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Results 71-80 of 131 (Search time: 0.004 seconds).
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PreviewIssue DateTitleAuthor(s)
2007Dissecting the catalytic mechanism of a plant beta-D-glucan glucohydrolase through structural biology using inhibitors and substrate analoguesHrmova, M.; Fincher, G.
2008Sexual and Apomictic Seed Formation in Hieracium Requires the Plant Polycomb-Group Gene fertilization independent endospermMacedo Rodrigues, J.; Tucker, M.; Johnson, S.; Hrmova, M.; Koltunow, A.
1998Crystallization and preliminary X-ray analysis of β-glucan exohydrolase isoenzyme Exol from barley (Hordeum vulgare)Hrmova, M.; Varghese, J.; Hoj, P.; Fincher, G.
2010The genetics, transcriptional profiles, and catalytic properties of UDP-α-D-xylose 4-epimerases from barleyZhang, Q.; Shirley, N.; Burton, R.; Lahnstein, J.; Hrmova, M.; Fincher, G.
2004Molecular modeling of family GH16 glycoside hydrolases: Potential roles for xyloglucan transglucosylases/hydrolases in cell wall modification in the poaceaeStrohmeier, M.; Hrmova, M.; Fischer, M.; Harvey, A.; Fincher, G.; Pleiss, J.
2002Structural basis for broad substrate specificity in higher plant beta-D-glucan glucohydrolasesHrmova, M.; De Gori, R.; Smith, B.; Fairweather, J.; Driguez, H.; Varghese, J.; Fincher, G.
2006Hydrolysis of (1,4)-beta-D-mannans in barley (Hordeum vulgare L.) is mediated by the concerted action of (1,4)-beta-D-mannan endohydrolase and beta-D-mannosidaseHrmova, M.; Burton, R.; Biely, P.; Lahnstein, J.; Fincher, G.
2004Three-dimensional structure of the barley beta-D-glucan glucohydrolase in complex with a transition state mimicHrmova, M.; De Gori, R.; Smith, B.; Vasella, A.; Varghese, J.; Fincher, G.
1995Subsite affinities and disposition of catalytic amino acids in the substrate-binding region of barley 1,3-β-glucanases. Implications in plant-pathogen interactionsHrmova, M.; Garrett, T.; Fincher, G.
2004The synthesis of 3-O-(beta-D-glucopyranosyl)- and 3-O-(beta-laminaribiosyl)-isofagomines, potent inhibitors of a 1,3-beta-D-glucan endo-hydrolaseMacdonald, J.; Hrmova, M.; Fincher, G.; Stick, R.