메뉴 건너뛰기




Volumn 27, Issue 4, 2010, Pages 435-444

Rescue of Drosophila Melanogaster l(2)35Aa lethality is only mediated by polypeptide GalNAc-transferase pgant35A, but not by the evolutionary conserved human ortholog GalNAc-transferase-T11

Author keywords

Drosophila; GalNAc transferase; GALNT11; Glycosyltransferase; Mucin type O glycosylation; Pgant35A

Indexed keywords

GENE PRODUCT; N ACETYLGALACTOSAMINYLTRANSFERASE; PROTEIN GALNT11; PROTEIN PGANT35AA; PROTEIN PGANT7; UNCLASSIFIED DRUG;

EID: 77955614342     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-010-9290-5     Document Type: Article
Times cited : (14)

References (55)
  • 1
    • 84961342241 scopus 로고    scopus 로고
    • Control of Mucin-Type O-Glycosylation: O-Glycan occupancy is directed by substrate specificities of polypeptide GalNAc-transferases
    • Ernst, B. Hart, H. Sinay, P. (eds.), Wiley-VCH Publishers, Weinheim
    • Hassan, H., Bennett, E.P., Mandel, U., Hollingsworth, M.A., Clausen, H.: Control of Mucin-Type O-Glycosylation: O-Glycan occupancy is directed by substrate specificities of polypeptide GalNAc-transferases. In: Ernst, B., Hart, H., Sinay, P. (eds.) Saccharides in chemistry and biology - a comprehension handbook, pp. 273-292. Wiley-VCH Publishers, Weinheim (2000).
    • (2000) Saccharides in Chemistry and Biology - A Comprehension Handbook , pp. 273-292
    • Hassan, H.1    Bennett, E.P.2    Mandel, U.3    Hollingsworth, M.A.4    Clausen, H.5
  • 2
    • 0037234565 scopus 로고    scopus 로고
    • All in the family: The UDP-GalNAc:polypeptide N- acetylgalactosaminyltransferases
    • Ten Hagen, K.G., Fritz, T.A., Tabak, L.A.: All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases. Glycobiology 13 (2002).
    • (2002) Glycobiology , vol.13
    • Ten Hagen, K.G.1    Fritz, T.A.2    Tabak, L.A.3
  • 3
    • 0032568506 scopus 로고    scopus 로고
    • Inactivation of the mouse sperm receptor, mZP3, by site-directed mutagenesis of individual serine residues located at the combining site for sperm
    • Chen, J., Litscher, E.S., Wassarman, P.M.: Inactivation of the mouse sperm receptor, mZP3, by site-directed mutagenesis of individual serine residues located at the combining site for sperm. PNAS 95, 6193-6197 (1998).
    • (1998) PNAS , vol.95 , pp. 6193-6197
    • Chen, J.1    Litscher, E.S.2    Wassarman, P.M.3
  • 4
    • 0037137491 scopus 로고    scopus 로고
    • Roles of mucin-type O-glycans in cell adhesion
    • Fukuda, M.: Roles of mucin-type O-glycans in cell adhesion. Biochim. Biophys. Acta 1573, 394-405 (2002).
    • (2002) Biochim. Biophys. Acta , vol.1573 , pp. 394-405
    • Fukuda, M.1
  • 5
    • 0023753410 scopus 로고
    • Use of a mutant cell line to study the kinetics and function of O-linked glycosylation of low density lipoprotein receptors
    • Kozarsky, K., Kingsley, D., Krieger, M.: Use of a mutant cell line to study the kinetics and function of O-linked glycosylation of low density lipoprotein receptors. Proc. Natl. Acad. Sci. U. S. A. 85, 4335-4339 (1988).
