Biosynthesis and Function of ß 1,6 Branched Mucin-Type Glycans
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Springer US
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http://link.springer.com/content/pdf/10.1007/978-1-4615-1267-7_19
Reference167 articles.
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2. Elhammer, A.P., Poorman, R.A., Brown, E., Maggiora, L.L., Hoogerheide, J.G. and Kezdy, F.J. (1993) The specificity of UDP-GaINAc:polypeptide N-acetylgalactosaminyltransferase as inferred from a database of in vivo substrates and from the in vitro glycosylation of proteins and peptides. J. Biol. Chem. 268, 10029–10038.
3. Wang, Y., Agrwal, N., Eckhardt, A.E., Stevens, R.D. and Hill, R.L. (1993) The acceptor specificity of porcine submaxillary UDP-GaINAc:polypeptide N-acetylgalactosaminyltransferase is dependent on the amino acid sequences adjacent to serine and threonine residues. J. Biol. Chem. 268, 22979–22983.
4. Wandall, H.H., Hassan, H., Mirgorodskaya, E., Kristensen, A.K., Roepstorff, P., Bennett, E.P., Nielsen, P.A., Hollingsworth, M.A., Burchell, J., Taylor-Papasimitriou, J., and Clausen, H. (1997) Substrate specificities of three members of the human UDP- N-acetyl-a-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase Family, GaINAc-T1, -T2, and -T3. J. Biol. Chem. 272, 23503–23514.
5. Nishimori, I., Johnson, N.R., Sanderson, S.D., Perini, F., Mountjoy, K., Cerny, R.L., Gross, M.L. and Hollingsworth, M.A. (1994) 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. J. Biol. Chem. 269, 16123–16130.
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