A family of UDP-GalNAc: polypeptide N-acetylgalactosaminyl-transferases control the initiation of mucin-type O-linked glycosylation.
暂无分享,去创建一个
[1] H. Ikenaga,et al. Cloning and expression of a porcine UDP-GalNAc: polypeptide N-acetylgalactosaminyl transferase. , 1995, Glycoconjugate journal.
[2] L. Tabak,et al. Purification, cloning, and expression of a bovine UDP-GalNAc: polypeptide N-acetyl-galactosaminyltransferase. , 1993, The Journal of biological chemistry.
[3] M. Gross,et al. N-acetylgalactosamine glycosylation of MUC1 tandem repeat peptides by pancreatic tumor cell extracts. , 1994, Cancer research.
[4] U. Galili,et al. Defining the minimal size of catalytically active primate alpha 1,3 galactosyltransferase: structure-function studies on the recombinant truncated enzyme. , 1994, Glycobiology.
[5] C. Hauer,et al. Novel, Specific O-Glycosylation of Secreted Flavobacterium meningosepticum Proteins. , 1995, The Journal of Biological Chemistry.
[6] H. Bussey,et al. Protein O-Glycosylation in Yeast , 1995, The Journal of Biological Chemistry.
[7] E. Berger,et al. The molecular and cell biology of glycosyltransferases. , 1993, Biochimica et biophysica acta.
[8] R. Hill,et al. Purification and characterization of a UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase specific for glycosylation of threonine residues. , 1992, The Journal of biological chemistry.
[9] K. Brew,et al. Structure and function in galactosyltransferase. Sequence locations of alpha-lactalbumin binding site, thiol groups, and disulfide bond. , 1991, The Journal of biological chemistry.
[10] M. Gross,et al. Influence of acceptor substrate primary amino acid sequence on the activity of human UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase. Studies with the MUC1 tandem repeat. , 1994, The Journal of biological chemistry.
[11] F. Homa,et al. Isolation and expression of a cDNA clone encoding a bovine UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase. , 1993, The Journal of biological chemistry.
[12] M. Fukuda,et al. Genomic organization of core 2 and I branching beta-1,6-N-acetylglucosaminyltransferases. Implication for evolution of the beta-1,6-N-acetylglucosaminyltransferase gene family. , 1995, Glycobiology.
[13] L. Tabak,et al. A Comparison of Serine and Threonine O-Glycosylation by UDP-GaINAc:Polypeptide N-Acetylgalactosaminyltransferase , 1993, Journal of dental research.
[14] M. Fukuda,et al. Biosynthesis of truncated O-glycans in the T cell line Jurkat. Localization of O-glycan initiation. , 1990, The Journal of biological chemistry.
[15] H. Wasteneys,et al. THE ENZYMATIC SYNTHESIS OF PROTEIN , 1930 .
[16] L. Tabak,et al. Charge Distribution of Flanking Amino Acids Influences O-Glycan Acquisition in Vivo(*) , 1996, The Journal of Biological Chemistry.
[17] S. Elliott,et al. Structural requirements for addition of O-linked carbohydrate to recombinant erythropoietin. , 1994, Biochemistry.
[18] J. Roth. Cytochemical localization of terminal N-acetyl-D-galactosamine residues in cellular compartments of intestinal goblet cells: implications for the topology of O-glycosylation , 1984, The Journal of cell biology.
[19] K L Williams,et al. Towards characterizing O-glycans: the relative merits of in vivo and in vitro approaches in seeking peptide motifs specifying O-glycosylation sites. , 1994, Glycobiology.
[20] R. Hill,et al. Subcellular localization of the UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary gland. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[21] K. Drickamer. A conserved disulphide bond in sialyltransferases. , 1993, Glycobiology.
[22] D. Weghuis,et al. Genomic cloning of the human histo-blood group ABO locus. , 1995, Biochemical and biophysical research communications.
[23] H. Schachter,et al. Control of glycoprotein synthesis. Purification of UDP-N-acetylglucosamine:alpha-D-mannoside beta 1-2 N-acetylglucosaminyltransferase II from rat liver. , 1987, The Journal of biological chemistry.
[24] A. Shilatifard,et al. gp160 of HIV-I synthesized by persistently infected Molt-3 cells is terminally glycosylated: evidence that cleavage of gp160 occurs subsequent to oligosaccharide processing. , 1991, Archives of biochemistry and biophysics.
[25] H. Hauri,et al. Localization of O-glycan initiation, sphingomyelin synthesis, and glucosylceramide synthesis in Vero cells with respect to the endoplasmic reticulum-Golgi intermediate compartment. , 1994, The Journal of biological chemistry.
[26] F. Homa,et al. Organization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase gene and a related processed pseudogene. , 1996, Glycobiology.
[27] J. Lowe,et al. Molecular cloning of a fourth member of a human alpha (1,3)fucosyltransferase gene family. Multiple homologous sequences that determine expression of the Lewis x, sialyl Lewis x, and difucosyl sialyl Lewis x epitopes. , 1992, The Journal of biological chemistry.
[28] E. Eylar,et al. Glycoprotein biosynthesis: studies on the receptor specificity of the polypeptidyl: N-acetylgalactosaminyl transferase from bovine submaxillary glands. , 1968, Archives of biochemistry and biophysics.
[29] L. Tabak,et al. Cloning and sequence homology of a rat UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase. , 1995, Glycoconjugate journal.
[30] S. Roseman,et al. Enzymatic synthesis of the protein-hexosamine linkage in sheep submaxillary mucin. , 1967, The Journal of biological chemistry.
[31] Reed J. Harris,et al. O-linked fucose and other post-translational modifications unique to EGF modules. , 1993, Glycobiology.
