Search


Current filters:

Start a new search
Add filters:

Use filters to refine the search results.


Results 31-40 of 58 (Search time: 0.004 seconds).
Item hits:
PreviewIssue DateTitleAuthor(s)
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.
2003Bifunctional family 3 glycoside hydrolases from barley with alpha-L-arabinofuranosidase and beta-D-xylosidase activity - Characterization, primary structures, and COOH-terminal processingLee, R.; Hrmova, M.; Burton, R.; Lahnstein, J.; Fincher, G.
1998Substrate binding and catalytic mechanism of a barley b-D-glucosidase (1,4)-b-D-glucan exohydrolaseHrmova, M.; MacGregor, E.; Biely, P.; Stewart, R.; Fincher, G.
2004Members of a new group of chitinase-like genes are expressed preferentially in cotton cells with secondary wallsZhang, D.; Hrmova, M.; Wan, C.; Wu, C.; Balzen, J.; Cai, W.; Wang, J.; Densmore, L.; Fincher, G.; Zhang, H.; Haigler, C.
2003Biochemical evidence linking a putative callose synthase gene with (1→3)-β-d-glucan biosynthesis in barleyLi, J.; Burton, R.; Harvey, A.; Hrmova, M.; Wardak, A.; Stone, B.; Fincher, G.
2005Structural rationale for low-nanomolar binding of transition state mimics to a family GH3 β-D-glucan glucohydrolase from barleyHrmova, M.; Streltsov, V.; Smith, B.; Vasella, A.; Varghese, J.; Fincher, G.