolysis and circulating fibrinogen breakdown products. J. Clin. Invest. 1962, 41(4), 896-916.
    • (1962) J. Clin. Invest. , vol.41 , Issue.4 , pp. 896-916
    • Fletcher, A.P.1    Alkjaersig, N.2    Sherry, S.3
  • 21
    • 0036257708 scopus 로고    scopus 로고
    • Non-peptide antagonists and agonists of the bradykinin B(2) receptor
    • Heitsch, H. Non-peptide antagonists and agonists of the bradykinin B(2) receptor. Curr. Med. Chem. 2002, 9, 913-928
    • (2002) Curr. Med. Chem. , vol.9 , pp. 913-928
    • Heitsch, H.1
  • 22
    • 0037077007 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of matrix metalloprotease inhibitors bearing cyclopropane-derived peptidomimetics as P1′ and P2′ replacements
    • Reichelt, A., Gaul, C., Frey, R.R., Kennedy, A., Martin, S.F. Design, synthesis, and evaluation of matrix metalloprotease inhibitors bearing cyclopropane-derived peptidomimetics as P1′ and P2′ replacements. J. Org. Chem. 2002, 67(12) 4062-4075.
    • (2002) J. Org. Chem. , vol.67 , Issue.12 , pp. 4062-4075
    • Reichelt, A.1    Gaul, C.2    Frey, R.R.3    Kennedy, A.4    Martin, S.F.5
  • 23
    • 0034777151 scopus 로고    scopus 로고
    • Peptide-nucleic acids (PNAs): A tool for the development of gene expression modifiers
    • Gambari, R. Peptide-nucleic acids (PNAs): a tool for the development of gene expression modifiers. Curr. Pharm. Des. 2001, 17, 1839-1362.
    • (2001) Curr. Pharm. Des. , vol.17 , pp. 1362-1839
    • Gambari, R.1
  • 25
    • 4544371858 scopus 로고    scopus 로고
    • Catalytic antibodies: Hapten design strategies and screening methods
    • Xu, Y., Yamamoto, N. and Janda, K. Catalytic antibodies: hapten design strategies and screening methods. Bioorg. Med. Chem. 2004, 12(20), 5247-5268.
    • (2004) Bioorg. Med. Chem. , vol.12 , Issue.20 , pp. 5247-5268
    • Xu, Y.1    Yamamoto, N.2    Janda, K.3
  • 26
    • 0028875452 scopus 로고
    • Recent developments in retro peptides and proteins - An ongoing topochemical exploration
    • Chorev, M. and Goodman, M. Recent developments in retro peptides and proteins - an ongoing topochemical exploration. Trends Biotechnol. 1995, 13(10), 438-45.
    • (1995) Trends Biotechnol. , vol.13 , Issue.10 , pp. 438-445
    • Chorev, M.1    Goodman, M.2
  • 27
    • 0020803141 scopus 로고
    • Computer simulation of the conformational properties of retro-inverso peptides. II. Ab initio study, spatial electron distribution, and population analysis of N-formylglycine methylamide, N-formyl N'-acetyldiaminomethane, and N-methylmalonamide
    • Stern, P.S., Chorev, M., Goodman, M., Hagler, A.T. Computer simulation of the conformational properties of retro-inverso peptides. II. Ab initio study, spatial electron distribution, and population analysis of N-formylglycine methylamide, N-formyl N'-acetyldiaminomethane, and N-methylmalonamide. Biopolymers. 1983, 22(8), 1901-1907.
    • (1983) Biopolymers , vol.22 , Issue.8 , pp. 1901-1907
    • Stern, P.S.1    Chorev, M.2    Goodman, M.3    Hagler, A.T.4
  • 28
    • 0020805678 scopus 로고
    • Proton NMR studies of partially modified retro- inverso peptides
    • Ribeiro, A., Chorev, M., Goodman, M. Proton NMR studies of partially modified retro- inverso peptides. Biopolymers. 1983, 22(8), 1869-1883.
