Year |
Citation |
Score |
2023 |
Campbell RP, Whittington AC, Zorio DAR, Miller BG. Recruitment of a Middling Promiscuous Enzyme Drives Adaptive Metabolic Evolution in Escherichia coli. Molecular Biology and Evolution. PMID 37708398 DOI: 10.1093/molbev/msad202 |
0.341 |
|
2020 |
Sternisha SM, Whittington AC, Martinez Fiesco JA, Porter C, McCray MM, Logan T, Olivieri C, Veglia G, Steinbach PJ, Miller BG. Nanosecond-Timescale Dynamics and Conformational Heterogeneity in Human GCK Regulation and Disease. Biophysical Journal. PMID 32023434 DOI: 10.1016/J.Bpj.2019.12.036 |
0.352 |
|
2019 |
Sternisha SM, Miller BG. Molecular and cellular regulation of human glucokinase. Archives of Biochemistry and Biophysics. PMID 30641049 DOI: 10.1016/J.Abb.2019.01.011 |
0.35 |
|
2019 |
Larion M, Hansen A, Bruschweiler-Li L, Tugarinov V, Brüschweiler R, Miller B. Specific 13CH3 Labeling and NMR Reveal the Role of Structural Dynamics to Enzymatic Function Biophysical Journal. 116: 470a. DOI: 10.1016/J.Bpj.2018.11.2540 |
0.619 |
|
2018 |
Paukovich N, Xue M, Elder JR, Redzic JS, Blue A, Pike H, Miller BG, Pitts TM, Pollock DD, Hansen K, D'Alessandro A, Eisenmesser EZ. Biliverdin reductase B dynamics are coupled to coenzyme binding. Journal of Molecular Biology. PMID 29932944 DOI: 10.1016/J.Jmb.2018.06.015 |
0.381 |
|
2018 |
Sternisha S, Liu P, Marshall AG, Miller BG. Mechanistic Origins of Enzyme Activation in Human Glucokinase Variants Associated with Congenital Hyperinsulinism. Biochemistry. PMID 29425029 DOI: 10.1021/Acs.Biochem.8B00022 |
0.373 |
|
2017 |
Martinez J, Xiao Q, Zakarian A, Miller BG. Antidiabetic disruptors of the glucokinase-glucokinase regulatory protein complex reorganize a coulombic interface. Biochemistry. PMID 28516783 DOI: 10.1021/Acs.Biochem.7B00377 |
0.351 |
|
2017 |
Rexford A, Zorio DA, Miller BG. Biochemical and biophysical investigations of the interaction between human glucokinase and pro-apoptotic BAD. Plos One. 12: e0171587. PMID 28182770 DOI: 10.1371/Journal.Pone.0171587 |
0.346 |
|
2017 |
Miller BG. Allokairic regulation of enzyme function Journal of Biotechnology & Biomaterials. 7. DOI: 10.4172/2155-952X.C1.070 |
0.38 |
|
2016 |
Casey AK, Miller BG. Kinetic Basis of Carbohydrate-mediated Inhibition of Human Glucokinase by the Glucokinase Regulatory Protein. Biochemistry. PMID 27174229 DOI: 10.1021/Acs.Biochem.6B00349 |
0.362 |
|
2015 |
Larion M, Miller B, Brüschweiler R. Conformational heterogeneity and intrinsic disorder in enzyme regulation: Glucokinase as a case study. Intrinsically Disordered Proteins. 3: e1011008. PMID 28232887 DOI: 10.1080/21690707.2015.1011008 |
0.682 |
|
2015 |
Whittington AC, Larion M, Bowler JM, Ramsey KM, Brüschweiler R, Miller BG. Dual allosteric activation mechanisms in monomeric human glucokinase. Proceedings of the National Academy of Sciences of the United States of America. 112: 11553-8. PMID 26283387 DOI: 10.1073/Pnas.1506664112 |
0.771 |
|
2015 |
Larion M, Hansen AL, Zhang F, Bruschweiler-Li L, Tugarinov V, Miller BG, Brüschweiler R. Kinetic Cooperativity in Human Pancreatic Glucokinase Originates from Millisecond Dynamics of the Small Domain. Angewandte Chemie (International Ed. in English). 54: 8129-32. PMID 26013420 DOI: 10.1002/Anie.201501204 |
0.685 |
|
2014 |
Martinez JA, Larion M, Conejo MS, Porter CM, Miller BG. Role of connecting loop I in catalysis and allosteric regulation of human glucokinase. Protein Science : a Publication of the Protein Society. 23: 915-22. PMID 24723372 DOI: 10.1002/Pro.2473 |
0.694 |
|
2014 |
Schulenburg C, Miller BG. Enzyme recruitment and its role in metabolic expansion. Biochemistry. 53: 836-45. PMID 24483367 DOI: 10.1021/Bi401667F |
0.385 |
|
2013 |
