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Volumn 478, Issue C, 2010, Pages 265-286

Multifaceted approaches including neoglycolipid oligosaccharide microarrays to ligand discovery for malectin

Author keywords

[No Author keywords available]

Indexed keywords

GLYCAN; LECTIN; MALECTIN; MANNOSE; NEOGLYCOLIPID OLIGOSACCHARIDE; OLIGOSACCHARIDE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 77956292791     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(10)78013-7     Document Type: Chapter
Times cited : (9)

References (27)
  • 1
    • 38749134509 scopus 로고    scopus 로고
    • Glucosylated free oligosaccharides are biomarkers of endoplasmic-reticulum alpha-glucosidase inhibition
    • Alonzi D.S., Neville D.C., Lachmann R.H., Dwek R.A., Butters T.D. Glucosylated free oligosaccharides are biomarkers of endoplasmic-reticulum alpha-glucosidase inhibition. Biochem. J. 2008, 409:571-580.
    • (2008) Biochem. J. , vol.409 , pp. 571-580
    • Alonzi, D.S.1    Neville, D.C.2    Lachmann, R.H.3    Dwek, R.A.4    Butters, T.D.5
  • 2
    • 65549085558 scopus 로고    scopus 로고
    • Improved cellular inhibitors for glycoprotein processing alpha-glucosidases: Biological characterisation of alkyl- and arylalkyl-N-substituted deoxynojirimycins
    • Alonzi D.S., Dwek R.A., Butters T.D. Improved cellular inhibitors for glycoprotein processing alpha-glucosidases: Biological characterisation of alkyl- and arylalkyl-N-substituted deoxynojirimycins. Tetrahedron Asymmetry 2009, 20:897-901.
    • (2009) Tetrahedron Asymmetry , vol.20 , pp. 897-901
    • Alonzi, D.S.1    Dwek, R.A.2    Butters, T.D.3
  • 3
    • 77949334636 scopus 로고    scopus 로고
    • Looking glass inhibitors: Scalable syntheses of DNJ, DMDP, and (3R)-3-hydroxy-l-bulgecinine from d-glucuronolactone and of l-DNJ, l-DMDP, and (3S)-3-hydroxy-d-bulgecinine from l-glucuronolactone. DMDP inhibits β-glucosidases and β-galactosidases whereas l-DMDP is a potent and specific inhibitor of α-glucosidases
    • Best D., Wang C., Weymouth-Wilson A.C., Clarkson R.A., Wilson F.X., Nash R.J., Miyauchi S., Kato A., Fleet G.W.J. Looking glass inhibitors: Scalable syntheses of DNJ, DMDP, and (3R)-3-hydroxy-l-bulgecinine from d-glucuronolactone and of l-DNJ, l-DMDP, and (3S)-3-hydroxy-d-bulgecinine from l-glucuronolactone. DMDP inhibits β-glucosidases and β-galactosidases whereas l-DMDP is a potent and specific inhibitor of α-glucosidases. Tetrahedron Asymmetry 2010, 21:311-319.
    • (2010) Tetrahedron Asymmetry , vol.21 , pp. 311-319
    • Best, D.1    Wang, C.2    Weymouth-Wilson, A.C.3    Clarkson, R.A.4    Wilson, F.X.5    Nash, R.J.6    Miyauchi, S.7    Kato, A.8    Fleet, G.W.J.9
  • 4
    • 57649089450 scopus 로고    scopus 로고
    • Screening of fusion partners for high yield expression and purification of bioactive viscotoxins
    • Bogomolovas J., Simon B., Sattler M., Stier G. Screening of fusion partners for high yield expression and purification of bioactive viscotoxins. Protein Expr. Purif. 2009, 64:16-23.
    • (2009) Protein Expr. Purif. , vol.64 , pp. 16-23
    • Bogomolovas, J.1    Simon, B.2    Sattler, M.3    Stier, G.4
  • 6
    • 0032787620 scopus 로고    scopus 로고
    • Effects of N-butyldeoxynojirimycin and the Lec3.2.8.1 mutant phenotype on N-glycan processing in Chinese hamster ovary cells: Application to glycoprotein crystallization
    • Butters T.D., Sparks L.M., Harlos K., Ikemizu S., Stuart D.I., Jones E.Y., Davis S.J. Effects of N-butyldeoxynojirimycin and the Lec3.2.8.1 mutant phenotype on N-glycan processing in Chinese hamster ovary cells: Application to glycoprotein crystallization. Protein Sci. 1999, 8:1696-1701.
    • (1999) Protein Sci. , vol.8 , pp. 1696-1701
    • Butters, T.D.1    Sparks, L.M.2    Harlos, K.3    Ikemizu, S.4    Stuart, D.I.5    Jones, E.Y.6    Davis, S.J.7
  • 7
    • 0030883428 scopus 로고    scopus 로고