    • (1983) Biopolymers , vol.22 , Issue.8 , pp. 1869-1883
    • Ribeiro, A.1    Chorev, M.2    Goodman, M.3
  • 29
    • 0011562608 scopus 로고    scopus 로고
    • Kates, S. and Albericio, F., eds. Marcel Dekker eds, New York
    • Guichard, G., In: Kates, S. and Albericio, F., eds. Solid-Phase Synthesis. Marcel Dekker eds, New York, 2000, pp 649-703.
    • (2000) Solid-Phase Synthesis , pp. 649-703
    • Guichard, G.1
  • 30
    • 0028116504 scopus 로고
    • An orally bioactive HIV-1 protease inhibitor containing an imidazole-derived peptide bond replacement: Crystallographic and pharmacokinetic analysis
    • Meguid, A., Metcalf, B. & Meek, T. An orally bioactive HIV-1 protease inhibitor containing an imidazole-derived peptide bond replacement: crystallographic and pharmacokinetic analysis. Biochemistry 1994, 33(39), 11671-11677.
    • (1994) Biochemistry , vol.33 , Issue.39 , pp. 11671-11677
    • Meguid, A.1    Metcalf, B.2    Meek, T.3
  • 31
    • 0025735602 scopus 로고
    • N]Pro linkages in HIV protease inhibitors
    • N]Pro linkages in HIV protease inhibitors. J. Org. Chem. 1991, 56, 4161-4167.
    • (1991) J. Org. Chem. , vol.56 , pp. 4161-4167
    • Cushman, M.1    Oh, Y.2
  • 32
    • 0026770573 scopus 로고
    • Crystallographic analysis of transition-state mimics bound to penecillopepsin: Phosporous-containing peptide analogues
    • Fraser, M., Strynadka, N., Bartlett, P., Hanson, J. and James, M. Crystallographic analysis of transition-state mimics bound to penecillopepsin: phosporous-containing peptide analogues. Biochem. 1992, 31, 5201-5214.
    • (1992) Biochem. , vol.31 , pp. 5201-5214
    • Fraser, M.1    Strynadka, N.2    Bartlett, P.3    Hanson, J.4    James, M.5
  • 33
    • 0027370067 scopus 로고
    • The crystallographic structure of the protease from human immunodeficiency virus type 2 with two synthetic peptidic transition state analog inhibitors
    • Mulichak, A., Hui, J., Tomasselli, A. The crystallographic structure of the protease from human immunodeficiency virus type 2 with two synthetic peptidic transition state analog inhibitors. J. Biol. Chem. 1993, 268(18), 13103-13109.
    • (1993) J. Biol. Chem. , vol.268 , Issue.18 , pp. 13103-13109
    • Mulichak, A.1    Hui, J.2    Tomasselli, A.3
  • 34
    • 0022067648 scopus 로고
    • Close structural resemblance between putative polymerase of a Drosophila transposable genetic element 17.6 and pol gene product of Moloney murine leukaemia virus
    • Toh, H., Kikuno, R., Hayashida, H., Miyata, T., Kugimiya, W., Inouye, S., Yuki, S., Saigo, K. Close structural resemblance between putative polymerase of a Drosophila transposable genetic element 17.6 and pol gene product of Moloney murine leukaemia virus. EMBO J. 1985, 4(5), 1267-1272.
    • (1985) EMBO J. , vol.4 , Issue.5 , pp. 1267-1272
    • Toh, H.1    Kikuno, R.2    Hayashida, H.3    Miyata, T.4    Kugimiya, W.5    Inouye, S.6    Yuki, S.7    Saigo, K.8
  • 36
  • 37
    • 1242328733 scopus 로고    scopus 로고
    • The virus-associated human immunodeficiency virus type 1 Gag-Pol carrying an active protease domain in the matrix region is severely defective both in autoprocessing and in trans processing of gag particles
    • Chen, S.W., Chiu, H.C., Liao, W.H., Wang, F.D., Chen, S.S., Wang, C.T. The virus-associated human immunodeficiency virus type 1 Gag-Pol carrying an active protease domain in the matrix region is severely defective both in autoprocessing and in trans processing of gag particles. Virology 2004, 318(2), 534-541.