[32] E. Eylar,et al. Glycoprotein biosynthesis: the purification and characterization of a polypeptide. N-acetylgalactosaminyl transferase from bovine submaxillary glands. , 1969, Archives of biochemistry and biophysics.
[33] F. Homa,et al. cDNA cloning, expression, and chromosomal localization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase. , 1995, Journal of biochemistry.
[34] Y. Wang,et al. Identification of functional cysteine residues in human galactosyltransferase. , 1994, Biochemical and biophysical research communications.
[35] R. Hill,et al. The acceptor substrate specificity of porcine submaxillary UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase is dependent on the amino acid sequences adjacent to serine and threonine residues. , 1993, The Journal of biological chemistry.
[36] A. Varki,et al. Biological roles of oligosaccharides: all of the theories are correct , 1993, Glycobiology.
[37] S. Bonatti,et al. Post-translational processing of an O-glycosylated protein, the human CD8 glycoprotein, during the intracellular transport to the plasma membrane. , 1992, The Journal of biological chemistry.
[38] J. Perez-Vilar,et al. Presence of terminal N-acetylgalactosamine residues in subregions of the endoplasmic reticulum is influenced by cell differentiation in culture. , 1991, The Journal of biological chemistry.
[39] R. Parekh. Site-specific protein glycosylation , 1994 .
[40] J. Paulson,et al. Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation. , 1989, The Journal of biological chemistry.
[41] S. Kornfeld,et al. Purification and characterization of UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase from bovine colostrum and murine lymphoma BW5147 cells. , 1986, The Journal of biological chemistry.
[42] P. Roepstorff,et al. UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. Identification and separation of two distinct transferase activities. , 1995, The Journal of biological chemistry.
[43] F. Hanisch,et al. Studies on the order and site specificity of GalNAc transfer to MUC1 tandem repeats by UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells. , 1995, European journal of biochemistry.
[44] T. Springer. Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm , 1994, Cell.
[45] D. Joziasse. Mammalian glycosyltransferases: genomic organization and protein structure. , 1992, Glycobiology.
[46] L. Tabak,et al. The influence of flanking sequence on the O-glycosylation of threonine in vitro. , 1992, The Journal of biological chemistry.
[47] G von Heijne,et al. Amino acid distributions around O-linked glycosylation sites. , 1991, The Biochemical journal.
[48] J. Tooze,et al. Site of addition of N-acetyl-galactosamine to the E1 glycoprotein of mouse hepatitis virus-A59 , 1988, The Journal of cell biology.
[49] L. Tabak,et al. T-cell-specific deletion of a polypeptide N-acetylgalactosaminyl-transferase gene by site-directed recombination. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[50] S. Rosen,et al. Biosynthesis of GlyCAM-1, a Mucin-like Ligand for L-Selectin (*) , 1995, The Journal of Biological Chemistry.
[51] R. Poorman,et al. The specificity of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase as inferred from a database of in vivo substrates and from the in vitro glycosylation of proteins and peptides. , 1993, The Journal of biological chemistry.
[52] J. Paulson,et al. Polymerase chain reaction cloning of a developmentally regulated member of the sialyltransferase gene family. , 1993, The Journal of biological chemistry.
[53] C. A. Thomas,et al. Molecular cloning. , 1977, Advances in pathobiology.
[54] K L Williams,et al. Glycosylation sites identified by detection of glycosylated amino acids released from Edman degradation: the identification of Xaa-Pro-Xaa-Xaa as a motif for Thr-O-glycosylation. , 1991, Biochemical and biophysical research communications.
[55] G. Hart,et al. Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase. , 1992, The Journal of biological chemistry.
[56] L. Tabak,et al. The influence of flanking sequences on O-glycosylation. , 1991, Biochemical and biophysical research communications.
[57] James R. Eshleman,et al. The Hydroxy Amino Acid in an Asn-X-Ser/Thr Sequon Can Influence N-Linked Core Glycosylation Efficiency and the Level of Expression of a Cell Surface Glycoprotein (*) , 1995, The Journal of Biological Chemistry.
[58] G. Palade,et al. Endoplasmic reticulum-through-Golgi transport assay based on O-glycosylation of native glycophorin in permeabilized erythroleukemia cells: role for Gi3. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[59] N. Tjandra,et al. Biophysical characterization of one-, two-, and three-tandem repeats of human mucin (muc-1) protein core. , 1993, Cancer research.
[60] S. Roseman. The synthesis of complex carbohydrates by multiglycosyltransferase systems and their potential function in intercellular adhesion. , 1970, Chemistry and physics of lipids.
[61] T. Kawasaki,et al. Purification and characterization of UDP-GalNAc:polypeptide N-acetylgalactosamine transferase from an ascites hepatoma, AH 66. , 1982, The Journal of biological chemistry.
[62] T. Yang-Feng,et al. Assignment of two human alpha-1,3-galactosyltransferase gene sequences (GGTA1 and GGTA1P) to chromosomes 9q33-q34 and 12q14-q15. , 1992, Genomics.
[63] W. Tanner,et al. PMT1, the gene for a key enzyme of protein O-glycosylation in Saccharomyces cerevisiae. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[64] J. Paulson,et al. The Sialyltransferase Sialylmotif Participates in Binding the Donor Substrate CMP-NeuAc (*) , 1995, The Journal of Biological Chemistry.
[65] N. Sharon,et al. Protein glycosylation. Structural and functional aspects. , 1993, European journal of biochemistry.
[66] R. Hill,et al. The subcellular localization of apomucin and nonreducing terminal N-acetylgalactosamine in porcine submaxillary glands. , 1988, The Journal of biological chemistry.