    • Nonreductive release of O-linked oligosaccharides from mucin glycoproteins for structure/function assignments as neoglycolipids: Application in the detection of novel ligands for E-selectin
    • Chai W., Feizi T., Yuen C.-T., Lawson A.M. Nonreductive release of O-linked oligosaccharides from mucin glycoproteins for structure/function assignments as neoglycolipids: Application in the detection of novel ligands for E-selectin. Glycobiology 1997, 7:861-872.
    • (1997) Glycobiology , vol.7 , pp. 861-872
    • Chai, W.1    Feizi, T.2    Yuen, C.-T.3    Lawson, A.M.4
  • 8
  • 9
    • 0008720662 scopus 로고
    • Dextran
    • Academic Press, New York, R.L. Whistler, J. BeMiller (Eds.)
    • de Belder A.N. Dextran. Industrial Gums 1993, 399-426. Academic Press, New York. R.L. Whistler, J. BeMiller (Eds.).
    • (1993) Industrial Gums , pp. 399-426
    • de Belder, A.N.1
  • 10
    • 0028987555 scopus 로고
    • Purification and characterization of an endo-beta-1,6-glucanase from Trichoderma harzianum that is related to its mycoparasitism
    • de la C.J., Pintor-Toro J.A., Benitez T., Llobell A. Purification and characterization of an endo-beta-1,6-glucanase from Trichoderma harzianum that is related to its mycoparasitism. J. Bacteriol. 1995, 177:1864-1871.
    • (1995) J. Bacteriol. , vol.177 , pp. 1864-1871
    • de la, C.J.1    Pintor-Toro, J.A.2    Benitez, T.3    Llobell, A.4
  • 11
    • 0028673927 scopus 로고
    • Neoglycolipids: Probes in structure/function assignments to oligosaccharides
    • Feizi T., Childs R.A. Neoglycolipids: Probes in structure/function assignments to oligosaccharides. Methods Enzymol. 1994, 242:205-217.
    • (1994) Methods Enzymol. , vol.242 , pp. 205-217
    • Feizi, T.1    Childs, R.A.2
  • 12
    • 0028201330 scopus 로고
    • Neoglycolipids: Probes of oligosaccharide structure, antigenicity and function
    • Feizi T., Stoll M.S., Yuen C.-T., Chai W., Lawson A.M. Neoglycolipids: Probes of oligosaccharide structure, antigenicity and function. Methods Enzymol. 1994, 230:484-519.
    • (1994) Methods Enzymol. , vol.230 , pp. 484-519
    • Feizi, T.1    Stoll, M.S.2    Yuen, C.-T.3    Chai, W.4    Lawson, A.M.5
  • 14
    • 0028262949 scopus 로고
    • Academic Press, San Diego, W.J. Lennarz, G.W. Hart (Eds.)
    • Jacob G.S., Scudder P. Methods Enzymology 1994, 280. Academic Press, San Diego. W.J. Lennarz, G.W. Hart (Eds.).
    • (1994) Methods Enzymology , pp. 280
    • Jacob, G.S.1    Scudder, P.2
  • 15
    • 77956272282 scopus 로고
    • Academic Press, San Diego, W.J. Lennarz, G.W. Hart (Eds.)
    • Kaushal G.P., Elbein A.D. Methods Enzymology 1994, 316. Academic Press, San Diego. W.J. Lennarz, G.W. Hart (Eds.).
    • (1994) Methods Enzymology , pp. 316
    • Kaushal, G.P.1    Elbein, A.D.2
  • 17
    • 33750993048 scopus 로고    scopus 로고
    • Preparation of neoglycolipids with ring-closed cores via chemoselective oxime-ligation for microarray analysis of carbohydrate-protein interactions
    • Liu Y., Chai W., Childs R.A., Feizi T. Preparation of neoglycolipids with ring-closed cores via chemoselective oxime-ligation for microarray analysis of carbohydrate-protein interactions. Methods Enzymol. 2006, 415C:326-340.
    • (2006) Methods Enzymol. , vol.415 C , pp. 326-340
    • Liu, Y.1    Chai, W.2    Childs, R.A.3    Feizi, T.4
  • 19
    • 0034663565 scopus 로고    scopus 로고
    • High-performance cation-exchange chromatography and pulsed amperometric detection for the separation, detection, and quantitation of N-alkylated imino sugars in biological samples
    • Mellor H.R., Adam A., Platt F.M., Dwek R.A., Butters T.D. High-performance cation-exchange chromatography and pulsed amperometric detection for the separation, detection, and quantitation of N-alkylated imino sugars in biological samples. Anal. Biochem. 2000, 284:136-142.
    • (2000) Anal. Biochem. , vol.284 , pp. 136-142
    • Mellor, H.R.1    Adam, A.2    Platt, F.M.3    Dwek, R.A.4    Butters, T.D.5
