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Volumn 587, Issue 21, 2013, Pages 3422-3427

Triose phosphate isomerase from the blood fluke Schistosoma mansoni: Biochemical characterisation of a potential drug and vaccine target

Author keywords

Bilharzia; Blood fluke; Glycolytic enzyme; Schistosomiasis; Vaccine target

Indexed keywords

DIHYDROXYACETONE PHOSPHATE; DIMER; EPITOPE; GLYCERALDEHYDE 3 PHOSPHATE; TRIOSEPHOSPHATE ISOMERASE;

EID: 84886242037     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.09.022     Document Type: Article
Times cited : (18)

References (67)
  • 2
    • 84865864418 scopus 로고    scopus 로고
    • The promise and pitfalls of mass drug administration to control intestinal helminth infections
    • D. Humphries, S. Nguyen, D. Boakye, M. Wilson, and M. Cappello The promise and pitfalls of mass drug administration to control intestinal helminth infections Curr. Opin. Infect. Dis. 25 2012 584 589
    • (2012) Curr. Opin. Infect. Dis. , vol.25 , pp. 584-589
    • Humphries, D.1    Nguyen, S.2    Boakye, D.3    Wilson, M.4    Cappello, M.5
  • 3
    • 84868122341 scopus 로고    scopus 로고
    • Susceptibility or resistance of praziquantel in human schistosomiasis: A review
    • W. Wang, L. Wang, and Y.S. Liang Susceptibility or resistance of praziquantel in human schistosomiasis: a review Parasitol. Res. 111 2012 1871 1877
    • (2012) Parasitol. Res. , vol.111 , pp. 1871-1877
    • Wang, W.1    Wang, L.2    Liang, Y.S.3
  • 4
    • 0028025029 scopus 로고
    • Drug-resistant schistosomiasis: Resistance to praziquantel and oxamniquine induced in Schistosoma mansoni in mice is drug specific
    • P.G. Fallon, and M.J. Doenhoff Drug-resistant schistosomiasis: resistance to praziquantel and oxamniquine induced in Schistosoma mansoni in mice is drug specific Am. J. Trop. Med. Hyg. 51 1994 83 88
    • (1994) Am. J. Trop. Med. Hyg. , vol.51 , pp. 83-88
    • Fallon, P.G.1    Doenhoff, M.J.2
  • 5
    • 33644915024 scopus 로고    scopus 로고
    • Ancient genes in contemporary persistent microbial pathogens
    • V. Srinivasan, and H.J. Morowitz Ancient genes in contemporary persistent microbial pathogens Biol. Bull. 210 2006 1 9
    • (2006) Biol. Bull. , vol.210 , pp. 1-9
    • Srinivasan, V.1    Morowitz, H.J.2
  • 6
    • 72149120003 scopus 로고    scopus 로고
    • Triosephosphate isomerase deficiency: New insights into an enigmatic disease
    • F. Orosz, J. Olah, and J. Ovadi Triosephosphate isomerase deficiency: new insights into an enigmatic disease Biochim. Biophys. Acta 1792 2009 1168 1174
    • (2009) Biochim. Biophys. Acta , vol.1792 , pp. 1168-1174
    • Orosz, F.1    Olah, J.2    Ovadi, J.3
  • 7
    • 34250165399 scopus 로고    scopus 로고
    • Triosephosphate isomerase deficiency: Facts and doubts
    • F. Orosz, J. Olah, and J. Ovadi Triosephosphate isomerase deficiency: facts and doubts IUBMB Life 58 2006 703 715
    • (2006) IUBMB Life , vol.58 , pp. 703-715
    • Orosz, F.1    Olah, J.2    Ovadi, J.3
  • 8
    • 0022996859 scopus 로고
    • Human triose-phosphate isomerase deficiency: A single amino acid substitution results in a thermolabile enzyme
    • I.O. Daar, P.J. Artymiuk, D.C. Phillips, and L.E. Maquat Human triose-phosphate isomerase deficiency: a single amino acid substitution results in a thermolabile enzyme Proc. Natl. Acad. Sci. USA 83 1986 7903 7907
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 7903-7907
    • Daar, I.O.1    Artymiuk, P.J.2    Phillips, D.C.3    Maquat, L.E.4
  • 9
    • 49849101871 scopus 로고    scopus 로고
