2020
Whittington, A. C., Kamalaldinezabadi, S., Santiago, J. I., Miller, B. G. (2020) Vertical investigations of enzyme evolution using ancestral sequence reconstruction, Comprehensive Natural Products III: Chemistry and Biology Elsevier, 640-653
Sternisha, S., Whittington, A. C., Martinez Fiesco, J. A., Porter, C., McCray, M. M., Logan, T., Olivieri, C., Veglia, G., Steinbach, P. J., Miller, B. G. (2020) Nanosecond-Timescale Dynamics and Conformational Heterogeneity in Human GCK Regulation and Disease, Biophys. J. 118, 1109-1118. PMID: 32023434.
Sengupta, A., Liriano, J., Bienkiewicz, E., Miller, B. G., Frederich, J. H. (2020) Probing the 14-3-3 Isoform-Specificity Profile of Protein–Protein Interactions Stabilized by Fusicoccin A, ACS Omega 5, 25029-25035. PMID: 33043180.
Sengupta, A., Liriano, J., Bienkiewicz, E., Miller, B. G., Frederich, J. H. (2020) Analysis of Interactions Stabilized by Fusicoccin A Reveals an Expanded Suite of Potential 14–3–3 Binding Partners, ACS Chem. Biol. 15, 305-310. PMID: 31971771.
Dardashti, R., Kumar, S., Sternisha, S. M., Reddy, P. S., Miller, B. G., Metanis, N. (2020) Selenolysine: a new tool for traceless isopeptide bond formation, Chem. Eur. J. 26, 4952-4957. PMID: 7184786.
2019
Sternisha, S.M., Miller, B.G. (2019) Molecular and cellular regulation of human glucokinase, Arch. Biochem. Biophys. doi:10.1016/j.abb..2019.01.011
2018
Paukovich, N., Xue, M., Elder, J.R., Redzic, J., Blue, A., Pike, H., Miller, B.G., Pitts, T., Pollock, D.D., Hansen, K., D’Alessandro, A., Eisenmesser, E.Z. (2018) Biliverdin Reductase B Dynamics Are Coupled to Coenzyme Binding, J. Mol. Biol. doi:10.1016/j.jmb.2018.06.015
Mailyan, A.K., Chen, J.L., Keller, A.A., Sternisha, S.M., Miller, B.G., Zakarian, A. (2018) Short Total Synthesis of [15N5]-Cylindrospermopsins from 15NH4Cl Enables Precise Quantification of Freshwater Cyanobacterial Contamination, J. Am. Chem. Soc. 140 (18), 6027-6032
Sternisha, S.M., Lie, P., Marshall, A.G., Miller, B.G. (2018) Mechanistic Origins of Enzyme Activation in Human Glucokinase Variants Associated with Congenital Hyperinsulinism, Biochemistry 57 (10), 1632-1639
2017
Martinez, J.A., Xiao, Q., Zakarian, A., Miller, B.G. (2017) Antidiabetic Disruptors of the Glucokinase−Glucokinase Regulatory Protein Complex Reorganize a Coulombic Interface, Biochemistry 56 (24), 3150-3157
Rexford, A., Zorio, D.A., Miller, B.G. (2017) Biochemical and biophysical investigations of the interaction between human glucokinase and pro-apoptotic BAD, PLOS One doi:10.1371/journal.pone.0171587
2016
Casey, A.K., Miller, B.G. (2016) Kinetic Basis of Carbohydrate-Mediated Inhibition of Human Glucokinase by the Glucokinase Regulatory Protein, Biochemistry 55 (21), 2899-2902
2015
Whittington, A. C., Larion, M., Bowler, J. M., Ramsey, K.M., Brüschweiler, R., Miller, B.G. (2015) Dual allosteric activation mechanisms in monomeric human glucokinase, Proceedings of the National Academy of Sciences doi:10.1073/pnas.1506664112
Larion, M., Miller, B., Brüschweiler, R. (2015) Conformational heterogeneity and intrinsic disorder in enzyme regulation: Glucokinase as a case study, Intrinsically Disordered Proteins 3 (1), 1-4
2014
Martinez, J. A., Larion M., Conejo M.S., Porter C.M., and Miller, B. G. (2014) Role of connecting loop I in catalysis and allosteric regulation of human glucokinase, Protein Science 23, 915-922.
