메뉴 건너뛰기




Volumn 10, Issue 7, 2011, Pages 985-997

Characterization, localization, essentiality, and high-resolution crystal structure of glucosamine 6-phosphate N-acetyltransferase from Trypanosoma brucei

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSAMINE PHOSPHATE ACETYLTRANSFERASE; POLY N ACETYLLACTOSAMINE; POLY-N-ACETYLLACTOSAMINE; POLYSACCHARIDE; PROTOZOAL PROTEIN; RECOMBINANT PROTEIN; VARIANT SURFACE GLYCOPROTEIN;

EID: 79960126726     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.05025-11     Document Type: Article
Times cited : (29)

References (57)
  • 1
    • 0037101948 scopus 로고    scopus 로고
    • Developmentally regulated trafficking of the lysosomal membrane protein p67 in Trypanosoma brucei
    • Alexander, D. L., K. J. Schwartz, A. E. Balber, and J. D. Bangs. 2002. Developmentally regulated trafficking of the lysosomal membrane protein p67 in Trypanosoma brucei. J. Cell Sci. 115:3253-3263.
    • (2002) J. Cell Sci. , vol.115 , pp. 3253-3263
    • Alexander, D.L.1    Schwartz, K.J.2    Balber, A.E.3    Bangs, J.D.4
  • 2
    • 33745256005 scopus 로고    scopus 로고
    • Approximate likelihood ratio test for branchs: A fast, accurate and powerful alternative
    • Anisimova, M., and O. Gascuel. 2006. Approximate likelihood ratio test for branchs: a fast, accurate and powerful alternative. Syst. Biol. 55:539-552.
    • (2006) Syst. Biol. , vol.55 , pp. 539-552
    • Anisimova, M.1    Gascuel, O.2
  • 3
    • 12544251963 scopus 로고    scopus 로고
    • Trypanosoma brucei glycoproteins contain novel giant poly-N-acetyllactosamine carbohydrate chains
    • Atrih, A., J. M. Richardson, A. R. Prescott, and M. A. Ferguson. 2005. Trypanosoma brucei glycoproteins contain novel giant poly-N-acetyllactosamine carbohydrate chains. J. Biol. Chem. 280:865-871.
    • (2005) J. Biol. Chem. , vol.280 , pp. 865-871
    • Atrih, A.1    Richardson, J.M.2    Prescott, A.R.3    Ferguson, M.A.4
  • 4
    • 10744222557 scopus 로고    scopus 로고
    • Interaction of substituted hexose analogues with the Trypanosoma brucei hexose transporter
    • Azema, L., et al. 2004. Interaction of substituted hexose analogues with the Trypanosoma brucei hexose transporter. Biochem. Pharmacol. 67:459-467.
    • (2004) Biochem. Pharmacol. , vol.67 , pp. 459-467
    • Azema, L.1
  • 5
    • 0034724727 scopus 로고    scopus 로고
    • Cloning and characterization of the murine glucosamine-6-phosphate acetyltransferase EMeg32. Differential expression and intracellular membrane association
    • Boehmelt, G., et al. 2000. Cloning and characterization of the murine glucosamine-6-phosphate acetyltransferase EMeg32. Differential expression and intracellular membrane association. J. Biol. Chem. 275:12821-12832.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12821-12832
    • Boehmelt, G.1
  • 6
    • 33745060757 scopus 로고    scopus 로고
    • Comparative proteomics of glycosomes from bloodstream form and procyclic culture form Trypanosoma brucei brucei
    • Colasante, C., M. Ellis, T. Ruppert, and F. Voncken. 2006. Comparative proteomics of glycosomes from bloodstream form and procyclic culture form Trypanosoma brucei brucei. Proteomics 6:3275-3293.
    • (2006) Proteomics , vol.6 , pp. 3275-3293
    • Colasante, C.1    Ellis, M.2    Ruppert, T.3    Voncken, F.4
  • 7
    • 0030131182 scopus 로고    scopus 로고
    • Antigenic variation in trypanosomes: Secrets surface slowly
    • Cross, G. A. 1996. Antigenic variation in trypanosomes: secrets surface slowly. Bioessays 18:283-291.
