Chapter 11

Where to Start

Glycochemistry and glycobiology. A series of review articles. 2007. Nature 446:999–1051.

Maeder, T. 2002. Sweet medicines. Sci. Am. 287(1):40–47.

Freeze, H. H. 2013. Understanding human glycosylation disorders. J. Biol. Chem. 288:6936–6945.

Coutinho, M. F., Prata M., J., and Alves, S. 2012. Mannose-6-phosphate pathway: A review on its role in lysosomal function and dysfunction. Mol. Gen. Metab. 105:542–550.

Books

Varki, A., Cummings, R., Esko, J., Freeze, H., Stanley, P., Bertozzi, C., Hart, G., and Etzler, M. E. 2009. Essentials of Glycobiology (2d ed.). Cold Spring Harbor Laboratory Press.

Stick, R. V., and Williams, S. 2008. Carbohydrates: The Essential Molecules of Life (2d ed.). Elsevier Science.

Sansome, C., and Markman, O. 2007. Glycobiology. Scion.

Lindhorst, T. K. 2007. Essentials of Carbohydrate Chemistry and Biochemistry (3d ed.). Wiley-VCH.

Taylor, M. E. 2006. Introduction to Glycobiology (2d ed.). Oxford University Press.

Glycoproteins

Tran, D. T., and Hagen, K. G. T. 2013. Mucin-type O-glycosylation during development. J. Biol. Chem. 288:6921–6929.

Gill, D. J., Clausen H., and Bard, F. 2011. Location, location, location: New insights into O-GalNAc protein glycosylation. Trends Cell Biol. 21:149–158.

Foley, R. N. 2008. Erythropoietin: Physiology and molecular mechanisms. Heart Failure Rev. 13:404–414.

Fisher, J. W. 2003. Erythropoietin: Physiology and pharmacology update. Exp. Biol. Med. 228:1–14.

Cheetham, J. C., Smith, D. M., Aoki, K. H., Stevenson, J. L., Hoeffel, T. J., Syed, R. S., Egrie, J., and Harvey, T. S. 1998. NMR structure of human erythropoietin and a comparison with its receptor bound conformation. Nat. Struct. Biol. 5:861–866.

Hattrup, C. L., and Gendler, S. J. 2008. Structure and function of the cell surface (tethered) mucins. Annu. Rev. Physiol. 70:431–457.

Thorton, D. J., Rousseau, K., and McGuckin, M. A. 2008. Structure and function of mucins in airways mucus. Annu. Rev. Physiol. 70:459–486.

Rose, M. C., and Voynow, J. A. 2007. Respiratory tract mucin genes and mucin glycoproteins in health and disease. Physiol. Rev. 86:245–278.

Lamoureux, F., Baud’huin, M., Duplomb, L., Heymann, D., and Rédini, F. 2007. Proteoglycans: Key partners in bone cell biology. Bioessays 29:758–771.

Carraway, K. L., Funes, M., Workman, H. C., and Sweeney, C. 2007. Contribution of membrane mucins to tumor progression through modulation of cellular growth signaling pathways. Curr. Top. Dev. Biol. 78:1–22.

Yan, A., and Lennarz, W. J. 2005. Unraveling the mechanism of protein N-glycosylation. J. Biol. Chem. 280:3121–3124.

Pratta, M. A., Yao, W., Decicco, C., Tortorella, M., Liu, R.-Q., Copeland, R. A., Magolda, R., Newton, R. C., Trzaskos, J. M., and Arner, E. C. 2003. Aggrecan protects cartilage collagen from proteolytic cleavage. J. Biol. Chem. 278:45539–45545.

Glycosyltransferases

Wells, L. 2013. The O-mannosylation pathway: Glycosyltransferases and proteins implicated in congenital muscular dystrophy. J. Biol. Chem. 288:6930–6935.

Vocadlo, D. J. 2012. O-GlcNAc processing enzymes: Catalytic mechanisms, substrate specificity, and enzyme regulation. Curr. Opin. Chem. Biol. 16:488–497.

Hurtado-Guerrero, R., and Davies, G. J. 2012. Recent structural and mechanistic insights into post-translational enzymatic glycosylation. Curr. Opin. Chem. Biol. 16:479–487.

Hart, G. W., Slawson, C., Ramirez-Correa, G., and Lagerlof, O. 2011. Cross talk between O-GlcNAcylation and phosphorylation: Roles in signaling, transcription, and chronic disease. Annu. Rev. Biochem. 80:825–858.

Lazarus, M. B., Nam, Y., Jiang, J., Sliz, P., and Walker, S. 2011. Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 469:564–569.

Lee, W.-S., Kang, C., Drayna, D., and Kornfeld, S. 2011. Analysis of mannose 6-phosphate uncovering enzyme mutations associated with persistent stuttering. J. Biol. Chem. 286:39786–39793.

Lairson, L. L., Henrissat, B., Davies, G. J., and Withers, S. G. 2008. Glycosyltransferases: Structures, functions and mechanisms. Annu. Rev. Biochem. 77:521–555.

Qasba, P. K., Ramakrishnan, B., and Boeggeman, E. 2005. Substrate-induced conformational changes in glycosyltransferases. Trends Biochem. Sci. 30:53–62.

Carbohydrate-Binding Proteins

Gabius, H.-J., André, S., Jiménez-Barbero, J., Romero, A., and Solís, D. 2011. From lectin structure to functional glycomics: Principles of the sugar code. Trends Biochem. Sci. 36:298–313.

Wasserman, P. M. 2008. Zona pellucida glycoproteins. J. Biol. Chem. 283:24285–24289.

Sharon, N. 2008. Lectins: Past, present and future. Biochem. Soc. Trans. 36:1457–1460.

Balzarini, J. 2007. Targeting the glycans of glycoproteins: A novel paradigm for antiviral therapy. Nat. Rev. Microbiol. 5:583–597.

Sharon, N. 2007. Lectins: Carbohydrate-specific reagents and biological recognition molecules. J. Biol. Chem. 282:2753–2764.

Stevens, J., Blixt, O., Tumpey, T. M., Taubenberger, J. K., Paulson, J. C., and Wilson, I. A. 2006. Structure and receptor specificity of hemagglutinin from an H5N1 influenza virus. Science 312:404–409.

B11

Cambi, A., Koopman, M., and Figdor, C. G. 2005. How C-type lectins detect pathogens. Cell. Microbiol. 7:481–488.

Clothia, C., and Jones, E. V. 1997. The molecular structure of cell adhesion molecules. Annu. Rev. Biochem. 66:823–862.

Bouckaert, J., Hamelryck, T., Wyns, L., and Loris, R. 1999. Novel structures of plant lectins and their complexes with carbohydrates. Curr. Opin. Struct. Biol. 9:572–577.

Weis, W. I., and Drickamer, K. 1996. Structural basis of lectin–carbohydrate recognition. Annu. Rev. Biochem. 65:441–473.

Carbohydrate Sequencing

Venkataraman, G., Shriver, Z., Raman, R., and Sasisekharan, R. 1999. Sequencing complex polysaccharides. Science 286:537–542.

Zhao, Y., Kent, S. B. H., and Chait, B. T. 1997. Rapid, sensitive structure analysis of oligosaccharides. Proc. Natl. Acad. Sci. U.S.A. 94:1629–1633.

Rudd, P. M., Guile, G. R., Küster, B., Harvey, D. J., Opdenakker, G., and Dwek, R. A. 1997. Oligosaccharide sequencing technology. Nature 388:205–207.