메뉴 건너뛰기




Volumn 51, Issue 9, 2008, Pages 2816-2832

Aza-peptidyl Michael acceptors. A new class of potent and selective inhibitors of asparaginyl endopeptidases (legumains) from evolutionarily diverse pathogens

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE; APC 3316; AZA PEPTIDE MICHAEL ACCEPTOR; CRA 3316; FUMARIC ACID; HOMOPHENYL ALANINE VINYL SULFONE; K 11777; LEGUMAIN; RUPRINTIVIR;

EID: 42949122012     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm701311r     Document Type: Article
Times cited : (45)

References (54)
  • 1
    • 0032435254 scopus 로고    scopus 로고
    • Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases
    • Chen, J. M.; Rawlings, N. D.; Stevens, R. A.; Barrett, A. J. Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases. FEBS Lett. 1998, 441, 361-365.
    • (1998) FEBS Lett , vol.441 , pp. 361-365
    • Chen, J.M.1    Rawlings, N.D.2    Stevens, R.A.3    Barrett, A.J.4
  • 2
    • 0023656149 scopus 로고
    • Cloning and gene expression of Schistosoma mansoni protease
    • Davis, A. H.; Nanduri, J.; Watson, D. C. Cloning and gene expression of Schistosoma mansoni protease. J. Biol. Chem. 1987, 262, 12851-12855.
    • (1987) J. Biol. Chem , vol.262 , pp. 12851-12855
    • Davis, A.H.1    Nanduri, J.2    Watson, D.C.3
  • 3
    • 0027688051 scopus 로고
    • Molecular characterization of a vacuolar processing enzyme related to a putative cysteine proteinase of Schistosoma mansoni
    • Hara-Nishimura, I.; Takeuchi, Y.; Nishimura, M. Molecular characterization of a vacuolar processing enzyme related to a putative cysteine proteinase of Schistosoma mansoni. Plant Cell 1993, 5, 1651-1659.
    • (1993) Plant Cell , vol.5 , pp. 1651-1659
    • Hara-Nishimura, I.1    Takeuchi, Y.2    Nishimura, M.3
  • 4
    • 0032189364 scopus 로고    scopus 로고
    • Cloning and expression of mouse legumain, a lysosomal endopeptidase
    • Chen, J. M.; Dando, P. M.; Stevens, R. A.; Fortunato, M.; Barrett, A. J. Cloning and expression of mouse legumain, a lysosomal endopeptidase. Biochem. J. 1998, 335 (Part 1), 111-117.
    • (1998) Biochem. J , vol.335 , Issue.PART 1 , pp. 111-117
    • Chen, J.M.1    Dando, P.M.2    Stevens, R.A.3    Fortunato, M.4    Barrett, A.J.5
  • 5
    • 0001460158 scopus 로고    scopus 로고
    • Identification of human asparaginyl endopeptidase (legumain) as an inhibitor of osteoclast formation and bone resorption
    • Choi, S. J.; Reddy, S. V.; Devlin, R. D.; Menaa, C.; Chung, H.; Boyce, B. F.; Roodman, G. D. Identification of human asparaginyl endopeptidase (legumain) as an inhibitor of osteoclast formation and bone resorption. J. Biol. Chem. 1999, 274, 27747-27753.
    • (1999) J. Biol. Chem , vol.274 , pp. 27747-27753
    • Choi, S.J.1    Reddy, S.V.2    Devlin, R.D.3    Menaa, C.4    Chung, H.5    Boyce, B.F.6    Roodman, G.D.7
  • 6
    • 0032542285 scopus 로고    scopus 로고
    • An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation
    • Manoury, B.; Hewitt, E. W.; Morrice, N.; Dando, P. M.; Barrett, A. J.; Watts, C. An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation. Nature 1998, 396, 695-699.
    • (1998) Nature , vol.396 , pp. 695-699
    • Manoury, B.1    Hewitt, E.W.2    Morrice, N.3    Dando, P.M.4    Barrett, A.J.5    Watts, C.6
  • 7
    • 0036499652 scopus 로고    scopus 로고
    • Classification of the caspase-hemoglobinase fold: Detection of new families and implications for the origin of the eukaryotic separins
    • Aravind, L.; Koonin, E. V. Classification of the caspase-hemoglobinase fold: detection of new families and implications for the origin of the eukaryotic separins. Proteins 2002, 46, 355-367.
