메뉴 건너뛰기




Volumn 44, Issue 35, 2005, Pages 11669-11675

Characterization of Vibrio cholerae neuraminidase by a novel mechanism-based fluorescent labeling reagent

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CRYSTALLOGRAPHY; ORGANIC ACIDS; PATHOLOGY; SUBSTRATES;

EID: 24344510734     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0509954     Document Type: Article
Times cited : (28)

References (17)
  • 1
    • 0030444832 scopus 로고    scopus 로고
    • Sialidases: Structures, biological significance and therapeutic potential
    • Taylor, G. (1996) Sialidases: Structures, biological significance and therapeutic potential, Curr. Opin. Struct. Biol. 6, 830-837.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 830-837
    • Taylor, G.1
  • 4
    • 0028325249 scopus 로고
    • Molecular modeling studies on ligand binding to sialidase from influenza virus and the mechanism of catalysis
    • Taylor, N. R., and Itzstein, M. (1994) Molecular modeling studies on ligand binding to sialidase from influenza virus and the mechanism of catalysis, J. Med. Client. 37, 616-624.
    • (1994) J. Med. Client. , vol.37 , pp. 616-624
    • Taylor, N.R.1    Itzstein, M.2
  • 5
    • 0028773635 scopus 로고
    • Crystal structure of Vibrio cholerae neuraminidase reveales dual lectin-like domains in addition to the catalytic domain
    • Crennell, S., Garman, E., Laver, G., Vimr, E., and Taylor, G. (1994) Crystal structure of Vibrio cholerae neuraminidase reveales dual lectin-like domains in addition to the catalytic domain, Structure 2, 535-544.
    • (1994) Structure , vol.2 , pp. 535-544
    • Crennell, S.1    Garman, E.2    Laver, G.3    Vimr, E.4    Taylor, G.5
  • 7
    • 0038546856 scopus 로고    scopus 로고
    • Trypanosoma cruzi trans-sialidase operates through a covalent sialyl-enzyme intermediate: Tyrosine is the catalytic nucleophile
    • Watts, A. G., Damager, I., Amaya, M. L., Buschiazzo, A., Alzari, P., Frasch, A. C., and Withers, S. G. (2003) Trypanosoma cruzi trans-sialidase operates through a covalent sialyl-enzyme intermediate: Tyrosine is the catalytic nucleophile, J. Am. Chem. Soc. 125, 7532-7533.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7532-7533
    • Watts, A.G.1    Damager, I.2    Amaya, M.L.3    Buschiazzo, A.4    Alzari, P.5    Frasch, A.C.6    Withers, S.G.7
  • 8
    • 0033963529 scopus 로고    scopus 로고
    • Glycosidase mechanisms: Anatomy of a finely tuned catalyst
    • Zechel, D., and Withers, S. G. (2000) Glycosidase mechanisms: Anatomy of a finely tuned catalyst, Acc. Chem. Res. 33, 11-18.
    • (2000) Acc. Chem. Res. , vol.33 , pp. 11-18
    • Zechel, D.1    Withers, S.G.2
  • 9
    • 7244245609 scopus 로고    scopus 로고
    • Mechanism-based fluorescent labeling of β-galactosidases: An efficient method in proteomics for glycoside hydrolases
    • Kurogochi, M., Nishimura, S.-I., and Lee, Y. C. (2004) Mechanism-based fluorescent labeling of β-galactosidases: An efficient method in proteomics for glycoside hydrolases, J. Biol. Chem. 279, 44704-44712.
    • (2004) J. Biol. Chem. , vol.279 , pp. 44704-44712
    • Kurogochi, M.1    Nishimura, S.-I.2    Lee, Y.C.3
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of inicrograin quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantification of inicrograin quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 0013879925 scopus 로고