    • Degradation of functional triose phosphate isomerase protein underlies sugarkill pathology
    • J.L. Seigle, A.M. Celotto, and M.J. Palladino Degradation of functional triose phosphate isomerase protein underlies sugarkill pathology Genetics 179 2008 855 862
    • (2008) Genetics , vol.179 , pp. 855-862
    • Seigle, J.L.1    Celotto, A.M.2    Palladino, M.J.3
  • 10
    • 55149086824 scopus 로고    scopus 로고
    • Triose phosphate isomerase deficiency is caused by altered dimerization - Not catalytic inactivity - Of the mutant enzymes
    • M. Ralser, G. Heeren, M. Breitenbach, H. Lehrach, and S. Krobitsch Triose phosphate isomerase deficiency is caused by altered dimerization - not catalytic inactivity - of the mutant enzymes PLoS ONE 1 2006 e30
    • (2006) PLoS ONE , vol.1 , pp. 30
    • Ralser, M.1    Heeren, G.2    Breitenbach, M.3    Lehrach, H.4    Krobitsch, S.5
  • 11
    • 29644434568 scopus 로고    scopus 로고
    • Triosephosphate isomerase deficiency: Consequences of an inherited mutation at mRNA, protein and metabolic levels
    • J. Olah, F. Orosz, L.G. Puskas, L. Hackler Jr, M. Horanyi, L. Polgar, S. Hollan, and J. Ovadi Triosephosphate isomerase deficiency: consequences of an inherited mutation at mRNA, protein and metabolic levels Biochem. J. 392 2005 675 683
    • (2005) Biochem. J. , vol.392 , pp. 675-683
    • Olah, J.1    Orosz, F.2    Puskas, L.G.3    Hackler, Jr.L.4    Horanyi, M.5    Polgar, L.6    Hollan, S.7    Ovadi, J.8
  • 12
    • 84876300285 scopus 로고    scopus 로고
    • Early mitochondrial dysfunction leads to altered redox chemistry underlying pathogenesis of TPI deficiency
    • S.L. Hrizo, I.J. Fisher, D.R. Long, J.A. Hutton, Z. Liu, and M.J. Palladino Early mitochondrial dysfunction leads to altered redox chemistry underlying pathogenesis of TPI deficiency Neurobiol. Dis. 54 2013 289 296
    • (2013) Neurobiol. Dis. , vol.54 , pp. 289-296
    • Hrizo, S.L.1    Fisher, I.J.2    Long, D.R.3    Hutton, J.A.4    Liu, Z.5    Palladino, M.J.6
  • 13
    • 3242703231 scopus 로고    scopus 로고
    • The strong inhibition of triosephosphate isomerase by the natural beta-carbolines may explain their neurotoxic actions
    • R. Bonnet, S. Pavlovic, J. Lehmann, and H. Rommelspacher The strong inhibition of triosephosphate isomerase by the natural beta-carbolines may explain their neurotoxic actions Neuroscience 127 2004 443 453
    • (2004) Neuroscience , vol.127 , pp. 443-453
    • Bonnet, R.1    Pavlovic, S.2    Lehmann, J.3    Rommelspacher, H.4
  • 14
    • 0026599022 scopus 로고
    • CDNA cloning and functional expression of the Schistosoma mansoni protective antigen triose-phosphate isomerase
    • C. Shoemaker, A. Gross, A. Gebremichael, and D. Harn CDNA cloning and functional expression of the Schistosoma mansoni protective antigen triose-phosphate isomerase Proc. Natl. Acad. Sci. USA 89 1992 1842 1846
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1842-1846
    • Shoemaker, C.1    Gross, A.2    Gebremichael, A.3    Harn, D.4
  • 15
    • 0026531647 scopus 로고
    • A protective monoclonal antibody specifically recognizes and alters the catalytic activity of schistosome triose-phosphate isomerase
    • D.A. Harn, W. Gu, L.D. Oligino, M. Mitsuyama, A. Gebremichael, and D. Richter A protective monoclonal antibody specifically recognizes and alters the catalytic activity of schistosome triose-phosphate isomerase J. Immunol. 148 1992 562 567
    • (1992) J. Immunol. , vol.148 , pp. 562-567