    • (1996) Bioessays , vol.18 , pp. 283-291
    • Cross, G.A.1
  • 8
    • 74049128731 scopus 로고    scopus 로고
    • Leishmania UDP-sugar pyrophosphorylase
    • Damerow, S., et al. 2010. Leishmania UDP-sugar pyrophosphorylase. J. Biol. Chem. 285:878-887.
    • (2010) J. Biol. Chem. , vol.285 , pp. 878-887
    • Damerow, S.1
  • 9
    • 1842425027 scopus 로고    scopus 로고
    • Properties of GDP-mannose pyrophosphorylase, a critical enzyme and drug target in Leishmania mexicana
    • Davis, A. J., et al. 2004. Properties of GDP-mannose pyrophosphorylase, a critical enzyme and drug target in Leishmania mexicana. J. Biol. Chem. 279:12462-12468.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12462-12468
    • Davis, A.J.1
  • 10
    • 74349118194 scopus 로고    scopus 로고
    • GDP-mannose pyrophosphorylase is essential in the bloodstream form of Trypanosoma brucei
    • Denton, H., S. Fyffe, and T. K. Smith. 2010. GDP-mannose pyrophosphorylase is essential in the bloodstream form of Trypanosoma brucei. Biochem. J. 425:603-614.
    • (2010) Biochem. J. , vol.425 , pp. 603-614
    • Denton, H.1    Fyffe, S.2    Smith, T.K.3
  • 11
    • 0024360658 scopus 로고
    • Biosynthesis of the glycosyl phosphatidylinositol membrane anchor of the trypanosome variant surface glycoprotein: Origin of the non-acetylated glucosamine
    • Doering, T. L., W. J. Masterson, P. T. Englund, and G. W. Hart. 1989. Biosynthesis of the glycosyl phosphatidylinositol membrane anchor of the trypanosome variant surface glycoprotein: origin of the non-acetylated glucosamine. J. Biol. Chem. 264:11168-11173.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11168-11173
    • Doering, T.L.1    Masterson, W.J.2    Englund, P.T.3    Hart, G.W.4
  • 13
    • 21044443776 scopus 로고    scopus 로고
    • The membrane-bound histidine acid phosphatase TbMBAP1 is essential for endocytosis and membrane recycling in Trypanosoma brucei
    • Engstler, M., et al. 2005. The membrane-bound histidine acid phosphatase TbMBAP1 is essential for endocytosis and membrane recycling in Trypanosoma brucei. J. Cell Sci. 118:2105-2118.
    • (2005) J. Cell Sci. , vol.118 , pp. 2105-2118
    • Engstler, M.1
  • 14
    • 0022635703 scopus 로고
    • Biosynthesis of Trypanosoma brucei variant surface glycoproteins. NGlycosylation and addition of a phosphatidylinositol membrane anchor
    • Ferguson, M. A., M. Duszenko, G. S. Lamont, P. Overath, and G. A. Cross. 1986. Biosynthesis of Trypanosoma brucei variant surface glycoproteins. NGlycosylation and addition of a phosphatidylinositol membrane anchor. J. Biol. Chem. 261:356-362.
    • (1986) J. Biol. Chem. , vol.261 , pp. 356-362
    • Ferguson, M.A.1    Duszenko, M.2    Lamont, G.S.3    Overath, P.4    Cross, G.A.5
  • 15
    • 84859858366 scopus 로고    scopus 로고
    • Glycosylation precursors
    • In A. Varki, R. D. Cummings, J. D. Esko, H. H. Freeze, P. Stanley, C. R. Bertozzi, G. W. Hart, and M. E. Etzler (ed.), 2nd ed. Cold Spring Harbor Laboratory Press, New York, NY
    • Freeze, H. H., and A. B. Elbein. 2008. Glycosylation precursors, p. 47-61. In A. Varki, R. D. Cummings, J. D. Esko, H. H. Freeze, P. Stanley, C. R. Bertozzi, G. W. Hart, and M. E. Etzler (ed.). Essentials of glycobiology, 2nd ed. Cold Spring Harbor Laboratory Press, New York, NY.