    • (2004) Virology , vol.318 , Issue.2 , pp. 534-541
    • Chen, S.W.1    Chiu, H.C.2    Liao, W.H.3    Wang, F.D.4    Chen, S.S.5    Wang, C.T.6
  • 38
    • 0026345896 scopus 로고
    • A cumulative specificity model for proteases from human immunodeficiency virus types 1 and 2, inferred from statistical analysis of an extended substrate data base
    • Poorman, R.A., Tomasselli, A. G., Heinrikson, R. L., Kezdy, F.J. A cumulative specificity model for proteases from human immunodeficiency virus types 1 and 2, inferred from statistical analysis of an extended substrate data base J. Biol. Chem. 1991, 266, 14554-14561.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14554-14561
    • Poorman, R.A.1    Tomasselli, A.G.2    Heinrikson, R.L.3    Kezdy, F.J.4
  • 39
    • 0026778802 scopus 로고
    • Analysis of substrate interactions of the Rous sarcoma virus wild type and mutant proteases and human immunodeficiency virus-1 protease using a set of systematically altered peptide substrates
    • Grinde, B., Cameron, C. E., Leis, J., Weber IT, Wlodawer A, Burstein H, Skalka AM. Analysis of substrate interactions of the Rous sarcoma virus wild type and mutant proteases and human immunodeficiency virus-1 protease using a set of systematically altered peptide substrates. J. Biol. Chem. 1992, 267, 9491-9498.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9491-9498
    • Grinde, B.1    Cameron, C.E.2    Leis, J.3    Weber, I.T.4    Wlodawer, A.5    Burstein, H.6    Skalka, A.M.7
  • 40
    • 0027082783 scopus 로고
    • Mechanism of inhibition of the retroviral protease by a Rous sarcoma virus peptide substrate representing the cleavage site between the gag p2 and p10 proteins
    • Cameron, C.E., Grinde, B., Jentoft, J., Leis, J., Weber, I.T., Copeland, T.D., Wlodawer, A. Mechanism of inhibition of the retroviral protease by a Rous sarcoma virus peptide substrate representing the cleavage site between the gag p2 and p10 proteins. J. Biol. Chem. 1992, 267(33), 23735-23741.
    • (1992) J. Biol. Chem. , vol.267 , Issue.33 , pp. 23735-23741
    • Cameron, C.E.1    Grinde, B.2    Jentoft, J.3    Leis, J.4    Weber, I.T.5    Copeland, T.D.6    Wlodawer, A.7
  • 41
    • 0141888592 scopus 로고    scopus 로고
    • Small hydroxyethylene-based peptidomimetics inhibiting both HIV-1 and C. albicans aspartic proteases
    • Tossi, A., Benedetti, F., Norbedo, S., Skrbec, D., Berti, F., Romeo, D. Small hydroxyethylene-based peptidomimetics inhibiting both HIV-1 and C. albicans aspartic proteases. Bioorg. Med. Chem. 2003, 11(22), 4719-4727.
    • (2003) Bioorg. Med. Chem. , vol.11 , Issue.22 , pp. 4719-4727
    • Tossi, A.1    Benedetti, F.2    Norbedo, S.3    Skrbec, D.4    Berti, F.5    Romeo, D.6
  • 45
    • 0023225534 scopus 로고
    • 2NH] pseudopeptide analogues of a highly potent somatostatin octapeptide
    • 2NH] pseudopeptide analogues of a highly potent somatostatin octapeptide. J. Med. Chem. 1987, 30, 1162-1166.
    • (1987) J. Med. Chem. , vol.30 , pp. 1162-1166
    • Sasaki, Y.1    Murphy, W.2    Coy, D.3
  • 46
    • 0011822184 scopus 로고    scopus 로고
    • Partially modified retro-inverso peptides: Development, synthesis and conformational behavior
    • Fletcher, M.D. and Campbell, M. (1998). Partially modified retro-inverso peptides: development, synthesis and conformational behavior. Chemical Reviews 1990, 98(2), 763-795.