    • (2002) Proteins , vol.46 , pp. 355-367
    • Aravind, L.1    Koonin, E.V.2
  • 8
    • 1942519435 scopus 로고    scopus 로고
    • Caffrey, C. R.; McKerrow, J. H.; Salter, J. P.; Sajid, M. Blood n guts: an update on schistosome digestive peptidases. Trends Parasitol. 2004, 20, 241-248.
    • Caffrey, C. R.; McKerrow, J. H.; Salter, J. P.; Sajid, M. Blood "n" guts: an update on schistosome digestive peptidases. Trends Parasitol. 2004, 20, 241-248.
  • 12
    • 0034925333 scopus 로고    scopus 로고
    • Legumain forms from plants and animals differ in their specificity
    • Rotari, V. I.; Dando, P. M.; Barrett, A. J. Legumain forms from plants and animals differ in their specificity. Biol. Chem. 2001, 382, 953-959.
    • (2001) Biol. Chem , vol.382 , pp. 953-959
    • Rotari, V.I.1    Dando, P.M.2    Barrett, A.J.3
  • 13
    • 0001474730 scopus 로고    scopus 로고
    • Schistosome asparaginyl endopeptidase Sm32 in hemoglobin digestion
    • Dalton, J. P.; Brindley, P. J. Schistosome asparaginyl endopeptidase Sm32 in hemoglobin digestion. Parasitol. Today 1996, 12, 125.
    • (1996) Parasitol. Today , vol.12 , pp. 125
    • Dalton, J.P.1    Brindley, P.J.2
  • 15
    • 0031060616 scopus 로고    scopus 로고
    • Caffrey, C. R.; Rheinberg, C. E.; Mone, H.; Jourdane, J.; Li, Y. L.; Ruppel, A. Schistosoma japonicum, S. mansoni, S. haematobium, S. intercalatum, and S. rodhaini: cysteine-class cathepsin activities in the vomitus of adult worms. Parasitol. Res. 1997, 83, 37-41.
    • Caffrey, C. R.; Rheinberg, C. E.; Mone, H.; Jourdane, J.; Li, Y. L.; Ruppel, A. Schistosoma japonicum, S. mansoni, S. haematobium, S. intercalatum, and S. rodhaini: cysteine-class cathepsin activities in the vomitus of adult worms. Parasitol. Res. 1997, 83, 37-41.
  • 17
    • 0141626757 scopus 로고    scopus 로고
    • Novel cell-permeable acyloxymethylketone inhibitors of asparaginyl endopeptidase
    • Loak, K.; Li, D. N.; Manoury, B.; Billson, J.; Morton, F.; Hewitt, E.; Watts, C. Novel cell-permeable acyloxymethylketone inhibitors of asparaginyl endopeptidase. Biol. Chem. 2003, 384, 1239-1246.
    • (2003) Biol. Chem , vol.384 , pp. 1239-1246
    • Loak, K.1    Li, D.N.2    Manoury, B.3    Billson, J.4    Morton, F.5    Hewitt, E.6    Watts, C.7
  • 20
    • 33846188177 scopus 로고    scopus 로고
    • Design of cell-permeable, fluorescent activity-based probes for the lysosomal cysteine protease asparaginyl endopeptidase (AEP)/legumain
    • Sexton, K. B.; Witte, M. D.; Blum, G.; Bogyo, M. Design of cell-permeable, fluorescent activity-based probes for the lysosomal cysteine protease asparaginyl endopeptidase (AEP)/legumain. Bioorg. Med. Chem. Lett. 2007, 17, 649-653.
    • (2007) Bioorg. Med. Chem. Lett , vol.17 , pp. 649-653
    • Sexton, K.B.1    Witte, M.D.2    Blum, G.3    Bogyo, M.4
  • 21
    • 0347358966 scopus 로고    scopus 로고
    • Aza-peptide epoxides: Potent and selective inhibitors of Schistosoma mansoni and pig kidney legumains (asparaginyl endopeptidases)
    • James, K. E.; Götz, M. G.; Caffrey, C. R.; Hansell, E.; McKerrow, J. H.; Carter, W.; Barrett, A.; Powers, J. C. Aza-peptide epoxides: potent and selective inhibitors of Schistosoma mansoni and pig kidney legumains (asparaginyl endopeptidases). Biol. Chem. 2003, 384, 1613-1618.