    • (2008) Essentials of glycobiology , pp. 47-61
    • Freeze, H.H.1    Elbein, A.B.2
  • 17
    • 33747494199 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationships of truncated bisubstrate inhibitors of aminoglycoside 6-N-acetyltransferases
    • Gao, F., et al. 2006. Synthesis and structure-activity relationships of truncated bisubstrate inhibitors of aminoglycoside 6-N-acetyltransferases. J. Med. Chem. 49:5273-5281.
    • (2006) J. Med. Chem. , vol.49 , pp. 5273-5281
    • Gao, F.1
  • 18
    • 56649116028 scopus 로고    scopus 로고
    • Compartmentation prevents a lethal turboexplosion of glycolysis in trypanosomes
    • Haanstra, J. R., et al. 2008. Compartmentation prevents a lethal turboexplosion of glycolysis in trypanosomes. Proc. Natl. Acad. Sci. U. S. A. 105:17718-17723.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 17718-17723
    • Haanstra, J.R.1
  • 19
    • 0032519629 scopus 로고    scopus 로고
    • Purification and characterization of N-acetylglucosamine kinase from rat liver-comparison with UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
    • Hinderlich, S., et al. 1998. Purification and characterization of N-acetylglucosamine kinase from rat liver-comparison with UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase. Eur. J. Biochem. 252:133-139.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 133-139
    • Hinderlich, S.1
  • 20
    • 54049143647 scopus 로고    scopus 로고
    • Structural and kinetic differences between human and Aspergillus fumigatus D-glucosamine-6-phosphate N-acetyltransferase
    • Hurtado-Guerrero, R., et al. 2008. Structural and kinetic differences between human and Aspergillus fumigatus D-glucosamine-6-phosphate N-acetyltransferase. Biochem. J. 415:217-223.
    • (2008) Biochem. J. , vol.415 , pp. 217-223
    • Hurtado-Guerrero, R.1
  • 21
    • 36549056086 scopus 로고    scopus 로고
    • Glucose-6-phosphate as a probe for the glucosamine-6-phosphate N-acetyltransferase Michaelis complex
    • Hurtado-Guerrero, R., O. Raimi, S. Shepherd, and D. D. van Aalten. 2007. Glucose-6-phosphate as a probe for the glucosamine-6-phosphate N-acetyltransferase Michaelis complex. FEBS Lett. 581:5597-5600.
    • (2007) FEBS Lett. , vol.581 , pp. 5597-5600
    • Hurtado-Guerrero, R.1    Raimi, O.2    Shepherd, S.3    van Aalten, D.D.4
  • 22
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. 1993. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26:795-800.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 23
    • 17844402766 scopus 로고    scopus 로고
    • Mosquito glucosamine-6-phosphate N-acetyltransferase: CDNA, gene structure and enzyme kinetics
    • Kato, N., C. R. Mueller, V. Wessely, Q. Lan, and B. M. Christensen. 2005. Mosquito glucosamine-6-phosphate N-acetyltransferase: cDNA, gene structure and enzyme kinetics. Insect Biochem. Mol. Biol. 35:637-646.
    • (2005) Insect Biochem. Mol. Biol. , vol.35 , pp. 637-646
    • Kato, N.1    Mueller, C.R.2    Wessely, V.3    Lan, Q.4    Christensen, B.M.5
  • 25
    • 33645902165 scopus 로고    scopus 로고
    • The suppression of galactose metabolism in Trypanosoma cruzi epimastigotes causes changes in cell surface molecular architecture and cell morphology
    • MacRae, J. I., et al. 2006. The suppression of galactose metabolism in Trypanosoma cruzi epimastigotes causes changes in cell surface molecular architecture and cell morphology. Mol. Biochem. Parasitol. 147:126-136.