Bowler JM, Hervert KL, Kearley ML, Miller BG. Small-Molecule Allosteric Activation of Human Glucokinase in the Absence of Glucose. Acs Medicinal Chemistry Letters. 4. PMID 24294411 DOI: 10.1021/Ml400061X |
0.424 |
|
2013 |
Beck T, Miller BG. Structural basis for regulation of human glucokinase by glucokinase regulatory protein. Biochemistry. 52: 6232-9. PMID 23957911 DOI: 10.1021/Bi400838T |
0.342 |
|
2013 |
Xiao Q, Jackson JJ, Basak A, Bowler JM, Miller BG, Zakarian A. Enantioselective synthesis of tatanans A-C and reinvestigation of their glucokinase-activating properties. Nature Chemistry. 5: 410-6. PMID 23609092 DOI: 10.1038/Nchem.1597 |
0.304 |
|
2012 |
Larion M, Salinas RK, Bruschweiler-Li L, Miller BG, Brüschweiler R. Order-Disorder Transitions Govern Kinetic Cooperativity and Allostery of Monomeric Human Glucokinase Plos Biology. 10. PMID 23271955 DOI: 10.1371/Journal.Pbio.1001452 |
0.689 |
|
2012 |
Porter CM, Miller BG. Cooperativity in monomeric enzymes with single ligand-binding sites Bioorganic Chemistry. 43: 44-50. PMID 22137502 DOI: 10.1016/J.Bioorg.2011.11.001 |
0.381 |
|
2012 |
Larion M, Miller BG. Homotropic allosteric regulation in monomeric mammalian glucokinase Archives of Biochemistry and Biophysics. 519: 103-111. PMID 22107947 DOI: 10.1016/J.Abb.2011.11.007 |
0.705 |
|
2011 |
Desai KK, Miller BG. Assessing and Exploiting the Persistence of Substrate Ambiguity in Modern Protein Catalysts Protein Engineering Handbook, Volume 1 & Volume 2. 1: 343-362. DOI: 10.1002/9783527634026.ch13 |
0.615 |
|
2010 |
Desai KK, Miller BG. Recruitment of genes and enzymes conferring resistance to the nonnatural toxin bromoacetate Proceedings of the National Academy of Sciences of the United States of America. 107: 17968-17973. PMID 20921376 DOI: 10.1073/Pnas.1007559107 |
0.687 |
|
2010 |
Larion M, Miller BG. Global fit analysis of glucose binding curves reveals a minimal model for kinetic cooperativity in human glucokinase Biochemistry. 49: 8902-8911. PMID 20828143 DOI: 10.1021/Bi1008672 |
0.715 |
|
2010 |
Larion M, Salinas RK, Bruschweiler-Li L, Brüschweiler R, Miller BG. Direct evidence of conformational heterogeneity in human pancreatic glucokinase from high-resolution nuclear magnetic resonance Biochemistry. 49: 7969-7971. PMID 20735087 DOI: 10.1021/Bi101098F |
0.686 |
|
2010 |
Conejo MS, Thompson SM, Miller BG. Evolutionary bases of carbohydrate recognition and substrate discrimination in the ROK protein family. Journal of Molecular Evolution. 70: 545-56. PMID 20512568 DOI: 10.1007/S00239-010-9351-1 |
0.338 |
|
2010 |
Desai KK, Miller BG. l-Glyceraldehyde 3-phosphate reductase from Escherichia coli is a heme binding protein Bioorganic Chemistry. 38: 37-41. PMID 20015532 DOI: 10.1016/J.Bioorg.2009.11.003 |
0.672 |
|
2009 |
Larion M, Miller BG. 23-Residue C-terminal α-helix governs kinetic cooperativity in monomeric human glucokinase Biochemistry. 48: 6157-6165. PMID 19473033 DOI: 10.1021/Bi9007534 |
0.691 |
|
2009 |
Pal P, Miller BG. Activating mutations in the human glucokinase gene revealed by genetic selection. Biochemistry. 48: 814-6. PMID 19146401 DOI: 10.1021/Bi802142Q |
0.31 |
|
2008 |
Desai KK, Miller BG. A metabolic bypass of the triosephosphate isomerase reaction Biochemistry. 47: 7983-7985. PMID 18620424 DOI: 10.1021/Bi801054V |
0.683 |
|
2008 |
Van Vleet JL, Reinhardt LA, Miller BG, Sievers A, Cleland WW. Carbon isotope effect study on orotidine 5'-monophosphate decarboxylase: support for an anionic intermediate. Biochemistry. 47: 798-803. PMID 18081312 DOI: 10.1021/Bi701664N |
0.563 |
|
2008 |
Van Vleet JL, Reinhardt LA, Miller BG, Sievers A, Cleland WW. Carbon isotope effect study on orotidine 5'-monophosphate decarboxylase: support for an anionic intermediate. Biochemistry. 47: 798-803. PMID 18081312 DOI: 10.1021/Bi701664N |