  • 20
    • 0037103782 scopus 로고    scopus 로고
    • Preparation, biochemical characterization and biological properties of radiolabelled N-alkylated deoxynojirimycins
    • Mellor H.R., Nolan J., Pickering L., Wormald M.R., Platt F.M., Dwek R.A., Fleet G.W., Butters T.D. Preparation, biochemical characterization and biological properties of radiolabelled N-alkylated deoxynojirimycins. Biochem. J. 2002, 366:225-233.
    • (2002) Biochem. J. , vol.366 , pp. 225-233
    • Mellor, H.R.1    Nolan, J.2    Pickering, L.3    Wormald, M.R.4    Platt, F.M.5    Dwek, R.A.6    Fleet, G.W.7    Butters, T.D.8
  • 21
    • 3242730231 scopus 로고    scopus 로고
    • Analysis of fluorescently labeled glycosphingolipid-derived oligosaccharides following ceramide glycanase digestion and anthranilic acid labeling
    • Neville D.C., Coquard V., Priestman D.A., te Vruchte D.J., Sillence D.J., Dwek R.A., Platt F.M., Butters T.D. Analysis of fluorescently labeled glycosphingolipid-derived oligosaccharides following ceramide glycanase digestion and anthranilic acid labeling. Anal. Biochem. 2004, 331:275-282.
    • (2004) Anal. Biochem. , vol.331 , pp. 275-282
    • Neville, D.C.1    Coquard, V.2    Priestman, D.A.3    te Vruchte, D.J.4    Sillence, D.J.5    Dwek, R.A.6    Platt, F.M.7    Butters, T.D.8
  • 22
    • 0026329037 scopus 로고
    • Structures of asparagine-linked oligosaccharides from hen egg-yolk antibody (IgY). Occurrence of unusual glucosylated oligo-mannose type oligosaccharides in a mature glycoprotein
    • Ohta M., Hamako J., Yamamoto S., Hatta H., Kim M., Yamamoto T., Oka S., Mizuochi T., Matsuura F. Structures of asparagine-linked oligosaccharides from hen egg-yolk antibody (IgY). Occurrence of unusual glucosylated oligo-mannose type oligosaccharides in a mature glycoprotein. Glycoconj. J. 1991, 8:400-413.
    • (1991) Glycoconj. J. , vol.8 , pp. 400-413
    • Ohta, M.1    Hamako, J.2    Yamamoto, S.3    Hatta, H.4    Kim, M.5    Yamamoto, T.6    Oka, S.7    Mizuochi, T.8    Matsuura, F.9
  • 23
    • 33646843444 scopus 로고    scopus 로고
    • Ligands for the beta-glucan receptor, Dectin-1, assigned using 'designer' microarrays of oligosaccharide probes (neoglycolipids) generated from glucan polysaccharides
    • Palma A.S., Feizi T., Zhang Y., Stoll M.S., Lawson A.M., Diaz-Rodríguez E., Campanero-Rhodes A.S., Costa J., Brown G.D., Chai W. Ligands for the beta-glucan receptor, Dectin-1, assigned using 'designer' microarrays of oligosaccharide probes (neoglycolipids) generated from glucan polysaccharides. J. Biol. Chem. 2006, 281:5771-5779.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5771-5779
    • Palma, A.S.1    Feizi, T.2    Zhang, Y.3    Stoll, M.S.4    Lawson, A.M.5    Diaz-Rodríguez, E.6    Campanero-Rhodes, A.S.7    Costa, J.8    Brown, G.D.9    Chai, W.10
  • 24
    • 0030839727 scopus 로고    scopus 로고
    • The solution NMR structure of glucosylated N-glycans involved in the early stages of glycoprotein biosynthesis and folding
    • Petrescu A.J., Butters T.D., Reinkensmeier G., Petrescu S., Platt F.M., Dwek R.A., Wormald M.R. The solution NMR structure of glucosylated N-glycans involved in the early stages of glycoprotein biosynthesis and folding. EMBO J. 1997, 16:4302-4310.
    • (1997) EMBO J. , vol.16 , pp. 4302-4310
    • Petrescu, A.J.1    Butters, T.D.2    Reinkensmeier, G.3    Petrescu, S.4    Platt, F.M.5    Dwek, R.A.6    Wormald, M.R.7
  • 26
    • 2442505584 scopus 로고    scopus 로고
    • Role of N-linked polymannose oligosaccharides in targeting glycoproteins for endoplasmic reticulum-associated degradation
    • Spiro R.G. Role of N-linked polymannose oligosaccharides in targeting glycoproteins for endoplasmic reticulum-associated degradation. Cell. Mol. Life Sci. 2004, 61:1025-1041.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 1025-1041
    • Spiro, R.G.1


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