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 4335-4339
    • Kozarsky, K.1    Kingsley, D.2    Krieger, M.3
  • 6
    • 0023807624 scopus 로고
    • Abnormal intracellular sorting of O-linked carbohydrate-deficient interleukin-2 receptors
    • Kozarsky, K.F., Call, S.M., Dower, S.K., Krieger, M.: Abnormal intracellular sorting of O-linked carbohydrate-deficient interleukin- 2 receptors. Mol. Cell Biol. 8, 3357-3363 (1988).
    • (1988) Mol. Cell Biol. , vol.8 , pp. 3357-3363
    • Kozarsky, K.F.1    Call, S.M.2    Dower, S.K.3    Krieger, M.4
  • 7
    • 0008519414 scopus 로고
    • Effects of preventing O-glycosylation on the secretion of human chorionic gonadotropin in Chinese hamster ovary cells
    • Matzuk, M.M., Krieger, M., Corless, C.L., Boime, I.: Effects of preventing O-glycosylation on the secretion of human chorionic gonadotropin in Chinese hamster ovary cells. Proc. Natl. Acad. Sci. U. S. A. 84, 6354-6358 (1987).
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 6354-6358
    • Matzuk, M.M.1    Krieger, M.2    Corless, C.L.3    Boime, I.4
  • 8
    • 0037059830 scopus 로고    scopus 로고
    • Evolution of lutropin to chorionic gonadotropin generates a specific routing signal for apical release in vivo
    • Jablonka-Shariff, A., Garcia-Campayo, V., Boime, I.: Evolution of lutropin to chorionic gonadotropin generates a specific routing signal for apical release in vivo. J. Biol. Chem. 277, 879-882 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 879-882
    • Jablonka-Shariff, A.1    Garcia-Campayo, V.2    Boime, I.3
  • 9
    • 0035824619 scopus 로고    scopus 로고
    • Characteristics and structural requirements of apical sorting of the rat growth hormone through the O-Glycosylated stalk region of intestinal sucraseisomaltase
    • Spodsberg, N., Alfalah, M., Naim, H.Y.: Characteristics and structural requirements of apical sorting of the rat growth hormone through the O-Glycosylated stalk region of intestinal sucraseisomaltase. J. Biol. Chem. 276, 46597-46604 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 46597-46604
    • Spodsberg, N.1    Alfalah, M.2    Naim, H.Y.3
  • 10
    • 0030833432 scopus 로고    scopus 로고
    • OGlycosylation of C-terminal tandem-repeated sequences regulates the secretion of rat pancreatic bile salt-dependent lipase
    • Bruneau, N., Nganga, A., Fisher, E.A., Lombardo, D.: OGlycosylation of C-terminal tandem-repeated sequences regulates the secretion of rat pancreatic bile salt-dependent lipase. J. Biol. Chem. 272, 27353-27361 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 27353-27361
    • Bruneau, N.1    Nganga, A.2    Fisher, E.A.3    Lombardo, D.4
  • 11
    • 0032541183 scopus 로고    scopus 로고
    • Post-translational processing of the insulin-like growth factor-2 precursor. Analysis of O-glycosylation and endoproteolysis
    • Duguay, S.J., Jin, Y., Stein, J., Duguay, A.N., Gardner, P., Steiner, D.F.: Post-translational processing of the insulin-like growth factor-2 precursor. analysis of O-glycosylation and endoproteolysis. J. Biol. Chem. 273, 18443-18451 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 18443-18451
    • Duguay, S.J.1    Jin, Y.2    Stein, J.3    Duguay, A.N.4    Gardner, P.5    Steiner, D.F.6
  • 12
    • 0036061463 scopus 로고    scopus 로고
    • Role of the membrane-proximal O-glycosylation site in sorting of the human receptor for neurotrophins to the apical membrane of MDCK cells
    • Breuza, L., Garcia, M., Delgrossi, M.H., Le Bivic, A.: Role of the membrane-proximal O-glycosylation site in sorting of the human receptor for neurotrophins to the apical membrane of MDCK cells. Exp. Cell Res. 273, 178-186 (2002).