    • (2006) Mol. Biochem. Parasitol. , vol.147 , pp. 126-136
    • McRae, J.I.1
  • 26
    • 42449115251 scopus 로고    scopus 로고
    • Deletion of the TbALG3 gene demonstrates site-specific N-glycosylation and N-glycan processing in Trypanosoma brucei
    • Manthri, S., M. L. S. Güther, L. Izquierdo, A. Acosta Serrano, and M. A. Ferguson. 2008. Deletion of the TbALG3 gene demonstrates site-specific N-glycosylation and N-glycan processing in Trypanosoma brucei. Glycobiology 18:367-383.
    • (2008) Glycobiology , vol.18 , pp. 367-383
    • Manthri, S.1    Güther, M.L.S.2    Izquierdo, L.3    Acosta Serrano, A.4    Ferguson, M.A.5
  • 27
    • 78149321649 scopus 로고    scopus 로고
    • Identification, subcellular localization, biochemical properties and high-resolution crystal structure of Trypanosoma brucei UDPglucose pyrophosphorylase
    • Mariño, K., et al. 2010. Identification, subcellular localization, biochemical properties and high-resolution crystal structure of Trypanosoma brucei UDPglucose pyrophosphorylase. Glycobiology 20:1619-1630.
    • (2010) Glycobiology , vol.20 , pp. 1619-1630
    • Mariño, K.1
  • 28
    • 0032029271 scopus 로고    scopus 로고
    • The glycosylation of the variant surface glycoproteins and procyclic acidic repetitive proteins of Trypanosoma brucei
    • Mehlert, A., N. Zitzmann, J. M. Richardson, A. Treumann, and M. A. J. Ferguson. 1998. The glycosylation of the variant surface glycoproteins and procyclic acidic repetitive proteins of Trypanosoma brucei. Mol. Biochem. Parasitol. 91:145-152.
    • (1998) Mol. Biochem. Parasitol. , vol.91 , pp. 145-152
    • Mehlert, A.1    Zitzmann, N.2    Richardson, J.M.3    Treumann, A.4    Ferguson, M.A.J.5
  • 30
    • 32544436403 scopus 로고    scopus 로고
    • Enzymes of UDP-GlcNAc biosynthesis in yeast
    • Milewski, S., I. Gabriel, and J. Olchowy. 2006. Enzymes of UDP-GlcNAc biosynthesis in yeast. Yeast 23:1-14.
    • (2006) Yeast , vol.23 , pp. 1-14
    • Milewski, S.1    Gabriel, I.2    Olchowy, J.3
  • 31
    • 0033940187 scopus 로고    scopus 로고
    • Reduced virulence of Candida albicans mutants lacking the GNA1 gene encoding glucosamine-6-phosphate acetyltransferase
    • Mio, T., M. Kokado, M. Arisawa, and H. Yamada-Okabe. 2000. Reduced virulence of Candida albicans mutants lacking the GNA1 gene encoding glucosamine-6-phosphate acetyltransferase. Microbiology 146:1753-1758.
    • (2000) Microbiology , vol.146 , pp. 1753-1758
    • Mio, T.1    Kokado, M.2    Arisawa, M.3    Yamada-Okabe, H.4
  • 32
    • 0032898932 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae GNA1, an essential gene encoding a novel acetyltransferase involved in UDP-N-acetylglucosamine synthesis
    • Mio, T., T. Yamada-Okabe, M. Arisawa, and H. Yamada-Okabe. 1999. Saccharomyces cerevisiae GNA1, an essential gene encoding a novel acetyltransferase involved in UDP-N-acetylglucosamine synthesis. J. Biol. Chem. 274: 424-429.