    • (2003) Biol. Chem , vol.384 , pp. 1613-1618
    • James, K.E.1    Götz, M.G.2    Caffrey, C.R.3    Hansell, E.4    McKerrow, J.H.5    Carter, W.6    Barrett, A.7    Powers, J.C.8
  • 23
    • 0021260942 scopus 로고
    • Vinylogous amino acid esters: A new class of inactivators for thiol proteases
    • Hanzlik, R. P.; Thompson, S. A. Vinylogous amino acid esters: a new class of inactivators for thiol proteases. J. Med. Chem. 1984, 27, 711-712.
    • (1984) J. Med. Chem , vol.27 , pp. 711-712
    • Hanzlik, R.P.1    Thompson, S.A.2
  • 24
    • 0022607084 scopus 로고
    • Carboxyl-modified amino acids and peptides as protease inhibitors
    • Thompson, S. A.; Andrews, P. R.; Hanzlik, R. P. Carboxyl-modified amino acids and peptides as protease inhibitors. J. Med. Chem. 1986, 29, 104-111.
    • (1986) J. Med. Chem , vol.29 , pp. 104-111
    • Thompson, S.A.1    Andrews, P.R.2    Hanzlik, R.P.3
  • 25
    • 0026517333 scopus 로고
    • Structure-activity relationships for inhibition of papain by peptide Michael acceptors
    • Liu, S.; Hanzlik, R. P. Structure-activity relationships for inhibition of papain by peptide Michael acceptors. J. Med. Chem. 1992, 35, 1067-1075.
    • (1992) J. Med. Chem , vol.35 , pp. 1067-1075
    • Liu, S.1    Hanzlik, R.P.2
  • 26
    • 0019948262 scopus 로고    scopus 로고
    • Barrett, A. J.; Kembhavi, A. A.; Brown, M. A.; Kirschke, H.; Knight, C. G.; Tama, M.; Hanada, K. L-trans-Epoxysuccinyl-leucylamido(4- guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsin B, H, and L. Biochem. J. 1982, 201, 189-198.
    • Barrett, A. J.; Kembhavi, A. A.; Brown, M. A.; Kirschke, H.; Knight, C. G.; Tama, M.; Hanada, K. L-trans-Epoxysuccinyl-leucylamido(4- guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsin B, H, and L. Biochem. J. 1982, 201, 189-198.
  • 27
    • 0029099619 scopus 로고
    • Vinyl sulfone as mechanism-based cysteine protease inhibitors
    • Palmer, J. T.; Rasnik, D.; Klaus, J. L.; Brömme, D. Vinyl sulfone as mechanism-based cysteine protease inhibitors. J. Med. Chem. 1995, 38, 3193-3196.
    • (1995) J. Med. Chem , vol.38 , pp. 3193-3196
    • Palmer, J.T.1    Rasnik, D.2    Klaus, J.L.3    Brömme, D.4
  • 29
    • 0032987794 scopus 로고    scopus 로고
    • Solid-phase synthesis of irreversible human rhinovirus 3C protease inhibitors. Part 1: Optimization of tripeptides incorporating N-terminal amides
    • Dragovich, P. S.; Zhou, R.; Skalitzky, D. J.; Fuhrman, S. A.; Patick, A. K.; Ford, C. E.; Meador, J. W., 3rd; Worland, S. T. Solid-phase synthesis of irreversible human rhinovirus 3C protease inhibitors. Part 1: Optimization of tripeptides incorporating N-terminal amides. Bioorg. Med. Chem. 1999, 7, 589-598.