    • (1998) Chemical Reviews 1990 , vol.98 , Issue.2 , pp. 763-795
    • Fletcher, M.D.1    Campbell, M.2
  • 47
    • 85004872164 scopus 로고
    • An efficient synthesis of optically active α-(t-butoxycarbonylamino)-aldehides from α-amino acids
    • Fehrentz, J.A. and Castro, B. An efficient synthesis of optically active α-(t-butoxycarbonylamino)-aldehides from α-amino acids. Synthesis 1983, 676-678.
    • (1983) Synthesis , pp. 676-678
    • Fehrentz, J.A.1    Castro, B.2
  • 48
    • 20744456789 scopus 로고
    • Solid phase peptide synthesis. I. The synthesis of a tetrapeptide
    • Merrifield, R.B. Solid phase peptide synthesis. I. The synthesis of a tetrapeptide. J. Am. Chem. Soc. 1963, 85, 2149.
    • (1963) J. Am. Chem. Soc. , vol.85 , pp. 2149
    • Merrifield, R.B.1
  • 49
    • 0000478940 scopus 로고
    • General method for the rapid solid-phase peptide synthesis of the large number of peptides: Specificity of antigen-antibody interactions of the level of individual amino acids
    • Houghten, R.A. General method for the rapid solid-phase peptide synthesis of the large number of peptides: specificity of antigen-antibody interactions of the level of individual amino acids. Proc. Natl. Acad. Sci. USA 1985, 82, 5131.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 5131
    • Houghten, R.A.1
  • 50
    • 23644432773 scopus 로고    scopus 로고
    • Colorimetric analysis of protein sulfhydyl groups in milk: Applications and processing effects
    • Owusu-Apenten, R. Colorimetric analysis of protein sulfhydyl groups in milk: applications and processing effects. Crit. Rev. Food Sci. Nutr. 2005, 45(1), 1-23.
    • (2005) Crit. Rev. Food Sci. Nutr. , vol.45 , Issue.1 , pp. 1-23
    • Owusu-Apenten, R.1
  • 51
    • 20344370972 scopus 로고    scopus 로고
    • The Partial Retro-Inverso Modification: A Road Traveled Together
    • Chorev, M. The Partial Retro-Inverso Modification: A Road Traveled Together. Biopolymers 2005, 80, 67-84.
    • (2005) Biopolymers , vol.80 , pp. 67-84
    • Chorev, M.1
  • 52
    • 3242727586 scopus 로고    scopus 로고
    • Characterization of a reduced peptide bond analogue of a promiscuos CD4 T cell epitope derived from the Plasmodium falciparum malaria vaccine candidate merozoite surface protein 1
    • Bastian, M., Lozano, J.M., Patarroyo, M. E., Pluschke, G. and Daubenberger, C.A. Characterization of a reduced peptide bond analogue of a promiscuos CD4 T cell epitope derived from the Plasmodium falciparum malaria vaccine candidate merozoite surface protein 1. Molecular Immunology. 2004, 41, 775-784.
    • (2004) Molecular Immunology , vol.41 , pp. 775-784
    • Bastian, M.1    Lozano, J.M.2    Patarroyo, M.E.3    Pluschke, G.4    Daubenberger, C.A.5
  • 53
    • 13944267446 scopus 로고    scopus 로고
    • N,N'-Linked Oligoureas as Foldamers: Chain Length Requirements for Helix Formation in Protic Solvent Investigated by Circular Dichroism, NMR Spectroscopy, and Molecular Dynamics
    • Violette, A., Averlant-Petit, M.C., Semetey, V., Hemmerlin, C., Casimir, R., Graff, R., Marraud, M., Briand, J.P., Rognan, D., Guichard, G. N,N'-Linked Oligoureas as Foldamers: Chain Length Requirements for Helix Formation in Protic Solvent Investigated by Circular Dichroism, NMR Spectroscopy, and Molecular Dynamics. J. Am. Chem. Soc. 2005, 127(7), 2156-2164.