    • Harn, D.A.1    Gu, W.2    Oligino, L.D.3    Mitsuyama, M.4    Gebremichael, A.5    Richter, D.6
  • 16
    • 0026098182 scopus 로고
    • The functional and immunological significance of some schistosome surface molecules
    • M.D. Wright, K.M. Davern, and G.F. Mitchell The functional and immunological significance of some schistosome surface molecules Parasitol. Today 7 1991 56 58
    • (1991) Parasitol. Today , vol.7 , pp. 56-58
    • Wright, M.D.1    Davern, K.M.2    Mitchell, G.F.3
  • 17
    • 80052309674 scopus 로고    scopus 로고
    • The adaptive evolution divergence of triosephosphate isomerases between parasitic and free-living flatworms and the discovery of a potential universal target against flatworm parasites
    • B. Chen, and J.F. Wen The adaptive evolution divergence of triosephosphate isomerases between parasitic and free-living flatworms and the discovery of a potential universal target against flatworm parasites Parasitol. Res. 109 2011 283 289
    • (2011) Parasitol. Res. , vol.109 , pp. 283-289
    • Chen, B.1    Wen, J.F.2
  • 19
    • 84864995354 scopus 로고    scopus 로고
    • Proteomics at the schistosome-mammalian host interface: Any prospects for diagnostics or vaccines?
    • R.A. Wilson Proteomics at the schistosome-mammalian host interface: any prospects for diagnostics or vaccines? Parasitology 139 2012 1178 1194
    • (2012) Parasitology , vol.139 , pp. 1178-1194
    • Wilson, R.A.1
  • 20
    • 33644674090 scopus 로고    scopus 로고
    • The tegument surface membranes of the human blood parasite Schistosoma mansoni: A proteomic analysis after differential extraction
    • S. Braschi, R.S. Curwen, P.D. Ashton, S. Verjovski-Almeida, and A. Wilson The tegument surface membranes of the human blood parasite Schistosoma mansoni: a proteomic analysis after differential extraction Proteomics 6 2006 1471 1482
    • (2006) Proteomics , vol.6 , pp. 1471-1482
    • Braschi, S.1    Curwen, R.S.2    Ashton, P.D.3    Verjovski-Almeida, S.4    Wilson, A.5
  • 21
    • 82655177934 scopus 로고    scopus 로고
    • Molecular determinants of the interaction between human high molecular weight kininogen and Candida albicans cell wall: Identification of kininogen-binding proteins on fungal cell wall and mapping the cell wall-binding regions on kininogen molecule
    • J. Karkowska-Kuleta, S. Kedracka-Krok, M. Rapala-Kozik, W. Kamysz, S. Bielinska, A. Karafova, and A. Kozik Molecular determinants of the interaction between human high molecular weight kininogen and Candida albicans cell wall: identification of kininogen-binding proteins on fungal cell wall and mapping the cell wall-binding regions on kininogen molecule Peptides 32 2011 2488 2496
    • (2011) Peptides , vol.32 , pp. 2488-2496
    • Karkowska-Kuleta, J.1    Kedracka-Krok, S.2    Rapala-Kozik, M.3    Kamysz, W.4    Bielinska, S.5    Karafova, A.6    Kozik, A.7
  • 22
    • 84855209384 scopus 로고    scopus 로고
    • Interaction of triosephosphate isomerase from Staphylococcus aureus with plasminogen
    • H. Furuya, and R. Ikeda Interaction of triosephosphate isomerase from Staphylococcus aureus with plasminogen Microbiol. Immunol. 55 2011 855 862
    • (2011) Microbiol. Immunol. , vol.55 , pp. 855-862
    • Furuya, H.1    Ikeda, R.2
  • 23
    • 69949148010 scopus 로고    scopus 로고
    • Interaction of triosephosphate isomerase from the cell surface of Staphylococcus aureus and α-(1 → 3)-mannooligosaccharides derived from glucuronoxylomannan of Cryptococcus neoformans
