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Volumn 50, Issue 1, 2011, Pages 37-46

Functional characterization of methionine sulfoxide reductase A from Trypanosoma spp.

Author keywords

Free radicals; Methionine sulfoxide; Oxidative stress; Trypanosoma; Trypanothione; Tryparedoxin

Indexed keywords

METHIONINE SULFOXIDE REDUCTASE A; REDUCING AGENT; TRYPAREDOXIN I; UNCLASSIFIED DRUG;

EID: 78650689658     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2010.10.695     Document Type: Article
Times cited : (33)

References (51)
  • 1
    • 0035584857 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system
    • J. Nordberg, and E.S. Arner Reactive oxygen species, antioxidants, and the mammalian thioredoxin system Free Radic. Biol. Med. 31 2001 1287 1312
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1287-1312
    • Nordberg, J.1    Arner, E.S.2
  • 2
    • 12844267504 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: Ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases
    • J. Moskovitz Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases Biochim. Biophys. Acta 1703 2005 213 219
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 213-219
    • Moskovitz, J.1
  • 3
    • 33646578189 scopus 로고    scopus 로고
    • Oxidized protein degradation and repair in ageing and oxidative stress
    • B. Friguet Oxidized protein degradation and repair in ageing and oxidative stress FEBS Lett. 580 2006 2910 2916
    • (2006) FEBS Lett. , vol.580 , pp. 2910-2916
    • Friguet, B.1
  • 4
    • 44549088533 scopus 로고    scopus 로고
    • The methionine sulfoxide reductases: Catalysis and substrate specificities
    • S. Boschi-Muller, A. Gand, and G. Branlant The methionine sulfoxide reductases: catalysis and substrate specificities Arch. Biochem. Biophys. 474 2008 266 273
    • (2008) Arch. Biochem. Biophys. , vol.474 , pp. 266-273
    • Boschi-Muller, S.1    Gand, A.2    Branlant, G.3
  • 5
    • 0032564345 scopus 로고    scopus 로고
    • Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress
    • J. Moskovitz, E. Flescher, B.S. Berlett, J. Azare, J.M. Poston, and E.R. Stadtman Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress Proc. Natl Acad. Sci. USA 95 1998 14071 14075
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 14071-14075
    • Moskovitz, J.1    Flescher, E.2    Berlett, B.S.3    Azare, J.4    Poston, J.M.5    Stadtman, E.R.6
  • 6
    • 1842712573 scopus 로고    scopus 로고
    • Arabidopsis peptide methionine sulfoxide reductase2 prevents cellular oxidative damage in long nights
    • U. Bechtold, D.J. Murphy, and P.M. Mullineaux Arabidopsis peptide methionine sulfoxide reductase2 prevents cellular oxidative damage in long nights Plant Cell 16 2004 908 919
    • (2004) Plant Cell , vol.16 , pp. 908-919
    • Bechtold, U.1    Murphy, D.J.2    Mullineaux, P.M.3
  • 7
    • 0037023730 scopus 로고    scopus 로고
    • Characterization of the methionine sulfoxide reductase activities of PILB, a probable virulence factor from Neisseria meningitidis
    • DOI 10.1074/jbc.M112350200
    • A. Olry, S. Boschi-Muller, M. Marraud, S. Sanglier-Cianferani, A. Van Dorsselear, and G. Branlant Characterization of the methionine sulfoxide reductase activities of PILB, a probable virulence factor from Neisseria meningitidis J. Biol. Chem. 277 2002 12016 12022 (Pubitemid 34952763)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.14 , pp. 12016-12022
    • Olry, A.1    Boschi-Muller, S.2    Marraud, M.3    Sanglier-Cianferani, S.4    Van Dorsselear, A.5    Branlant, G.6
  • 8
    • 0036297758 scopus 로고    scopus 로고
    • Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity
    • J. Moskovitz, V.K. Singh, J. Requena, B.J. Wilkinson, R.K. Jayaswal, and E.R. Stadtman Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity Biochem. Biophys. Res. Commun. 290 2002 62 65
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 62-65
    • Moskovitz, J.1    Singh, V.K.2    Requena, J.3    Wilkinson, B.J.4    Jayaswal, R.K.5    Stadtman, E.R.6
  • 10
    • 0034640506 scopus 로고    scopus 로고
    • Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity
    • J. Moskovitz, J.M. Poston, B.S. Berlett, N.J. Nosworthy, R. Szczepanowski, and E.R. Stadtman Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity J. Biol. Chem. 275 2000 14167 14172