    • (1999) J. Biol. Chem. , vol.274 , pp. 424-429
    • Mio, T.1    Yamada-Okabe, T.2    Arisawa, M.3    Yamada-Okabe, H.4
  • 34
    • 78651235167 scopus 로고    scopus 로고
    • Evidence that intracellular stages of Leishmania major utilize amino sugars as a major carbon source
    • Naderer, T., J. Heng, and M. J. McConville. 2010. Evidence that intracellular stages of Leishmania major utilize amino sugars as a major carbon source. PLoS Pathog. 6:e1001245.
    • (2010) PLoS Pathog. , vol.6
    • Naderer, T.1    Heng, J.2    McConville, M.J.3
  • 35
    • 2542501651 scopus 로고    scopus 로고
    • Surface sialic acids taken from the host allow trypanosome survival in tsetse fly vectors
    • Nagamune, K., et al. 2004. Surface sialic acids taken from the host allow trypanosome survival in tsetse fly vectors. J. Exp. Med. 199:1445-1450.
    • (2004) J. Exp. Med. , vol.199 , pp. 1445-1450
    • Nagamune, K.1
  • 36
    • 0033592539 scopus 로고    scopus 로고
    • N-Linked glycans containing linear poly-N-acetyllactosamine as sorting signals in endocytosis in Trypanosoma brucei
    • Nolan, D. P., M. Geuskens, and E. Pays. 1999. N-Linked glycans containing linear poly-N-acetyllactosamine as sorting signals in endocytosis in Trypanosoma brucei. Curr. Biol. 9:1169-1172.
    • (1999) Curr. Biol. , vol.9 , pp. 1169-1172
    • Nolan, D.P.1    Geuskens, M.2    Pays, E.3
  • 37
    • 33646074032 scopus 로고    scopus 로고
    • In silico prediction of the glycosomal enzymes of Leishmania major and trypanosomes
    • Opperdoes, F. R., and J. P. Szikora. 2006. In silico prediction of the glycosomal enzymes of Leishmania major and trypanosomes. Mol. Biochem. Parasitol. 147:193-206.
    • (2006) Mol. Biochem. Parasitol. , vol.147 , pp. 193-206
    • Opperdoes, F.R.1    Szikora, J.P.2
  • 38
    • 42549120380 scopus 로고    scopus 로고
    • The LAMP-like protein p67 plays an essential role in the lysosome of African trypanosomes
    • Peck, R. F., et al. 2008. The LAMP-like protein p67 plays an essential role in the lysosome of African trypanosomes. Mol. Microbiol. 68:933-946.
    • (2008) Mol. Microbiol. , vol.68 , pp. 933-946
    • Peck, R.F.1
  • 39
    • 0035844169 scopus 로고    scopus 로고
    • The crystal structures of apo and complexed Saccharomyces cerevisiae GNA1 shed light on the catalytic mechanism of an amino-sugar N-acetyltransferase
    • Peneff, C., D. Mengin-Lecreulx, and Y. Bourne. 2001. The crystal structures of apo and complexed Saccharomyces cerevisiae GNA1 shed light on the catalytic mechanism of an amino-sugar N-acetyltransferase. J. Biol. Chem. 276:16328-16334.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16328-16334
    • Peneff, C.1    Mengin-Lecreulx, D.2    Bourne, Y.3
  • 42
    • 21244496004 scopus 로고    scopus 로고
    • The suppression of galactose metabolism in procylic form Trypanosoma brucei causes cessation of cell growth and alters procyclin glycoprotein structure and copy number
    • Roper, J. R., et al. 2005. The suppression of galactose metabolism in procylic form Trypanosoma brucei causes cessation of cell growth and alters procyclin glycoprotein structure and copy number. J. Biol. Chem. 280:19728-19736.
