The Search for Novel Human Pancreatic Alpha-Amylase Inhibitors: High-Throughput Screening of Terrestrial and Marine Natural Product Extracts
Tarling , C.A. , Woods, K., Zhang, R., Brastianos, H.C., Brayer, G.D., Andersen, R.J. and Withers, S.G. ChemBioChem 9, 433-438 (2008)
Alternative Catalytic Anions Differentially Modulate Human Alpha-Amylase Activity and Specificity
Maurus, R., Begum, A., Williams, L.K., Fredriksen, J.R., Zhang, R., Withers, S.G. and Brayer, G.D. Biochemistry 47, 3332-3344 (2008)
Synthesis and Testing of 2-Deoxy-2,2-Dihaloglycosides as Mechanism-Based Inhibitors for Alpha-Glycosidases
Zhang, R., McCarter, J.D., Braun, C., Yeung, W., Brayer, G.D. and Withers, S.G.
J. Organic Chemistry 73, 3070-3077 (2008)
Lumenal Substrate “Brake” on Mucosal Maltase-Glucoamylase Activity Regulates Total Rate of Starch Digestion to Glucose
Quezada-Calvillo, R., Robayo-Torres, C.C., Ao, Z., Hamaker, B.R., Quaroni, A., Brayer, G.D., Sterchi, E.E., Baker, S.S. and Nichols, B.L.
Journal of Pediatric Gastroenterology and Nutrition 45, 32-43 (2007)
The Biological Crystallization Resource: Facilitating Knowledge-Based Protein Crystallizations
Li, C., Kirkwood , K.L. and Brayer, G.D.
Crystal Growth and Design 7, 2147-2152 (2007)
Structural and mechanistic studies of chloride induced activation of human pancreatic alpha-amylase.
R. Maurus, A. Begum, H.H Kuo, A. Racaza, S. Numao, C. Andersen, J.W. Tams, J. Vind, C.M. Overall, S.G. Withers, and G.D. Brayer
Protein Science 14, 743-755 (2005)
Acarbose rearrangement mechanism implied by the kinetic and structural analysis of human pancreatic alpha-amylase in complex with analogues and their elongated counterparts.
C. Li, A. Begum, S. Numao, K.H. Park , S.G. Withers, and G.D. Brayer
Biochemistry 44, 3347-3357 (2005)
In situ extension as an approach for identifying novel alpha-amylase inhibitors.
S. Numao, I. Damager, C. Li, T.M. Wrodnigg, A. Begum, C.M. Overall, G.D. Brayer, and S.G. Withers
J. Biol. Chem. 279, 48282-48291 (2004)
Synthesis and characterisation of novel chromogenic substrates for human pancreatic alpha-amylase.
I. Damager, S. Numao, H. Chen, G.D. Brayer, and S.G. Withers
Carbohydrate Research 339, 1727-1737 (2004)
Probing the roles of key residues in the unique regulatory NADH binding site of type II citrate synthase of E. coli .
D.J. Stokell, L.J. Donald, R. Maurus, N.T. Nguyen, G. Sadler, K. Choudhary, P.G. Hultin, G.D. Brayer, and H.W. Duckworth
J. Biol. Chem. 278, 35435-35443 (2003)
Insights into the evolution of allosteric properties. The NADH binding site of hexameric type II citrate synthases.
R. Maurus, N.T. Nguyen, D.J. Stokell, A. Ayed, P.G. Hultin, H.W. Duckworth, and G.D. Brayer
Biochemistry 42, 5555-5565 (2003)
Mechanistic analyses of catalysis in human pancreatic alpha-amylase: Detailed kinetic and structural studies of mutants of three conserved carboxylic acids.
E.H. Rydberg, C. Li, R. Maurus, C.M. Overall, G.D. Brayer, and S.G. Withers
Biochemistry 41, 4492-4502 (2002)
Probing the role of the chloride ion in the mechanism of human pancreatic alpha-amylase.
S. Numao, R. Maurus, G. Sidhu, Y. Wang, C.M. Overall, G.D. Brayer, and S.G. Withers
Biochemistry 41, 215-225 (2002)
Comparative analysis of folding and substrate binding sites between regulated hexameric type II citrate synthases and unregulated dimeric type I enzymes.
N.T. Nguyen, R. Maurus, D.J. Stokell, A. Ayed, H.W. Duckworth, and G.D. Brayer
Biochemistry 40, 13177-13187 (2001)