    • (2000) J. Biol. Chem. , vol.275 , pp. 14167-14172
    • Moskovitz, J.1    Poston, J.M.2    Berlett, B.S.3    Nosworthy, N.J.4    Szczepanowski, R.5    Stadtman, E.R.6
  • 11
    • 49349112856 scopus 로고    scopus 로고
    • Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism
    • R.L. Krauth-Siegel, and M.A. Comini Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism Biochim. Biophys. Acta 1780 2008 1236 1248
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 1236-1248
    • Krauth-Siegel, R.L.1    Comini, M.A.2
  • 12
    • 54949087530 scopus 로고    scopus 로고
    • Insights into the redox biology of Trypanosoma cruzi: Trypanothione metabolism and oxidant detoxification
    • F. Irigoin, L. Cibils, M.A. Comini, S.R. Wilkinson, L. Flohe, and R. Radi Insights into the redox biology of Trypanosoma cruzi: trypanothione metabolism and oxidant detoxification Free Radic. Biol. Med. 45 2008 733 742
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 733-742
    • Irigoin, F.1    Cibils, L.2    Comini, M.A.3    Wilkinson, S.R.4    Flohe, L.5    Radi, R.6
  • 14
    • 0033230579 scopus 로고    scopus 로고
    • Glutathione and trypanothione in parasitic hydroperoxide metabolism
    • L. Flohe, H.J. Hecht, and P. Steinert Glutathione and trypanothione in parasitic hydroperoxide metabolism Free Radic. Biol. Med. 27 1999 966 984
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 966-984
    • Flohe, L.1    Hecht, H.J.2    Steinert, P.3
  • 16
    • 68049131348 scopus 로고    scopus 로고
    • Fighting the oxidative assault: The Trypanosoma cruzi journey to infection
    • L. Piacenza, M.N. Alvarez, G. Peluffo, and R. Radi Fighting the oxidative assault: the Trypanosoma cruzi journey to infection Curr. Opin. Microbiol. 12 2009 415 421
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 415-421
    • Piacenza, L.1    Alvarez, M.N.2    Peluffo, G.3    Radi, R.4
  • 17
    • 0024322313 scopus 로고
    • Protein kinase C in Trypanosoma cruzi epimastigote forms: Partial purification and characterization
    • M.L. Gomez, L. Erijman, S. Arauzo, H.N. Torres, and M.T. Tellez-Inon Protein kinase C in Trypanosoma cruzi epimastigote forms: partial purification and characterization Mol. Biochem. Parasitol. 36 1989 101 108
    • (1989) Mol. Biochem. Parasitol. , vol.36 , pp. 101-108
    • Gomez, M.L.1    Erijman, L.2    Arauzo, S.3    Torres, H.N.4    Tellez-Inon, M.T.5
  • 18
    • 0032991708 scopus 로고    scopus 로고
    • Intracellular growth and metacyclogenesis defects in Trypanosoma cruzi carrying a targeted deletion of a Tc52 protein-encoding allele
    • A. Allaoui, C. Francois, K. Zemzoumi, E. Guilvard, and A. Ouaissi Intracellular growth and metacyclogenesis defects in Trypanosoma cruzi carrying a targeted deletion of a Tc52 protein-encoding allele Mol. Microbiol. 32 1999 1273 1286
    • (1999) Mol. Microbiol. , vol.32 , pp. 1273-1286
    • Allaoui, A.1    Francois, C.2    Zemzoumi, K.3    Guilvard, E.4    Ouaissi, A.5
  • 19
    • 0020318215 scopus 로고
    • Adhesion and interiorization of Trypanosoma cruzi in mammalian cells
    • N.W. Andrews, and W. Colli Adhesion and interiorization of Trypanosoma cruzi in mammalian cells J. Protozool. 29 1982 264 269
    • (1982) J. Protozool. , vol.29 , pp. 264-269
    • Andrews, N.W.1    Colli, W.2
  • 21
    • 0037053395 scopus 로고    scopus 로고
    • The Trypanosoma cruzi enzyme TcGPXI is a glycosomal peroxidase and can be linked to trypanothione reduction by glutathione or tryparedoxin
    • S.R. Wilkinson, D.J. Meyer, M.C. Taylor, E.V. Bromley, M.A. Miles, and J.M. Kelly The Trypanosoma cruzi enzyme TcGPXI is a glycosomal peroxidase and can be linked to trypanothione reduction by glutathione or tryparedoxin J. Biol. Chem. 277 2002 17062 17071
    • (2002) J. Biol. Chem. , vol.277 , pp. 17062-17071
    • Wilkinson, S.R.1    Meyer, D.J.2    Taylor, M.C.3    Bromley, E.V.4    Miles, M.A.5    Kelly, J.M.6
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 25
    • 0001522673 scopus 로고
    • Starch-gel electrophoresis-application to the classification of pituitary proteins and polypeptides
    • K.A. Ferguson Starch-gel electrophoresis-application to the classification of pituitary proteins and polypeptides Metabolism 13 1964 985 1002 (Suppl.)
