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Sialidase Trypanosoma cruzi

Schroven A (2007) Synthesis and investigations on modified neuraminic acid donors for regio-and stereoselective sialylation with trans sialidase (Trypanosoma cruzi). PhD thesis, University of Hamburg... [Pg.250]

F. Vandekerckhove, S. Schenkman, L. Pontes de Carvalho, S. Tomlinson, M. Kiso, M. Yoshida, A. Hasegawa, and V. Nussenzweig, Substrate specificity of the Trypanosoma cruzi trans-sialidase, Glycobiology 2 541 (1992). [Pg.375]

A. C. C. Frash, Functional diversity in the trans-sialidase and mucin families in Trypanosoma cruzi, Parasitol. Today, 16 (2000) 282-286. [Pg.205]

T. cruzi small mucin-like gene family TcTS, Trypanosoma cruzi trans-sialidase THF, tetrahydrofuran TMSOTf, trimethylsilyl trifluoromethanesulfonate TRR, Thr-rich region TSSA, trypomastigote small surface antigen UDP, uridine diphosphate VSG, variant surface glycoprotein. [Pg.312]

SCHEME 12. Selective sialylation of 2,3-di-0-(/i-D-galactopyranosyl)-i)-galactose catalyzed by Trypanosoma cruzi trans-sialidase. [Pg.341]

SCHEME 20. /Y-(il ycoIyIncuraminic acid transfer by Trypanosoma cruzi trans-sialidase from donors 107 and 108 to lactitol. [Pg.347]

R. Agusti, A. S. Couto, O. Campetella, A. C. C. Frasch, and R. M. de Lederkremer, Structure of the glycosylphosphatidylinositol-anchor of the frans-sialidase from Trypanosoma cruzi metacyclic trypomastigote forms, Mol. Biochem. Parasitol., 97 (1998) 123-131. [Pg.357]

M. J. M. Alves and W. Colli, Role of the gp85/trans-sialidase superfamily of glycoproteins in the interaction of Trypanosoma cruzi with host structures, in B. A. Burleigh and D. Soldati-Favre, (Eds.), Molecular Mechanisms of Parasite Invasion, 47 pp. 58-96. [Pg.357]

S. Schenkman, M. A. J. Ferguson, N. Heise, M. L. de Almeida, R. A. Mortara, andN. Yoshida, Mucinlike glycoproteins linked to the membrane by glycosylphosphatidylinositol anchor are the major acceptors of sialic acid in a reaction catalyzed by trans-sialidase in metacyclic forms of Trypanosoma cruzi, Mol. Biochem. Parasitol., 59 (1993) 293-303. [Pg.360]

C. A. Buscaglia, V. A. Campo, A. C. C. Frasch, and J. M. Di Noia, Trypanosoma cruzi surface mucins host-dependent coat diversity, Nat. Rev. Microbiol, 4 (2006) 229-236 A. C. C. Frasch, Functional diversity in the trans-sialidase and mucin families in Trypanosoma cruzi, Parasitol. Today, 16 (2000) 282-286. [Pg.360]

S. Schenkman and M. Jiang, G.W. Hart and V. Nussenzweig. A novel cell surface trans-sialidase of Trypanosoma cruzi generates a stage-specific epitope required for invasion of mammalian cells, Cell, 65 (1991) 1117-1125. [Pg.360]

V. M. Mendoza, R. Agusti, C. Gallo-Rodriguez, and R. M. de Lederkremer, Synthesis of the O-linked pentasaccharide in glycoproteins of Trypanosoma cruzi and selective sialylation by recombinant frans-sialidase, Carbohydr. Res., 341 (2006) 1488-1497. [Pg.362]

M. Chuenkova and M. E. S. Pereira, Trypanosoma cruzi trans-sialidase enhancement of virulence in a murine model of Chagas disease, J. Exp. Med., 181 (1995) 1693-1703. [Pg.363]

R. Agusti, M. E. Giorgi, and R. M. de Lederkremer, The trans-sialidase from Trypanosoma cruzi efficiently transfers alpha-(2—>3)-linked N-glycolylneuraminic acid to terminal beta-galactosyl units,... [Pg.363]

M. L. Cremona, O. Campetella, D. O. Sanchez, and A. C. C. Frasch, Enzymically inactive members of the trans-sialidase family from Trypanosoma cruzi display beta-galactose binding activity, Glycobiology, 9 (1999) 581-587. [Pg.363]

A. Buschiazzo, M. F. Amaya, M. L. Cremona, A. C. C. Frasch, and P. M. Alzari, The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis, Mol. Cell,... [Pg.364]