Schulenburg C. and Miller, B. G. (2014) Enzyme Recruitment and Its Role in Metabolic Expansion, Biochemistry 53, 836–845.
2013
Beck, T. and Miller, B. G. (2013) Structural basis for regulation of human glucokinase by glucokinase regulatory protein, Biochemistry 52.Xiao, Q., Jackson, J. J., Basak, A., Bowler, J. M., Miller B. G. and Zakarian, A. (2013) Enantioselective synthesis of tatanans A-C and reinvestigation of their glucokinase activating properties, Nature Chem. 5, 410-416.
Bowler, J. M., Hervert, K. L., Kearley, M. L., and Miller B. G. (2013) Small-molecule allosteric activation of human glucokinase in the absence of glucose, ACS Med. Chem. Lett. 4, 580-584.
2012
Larion, M., Salinas, R. K., Bruschweiler-Li, L., Miller, B. G., and Brüschweiler, R. (2012) Order-disorder transitions govern kinetic cooperativity and allostery of monomeric human glucokinase, PLoS Biol. 10, e1001452.Larion, M. and Miller, B. G. (2012) Homotropic allosteric regulation in monomeric mammalian glucokinase, Arch. Biochem. Biophys. 519, 103-111.
Porter, C. M., and Miller B. G. (2012) Cooperativity in monomeric enzymes with single ligand-binding sites, Bioorg. Chem. 43, 44-50.
2010
Larion, M. and Miller, B. G. (2010) Global fit analysis of glucose binding curves reveals a minimal model for kinetic cooperativity in human glucokinase, Biochemistry 49, 8902-8911.
Desai, K. K., and Miller B. G. (2010) Recruitment of genes and enzymes conferring resistance to the nonnatural toxin bromoacetate, Proc. Natl. Acad. Sci. USA 107, 17968-17973.
Larion, M., Salinas, R.K., Bruschweiler-Li, L., Brüschweiler, R., and Miller B. G. (2010) Direct evidence for conformational heterogeneity in human pancreatic glucokinase from high-resolution NMR, Biochemistry 49, 7969-7971.
Conejo, M. S., Thompson, S. M., and Miller B. G. (2010) Evolutionary bases of carbohydrate recognition and substrate discrimination in the ROK protein family, J. Mol. Evol. 70, 545-556.
Desai, K. K., and Miller, B. G. (2010) L-Glyceraldehyde 3-phosphate reductase from Escherichia coli is a heme binding protein, Bioorg. Chem. 38, 37-41.
2009
Larion, M., and Miller, B. G. (2009) 23-residue C-terminal α-helix governs kinetic cooperativity in monomeric human glucokinase, Biochemistry 48, 6157-6165.
Desai, K. K.; Miller, B. G. (2009) Assessing and exploiting the persistence of substrate ambiguity in modern protein catalysts. In Protein Engineering Handbook; Bornscheuer, U. and Lutz, S. Eds. Wiley-VCH, 343-359.
Pal, P., and Miller, B. G. (2009) Activating mutations in the human glucokinase gene revealed by genetic selection, Biochemistry 48, 814-816.
2008
Desai, K. K., and Miller, B. G. (2008) A metabolic bypass of the triosephosphate isomerase reaction, Biochemistry 47, 7983-7985.
Van Vleet, J. L., Reinhardt, L. A., Miller, B. G., Sievers, A. and Cleland, W. W. (2008) Carbon isotope effect study on orotidine 5’-monophosphate decarboxylase: support for an anionic intermediate, Biochemistry 47, 798-803.