    • (1964) Metabolism , vol.13 , Issue.SUPPL. , pp. 985-1002
    • Ferguson, K.A.1
  • 27
    • 0026673614 scopus 로고
    • A shuttle vector which facilitates the expression of transfected genes in Trypanosoma cruzi and Leishmania
    • J.M. Kelly, H.M. Ward, M.A. Miles, and G. Kendall A shuttle vector which facilitates the expression of transfected genes in Trypanosoma cruzi and Leishmania Nucleic Acids Res. 20 1992 3963 3969
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3963-3969
    • Kelly, J.M.1    Ward, H.M.2    Miles, M.A.3    Kendall, G.4
  • 29
    • 43749107283 scopus 로고    scopus 로고
    • Comparative protein structure modeling using MODELLER
    • John Wiley & Sons, Inc., 5.6.1-5.6.30 University of California at San Francisco, San Francisco, California, USA
    • N. Eswar, B. Webb, M.A. Marti-Renom, M.S. Madhusudhan, D. Eramian, M.Y. Shen, U. Pieper, and A. Sali Comparative protein structure modeling using MODELLER Current Protocols in Protein Science 2006 John Wiley & Sons, Inc., Supplement 15, 5.6.1-5.6.30 University of California at San Francisco, San Francisco, California, USA
    • (2006) Current Protocols in Protein Science , Issue.SUPPL. 15
    • Eswar, N.1    Webb, B.2    Marti-Renom, M.A.3    Madhusudhan, M.S.4    Eramian, D.5    Shen, M.Y.6    Pieper, U.7    Sali, A.8
  • 30
    • 12844273604 scopus 로고    scopus 로고
    • The three-dimensional structures of peptide methionine sulfoxide reductases: Current knowledge and open questions
    • B. Kauffmann, A. Aubry, and F. Favier The three-dimensional structures of peptide methionine sulfoxide reductases: current knowledge and open questions Biochim. Biophys. Acta 1703 2005 249 260
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 249-260
    • Kauffmann, B.1    Aubry, A.2    Favier, F.3
  • 32
    • 0034775194 scopus 로고    scopus 로고
    • E. coli methionine sulfoxide reductase with a truncated N terminus or C terminus, or both, retains the ability to reduce methionine sulfoxide
    • S. Boschi-Muller, S. Azza, and G. Branlant E. coli methionine sulfoxide reductase with a truncated N terminus or C terminus, or both, retains the ability to reduce methionine sulfoxide Protein Sci. 10 2001 2272 2279
    • (2001) Protein Sci. , vol.10 , pp. 2272-2279
    • Boschi-Muller, S.1    Azza, S.2    Branlant, G.3
  • 33
    • 0014767988 scopus 로고
    • Unified theory for gel electrophoresis and gel filtration
    • D. Rodbard, and A. Chrambach Unified theory for gel electrophoresis and gel filtration Proc. Natl Acad. Sci. USA 65 1970 970 977
    • (1970) Proc. Natl Acad. Sci. USA , vol.65 , pp. 970-977
    • Rodbard, D.1    Chrambach, A.2
  • 34
    • 33846291686 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of the reduced form and an oxidized form of E. coli methionine sulfoxide reductase A (MsrA): Structural insight of the MsrA catalytic cycle
    • N. Coudevylle, M. Antoine, S. Bouguet-Bonnet, P. Mutzenhardt, S. Boschi-Muller, G. Branlant, and M.T. Cung Solution structure and backbone dynamics of the reduced form and an oxidized form of E. coli methionine sulfoxide reductase A (MsrA): structural insight of the MsrA catalytic cycle J. Mol. Biol. 366 2007 193 206
    • (2007) J. Mol. Biol. , vol.366 , pp. 193-206
    • Coudevylle, N.1    Antoine, M.2    Bouguet-Bonnet, S.3    Mutzenhardt, P.4    Boschi-Muller, S.5    Branlant, G.6    Cung, M.T.7
  • 35
    • 0038154089 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine
    • A.B. Taylor, D.M. Benglis Jr., S. Dhandayuthapani, and P.J. Hart Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine J. Bacteriol. 185 2003 4119 4126