    • (2002) Exp. Cell Res. , vol.273 , pp. 178-186
    • Breuza, L.1    Garcia, M.2    Delgrossi, M.H.3    Le Bivic, A.4
  • 13
    • 0030726211 scopus 로고    scopus 로고
    • The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK cells
    • Yeaman, C., Gall, A.H., Baldwin, A.N., Monlauzeur, L., Bivic, A. L., Rodriguez-Boulan, E.: The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK cells. J. Cell Biol. 139, 929-940 (1997).
    • (1997) J. Cell Biol. , vol.139 , pp. 929-940
    • Yeaman, C.1    Gall, A.H.2    Baldwin, A.N.3    Monlauzeur, L.4    Bivic, A.L.5    Rodriguez-Boulan, E.6
  • 14
    • 0037698348 scopus 로고    scopus 로고
    • Model glycosulfopeptides from P-selectin glycoprotein Ligand-1 require tyrosine sulfation and a core 2-branched O-Glycan to bind to L-selectin
    • Leppanen, A., Yago, T., Otto, V.I., McEver, R.P., Cummings, R.D.: Model glycosulfopeptides from P-selectin glycoprotein Ligand-1 require tyrosine sulfation and a core 2-branched O-Glycan to bind to L-selectin. J. Biol. Chem. 278, 26391-26400 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 26391-26400
    • Leppanen, A.1    Yago, T.2    Otto, V.I.3    McEver, R.P.4    Cummings, R.D.5
  • 15
    • 0036775765 scopus 로고    scopus 로고
    • Selectins: Lectins that initiate cell adhesion under flow
    • McEver, R.P.: Selectins: lectins that initiate cell adhesion under flow. Curr. Opin. Cell Biol. 14, 581-586 (2002).
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 581-586
    • McEver, R.P.1
  • 16
    • 0141756182 scopus 로고    scopus 로고
    • Glycan-dependent leukocyte adhesion and recruitment in inflammation
    • Lowe, J.B.: Glycan-dependent leukocyte adhesion and recruitment in inflammation. Curr. Opin. Cell Biol. 15, 531-538 (2003).
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 531-538
    • Lowe, J.B.1
  • 17
    • 0029989766 scopus 로고    scopus 로고
    • Possible roles of tumor-associated carbohydrate antigens
    • Fukuda, M.: Possible roles of tumor-associated carbohydrate antigens. Cancer Res 56, 2237-2244 (1996).
    • (1996) Cancer Res , vol.56 , pp. 2237-2244
    • Fukuda, M.1
  • 18
    • 77955620768 scopus 로고    scopus 로고
    • Recent insights into the biological roles of mucin-type O-glycosylation
    • Tian, E., Ten Hagen, K.G.: Recent insights into the biological roles of mucin-type O-glycosylation. Glycoconj. J. (2008).
    • (2008) Glycoconj. J.
    • Tian, E.1    Ten Hagen, K.G.2
  • 20
    • 0030035111 scopus 로고    scopus 로고
    • cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D- galactosamine polypeptide N-acetylgalactosaminyltransfersae, GalNAc-T3
    • Bennett, E.P., Hassan, H., Clausen, H.: cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine polypeptide N- acetylgalactosaminyltransfersae, GalNAc-T3. J. Biol. Chem. 271, 17006-17012 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 17006-17012
    • Bennett, E.P.1    Hassan, H.2    Clausen, H.3
  • 21
    • 0034491921 scopus 로고    scopus 로고
    • Diverse spatial expression patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyl-transferase family member mRNAs during mouse development
    • Kingsley, P.D., Hagen, K.G.T., Maltby, K.M., Zara, J., Tabak, L. A.: Diverse spatial expression patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyl-transferase family member mRNAs during mouse development. Glycobiology 10, 1317-1323 (2000).