    • (2005) J. Biol. Chem. , vol.280 , pp. 19728-19736
    • Roper, J.R.1
  • 43
    • 0037197847 scopus 로고    scopus 로고
    • Galactose metabolism is essential for the African sleeping sickness parasite Trypanosoma brucei
    • Roper, J. R., M. L. Guther, K. Milne, and M. A. Ferguson. 2002. Galactose metabolism is essential for the African sleeping sickness parasite Trypanosoma brucei. Proc. Natl. Acad. Sci. U. S. A. 99:5884-5889.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 5884-5889
    • Roper, J.R.1    Guther, M.L.2    Milne, K.3    Ferguson, M.A.4
  • 44
    • 1642293193 scopus 로고    scopus 로고
    • A model for sedimentation in inhomogeneous media. I. Dynamic density gradients from sedimenting co-solutes
    • Schuck, P. 2004. A model for sedimentation in inhomogeneous media. I. Dynamic density gradients from sedimenting co-solutes. Biophys. Chem. 108:187-200.
    • (2004) Biophys. Chem. , vol.108 , pp. 187-200
    • Schuck, P.1
  • 45
    • 0031832325 scopus 로고    scopus 로고
    • An improved method for the purification of Trypanosoma brucei variant surface glycoprotein (VSG)
    • Steverding, D., and K. Kremp. 1998. An improved method for the purification of Trypanosoma brucei variant surface glycoprotein (VSG). Parasitol. Res. 84:524-525.
    • (1998) Parasitol. Res. , vol.84 , pp. 524-525
    • Steverding, D.1    Kremp, K.2
  • 46
    • 47049088391 scopus 로고    scopus 로고
    • The synthesis of UDP-N-acetylglucosamine is essential for bloodstream form Trypanosoma brucei in vitro and in vivo and UDP-N-acetylglucosamine starvation reveals a hierarchy in parasite protein glycosylation
    • Stokes, M. J., et al. 2008. The synthesis of UDP-N-acetylglucosamine is essential for bloodstream form Trypanosoma brucei in vitro and in vivo and UDP-N-acetylglucosamine starvation reveals a hierarchy in parasite protein glycosylation. J. Biol. Chem. 283:16147-16161.
    • (2008) J. Biol. Chem. , vol.283 , pp. 16147-16161
    • Stokes, M.J.1
  • 47
    • 0037017402 scopus 로고    scopus 로고
    • Acyl-CoA oxidase is imported as a heteropentameric, cofactor-containing complex into peroxisomes of Yarrowia lipolytica
    • Titorenko, V. I., J. M. Nicaud, H. Wang, H. Chan, and R. A. Rachubinski. 2002. Acyl-CoA oxidase is imported as a heteropentameric, cofactor-containing complex into peroxisomes of Yarrowia lipolytica. J. Cell Biol. 156: 481-494.
    • (2002) J. Cell Biol. , vol.156 , pp. 481-494
    • Titorenko, V.I.1    Nicaud, J.M.2    Wang, H.3    Chan, H.4    Rachubinski, R.A.5
  • 48
    • 0031580206 scopus 로고    scopus 로고
    • Structural characterisation of two forms of procyclic acidic repetitive protein expressed by procyclic forms of Trypanosoma brucei
    • Treumann, A., et al. 1997. Structural characterisation of two forms of procyclic acidic repetitive protein expressed by procyclic forms of Trypanosoma brucei. J. Mol. Biol. 269:529-547.
    • (1997) J. Mol. Biol. , vol.269 , pp. 529-547
    • Treumann, A.1
  • 49
    • 34547911022 scopus 로고    scopus 로고
    • Sugar nucleotide pools of Trypanosoma brucei, Trypanosoma cruzi, and Leishmania major
    • Turnock, D. C., and M. A. J. Ferguson. 2007. Sugar nucleotide pools of Trypanosoma brucei, Trypanosoma cruzi, and Leishmania major. Eukaryot. Cell 6:1450-1463.
    • (2007) Eukaryot. Cell , vol.6 , pp. 1450-1463
    • Turnock, D.C.1    Ferguson, M.A.J.2
  • 50
    • 35348963515 scopus 로고    scopus 로고
    • The de novo synthesis of GDP-fucose is essential for flagellar adhesion and cell growth in Trypanosoma brucei
    • Turnock, D. C., L. Izquierdo, and M. A. Ferguson. 2007. The de novo synthesis of GDP-fucose is essential for flagellar adhesion and cell growth in Trypanosoma brucei. J. Biol. Chem. 282:28853-28863.