    • Synthesis of the anomer sialic acid-methylketoside
    • Kuhn, R., Lutz, P., and MacDonald, P. L. (1966) Synthesis of the anomer sialic acid-methylketoside, Chem. Ber. 99, 611-617.
    • (1966) Chem. Ber. , vol.99 , pp. 611-617
    • Kuhn, R.1    Lutz, P.2    MacDonald, P.L.3
  • 12
    • 0024992737 scopus 로고
    • Ortho- And para-(difluoromethyl)aryl-β-D-glucosides: A new class of enzyme-activated irreversible inhibitors of β-glucosidases
    • Halazy, S., Berges, V., Ehrhard, A., and Danzin, C. (1990) Ortho- and para-(difluoromethyl)aryl-β-D-glucosides: A new class of enzyme-activated irreversible inhibitors of β-glucosidases, Bioorg. Chem. 18, 330-344.
    • (1990) Bioorg. Chem. , vol.18 , pp. 330-344
    • Halazy, S.1    Berges, V.2    Ehrhard, A.3    Danzin, C.4
  • 13
    • 0026457003 scopus 로고
    • Synthesis of sodium salt of ortho-(difluoiOinethyl)phenyl-α- ketoside of N-acetylneuraminic acid: A mechanism-based inhibitor of Clostridium perfringens neuraminidase
    • Drigtiez, P.-A., Barrere, B., Chantegrel, B., Deshayes, C., Doutheau, A., and Quash, G. (1992) Synthesis of sodium salt of ortho-(difluoiOinethyl)phenyl- α-ketoside of N-acetylneuraminic acid: A mechanism-based inhibitor of Clostridium perfringens neuraminidase, Bioorg. Med. Chem. Lett. 2, 1361-1366.
    • (1992) Bioorg. Med. Chem. Lett. , vol.2 , pp. 1361-1366
    • Drigtiez, P.-A.1    Barrere, B.2    Chantegrel, B.3    Deshayes, C.4    Doutheau, A.5    Quash, G.6
  • 14
    • 73649151319 scopus 로고
    • Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase
    • Kitz, R., and Wilson, I. B. (1962) Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase, J. Biol. Chem. 237, 3245-3249.
    • (1962) J. Biol. Chem. , vol.237 , pp. 3245-3249
    • Kitz, R.1    Wilson, I.B.2
  • 15
    • 7244262017 scopus 로고    scopus 로고
    • (Engel. P. C., Ed.). Academic Press. Orlando, FL
    • Tipton, K. F. (1996) in Enzymology LABFAX (Engel. P. C., Ed.) pp 151-171. Academic Press. Orlando, FL.
    • (1996) Enzymology LABFAX , pp. 151-171
    • Tipton, K.F.1
  • 16
    • 12844253114 scopus 로고    scopus 로고
    • Crystal structure of the human cytosolic sialidase Neu2: Evidence for the dynamic nature of substrate recognition
    • Chavas, L. M. G., Tringali, C., Fusi, P., Venerando, B., Tettamanti, G., Kato, R., Monti, E., and Wakatsuki, S. (2005) Crystal structure of the human cytosolic sialidase Neu2: Evidence for the dynamic nature of substrate recognition, J. Biol. Chem. 280, 469-475.
    • (2005) J. Biol. Chem. , vol.280 , pp. 469-475
    • Chavas, L.M.G.1    Tringali, C.2    Fusi, P.3    Venerando, B.4    Tettamanti, G.5    Kato, R.6    Monti, E.7    Wakatsuki, S.8
  • 17
    • 0036678137 scopus 로고    scopus 로고
    • Up-regulation of plasma membrane-associated ganglioside sialidase (Neu3) in human colon cancer and its involvement in apoptosis suppression
    • Kakugata, Y., Wada, T., Yamaguchi, K., Yamanami, H., Ouchi, K., Sato, I., and Miyagi, T. (2002) Up-regulation of plasma membrane-associated ganglioside sialidase (Neu3) in human colon cancer and its involvement in apoptosis suppression, Proc. Natl. Acad. Sci. U.S.A. 99, 10718-10723.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 10718-10723
    • Kakugata, Y.1    Wada, T.2    Yamaguchi, K.3    Yamanami, H.4    Ouchi, K.5    Sato, I.6    Miyagi, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.