    • (2000) Glycobiology , vol.10 , pp. 1317-1323
    • Kingsley, P.D.1    Hagen, K.G.T.2    Maltby, K.M.3    Zara, J.4    Tabak, L.A.5
  • 26
    • 0037151043 scopus 로고    scopus 로고
    • A UDP-GalNAc:Polypeptide NAcetylgalactosaminyltransferase is essential for viability in Drosophila melanogaster
    • Hagen, K.G.T., Tran, D.T.: A UDP-GalNAc:Polypeptide NAcetylgalactosaminyltransferase is essential for viability in Drosophila melanogaster. J. Biol. Chem. 277, 22616-22622 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 22616-22622
    • Hagen, K.G.T.1    Tran, D.T.2
  • 28
    • 33846992688 scopus 로고    scopus 로고
    • A UDP-GalNAc: Polypeptide Nacetylgalactosaminyltransferase is required for epithelial tube formation
    • Tian, E., Ten Hagen, K.G.: A UDP-GalNAc:polypeptide Nacetylgalactosaminyltransferase is required for epithelial tube formation. J. Biol. Chem. 282, 606-614 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 606-614
    • Tian, E.1    Ten Hagen, K.G.2
  • 29
    • 0032980501 scopus 로고    scopus 로고
    • Microsatellite instability in Drosophila spellchecker1 (MutS homolog) mutants
    • Flores, C., Engels, W.: Microsatellite instability in Drosophila spellchecker1 (MutS homolog) mutants. Proc. Natl. Acad. Sci. U. S. A. 96, 2964-2969 (1999).
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 2964-2969
    • Flores, C.1    Engels, W.2
  • 30
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand, A.H., Perrimon, N.: Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 118, 401-415 (1993).
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 32
    • 33947198189 scopus 로고    scopus 로고
    • The lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate binding specificity for GalNAc: Lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O- glycosylation
    • Wandall, H.H., Irazoqui, F., Tarp, M.A., Bennett, E.P., Mandel, U., Takeuchi, H., Kato, K., Irimura, T., Suryanarayanan, G., Hollingsworth, M.A., Clausen, H., The lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate binding specificity for GalNAc: lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O- glycosylation. Glycobiology (2007).
    • (2007) Glycobiology
    • Wandall, H.H.1    Irazoqui, F.2    Tarp, M.A.3    Bennett, E.P.4    Mandel, U.5    Takeuchi, H.6    Kato, K.7    Irimura, T.8    Suryanarayanan, G.9    Hollingsworth, M.A.10    Clausen, H.11
  • 33
    • 0036111641 scopus 로고    scopus 로고
    • HSPG modification by the secreted enzyme Notum shapes the wingless morphogen gradient
    • Giraldez, A.J., Copley, R.R., Cohen, S.M.: HSPG modification by the secreted enzyme Notum shapes the wingless morphogen gradient. Dev. Cell. 2, 667-676 (2002).
    • (2002) Dev. Cell. , vol.2 , pp. 667-676
    • Giraldez, A.J.1    Copley, R.R.2    Cohen, S.M.3
  • 34
    • 0042317189 scopus 로고    scopus 로고
    • Functional characterization and expression analysis of members of the UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase family from Drosophila melanogaster
    • Ten Hagen, K.G., Tran, D.T., Gerken, T.A., Stein, D.S., Zhang, Z.: Functional characterization and expression analysis of members of the UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase family from Drosophila melanogaster. J. Biol. Chem. 278, 35039- 35048 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 35039-35048
    • Ten Hagen, K.G.1    Tran, D.T.2    Gerken, T.A.3    Stein, D.S.4    Zhang, Z.5
  • 35
    • 22544465243 scopus 로고    scopus 로고
    • Human SRCAP and Drosophila melanogaster DOM are homologs that function in the notch signaling pathway
    • Eissenberg, J.C., Wong, M., Chrivia, J.C.: Human SRCAP and Drosophila melanogaster DOM are homologs that function in the notch signaling pathway. Mol. Cell Biol. 25, 6559-6569 (2005).