    • (2005) J. Am. Chem. Soc. , vol.127 , Issue.7 , pp. 2156-2164
    • Violette, A.1    Averlant-Petit, M.C.2    Semetey, V.3    Hemmerlin, C.4    Casimir, R.5    Graff, R.6    Marraud, M.7    Briand, J.P.8    Rognan, D.9    Guichard, G.10
  • 55
    • 0037591271 scopus 로고    scopus 로고
    • The Merozoite Surface Protein 1 complex of human malaria parasite Plasmodium falciparum
    • Kauth, C., Epp, C., Bujard, H. and Lutz, R. The Merozoite Surface Protein 1 complex of human malaria parasite Plasmodium falciparum. J. Biol. Chem. 2003, 278: 22257-22264.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22257-22264
    • Kauth, C.1    Epp, C.2    Bujard, H.3    Lutz, R.4
  • 56
    • 0023236613 scopus 로고
    • Allelic dimorphism in a surface antigen gene of the malaria parasite Plasmodium falciparum
    • Tanabe, K., Makay, M., Goman, M., Scaife, J.G. Allelic dimorphism in a surface antigen gene of the malaria parasite Plasmodium falciparum. J. Mol. Biol. 1987, 195, 273-287.
    • (1987) J. Mol. Biol. , vol.195 , pp. 273-287
    • Tanabe, K.1    Makay, M.2    Goman, M.3    Scaife, J.G.4
  • 58
    • 0033990381 scopus 로고    scopus 로고
    • Sequence diversity of the merozoite surface protein 1 of Plasmodium falciparum in clinical isolates from the Kilombero District, Tanzania
    • Jiang, G., Daubenberger, C., Huber, W., Matile, H., Tanner, M. and Pluschke, G. Sequence diversity of the merozoite surface protein 1 of Plasmodium falciparum in clinical isolates from the Kilombero District, Tanzania. Acta Trop. 2000, 74, 51-61.
    • (2000) Acta Trop. , vol.74 , pp. 51-61
    • Jiang, G.1    Daubenberger, C.2    Huber, W.3    Matile, H.4    Tanner, M.5    Pluschke, G.6
  • 59
    • 0031754987 scopus 로고    scopus 로고
    • Vaccines against the blood stages of falciparum malaria
    • Miller, L. H., Good M. F. and Kaslow, D. C. Vaccines against the blood stages of falciparum malaria. Adv. Exp. Med. Biol. 1998, 452, 193-205.
    • (1998) Adv. Exp. Med. Biol. , vol.452 , pp. 193-205
    • Miller, L.H.1    Good, M.F.2    Kaslow, D.C.3
  • 61
    • 0031569180 scopus 로고    scopus 로고
    • Precursor frequency analysis of cytotoxic T lymphocytes to pre-erythrocytic antigens of Plasmodium falciparum in West Africa
    • Plebanski, M., Aidoo, M., Whittle, H.C., Hill, A.V. Precursor frequency analysis of cytotoxic T lymphocytes to pre-erythrocytic antigens of Plasmodium falciparum in West Africa. J. Immunol. 1997, 158(6), 2849-2855.
    • (1997) J. Immunol. , vol.158 , Issue.6 , pp. 2849-2855
    • Plebanski, M.1    Aidoo, M.2    Whittle, H.C.3    Hill, A.V.4
  • 62
    • 0026514240 scopus 로고
    • 33 as a non-covalently associated complex with other fragments of the MSP-1
    • 33 as a non-covalently associated complex with other fragments of the MSP-1. Mol. Biochem. Parasitol. 1992, 50, 307-316.