    • (1999) Bioorg. Med. Chem , vol.7 , pp. 589-598
    • Dragovich, P.S.1    Zhou, R.2    Skalitzky, D.J.3    Fuhrman, S.A.4    Patick, A.K.5    Ford, C.E.6    Meador 3rd, J.W.7    Worland, S.T.8
  • 30
    • 0033791657 scopus 로고    scopus 로고
    • In vitro evaluation of the disposition of A novel cysteine protease inhibitor
    • Jacobsen, W.; Christians, U.; Benet, L. Z. In vitro evaluation of the disposition of A novel cysteine protease inhibitor. Drug Metab. Dispos. 2000, 28, 1343-1351.
    • (2000) Drug Metab. Dispos , vol.28 , pp. 1343-1351
    • Jacobsen, W.1    Christians, U.2    Benet, L.Z.3
  • 31
    • 0343114370 scopus 로고    scopus 로고
    • AG-7088: Anti-rhinovirus drug, HRV 3C protease inhibitor
    • Graul, A.; Castaner, J. AG-7088: anti-rhinovirus drug, HRV 3C protease inhibitor. Drugs Future 2000, 25, 9-15.
    • (2000) Drugs Future , vol.25 , pp. 9-15
    • Graul, A.1    Castaner, J.2
  • 32
    • 13044300859 scopus 로고    scopus 로고
    • Matthews, D. A.; Dragovich, P. S.; Webber, S. E.; Fuhrman, S. A.; Patick, A. K.; Zalman, L. S.; Hendrickson, T. F.; Love, R. A.; Prins, T. J.; Marakovits, J. T.; Zhou, R.; Tikhe, J.; Ford, C. E.; Meador, J. W.; Ferre, R. A.; Brown, E. L.; Binford, S. L.; Brothers, M. A.; DeLisle, D. M.; Worland, S. T. Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes. Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 11000-11007.
    • Matthews, D. A.; Dragovich, P. S.; Webber, S. E.; Fuhrman, S. A.; Patick, A. K.; Zalman, L. S.; Hendrickson, T. F.; Love, R. A.; Prins, T. J.; Marakovits, J. T.; Zhou, R.; Tikhe, J.; Ford, C. E.; Meador, J. W.; Ferre, R. A.; Brown, E. L.; Binford, S. L.; Brothers, M. A.; DeLisle, D. M.; Worland, S. T. Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes. Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 11000-11007.
  • 33
    • 33751080094 scopus 로고    scopus 로고
    • Drug discovery and development for neglected parasitic diseases
    • Renslo, A. R.; McKerrow, J. H. Drug discovery and development for neglected parasitic diseases. Nat. Chem. Biol. 2006, 2, 701-710.
    • (2006) Nat. Chem. Biol , vol.2 , pp. 701-710
    • Renslo, A.R.1    McKerrow, J.H.2
  • 34
    • 2942521200 scopus 로고    scopus 로고
    • Two novel asparaginyl endopeptidase-like cysteine proteinases from the protist Trichomonas vaginalis: Their evolutionary relationship within the clan CD cysteine proteinases
    • Leon-Felix, J.; Ortega-Lopez, J.; Orozco-Solis, R.; Arroyo, R. Two novel asparaginyl endopeptidase-like cysteine proteinases from the protist Trichomonas vaginalis: their evolutionary relationship within the clan CD cysteine proteinases. Gene 2004, 335, 25-35.
    • (2004) Gene , vol.335 , pp. 25-35
    • Leon-Felix, J.1    Ortega-Lopez, J.2    Orozco-Solis, R.3    Arroyo, R.4
  • 36
    • 34547809297 scopus 로고
    • N-Aminoacyl-hydrazinoessigsaeure- derivate
    • Knobloch, W.; Niedrich, H. N-Aminoacyl-hydrazinoessigsaeure- derivate. J. Prakt. Chem. 1962, 4, 263-281.
    • (1962) J. Prakt. Chem , vol.4 , pp. 263-281
    • Knobloch, W.1    Niedrich, H.2
  • 37
    • 0014449860 scopus 로고
    • Hydrazine compounds as hetero constituents in peptides. XI. Synthesis of sustituted 2,4-bis-carboxymethyl-1-acyl-semicarbazide, the alpha-aza-asparagine peptides
    • Niedrich, H. Hydrazine compounds as hetero constituents in peptides. XI. Synthesis of sustituted 2,4-bis-carboxymethyl-1-acyl-semicarbazide, the alpha-aza-asparagine peptides. Chem. Ber. 1969, 102, 1557-1569.