0.563 |
|
2007 |
Larion M, Moore LB, Thompson SM, Miller BG. Divergent evolution of function in the ROK sugar kinase superfamily: role of enzyme loops in substrate specificity. Biochemistry. 46: 13564-72. PMID 17979299 DOI: 10.1021/Bi700924D |
0.692 |
|
2007 |
Larion M, Moore LB, Thompson SM, Miller BG. Divergent evolution of function in the ROK sugar kinase superfamily: role of enzyme loops in substrate specificity. Biochemistry. 46: 13564-72. PMID 17979299 DOI: 10.1021/Bi700924D |
0.692 |
|
2007 |
Callahan BP, Miller BG. OMP decarboxylase-An enigma persists Bioorganic Chemistry. 35: 465-469. PMID 17889251 DOI: 10.1016/J.Bioorg.2007.07.004 |
0.67 |
|
2007 |
Miller BG. The mutability of enzyme active-site shape determinants Protein Science. 16: 1965-1968. PMID 17766388 DOI: 10.1110/Ps.073040307 |
0.399 |
|
2005 |
Miller BG, Raines RT. Reconstitution of a defunct glycolytic pathway via recruitment of ambiguous sugar kinases. Biochemistry. 44: 10776-83. PMID 16086580 DOI: 10.1021/Bi0506268 |
0.655 |
|
2004 |
Miller BG, Raines RT. Identifying latent enzyme activities: substrate ambiguity within modern bacterial sugar kinases. Biochemistry. 43: 6387-92. PMID 15157072 DOI: 10.1021/Bi049424M |
0.675 |
|
2002 |
Miller BG, Wolfenden R. Catalytic proficiency: the unusual case of OMP decarboxylase. Annual Review of Biochemistry. 71: 847-85. PMID 12045113 DOI: 10.1146/Annurev.Biochem.71.110601.135446 |
0.615 |
|
2001 |
Miller BG, Butterfoss GL, Short SA, Wolfenden R. Role of enzyme-ribofuranosyl contacts in the ground state and transition state for orotidine 5'-phosphate decarboxylase: a role for substrate destabilization? Biochemistry. 40: 6227-32. PMID 11371183 DOI: 10.1021/Bi0028993 |
0.636 |
|
2001 |
Miller BG, Snider MJ, Wolfenden R, Short SA. Dissecting a charged network at the active site of orotidine-5'-phosphate decarboxylase. The Journal of Biological Chemistry. 276: 15174-6. PMID 11278904 DOI: 10.1074/Jbc.M011429200 |
0.759 |
|
2000 |
Miller BG, Snider MJ, Short SA, Wolfenden R. Contribution of enzyme-phosphoribosyl contacts to catalysis by orotidine 5'-phosphate decarboxylase. Biochemistry. 39: 8113-8. PMID 10889016 DOI: 10.1021/Bi000818X |
0.744 |
|
2000 |
Miller BG, Hassell AM, Wolfenden R, Milburn MV, Short SA. Anatomy of a proficient enzyme: the structure of orotidine 5'-monophosphate decarboxylase in the presence and absence of a potential transition state analog. Proceedings of the National Academy of Sciences of the United States of America. 97: 2011-6. PMID 10681417 DOI: 10.1073/Pnas.030409797 |
0.605 |
|
2000 |
Miller BG, Snider MJ, Short SA, Wolfenden R. Contribution of enzyme - Phosphoribosyl contacts to catalysis by orotidine 5′-phosphate decarboxylase Biochemistry. 39: X-8118. |
0.738 |
|
1999 |
Miller BG, Smiley JA, Short SA, Wolfenden R. Activity of yeast orotidine-5'-phosphate decarboxylase in the absence of metals. The Journal of Biological Chemistry. 274: 23841-3. PMID 10446147 DOI: 10.1074/Jbc.274.34.23841 |
0.598 |
|
1999 |
Wolfenden R, Snider M, Ridgway C, Miller B. The temperature dependence of enzyme rate enhancements [8] Journal of the American Chemical Society. 121: 7419-7420. DOI: 10.1021/Ja991280P |
0.73 |
|
1998 |
Miller BG, Traut TW, Wolfenden R. A role for zinc in OMP decarboxylase, an unusually proficient enzyme [9] Journal of the American Chemical Society. 120: 2666-2667. DOI: 10.1021/Ja980066I |
0.59 |
|
1998 |
Miller BG, Traut TW, Wolfenden R. Effects of substrate binding determinants in the transition state for orotidine 5'-monophosphate decarboxylase Bioorganic Chemistry. 26: 283-288. DOI: 10.1006/Bioo.1998.1105 |
0.579 |
|
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