    • (2003) J. Bacteriol. , vol.185 , pp. 4119-4126
    • Taylor, A.B.1    Benglis Jr., D.M.2    Dhandayuthapani, S.3    Hart, P.J.4
  • 36
    • 67349114539 scopus 로고    scopus 로고
    • Electric charge divergence in proteins: Insights into the evolution of their three-dimensional properties
    • Y. Sato, and M. Nishida Electric charge divergence in proteins: insights into the evolution of their three-dimensional properties Gene 441 2009 3 11
    • (2009) Gene , vol.441 , pp. 3-11
    • Sato, Y.1    Nishida, M.2
  • 38
    • 0037108740 scopus 로고    scopus 로고
    • Trypanosoma cruzi expresses a plant-like ascorbate-dependent hemoperoxidase localized to the endoplasmic reticulum
    • S.R. Wilkinson, S.O. Obado, I.L. Mauricio, and J.M. Kelly Trypanosoma cruzi expresses a plant-like ascorbate-dependent hemoperoxidase localized to the endoplasmic reticulum Proc. Natl Acad. Sci. USA 99 2002 13453 13458
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 13453-13458
    • Wilkinson, S.R.1    Obado, S.O.2    Mauricio, I.L.3    Kelly, J.M.4
  • 39
    • 49349112856 scopus 로고    scopus 로고
    • Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism
    • R.L. Krauth-Siegel, and M.A. Comini Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism Biochim. Biophys. Acta 1780 2008 1236 1248
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 1236-1248
    • Krauth-Siegel, R.L.1    Comini, M.A.2
  • 40
    • 37549058462 scopus 로고    scopus 로고
    • Peroxiredoxins from Trypanosoma cruzi: Virulence factors and drug targets for treatment of Chagas disease?
    • M.D. Pineyro, A. Parodi-Talice, T. Arcari, and C. Robello Peroxiredoxins from Trypanosoma cruzi: virulence factors and drug targets for treatment of Chagas disease? Gene 408 2008 45 50
    • (2008) Gene , vol.408 , pp. 45-50
    • Pineyro, M.D.1    Parodi-Talice, A.2    Arcari, T.3    Robello, C.4
  • 42
    • 11444253845 scopus 로고    scopus 로고
    • Cloning and characterization of antioxidant enzyme methionine sulfoxide-S-reductase from Caenorhabditis elegans
    • B.C. Lee, Y.K. Lee, H.J. Lee, E.R. Stadtman, K.H. Lee, and N. Chung Cloning and characterization of antioxidant enzyme methionine sulfoxide-S-reductase from Caenorhabditis elegans Arch. Biochem. Biophys. 434 2005 275 281
    • (2005) Arch. Biochem. Biophys. , vol.434 , pp. 275-281
    • Lee, B.C.1    Lee, Y.K.2    Lee, H.J.3    Stadtman, E.R.4    Lee, K.H.5    Chung, N.6
  • 43
    • 0344875617 scopus 로고    scopus 로고
    • Functional and physicochemical characterization of the thioredoxin system in Trypanosoma brucei
    • H. Schmidt, and R.L. Krauth-Siegel Functional and physicochemical characterization of the thioredoxin system in Trypanosoma brucei J. Biol. Chem. 278 2003 46329 46336
    • (2003) J. Biol. Chem. , vol.278 , pp. 46329-46336
    • Schmidt, H.1    Krauth-Siegel, R.L.2
  • 44
    • 0028222670 scopus 로고
    • Treatment of electrostatic effects in proteins: Multigrid-based Newton iterative method for solution of the full nonlinear Poisson-Boltzmann equation
    • M. Holst, R.E. Kozack, F. Saied, and S. Subramaniam Treatment of electrostatic effects in proteins: multigrid-based Newton iterative method for solution of the full nonlinear Poisson-Boltzmann equation Proteins 18 1994 231 245 (Pubitemid 24096734)
    • (1994) Proteins: Structure, Function and Genetics , vol.18 , Issue.3 , pp. 231-245
    • Holst, M.1    Kozack, R.E.2    Saied, F.3    Subramaniam, S.4
  • 45
    • 0032535514 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase inactivation by peroxynitrite
