@article { ISI:000271472300015,
	title = {Structural insight into mammalian sialyltransferases},
	journal = {NATURE STRUCTURAL \& MOLECULAR BIOLOGY},
	volume = {16},
	number = {11},
	year = {2009},
	month = {NOV},
	pages = {1186-1188},
	abstract = {Mammalian cell surfaces are modified by complex arrays of glycoproteins, glycolipids and polysaccharides, many of which terminate in sialic acid and have central roles in essential processes including cell recognition, adhesion and immunogenicity. Sialylation of glycoconjugates is performed by a set of sequence-related enzymes known as sialyltransferases (STs). Here we present the crystal structure of a mammalian ST, porcine ST3Gal-I, providing a structural basis for understanding the mechanism and specificity of these enzymes and for the design of selective inhibitors.},
	issn = {1545-9993},
	doi = {10.1038/nsmb.1685},
	author = {Rao, Francesco V. and Rich, Jamie R. and Rakic, Bojana and Buddai, Sai and Schwartz, Marc F. and Johnson, Karl and Bowe, Caryn and Wakarchuk, Warren W. and DeFrees, Shawn and Withers, Stephen G. and Strynadka, Natalie C. J.}
}