    • H. Furuya, and R. Ikeda Interaction of triosephosphate isomerase from the cell surface of Staphylococcus aureus and α-(1 → 3)-mannooligosaccharides derived from glucuronoxylomannan of Cryptococcus neoformans Microbiology 155 2009 2707 2713
    • (2009) Microbiology , vol.155 , pp. 2707-2713
    • Furuya, H.1    Ikeda, R.2
  • 25
    • 77954958354 scopus 로고    scopus 로고
    • Synergistic enhancement of immunogenicity and protection in mice against Schistosoma japonicum with codon optimization and electroporation delivery of SjTPI DNA vaccines
    • Y. Zhu, F. Lu, Y. Dai, X. Wang, J. Tang, S. Zhao, C. Zhang, H. Zhang, S. Lu, and S. Wang Synergistic enhancement of immunogenicity and protection in mice against Schistosoma japonicum with codon optimization and electroporation delivery of SjTPI DNA vaccines Vaccine 28 2010 5347 5355
    • (2010) Vaccine , vol.28 , pp. 5347-5355
    • Zhu, Y.1    Lu, F.2    Dai, Y.3    Wang, X.4    Tang, J.5    Zhao, S.6    Zhang, C.7    Zhang, H.8    Lu, S.9    Wang, S.10
  • 26
    • 73449112633 scopus 로고    scopus 로고
    • DNA vaccination by electroporation and boosting with recombinant proteins enhances the efficacy of DNA vaccines for Schistosomiasis japonica
    • Y. Dai, Y. Zhu, D.A. Harn, X. Wang, J. Tang, S. Zhao, F. Lu, and X. Guan DNA vaccination by electroporation and boosting with recombinant proteins enhances the efficacy of DNA vaccines for Schistosomiasis japonica Clin. Vaccine Immunol. 16 2009 1796 1803
    • (2009) Clin. Vaccine Immunol. , vol.16 , pp. 1796-1803
    • Dai, Y.1    Zhu, Y.2    Harn, D.A.3    Wang, X.4    Tang, J.5    Zhao, S.6    Lu, F.7    Guan, X.8
  • 28
    • 30144445625 scopus 로고    scopus 로고
    • Schistosoma japonicum triose-phosphate isomerase plasmid DNA vaccine protects pigs against challenge infection
    • Y. Zhu, J. Si, D.A. Harn, M. Xu, J. Ren, C. Yu, Y. Liang, X. Yin, W. He, and G. Cao Schistosoma japonicum triose-phosphate isomerase plasmid DNA vaccine protects pigs against challenge infection Parasitology 132 2006 67 71
    • (2006) Parasitology , vol.132 , pp. 67-71
    • Zhu, Y.1    Si, J.2    Harn, D.A.3    Xu, M.4    Ren, J.5    Yu, C.6    Liang, Y.7    Yin, X.8    He, W.9    Cao, G.10
  • 29
    • 8444239770 scopus 로고    scopus 로고
    • The protective immunity of a DNA vaccine encoding Schistosoma japonicum Chinese strain triose-phosphate isomerase in infected BALB/C mice
    • Y. Zhu, J. Si, D.A. Harn, C. Yu, Y. Liang, J. Ren, X. Yin, W. He, and W. Hua The protective immunity of a DNA vaccine encoding Schistosoma japonicum Chinese strain triose-phosphate isomerase in infected BALB/C mice Southeast Asian J. Trop. Med. Public Health 35 2004 518 522
    • (2004) Southeast Asian J. Trop. Med. Public Health , vol.35 , pp. 518-522
    • Zhu, Y.1    Si, J.2    Harn, D.A.3    Yu, C.4    Liang, Y.5    Ren, J.6    Yin, X.7    He, W.8    Hua, W.9
  • 30
    • 0036596660 scopus 로고    scopus 로고
    • The protective immunity produced in infected C57BL/6 mice of a DNA vaccine encoding Schistosoma japonicum Chinese strain triose-phosphate isomerase
    • Y. Zhu, J. Si, D.A. Ham, C. Yu, W. He, W. Hua, X. Yin, Y. Liang, M. Xu, and R. Xu The protective immunity produced in infected C57BL/6 mice of a DNA vaccine encoding Schistosoma japonicum Chinese strain triose-phosphate isomerase Southeast Asian J. Trop. Med. Public Health 33 2002 207 213
    • (2002) Southeast Asian J. Trop. Med. Public Health , vol.33 , pp. 207-213
    • Zhu, Y.1    Si, J.2    Ham, D.A.3    Yu, C.4    He, W.5    Hua, W.6    Yin, X.7    Liang, Y.8    Xu, M.9    Xu, R.10
  • 31
    • 84879482998 scopus 로고    scopus 로고