    • (2005) Mol. Cell Biol. , vol.25 , pp. 6559-6569
    • Eissenberg, J.C.1    Wong, M.2    Chrivia, J.C.3
  • 36
    • 27644514167 scopus 로고    scopus 로고
    • Human c-Myc isoforms differentially regulate cell growth and apoptosis in Drosophila melanogaster
    • Benassayag, C., Montero, L., Colombie, N., Gallant, P., Cribbs, D., Morello, D.: Human c-Myc isoforms differentially regulate cell growth and apoptosis in Drosophila melanogaster. Mol. Cell Biol. 25, 9897-9909 (2005).
    • (2005) Mol. Cell Biol. , vol.25 , pp. 9897-9909
    • Benassayag, C.1    Montero, L.2    Colombie, N.3    Gallant, P.4    Cribbs, D.5    Morello, D.6
  • 38
    • 0031404510 scopus 로고    scopus 로고
    • Fold recognition and molecular modeling of a lectin-like domain in UDP-GalNac: Polypeptide N-acetylgalactosaminyltransferases
    • Imberty, A., Piller, V., Piller, F., Breton, C.: Fold recognition and molecular modeling of a lectin-like domain in UDP- GalNac: polypeptide N-acetylgalactosaminyltransferases. Protein Eng. 10, 1353-1356 (1997).
    • (1997) Protein Eng. , vol.10 , pp. 1353-1356
    • Imberty, A.1    Piller, V.2    Piller, F.3    Breton, C.4
  • 39
    • 33646828699 scopus 로고    scopus 로고
    • Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:Polypeptide alpha-N-acetylgalactosaminyltransferase-2
    • Fritz, T.A., Raman, J., Tabak, L.A.:Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2. J. Biol. Chem. (2006).
    • (2006) J. Biol. Chem.
    • Fritz, T.A.1    Raman, J.2    Tabak, L.A.3
  • 41
    • 0036435680 scopus 로고    scopus 로고
    • Function of the lectin domain of polypeptide N- acetylgalactosaminyltransferase 1
    • Tenno, M., Kezdy, F.J., Elhammer, A.P., Kurosaka, A.: Function of the lectin domain of polypeptide N-acetylgalactosaminyltransferase 1. Biochem. Biophys. Res. Commun. 298, 755-759 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.298 , pp. 755-759
    • Tenno, M.1    Kezdy, F.J.2    Elhammer, A.P.3    Kurosaka, A.4
  • 42
    • 0037032994 scopus 로고    scopus 로고
    • The lectin domain of UDP-GalNAc:Polypeptide N-Acetylgalactosaminyl transferase 1 is involved in O-Glycosylation of a polypeptide with multiple acceptor sites
    • Tenno, M., Saeki, A., Kezdy, F.J., Elhammer, A.P., Kurosaka, A.: The lectin domain of UDP-GalNAc:Polypeptide N-Acetylgalactosaminyl transferase 1 is involved in O-Glycosylation of a polypeptide with multiple acceptor sites. J. Biol. Chem. 277, 47088-47096 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 47088-47096
    • Tenno, M.1    Saeki, A.2    Kezdy, F.J.3    Elhammer, A.P.4    Kurosaka, A.5
  • 43
    • 53149142512 scopus 로고    scopus 로고
    • The catalytic and lectin domains of UDPGalNAc :Polypeptide alpha-N-Acetylgalactosaminyltransferase function in concert to direct glycosylation site selection
    • M803387200
    • Raman, J., Fritz, T.A., Gerken, T.A., Jamison, O., Live, D., Lu, M., Tabak, L.A.: The catalytic and lectin domains of UDPGalNAc :Polypeptide alpha-N-Acetylgalactosaminyltransferase function in concert to direct glycosylation site selection. J. Biol. Chem. (2008) M803387200.
    • (2008) J. Biol. Chem.