    • (1969) Chem. Ber , vol.102 , pp. 1557-1569
    • Niedrich, H.1
  • 38
    • 33845283356 scopus 로고
    • Cyanide as an efficient and mild catalyst in the aminolysis of esters
    • Hogberg, T.; Strom, P.; Ebner, M.; Ramsby, S. Cyanide as an efficient and mild catalyst in the aminolysis of esters. J. Org. Chem. 1987, 2033-2036.
    • (1987) J. Org. Chem , pp. 2033-2036
    • Hogberg, T.1    Strom, P.2    Ebner, M.3    Ramsby, S.4
  • 40
    • 0037170771 scopus 로고    scopus 로고
    • Bivalent inhibition of beta-tryptase: Distance scan of neighboring subunits by dibasic inhibitors
    • Schaschke, N.; Dominik, A.; Matschiner, G.; Sommerhoff, C. P. Bivalent inhibition of beta-tryptase: distance scan of neighboring subunits by dibasic inhibitors. Bioorg. Med. Chem. Lett. 2002, 12, 985-988.
    • (2002) Bioorg. Med. Chem. Lett , vol.12 , pp. 985-988
    • Schaschke, N.1    Dominik, A.2    Matschiner, G.3    Sommerhoff, C.P.4
  • 41
    • 0026494941 scopus 로고
    • Cysteine protease inhibition by azapeptide esters
    • Magrath, J.; Abeles, R. H. Cysteine protease inhibition by azapeptide esters. J. Med. Chem. 1992, 35, 4279-4283.
    • (1992) J. Med. Chem , vol.35 , pp. 4279-4283
    • Magrath, J.1    Abeles, R.H.2
  • 42
    • 0021227695 scopus 로고
    • Reaction of azapeptides with human leukocyte elastase and porcine pancreatic elastase. New inhibitors and active site titrants
    • Powers, J. C.; Boone, R.; Carroll, D. L.; Gupton, B. F.; Kam, C. M.; Nishino, N.; Sakamoto, M.; Tuhy, P. M. Reaction of azapeptides with human leukocyte elastase and porcine pancreatic elastase. New inhibitors and active site titrants. J. Biol. Chem. 1984, 259, 4288-4294.
    • (1984) J. Biol. Chem , vol.259 , pp. 4288-4294
    • Powers, J.C.1    Boone, R.2    Carroll, D.L.3    Gupton, B.F.4    Kam, C.M.5    Nishino, N.6    Sakamoto, M.7    Tuhy, P.M.8
  • 43
    • 0017326665 scopus 로고
    • Reaction of serine proteases with aza-amino acid and aza-peptide derivatives
    • Powers, J. C.; Gupton, B. F. Reaction of serine proteases with aza-amino acid and aza-peptide derivatives. Methods Enzymol. 1977, 46, 208-216.
    • (1977) Methods Enzymol , vol.46 , pp. 208-216
    • Powers, J.C.1    Gupton, B.F.2
  • 44
    • 0021186126 scopus 로고
    • Reaction of azapeptides with chymotrypsin-like enzymes. New inhibitors and active site titrants for chymnotrypsin Aα, subtilisin BPN′, subtilisin carlsberg, and human leukocyte cathepsin G
    • Gupton, B. F.; Carroll, D. L.; Tuhy, P. M.; Kam, C.-M.; Powers, J. C. Reaction of azapeptides with chymotrypsin-like enzymes. New inhibitors and active site titrants for chymnotrypsin Aα, subtilisin BPN′, subtilisin carlsberg, and human leukocyte cathepsin G. J. Biol. Chem. 1984, 259, 4279-4287.
    • (1984) J. Biol. Chem , vol.259 , pp. 4279-4287
    • Gupton, B.F.1    Carroll, D.L.2    Tuhy, P.M.3    Kam, C.-M.4    Powers, J.C.5
  • 46
    • 0031008093 scopus 로고    scopus 로고
    • Titration and mapping of the active site of cysteine proteinases from Porphyromonas gingivalis (gingipains) using peptidyl chloromethanes
    • Potempa, J.; Pike, R.; Travis, J. Titration and mapping of the active site of cysteine proteinases from Porphyromonas gingivalis (gingipains) using peptidyl chloromethanes. Biol. Chem. 1997, 378, 223-230.