    • (1992) Mol. Biochem. Parasitol. , vol.50 , pp. 307-316
    • Blackman, M.J.1    Holder, A.2
  • 63
    • 85195242836 scopus 로고
    • Primary structure of the precursor to the three major antigens of Plasmodium falciparum merozoites
    • Holder, A., Lockyer, M.J., Odink, K.G. Primary structure of the precursor to the three major antigens of Plasmodium falciparum merozoites, Nature 1985, 317270-31273.
    • (1985) Nature , pp. 317270-317273
    • Holder, A.1    Lockyer, M.J.2    Odink, K.G.3
  • 64
    • 85195241935 scopus 로고    scopus 로고
    • Human antibodies to the 19kDa C-terminal fragment of Plasmodium falciparum merozoite surface protein 1 inhibit parasite growth in vitro
    • Egan, A. F., Burghaus, P., Druilhe, P., Holder, A.A., Riley, E.M. Human antibodies to the 19kDa C-terminal fragment of Plasmodium falciparum merozoite surface protein 1 inhibit parasite growth in vitro, Parasite Immunol. 1999, 21133-21139.
    • (1999) Parasite Immunol. , pp. 21133-21139
    • Egan, A.F.1    Burghaus, P.2    Druilhe, P.3    Holder, A.A.4    Riley, E.M.5
  • 67
    • 0025010601 scopus 로고
    • Studies in owl monkeys leading to the development of a synthetic vaccine against the asexual blood stages of Plasmodium falciparum
    • Rodriguez, R., Moreno, A., Guzmán, F., Calvo, M. and Patarroyo, M.E. Studies in owl monkeys leading to the development of a synthetic vaccine against the asexual blood stages of Plasmodium falciparum. Am. J. Trop. Med. Hyg. 1990, 43, 339-354.
    • (1990) Am. J. Trop. Med. Hyg. , vol.43 , pp. 339-354
    • Rodriguez, R.1    Moreno, A.2    Guzmán, F.3    Calvo, M.4    Patarroyo, M.E.5
  • 69
    • 0035699903 scopus 로고    scopus 로고
    • Antigenicity and immunogenicity of synthetic peptides
    • Van Regenmortel, M.H. Antigenicity and immunogenicity of synthetic peptides. Biologicals. 2001, 29(3-4), 209-213.
    • (2001) Biologicals. , vol.29 , Issue.3-4 , pp. 209-213
    • Van Regenmortel, M.H.1
  • 70
    • 0035898447 scopus 로고    scopus 로고
    • Synthesis, Biological, and Immunological Properties of Cyclic Peptides from Plasmodium Falciparum Merozoite Surface Protein-1
    • Lioy, E., Suarez, J., Guzmán, F., Siegrist, S., Pluschke, G. and Patarroyo, M. E. Synthesis, Biological, and Immunological Properties of Cyclic Peptides from Plasmodium Falciparum Merozoite Surface Protein-1. Angewandte Chemie Int. Ed. 2001, 40, 2631-2635.
    • (2001) Angewandte Chemie Int. Ed. , vol.40 , pp. 2631-2635
    • Lioy, E.1    Suarez, J.2    Guzmán, F.3    Siegrist, S.4    Pluschke, G.5    Patarroyo, M.E.6
  • 71
    • 0034013532 scopus 로고    scopus 로고
    • Native-like cyclic peptide models of a viral antigenic site: Finding a balance between rigidity and flexibility
    • Valero, M.L., Camarero, J.A., Haack, T., Mateu, M.G., Domingo, E., Giralt, E., Andreu, D. Native-like cyclic peptide models of a viral antigenic site: finding a balance between rigidity and flexibility. J. Mol. Recognit. 2000, 13(1), 5-13.
    • (2000) J. Mol. Recognit. , vol.13 , Issue.1 , pp. 5-13
    • Valero, M.L.1    Camarero, J.A.2    Haack, T.3    Mateu, M.G.4    Domingo, E.5    Giralt, E.6    Andreu, D.7
  • 72
    • 0035814134 scopus 로고    scopus 로고
    • Exploiting conformationally constrained peptidomimetics and an efficient human-compatible delivery system in synthetic vaccine design
    • Moreno, R., Jiang, L., Moehle, K., Zurbriggen, R., Gluck, R., Robinson, J.A., Pluschke, G. Exploiting conformationally constrained peptidomimetics and an efficient human-compatible delivery system in synthetic vaccine design. Chembiochem. 2001, 2(11), 838-843.