    • (2007) J. Biol. Chem. , vol.282 , pp. 28853-28863
    • Turnock, D.C.1    Izquierdo, L.2    Ferguson, M.A.3
  • 51
    • 33845482665 scopus 로고    scopus 로고
    • Genome-scale protein expression and structural biology of Plasmodium falciparum and related apicomplexan organisms
    • Vedadi, M., et al. 2007. Genome-scale protein expression and structural biology of Plasmodium falciparum and related apicomplexan organisms. Mol. Biochem. Parasitol. 151:100-110.
    • (2007) Mol. Biochem. Parasitol. , vol.151 , pp. 100-110
    • Vedadi, M.1
  • 52
    • 9744255506 scopus 로고    scopus 로고
    • Structure and functions of the GNAT superfamily of acetyltransferases
    • Vetting, M. W., et al. 2005. Structure and functions of the GNAT superfamily of acetyltransferases. Arch. Biochem. Biophys. 433:212-226.
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 212-226
    • Vetting, M.W.1
  • 53
    • 49649097025 scopus 로고    scopus 로고
    • Acceptor substrate binding revealed by crystal structure of human glucosamine-6-phosphate N-acetyltransferase 1
    • Wang, J., X. Liu, Y. H. Liang, L. F. Li, and X. D. Su. 2008. Acceptor substrate binding revealed by crystal structure of human glucosamine-6-phosphate N-acetyltransferase 1. FEBS Lett. 582:2973-2978.
    • (2008) FEBS Lett. , vol.582 , pp. 2973-2978
    • Wang, J.1    Liu, X.2    Liang, Y.H.3    Li, L.F.4    Su, X.D.5
  • 54
    • 65449188232 scopus 로고    scopus 로고
    • Jalview version 2-a multiple sequence alignment editor and analysis workbench
    • Waterhouse, A. M., J. B. Procter, D. M. A. Martin, M. Clamp, and G. J. Barton. 2009. Jalview version 2-a multiple sequence alignment editor and analysis workbench. Bioinformatics 25:1189-1191.
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.A.3    Clamp, M.4    Barton, G.J.5
  • 55
    • 0033525524 scopus 로고    scopus 로고
    • A tightly regulated inducible expression system for conditional gene knock-outs and dominantnegative genetics in Trypanosoma brucei
    • Wirtz, E., S. Leal, C. Ochatt, and G. A. Cross. 1999. A tightly regulated inducible expression system for conditional gene knock-outs and dominantnegative genetics in Trypanosoma brucei. Mol. Biochem. Parasitol. 99:89-101.
    • (1999) Mol. Biochem. Parasitol. , vol.99 , pp. 89-101
    • Wirtz, E.1    Leal, S.2    Ochatt, C.3    Cross, G.A.4
  • 56
    • 0036299021 scopus 로고    scopus 로고
    • X-ray crystallographic studies of serotonin N-acetyltransferase catalysis and inhibition
    • Wolf, E., J. De Angelis, E. M. Khalil, P. A. Cole, and S. K. Burley. 2002. X-ray crystallographic studies of serotonin N-acetyltransferase catalysis and inhibition. J. Mol. Biol. 317:215-224.
    • (2002) J. Mol. Biol. , vol.317 , pp. 215-224
    • Wolf, E.1    de Angelis, J.2    Khalil, E.M.3    Cole, P.A.4    Burley, S.K.5
  • 57
    • 77955069388 scopus 로고    scopus 로고
    • Identification of a novel UDP-sugar pyrophosphorylase with a broad substrate specificity in Trypanosoma cruzi
    • Yang, T., and M. Bar-Peled. 2010. Identification of a novel UDP-sugar pyrophosphorylase with a broad substrate specificity in Trypanosoma cruzi. Biochem. J. 429:533-543.
    • (2010) Biochem. J. , vol.429 , pp. 533-543
    • Yang, T.1    Bar-Peled, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.