    • J.M. Souza, and R. Radi Glyceraldehyde-3-phosphate dehydrogenase inactivation by peroxynitrite Arch. Biochem. Biophys. 360 1998 187 194
    • (1998) Arch. Biochem. Biophys. , vol.360 , pp. 187-194
    • Souza, J.M.1    Radi, R.2
  • 46
    • 0034680847 scopus 로고    scopus 로고
    • A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli
    • S. Boschi-Muller, S. Azza, S. Sanglier-Cianferani, F. Talfournier, A. Van Dorsselear, and G. Branlant A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli J. Biol. Chem. 275 2000 35908 35913
    • (2000) J. Biol. Chem. , vol.275 , pp. 35908-35913
    • Boschi-Muller, S.1    Azza, S.2    Sanglier-Cianferani, S.3    Talfournier, F.4    Van Dorsselear, A.5    Branlant, G.6
  • 47
    • 0027494350 scopus 로고
    • Phenotype of recombinant Leishmania donovani and Trypanosoma cruzi which over-express trypanothione reductase: Sensitivity towards agents that are thought to induce oxidative stress
    • J.M. Kelly, M.C. Taylor, K. Smith, K.J. Hunter, and A.H. Fairlamb Phenotype of recombinant Leishmania donovani and Trypanosoma cruzi which over-express trypanothione reductase: sensitivity towards agents that are thought to induce oxidative stress Eur. J. Biochem. 218 1993 29 37
    • (1993) Eur. J. Biochem. , vol.218 , pp. 29-37
    • Kelly, J.M.1    Taylor, M.C.2    Smith, K.3    Hunter, K.J.4    Fairlamb, A.H.5
  • 48
    • 40449096623 scopus 로고    scopus 로고
    • Peroxiredoxins play a major role in protecting Trypanosoma cruzi against macrophage- and endogenously-derived peroxynitrite
    • L. Piacenza, G. Peluffo, M.N. Alvarez, J.M. Kelly, S.R. Wilkinson, and R. Radi Peroxiredoxins play a major role in protecting Trypanosoma cruzi against macrophage- and endogenously-derived peroxynitrite Biochem. J. 410 2008 359 368
    • (2008) Biochem. J. , vol.410 , pp. 359-368
    • Piacenza, L.1    Peluffo, G.2    Alvarez, M.N.3    Kelly, J.M.4    Wilkinson, S.R.5    Radi, R.6
  • 49
    • 0035859807 scopus 로고    scopus 로고
    • Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates
    • G. St John, N. Brot, J. Ruan, H. Erdjument-Bromage, P. Tempst, H. Weissbach, and C. Nathan Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates Proc. Natl Acad. Sci. USA 98 2001 9901 9906
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 9901-9906
    • St John, G.1    Brot, N.2    Ruan, J.3    Erdjument-Bromage, H.4    Tempst, P.5    Weissbach, H.6    Nathan, C.7
  • 50
    • 58149100981 scopus 로고    scopus 로고
    • Overexpression of methionine sulfoxide reductases A and B2 protects MOLT-4 cells against zinc-induced oxidative stress
    • F. Cabreiro, C.R. Picot, M. Perichon, B. Friguet, and I. Petropoulos Overexpression of methionine sulfoxide reductases A and B2 protects MOLT-4 cells against zinc-induced oxidative stress Antioxid. Redox Signaling 11 2009 215 225
    • (2009) Antioxid. Redox Signaling , vol.11 , pp. 215-225
    • Cabreiro, F.1    Picot, C.R.2    Perichon, M.3    Friguet, B.4    Petropoulos, I.5
  • 51
    • 0033014601 scopus 로고    scopus 로고
    • Enantioselective synthesis and pharmacological evaluation of a new type of verapamil analog with hypotensive and calcium antagonist activities
    • H.L. Holland, J.X Gu, F. Orallo, M. Camina, P. Fabeiro, and A.J. Willetts Enantioselective synthesis and pharmacological evaluation of a new type of verapamil analog with hypotensive and calcium antagonist activities Pharm Res 16 1999 281 287
    • (1999) Pharm Res , vol.16 , pp. 281-287
    • Holland, H.L.1    Gu, J.X.2    Orallo, F.3    Camina, M.4    Fabeiro, P.5    Willetts, A.J.6


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