    • (2001) Chembiochem. , vol.2 , Issue.11 , pp. 838-843
    • Moreno, R.1    Jiang, L.2    Moehle, K.3    Zurbriggen, R.4    Gluck, R.5    Robinson, J.A.6    Pluschke, G.7
  • 73
    • 0032234025 scopus 로고    scopus 로고
    • N-Hydroxy-amide analogues of MHC-class I peptide ligands with nanomolar binding affinities
    • Bianco, A., Zabel, C., Walden, P., Jung, G. N-Hydroxy-amide analogues of MHC-class I peptide ligands with nanomolar binding affinities. J. Pept. Sci. 1998, 4(8), 471-478.
    • (1998) J. Pept. Sci. , vol.4 , Issue.8 , pp. 471-478
    • Bianco, A.1    Zabel, C.2    Walden, P.3    Jung, G.4
  • 74
    • 0033970468 scopus 로고    scopus 로고
    • Antitumor vaccination using a major histocompatibility complex (MHC) class I-restricted pseudopeptide with reduced peptide bond
    • Calbo, S., Guichard, G., Muller, S., Kourilsky, P., Briand, J.P., Abastado, J.P. Antitumor vaccination using a major histocompatibility complex (MHC) class I-restricted pseudopeptide with reduced peptide bond. J. Immunother. 2000, 23(1), 125-130.
    • (2000) J. Immunother. , vol.23 , Issue.1 , pp. 125-130
    • Calbo, S.1    Guichard, G.2    Muller, S.3    Kourilsky, P.4    Briand, J.P.5    Abastado, J.P.6
  • 75
    • 0032430143 scopus 로고    scopus 로고
    • Reduced amide pseudopeptide analogs of a malaria peptide possess secondary structural elements responsible for induction of functional antibodies which react with native proteins expressed in Plasmodium falciparum erythrocyte stages
    • Lozano, J.M., Espejo, F., Diaz, D., Salazar, L.M., Rodriguez, J., Pinzón, C., Calvo, J.C., Guzmán, F., Patarroyo, M.E. Reduced amide pseudopeptide analogs of a malaria peptide possess secondary structural elements responsible for induction of functional antibodies which react with native proteins expressed in Plasmodium falciparum erythrocyte stages, J. Peptide Res. 1998, 52(6) 457-469.
    • (1998) J. Peptide Res. , vol.52 , Issue.6 , pp. 457-469
    • Lozano, J.M.1    Espejo, F.2    Diaz, D.3    Salazar, L.M.4    Rodriguez, J.5    Pinzón, C.6    Calvo, J.C.7    Guzmán, F.8    Patarroyo, M.E.9
  • 76
    • 0033605331 scopus 로고    scopus 로고
    • Protection against lymphocytic choriomeningitis virus infection induced by a reduced peptide bond analogue of the H-2Db-restricted CD8(+) T cell epitope GP33
    • Stemmer, C., Quesnel, A., Prevost-Blondel, A., Zimmermann, C., Muller, S., Briand, J.P., Pircher, H. Protection against lymphocytic choriomeningitis virus infection induced by a reduced peptide bond analogue of the H-2Db-restricted CD8(+) T cell epitope GP33. J. Biol. Chem. 1999, 274(9), 5550-5556.