    • Raman, J.1    Fritz, T.A.2    Gerken, T.A.3    Jamison, O.4    Live, D.5    Lu, M.6    Tabak, L.A.7
  • 44
    • 34948818346 scopus 로고    scopus 로고
    • A serial lectin approach to the mucin-type O-glycoproteome of Drosophila melanogaster S2 cells
    • Schwientek, T., Mandel, U., Roth, U., Muller, S., Hanisch, F.G.: A serial lectin approach to the mucin-type O-glycoproteome of Drosophila melanogaster S2 cells. Proteomics 7, 3264-3277 (2007).
    • (2007) Proteomics , vol.7 , pp. 3264-3277
    • Schwientek, T.1    Mandel, U.2    Roth, U.3    Muller, S.4    Hanisch, F.G.5
  • 45
    • 0027370882 scopus 로고
    • Specific sequences in the signal anchor of the beta-galactoside alpha-2, 6-sialyltransferase are not essential for Golgi localization. Membrane flanking sequences may specify Golgi retention
    • Dahdal, R.Y., Colley, K.J.: Specific sequences in the signal anchor of the beta-galactoside alpha-2, 6-sialyltransferase are not essential for Golgi localization. Membrane flanking sequences may specify Golgi retention. J. Biol. Chem. 268, 26310-26319 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 26310-26319
    • Dahdal, R.Y.1    Colley, K.J.2
  • 46
    • 0024431691 scopus 로고
    • Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation
    • Paulson, J.C., Colley, K.J.: Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation. J. Biol. Chem. 264, 17615-17618 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 17615-17618
    • Paulson, J.C.1    Colley, K.J.2
  • 48
    • 0037193464 scopus 로고    scopus 로고
    • Characterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and function
    • Ungar, D., Oka, T., Brittle, E.E., Vasile, E., Lupashin, V.V., Chatterton, J.E., Heuser, J.E., Krieger, M., Waters, M.G.: Characterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and function. J Cell Biol. 157, 405-415 (2002).
    • (2002) J Cell Biol. , vol.157 , pp. 405-415
    • Ungar, D.1    Oka, T.2    Brittle, E.E.3    Vasile, E.4    Lupashin, V.V.5    Chatterton, J.E.6    Heuser, J.E.7    Krieger, M.8    Waters, M.G.9
  • 49
    • 47749141468 scopus 로고    scopus 로고
    • Signal-mediated dynamic retention of glycosyltransferases in the Golgi
    • Tu, L., Tai, W.C.S., Chen, L., Banfield, D.K.: Signal-mediated dynamic retention of glycosyltransferases in the Golgi. Science 321, 404-407 (2008).
    • (2008) Science , vol.321 , pp. 404-407
    • Tu, L.1    Tai, W.C.S.2    Chen, L.3    Banfield, D.K.4
  • 52
    • 0141890299 scopus 로고    scopus 로고
    • Ganglioside glycosyltransferases organize in distinct multienzyme complexes in CHO-K1 cells
    • Giraudo, C.G., Maccioni, H.J.: Ganglioside glycosyltransferases organize in distinct multienzyme complexes in CHO-K1 cells. J Biol. Chem. 278, 40262-40271 (2003).
    • (2003) J Biol. Chem. , vol.278 , pp. 40262-40271
    • Giraudo, C.G.1    Maccioni, H.J.2
  • 54
    • 58149343579 scopus 로고    scopus 로고
    • Glycobiology on the fly: Developmental and mechanistic insights from Drosophila
    • Ten Hagen, K.G., Zhang, L., Tian, E., Zhang, Y.: Glycobiology on the fly: developmental and mechanistic insights from Drosophila. Glycobiology 19, 102-111 (2009).
    • (2009) Glycobiology , vol.19 , pp. 102-111
    • Ten Hagen, K.G.1    Zhang, L.2    Tian, E.3    Zhang, Y.4
  • 55
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F., Higgins, D.G.: The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25, 4876-4882 (1997).
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.