    • Characterization of a monoclonal antibody that specifically inhibits triosephosphate isomerase activity of Taenia solium
    • S.A. Victor, M.F. Yolanda, Z.C. Araceli, J. Lucia, and L. Abraham Characterization of a monoclonal antibody that specifically inhibits triosephosphate isomerase activity of Taenia solium Exp. Parasitol. 134 2013 495 503
    • (2013) Exp. Parasitol. , vol.134 , pp. 495-503
    • Victor, S.A.1    Yolanda, M.F.2    Araceli, Z.C.3    Lucia, J.4    Abraham, L.5
  • 32
    • 84867800354 scopus 로고    scopus 로고
    • Inhibition of Enzyme Activity of Rhipicephalus (Boophilus) microplus triosephosphate isomerase and BME26 cell growth by monoclonal antibodies
    • L. Saramago, M. Franceschi, C. Logullo, A. Masuda, S. Vaz Ida, S.E. Farias, and J. Moraes Inhibition of Enzyme Activity of Rhipicephalus (Boophilus) microplus triosephosphate isomerase and BME26 cell growth by monoclonal antibodies Int. J. Mol. Sci. 13 2012 13118 13133
    • (2012) Int. J. Mol. Sci. , vol.13 , pp. 13118-13133
    • Saramago, L.1    Franceschi, M.2    Logullo, C.3    Masuda, A.4    Vaz Ida, S.5    Farias, S.E.6    Moraes, J.7
  • 35
    • 79952199366 scopus 로고    scopus 로고
    • Purification of proteins fused to glutathione S-transferase
    • S. Harper, and D.W. Speicher Purification of proteins fused to glutathione S-transferase Methods Mol. Biol. 681 2011 259 280
    • (2011) Methods Mol. Biol. , vol.681 , pp. 259-280
    • Harper, S.1    Speicher, D.W.2
  • 38
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the web: A case study using the Phyre server
    • L.A. Kelley, and M.J. Sternberg Protein structure prediction on the web: a case study using the Phyre server Nat. Protoc. 4 2009 363 371
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 40
    • 74249090260 scopus 로고    scopus 로고
    • Improving physical realism, stereochemistry, and side-chain accuracy in homology modeling: Four approaches that performed well in CASP8
    • E. Krieger, K. Joo, J. Lee, J. Lee, S. Raman, J. Thompson, M. Tyka, D. Baker, and K. Karplus Improving physical realism, stereochemistry, and side-chain accuracy in homology modeling: four approaches that performed well in CASP8 Proteins 77 Suppl. 9 2009 114 122
    • (2009) Proteins , vol.77 , Issue.SUPPL. 9 , pp. 114-122
    • Krieger, E.1    Joo, K.2    Lee, J.3    Lee, J.4    Raman, S.5    Thompson, J.6    Tyka, M.7    Baker, D.8    Karplus, K.9
  • 41
    • 0021014195 scopus 로고
    • Cross-linking of protein by ω-maleimido alkanoyl N-hydroxysuccinimido esters
    • M.D. Partis, D.G. Griffiths, G.C. Roberts, and R.D. Beechey Cross-linking of protein by ω-maleimido alkanoyl N-hydroxysuccinimido esters J. Protein Chem. 2 1983 263 277
    • (1983) J. Protein Chem. , vol.2 , pp. 263-277
    • Partis, M.D.1    Griffiths, D.G.2    Roberts, G.C.3    Beechey, R.D.4
  • 42
    • 84885077811 scopus 로고    scopus 로고
    • Triose phosphate isomerase from the liver fluke Fasciola hepatica
    • 10.1016/j.biochi.2013.08.014 in press
    • V.L. Zinsser, E.M. Hoey, A. Trudgett, and D.J. Timson Triose phosphate isomerase from the liver fluke Fasciola hepatica Biochimie 2013 10.1016/j.biochi.2013.08.014 in press
    • (2013) Biochimie
    • Zinsser, V.L.1    Hoey, E.M.2    Trudgett, A.3    Timson, D.J.4
  • 43
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • U.B. Ericsson, B.M. Hallberg, G.T. Detitta, N. Dekker, and P. Nordlund Thermofluor-based high-throughput stability optimization of proteins for structural studies Anal. Biochem. 357 2006 289 298