2007
Larion, M., Moore, L. B., Thompson, S. T., and Miller, B. G. (2007) Divergent evolution of function in the ROK sugar kinase superfamily: role of enzyme loops in substrate specificity, Biochemistry 46, 13564-13772.
Callahan, B. P. and Miller, B. G. (2007) OMP decarboxylase – an enigma persists,Bioorg. Chem. 35, 465-469.
Miller, B. G. (2007) The mutability of enzyme active-site shape determinants, Prot. Sci. 16, 1965-1968.
Dhar, P., Cao, Y., Kline, T., Pal, P., Swayne, C., Fischer, T., Miller, B., Sen, A. and Johansen, T. (2007) Autonomously moving local nanoprobes in heterogeneous magnetic fields, J. Phys. Chem. C. 111, 3607-3613.
Publications prior to 2007
Miller, B. G., and Raines, R. T. (2005) Reconstitution of a defunct glycolytic pathway via recruitment of ambiguous sugar kinases, Biochemistry 44, 10776-10783.
Miller, B. G. (2004) Insight into the catalytic mechanism of orotidine 5´-phosphate decarboxylase from crystallography and mutagenesis, Topics in Curr. Chem. 238, 43-62.
Miller, B. G., and Raines, R. T. (2004) Identifying latent enzyme activities: substrate ambiguity within modern bacterial sugar kinases, Biochemistry 43, 6387-6392.
Miller, B. G., and Wolfenden, R. (2002) Catalytic proficiency: the unusual case of OMP decarboxylase, Annu. Rev. Biochem. 71, 847-885.
Miller, B. G., Snider, M. J., Wolfenden, R., and Short, S. A. (2001) Dissecting a charged network at the active site of orotidine 5´-phosphate decarboxylase, J. Biol. Chem. 276, 15174-15176.
Miller, B. G., Butterfoss, G. L., Short, S. A., and Wolfenden, R. (2001) Role for enzyme-ribofuranosyl contacts in the ground state and transition state for orotidine 5´-phosphate decarboxylase: a role for substrate destabilization? Biochemistry 40, 6227-6232.
Miller, B. G., Snider, M. J., Short, S. A., and Wolfenden, R. (2000) Contribution of enzyme-phosphoribosyl contacts to catalysis by orotidine 5´-phosphate decarboxylase, Biochemistry 39, 8113-8118.
Miller, B. G., Hassell, A. M., Milburn, M. V., and Short, S. A. (2000) Crystallization of native and selenomethionyl yeast orotidine 5´-phosphate decarboxylase, Acta Crystallogr. Sect. D: Biol. Crystallogr. 56, 474-474.
Miller, B. G., Hassell, A. M., Wolfenden, R., Milburn, M. V., and Short, S. A. (2000) Anatomy of a proficient enzyme: the structure of orotidine 5´-monophosphate decarboxylase in the presence and absence of a potential transition state analog, Proc. Natl. Acad. Sci. USA 97, 2011-2016.
Miller, B. G., Smiley, J. A., Short, S. A., and Wolfenden, R. (1999) Activity of yeast orotidine 5´-phosphate decarboxylase in the absence of metals, J. Biol. Chem. 274, 23841-23843.
Wolfenden, R., Snider, M., Ridgway, C., and Miller, B. (1999) The temperature dependence of enzyme rate enhancements, J. Am. Chem. Soc. 121, 7419-7420.
Miller, B. G., Traut, T. W., and Wolfenden, R. (1998) Effects of substrate binding determinants in the transition state for orotidine 5´-monophosphate decarboxylase, Bioorg. Chem. 26, 283-288.
Miller, B. G., Traut, T. W., and Wolfenden, R. (1998) A role for zinc in OMP decarboxylase, an unusually proficient enzyme, J. Am. Chem. Soc. 120, 2666-2667.