David Rose
David Rose
Professor of Biology, University of Waterloo
Bestätigte E-Mail-Adresse bei - Startseite
Zitiert von
Zitiert von
Indole-3-acetic acid in plant–microbe interactions
D Duca, J Lorv, CL Patten, D Rose, BR Glick
Antonie Van Leeuwenhoek 106, 85-125, 2014
Recognition of a cell-surface oligosaccharide of pathogenic Salmonella by an antibody Fab fragment
M Cygler, DR Rose, DR Bundle
Science 253 (5018), 442-445, 1991
Structure of yeast triosephosphate isomerase at 1.9-. ANG. resolution
E Lolis, T Alber, RC Davenport, D Rose, FC Hartman, GA Petsko
Biochemistry 29 (28), 6609-6618, 1990
Human intestinal maltase–glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity
L Sim, R Quezada-Calvillo, EE Sterchi, BL Nichols, DR Rose
Journal of Molecular Biology 375 (3), 782-792, 2008
Structure of Golgi α-mannosidase II: a target for inhibition of growth and metastasis of cancer cells
JMH Van Den Elsen, DA Kuntz, DR Rose
The EMBO Journal 20 (12), 3008-3017, 2001
Crystallographic observation of a covalent catalytic intermediate in a β-glycosidase
A White, D Tull, K Johns, SG Withers, DR Rose
Nature structural biology 3 (2), 149-154, 1996
Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains
L Sim, C Willemsma, S Mohan, HY Naim, BM Pinto, DR Rose
Journal of Biological Chemistry 285 (23), 17763-17770, 2010
Crystal structure of the catalytic domain of the. beta.-1, 4-glycanase Cex from Cellulomonas fimi
A White, SG Withers, NR Gilkes, DR Rose
Biochemistry 33 (42), 12546-12552, 1994
New glucosidase inhibitors from an ayurvedic herbal treatment for type 2 diabetes: structures and inhibition of human intestinal maltase-glucoamylase with compounds from …
L Sim, K Jayakanthan, S Mohan, R Nasi, BD Johnston, BM Pinto, ...
Biochemistry 49 (3), 443-451, 2010
Mechanism of catalysis by retaining β-glycosyl hydrolases
A White, DR Rose
Current opinion in structural biology 7 (5), 645-651, 1997
The ubiquitin-activating enzyme E1 as a therapeutic target for the treatment of leukemia and multiple myeloma
GW Xu, M Ali, TE Wood, D Wong, N Maclean, X Wang, M Gronda, M Skrtic, ...
Blood, The Journal of the American Society of Hematology 115 (11), 2251-2259, 2010
Differential oligosaccharide recognition by evolutionarily-related β-1, 4 and β-1, 3 glucan-binding modules
AB Boraston, D Nurizzo, V Notenboom, V Ducros, DR Rose, DG Kilburn, ...
Journal of molecular biology 319 (5), 1143-1156, 2002
Crystal Structures of the Family 9 Carbohydrate-Binding Module from Thermotoga maritima Xylanase 10A in Native and Ligand-Bound Forms,
V Notenboom, AB Boraston, DG Kilburn, DR Rose
Biochemistry 40 (21), 6248-6256, 2001
Insights into transition state stabilization of the β-1, 4-glycosidase Cex by covalent intermediate accumulation in active site mutants
V Notenboom, C Birsan, M Nitz, DR Rose, RAJ Warren, SG Withers
Nature structural biology 5 (9), 812-818, 1998
Clioquinol inhibits the proteasome and displays preclinical activity in leukemia and myeloma
X Mao, X Li, R Sprangers, X Wang, A Venugopal, T Wood, Y Zhang, ...
Leukemia 23 (3), 585-590, 2009
Insights into the mechanism of Drosophila melanogaster Golgi α-mannosidase II through the structural analysis of covalent reaction intermediates
S Numao, DA Kuntz, SG Withers, DR Rose
Journal of Biological Chemistry 278 (48), 48074-48083, 2003
Golgi α-mannosidase II cleaves two sugars sequentially in the same catalytic site
N Shah, DA Kuntz, DR Rose
Proceedings of the National Academy of Sciences 105 (28), 9570-9575, 2008
Exploring the Cellulose/Xylan Specificity of the β-1,4-Glycanase Cex from Cellulomonas fimi through Crystallography and Mutation,
V Notenboom, C Birsan, RAJ Warren, SG Withers, DR Rose
Biochemistry 37 (14), 4751-4758, 1998
Multisubstrate isotope labeling and metagenomic analysis of active soil bacterial communities
Y Verastegui, J Cheng, K Engel, D Kolczynski, S Mortimer, J Lavigne, ...
MBio 5 (4), 10.1128/mbio. 01157-14, 2014
Enzyme-synthesized highly branched maltodextrins have slow glucose generation at the mucosal α-glucosidase level and are slowly digestible in vivo
BH Lee, L Yan, RJ Phillips, BL Reuhs, K Jones, DR Rose, BL Nichols, ...
PloS one 8 (4), e59745, 2013
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