    • (2006) Anal. Biochem. , vol.357 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    Detitta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 44
    • 0015305282 scopus 로고
    • Tris/tris-HCl: A standard buffer for use in the physiologic pH range
    • R.A. Durst, and B.R. Staples Tris/tris-HCl: a standard buffer for use in the physiologic pH range Clin. Chem. 18 1972 206 208
    • (1972) Clin. Chem. , vol.18 , pp. 206-208
    • Durst, R.A.1    Staples, B.R.2
  • 45
    • 0015394088 scopus 로고
    • PH-dependence of the triose phosphate isomerase reaction
    • B. Plaut, and J.R. Knowles PH-dependence of the triose phosphate isomerase reaction Biochem. J. 129 1972 311 320
    • (1972) Biochem. J. , vol.129 , pp. 311-320
    • Plaut, B.1    Knowles, J.R.2
  • 46
    • 0023428359 scopus 로고
    • Kinetic properties of triose-phosphate isomerase from Trypanosoma brucei brucei. A comparison with the rabbit muscle and yeast enzymes
    • A.M. Lambeir, F.R. Opperdoes, and R.K. Wierenga Kinetic properties of triose-phosphate isomerase from Trypanosoma brucei brucei. A comparison with the rabbit muscle and yeast enzymes Eur. J. Biochem. 168 1987 69 74
    • (1987) Eur. J. Biochem. , vol.168 , pp. 69-74
    • Lambeir, A.M.1    Opperdoes, F.R.2    Wierenga, R.K.3
  • 49
    • 40849092636 scopus 로고    scopus 로고
    • Key residues of loop 3 in the interaction with the interface residue at position 14 in triosephosphate isomerase from Trypanosoma brucei
    • N. Cabrera, G. Hernandez-Alcantara, G. Mendoza-Hernandez, A. Gomez-Puyou, and R. Perez-Montfort Key residues of loop 3 in the interaction with the interface residue at position 14 in triosephosphate isomerase from Trypanosoma brucei Biochemistry 47 2008 3499 3506
    • (2008) Biochemistry , vol.47 , pp. 3499-3506
    • Cabrera, N.1    Hernandez-Alcantara, G.2    Mendoza-Hernandez, G.3    Gomez-Puyou, A.4    Perez-Montfort, R.5
  • 52
    • 0037067778 scopus 로고    scopus 로고
    • Inhibition of Plasmodium falciparum triose-phosphate isomerase by chemical modification of an interface cysteine. Electrospray ionization mass spectrometric analysis of differential cysteine reactivities
    • K. Maithal, G. Ravindra, H. Balaram, and P. Balaram Inhibition of Plasmodium falciparum triose-phosphate isomerase by chemical modification of an interface cysteine. Electrospray ionization mass spectrometric analysis of differential cysteine reactivities J. Biol. Chem. 277 2002 25106 25114
    • (2002) J. Biol. Chem. , vol.277 , pp. 25106-25114
    • Maithal, K.1    Ravindra, G.2    Balaram, H.3    Balaram, P.4
  • 53
    • 0032079362 scopus 로고    scopus 로고
    • Sulfhydryl reagent susceptibility in proteins with high sequence similarity - Triosephosphate isomerase from Trypanosoma brucei, Trypanosoma cruzi and Leishmania mexicana
    • G. Garza-Ramos, N. Cabrera, E. Saavedra-Lira, M. Tuena de Gomez-Puyou, P. Ostoa-Saloma, R. Perez-Montfort, and A. Gomez-Puyou Sulfhydryl reagent susceptibility in proteins with high sequence similarity - triosephosphate isomerase from Trypanosoma brucei, Trypanosoma cruzi and Leishmania mexicana Eur. J. Biochem. 253 1998 684 691
    • (1998) Eur. J. Biochem. , vol.253 , pp. 684-691
    • Garza-Ramos, G.1    Cabrera, N.2    Saavedra-Lira, E.3    Tuena De Gomez-Puyou, M.4    Ostoa-Saloma, P.5    Perez-Montfort, R.6    Gomez-Puyou, A.7
  • 57
    • 84864189088 scopus 로고    scopus 로고
    • Altered cofactor binding affects stability and activity of human UDP-galactose 4′-epimerase: Implications for type III galactosemia