    • (1997) Biol. Chem , vol.378 , pp. 223-230
    • Potempa, J.1    Pike, R.2    Travis, J.3
  • 47
    • 0036882396 scopus 로고    scopus 로고
    • Irreversible inhibitors of serine, cysteine, and threonine proteases
    • Powers, J. C.; Asgian, J. L.; Ekici, O. D.; James, K. E. Irreversible inhibitors of serine, cysteine, and threonine proteases. Chem. Rev. 2002, 102, 4639-4750.
    • (2002) Chem. Rev , vol.102 , pp. 4639-4750
    • Powers, J.C.1    Asgian, J.L.2    Ekici, O.D.3    James, K.E.4
  • 48
    • 1542328053 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of aza-peptide epoxides as selective and potent inhibitors of caspases-1, -3, -6, and -8
    • James, K. E.; Asgian, J. L.; Li, Z. Z.; Ekici, O. D.; Rubin, J. R.; Mikolajczyk, J.; Salvesen, G. S.; Powers, J. C. Design, synthesis, and evaluation of aza-peptide epoxides as selective and potent inhibitors of caspases-1, -3, -6, and -8. J. Med. Chem. 2004, 47, 1553-1574.
    • (2004) J. Med. Chem , vol.47 , pp. 1553-1574
    • James, K.E.1    Asgian, J.L.2    Li, Z.Z.3    Ekici, O.D.4    Rubin, J.R.5    Mikolajczyk, J.6    Salvesen, G.S.7    Powers, J.C.8
  • 49
    • 33746646754 scopus 로고    scopus 로고
    • Exploring the S4 and S1 prime subsite specificities in caspase-3 with aza-peptide epoxide inhibitors
    • Ganesan, R.; Jelakovic, S.; Campbell, A. J.; Li, Z. Z.; Asgian, J. L.; Powers, J. C.; Grutter, M. G. Exploring the S4 and S1 prime subsite specificities in caspase-3 with aza-peptide epoxide inhibitors. Biochemistry 2006, 45, 9059-9067.
    • (2006) Biochemistry , vol.45 , pp. 9059-9067
    • Ganesan, R.1    Jelakovic, S.2    Campbell, A.J.3    Li, Z.Z.4    Asgian, J.L.5    Powers, J.C.6    Grutter, M.G.7
  • 50
    • 0033200047 scopus 로고    scopus 로고
    • Comparing the potency of chemicals with multiple modes of action in aquatic toxicology: Acute toxicity due to narcosis versus reactive toxicity of acrylic compounds
    • Freidig, A. P.; Verhaar, H. J. M.; Hermens, J. L. M. Comparing the potency of chemicals with multiple modes of action in aquatic toxicology: acute toxicity due to narcosis versus reactive toxicity of acrylic compounds. Environ. Sci. Technol. 1999, 33, 3038-3043.
    • (1999) Environ. Sci. Technol , vol.33 , pp. 3038-3043
    • Freidig, A.P.1    Verhaar, H.J.M.2    Hermens, J.L.M.3
  • 53
    • 0033963651 scopus 로고    scopus 로고
    • Identification of a cDNA encoding an active asparaginyl endopeptidase of Schistosoma mansoni and its expression in Pichia pastoris
    • Caffrey, C. R.; Mathieu, M. A.; Gaffney, A. M.; Salter, J. P.; Sajid, M.; Lucas, K. D.; Franklin, C.; Bogyo, M.; McKerrow, J. H. Identification of a cDNA encoding an active asparaginyl endopeptidase of Schistosoma mansoni and its expression in Pichia pastoris. FEBS Lett. 2000, 466, 244-248.
    • (2000) FEBS Lett , vol.466 , pp. 244-248
    • Caffrey, C.R.1    Mathieu, M.A.2    Gaffney, A.M.3    Salter, J.P.4    Sajid, M.5    Lucas, K.D.6    Franklin, C.7    Bogyo, M.8    McKerrow, J.H.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.