S. Buchini, A. Buschiazzo, and S. G. Withers, A new generation of specific Trypanosoma cruzi trans-sialidase inhibitors, Angew. Chem. Ini. Ed., 47 (2008) 2700-2703. [Pg.364]

A. R. Todeschini, W. B. Dias, M. F. Girard, J. M. Wieruszeski, L. Mendonga-Previato, and J. O. Previato, Enzymatically inactive trans-sialidase from Trypanosoma cruzi binds sialyl and beta-galactopyranosyl residues in a sequential ordered mechanism, J. Biol. Chem., 279 (2004) 5323-5328. [Pg.364]

P. Scudder, J. P. Doom, M. Chenkova, I. D. Manger, and M. E. S. Pereira, Enzymatic characterization of beta-D-galactoside alpha 2,3-trans-sialidase from Trypanosoma cruzi, J. Biol. Chem., 268 (1993) 9886-9891. [Pg.364]

M. Ribeirao, V. L. Pereira-Chioccola, D. Eichinger, M. M. Rodrigues, and S. Schenkman, Temperature differences for frans-glycosylation and hydrolysis reaction reveal an acceptor binding site in the catalytic mechanism of Trypanosoma cruzi trans-sialidase, Glycobiology, 1 (1997) 1237-1246. [Pg.364]

J. A. Harrison, K. P. Kartha, W. B. Turnbull, S. L. Scheuerl, J. H. Naismith, S. Schenkman, and R. A. Field, Hydrolase and sialyltransferase activities of trypanosoma cruzi trans-sialidase towards NeuAc-alpha-2,3-gal-Gal-beta-0-PNP, Bioorg. Med. Chem. Lett., 11 (2001) 141-144. [Pg.364]

S. Singh, M. Scigelova, M. L. Hallberg, O. W. Howarth, D. H. G. Crout, and S. Schenkman, Synthesis of sialyloligosaccharides using the trans-sialidase from Trypanosoma cruzi novel branched and di-sialylated products from digalactoside acceptors, Chem. Commun., 12 (2000) 1013-1014. [Pg.364]

B. Neubacher, D. Schmidt, P. Ziegelmuller, and J. Thiem, Preparation of sialylated oligosaccharides employing recombinant trans-sialidase from Trypanosoma cruzi, Org. Biomol. Chem., 3 (2005) 1551-1556. [Pg.365]

K. B. Lee and Y. C. Lee, Transfer of modified sialic acids by Trypanosoma cruzi trans-sialidase for attachment of functional groups to oligosaccharide, Anal. Biochem., 216 (1994) 358—364. [Pg.365]

M. Engstler, R. Schauer, M. A. Ferrero-Garcia, A. J. Parodi, T. Storz-Eckerlin, A. Vasella, C. Witzig, and X. Zhu, N-(4-Nitrophenyl)oxamic Acid and Related N-Acylanilines Are Non-competitive Inhibitors of vibrio cholerae sialidase but do not inhibit trypanosoma cruzi or trypanosoma brucei trans-sialidases, Helv. Chim. Acta., 77 (1994) 1166-1174. [Pg.365]

M. G. Risso, G. B. Garbarino, E. Mocetti, O. Campetella, S. M. Gonzalez Cappa, C. A. Buscaglia, and M. S. Leguizamon, Differential expression of a virulence factor, the trans-sialidase, by the main Trypanosoma cruzi phylogenetic lineages, J. Infect. Dis., 189 (2004) 2250-2259. [Pg.365]

J. Mucci, A. Hidalgo, E. Mocetti, P. F. Argibay, M. S. Leguizamon, and O. Campetella, Thymocyte depletion in Trypanosoma cruzi infection is mediated by frans-sialidase-induced apoptosis on nurse cells complex, Proc. Natl. Acad. Sci. USA, 99 (2002) 3896-3901. [Pg.365]


See other pages where Sialidase Trypanosoma cruzi is mentioned: [Pg.404]    [Pg.1399]    [Pg.2245]    [Pg.1]    [Pg.52]    [Pg.337]    [Pg.357]    [Pg.362]    [Pg.363]    [Pg.363]    [Pg.365]   
See also in sourсe #XX -- [ Pg.333 , Pg.337 ]




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Sialidase

Sialidases

Trypanosoma cruzi

Trypanosoma cruzi trans-sialidase

Trypanosoma cruzi trans-sialidases

Trypanosoma cruzi trans-sialidases mechanism

Trypanosoma cruzi trans-sialidases oligosaccharides

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