    • (1999) J. Biol. Chem. , vol.274 , Issue.9 , pp. 5550-5556
    • Stemmer, C.1    Quesnel, A.2    Prevost-Blondel, A.3    Zimmermann, C.4    Muller, S.5    Briand, J.P.6    Pircher, H.7
  • 78
    • 4444306894 scopus 로고    scopus 로고
    • Mapping the anatomy of a Plasmodium falciparum MSP-1 epitope using pseudopeptide-induced mono- and poly-clonal antibodies and CD and NMR conformation analysis
    • Lozano, J.M., Espejo, F., Ocampo, M., Salazar, L.M., Tovar, D., Barrera, N., Guzmán, F. and Patarroyo M.E. Mapping the anatomy of a Plasmodium falciparum MSP-1 epitope using pseudopeptide-induced mono- and poly-clonal antibodies and CD and NMR conformation analysis. J. Struct. Biol. 2004, 148, 110-122.
    • (2004) J. Struct. Biol. , vol.148 , pp. 110-122
    • Lozano, J.M.1    Espejo, F.2    Ocampo, M.3    Salazar, L.M.4    Tovar, D.5    Barrera, N.6    Guzmán, F.7    Patarroyo, M.E.8
  • 79
    • 0038343611 scopus 로고    scopus 로고
    • A virosome-mimotope approach to synthetic vaccine design and optimgation: Synthesis, conformation, and immune recognition of a potential malaria-vaccine candidate
    • Pfeiffer, B., Peduzzi, E., Moehle, K., Zurbriggen, R., Gluck, R., Pluschke, G., Robinson, J.A. A virosome-mimotope approach to synthetic vaccine design and optimgation: synthesis, conformation, and immune recognition of a potential malaria-vaccine candidate. Angew. Chem. Int. Ed. Engl. 2003, 42(21), 2368-2371.
    • (2003) Angew. Chem. Int. Ed. Engl. , vol.42 , Issue.21 , pp. 2368-2371
    • Pfeiffer, B.1    Peduzzi, E.2    Moehle, K.3    Zurbriggen, R.4    Gluck, R.5    Pluschke, G.6    Robinson, J.A.7
  • 80
    • 19944369747 scopus 로고    scopus 로고
    • The clinical-grade 42-kilodalton fragment of merozoite surface protein 1 of Plasmodium falciparum strain FVO expressed in Escherichia coli protects Aotus nancymai against challenge with homologous crythrocytic-stage parasites
    • Darko, C.A., Angov, E., Collins, W.E., Bergmann-Leitner, E.S., Girouard, A.S., Hitt, S.L., McBride, J.S., Diggs, C.L., Holder, A.A., Long, C.A., Barnwell, J.W., Lyon, J.A. The clinical-grade 42-kilodalton fragment of merozoite surface protein 1 of Plasmodium falciparum strain FVO expressed in Escherichia coli protects Aotus nancymai against challenge with homologous crythrocytic-stage parasites. Infect Immun. 2005, 73(1), 287-297.
    • (2005) Infect Immun. , vol.73 , Issue.1 , pp. 287-297
    • Darko, C.A.1    Angov, E.2    Collins, W.E.3    Bergmann-Leitner, E.S.4    Girouard, A.S.5    Hitt, S.L.6    McBride, J.S.7    Diggs, C.L.8    Holder, A.A.9    Long, C.A.10    Barnwell, J.W.11    Lyon, J.A.12
  • 83
    • 33646003216 scopus 로고    scopus 로고
    • Effects of a Specific Peptide Bond Replacement on a Plasmodium falciparum Protein Primary Processing
    • Michael Chorev and Tomi K. Sawyer (Eds). American Peptide Society, San Diego
    • Lozano, J.M., Tovar, D.R., Salazar, L.M., Ocampo, M., Guzmán F. and Patarroyo, M.E. Effects of a Specific Peptide Bond Replacement on a Plasmodium falciparum Protein Primary Processing In: Peptide Revolution: Genomics, Proteomics & Therapeutics, Michael Chorev and Tomi K. Sawyer (Eds). American Peptide Society, San Diego, 2003, pp. 991-993.
    • (2003) Peptide Revolution: Genomics, Proteomics & Therapeutics , pp. 991-993
    • Lozano, J.M.1    Tovar, D.R.2    Salazar, L.M.3    Ocampo, M.4    Guzmán, F.5    Patarroyo, M.E.6


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