    • T.J. McCorvie, Y. Liu, A. Frazer, T.J. Gleason, J.L. Fridovich-Keil, and D.J. Timson Altered cofactor binding affects stability and activity of human UDP-galactose 4′-epimerase: implications for type III galactosemia Biochim. Biophys. Acta 1822 2012 1516 1526
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 1516-1526
    • McCorvie, T.J.1    Liu, Y.2    Frazer, A.3    Gleason, T.J.4    Fridovich-Keil, J.L.5    Timson, D.J.6
  • 58
    • 84877322610 scopus 로고    scopus 로고
    • Misfolding of galactose 1-phosphate uridylyltransferase can result in type i galactosemia
    • T.J. McCorvie, T.J. Gleason, J.L. Fridovich-Keil, and D.J. Timson Misfolding of galactose 1-phosphate uridylyltransferase can result in type I galactosemia Biochim. Biophys. Acta 1832 2013 1279 1293
    • (2013) Biochim. Biophys. Acta , vol.1832 , pp. 1279-1293
    • McCorvie, T.J.1    Gleason, T.J.2    Fridovich-Keil, J.L.3    Timson, D.J.4
  • 59
    • 0033200357 scopus 로고    scopus 로고
    • Unusual stability of a multiply nicked form of Plasmodium falciparum triosephosphate isomerase
    • S.S. Ray, H. Balaram, and P. Balaram Unusual stability of a multiply nicked form of Plasmodium falciparum triosephosphate isomerase Chem. Biol. 6 1999 625 637
    • (1999) Chem. Biol. , vol.6 , pp. 625-637
    • Ray, S.S.1    Balaram, H.2    Balaram, P.3
  • 62
    • 0032929094 scopus 로고    scopus 로고
    • Structural and mutagenesis studies of Leishmania triosephosphate isomerase: A point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power
    • J.C. Williams, J.P. Zeelen, G. Neubauer, G. Vriend, J. Backmann, P.A. Michels, A.M. Lambeir, and R.K. Wierenga Structural and mutagenesis studies of Leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power Protein Eng. 12 1999 243 250
    • (1999) Protein Eng. , vol.12 , pp. 243-250
    • Williams, J.C.1    Zeelen, J.P.2    Neubauer, G.3    Vriend, G.4    Backmann, J.5    Michels, P.A.6    Lambeir, A.M.7    Wierenga, R.K.8
  • 63
    • 0033486165 scopus 로고    scopus 로고
    • Bacterial expression and characterization of functional recombinant triosephosphate isomerase from Schistosoma japonicum
    • W. Sun, S. Liu, P.J. Brindley, and D.P. McManus Bacterial expression and characterization of functional recombinant triosephosphate isomerase from Schistosoma japonicum Protein Expr. Purif. 17 1999 410 413
    • (1999) Protein Expr. Purif. , vol.17 , pp. 410-413
    • Sun, W.1    Liu, S.2    Brindley, P.J.3    McManus, D.P.4
  • 64
    • 0018232574 scopus 로고
    • Purification, crystallization and properties of triosephosphate isomerase from human skeletal muscle
    • A. Dabrowska, I. Kamrowska, and T. Baranowski Purification, crystallization and properties of triosephosphate isomerase from human skeletal muscle Acta Biochim. Pol. 25 1978 247 256
    • (1978) Acta Biochim. Pol. , vol.25 , pp. 247-256
    • Dabrowska, A.1    Kamrowska, I.2    Baranowski, T.3
  • 65
    • 0035854727 scopus 로고    scopus 로고
    • Synthetic peptides as inactivators of multimeric enzymes: Inhibition of Plasmodium falciparum triosephosphate isomerase by interface peptides
    • S.K. Singh, K. Maithal, H. Balaram, and P. Balaram Synthetic peptides as inactivators of multimeric enzymes: inhibition of Plasmodium falciparum triosephosphate isomerase by interface peptides FEBS Lett. 501 2001 19 23
    • (2001) FEBS Lett. , vol.501 , pp. 19-23
    • Singh, S.K.1    Maithal, K.2    Balaram, H.3    Balaram, P.4


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