@article { ISI:000224957000104,
	title = {In situ extension as an approach for identifying novel alpha-amylase inhibitors},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {279},
	number = {46},
	year = {2004},
	month = {NOV 12},
	pages = {48282-48291},
	abstract = {A new approach for the discovery and subsequent structural elucidation of oligosaccharide-based inhibitors of alpha-amylases based upon autoglucosylation of known alpha-glucosidase inhibitors is presented. This concept, highly analogous to what is hypothesized to occur with acarbose, is demonstrated with the known alpha-glucosidase inhibitor, D-gluconohydroximino-1,5-lactam. This was transformed from an inhibitor of human pancreatic alpha-amylase with a K-i value of 18 mM to a trisaccharide analogue with a K-i value of 25 muM. The three-dimensional structure of this complex was determined by x-ray crystallography and represents the first such structure determined with this class of inhibitors in any alpha-glycosidase. This approach to the discovery and structural analysis of amylase inhibitors should be generally applicable to other endoglucosidases and readily adaptable to a high throughput format.},
	issn = {0021-9258},
	doi = {10.1074/jbc.M406804200},
	author = {Numao, S and Damager, I and Li, CM and Wrodnigg, TM and Begum, A and Overall, CM and BRAYER, GD and Withers, SG}
}
