Year |
Citation |
Score |
2023 |
Glockzin K, Meneely KM, Hughes R, Maatouk SW, Piña GE, Suthagar K, Clinch K, Buckler JN, Lamb AL, Tyler PC, Meek TD, Katzfuss A. Kinetic and Structural Characterization of Hypoxanthine-Guanine-Xanthine Phosphoribosyltransferases and Repurposing of Transition-State Analogue Inhibitors. Biochemistry. 62: 2182-2201. PMID 37418678 DOI: 10.1021/acs.biochem.3c00116 |
0.651 |
|
2023 |
Meneely KM, McFarlane JS, Wright CL, Vela K, Swint-Kruse L, Fenton AW, Lamb AL. The 2.4 Å structure of Zymomonas mobilis pyruvate kinase: Implications for stability and regulation. Archives of Biochemistry and Biophysics. 744: 109679. PMID 37393983 DOI: 10.1016/j.abb.2023.109679 |
0.772 |
|
2022 |
Kenjić N, Meneely KM, Wherritt DJ, Denler MC, Jackson TA, Moran GR, Lamb AL. Evidence for the Chemical Mechanism of RibB (3,4-Dihydroxy-2-butanone 4-phosphate Synthase) of Riboflavin Biosynthesis. Journal of the American Chemical Society. PMID 35802469 DOI: 10.1021/jacs.2c03376 |
0.646 |
|
2022 |
Shelton CL, Meneely KM, Ronnebaum TA, Chilton AS, Riley AP, Prisinzano TE, Lamb AL. Rational inhibitor design for Pseudomonas aeruginosa salicylate adenylation enzyme PchD. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 35513576 DOI: 10.1007/s00775-022-01941-8 |
0.755 |
|
2021 |
Fenton KD, Meneely KM, Wu T, Martin TA, Swint-Kruse L, Fenton AW, Lamb AL. Substitutions at a rheostat position in human aldolase A cause a shift in the conformational population. Protein Science : a Publication of the Protein Society. PMID 34734672 DOI: 10.1002/pro.4222 |
0.629 |
|
2021 |
Smith MM, Beaupre BA, Fourozesh DC, Meneely KM, Lamb AL, Moran GR. Finding Ways to Relax: A Revisionistic Analysis of the Chemistry of GTP Cyclohydrolase II. Biochemistry. 60: 3027-3039. PMID 34569786 DOI: 10.1021/acs.biochem.1c00511 |
0.652 |
|
2020 |
Forbes D, Meneely KM, Chilton A, Lamb AL, Ellis HR. 3-His Metal Coordination Site Promotes the Coupling of Oxygen Activation to Cysteine Oxidation in Cysteine Dioxygenase. Biochemistry. PMID 32368901 DOI: 10.1021/Acs.Biochem.9B01085 |
0.705 |
|
2020 |
Bhattarai S, Devkota S, Meneely KM, Xing M, Douglas JT, Wolfe MS. Design of substrate transmembrane mimetics as structural probes for γ-secretase. Journal of the American Chemical Society. PMID 31999444 DOI: 10.1021/Jacs.9B13405 |
0.53 |
|
2019 |
Philip AT, Devkota S, Malvankar S, Bhattarai S, Meneely KM, Williams TD, Wolfe MS. Designed helical peptides as functional probes for γ-secretase. Biochemistry. PMID 31625391 DOI: 10.1021/Acs.Biochem.9B00639 |
0.327 |
|
2019 |
McFarlane JS, Ronnebaum TA, Meneely KM, Chilton A, Fenton AW, Lamb AL. Changes in the allosteric site of human liver pyruvate kinase upon activator binding include the breakage of an intersubunit cation-π bond. Acta Crystallographica. Section F, Structural Biology Communications. 75: 461-469. PMID 31204694 DOI: 10.1107/S2053230X19007209 |
0.725 |
|
2016 |
Beaupre BA, Roman JV, Hoag MR, Meneely KM, Silvaggi NR, Lamb AL, Moran GR. Ligand binding phenomena that pertain to the metabolic function of renalase. Archives of Biochemistry and Biophysics. PMID 27769837 DOI: 10.1016/J.Abb.2016.10.011 |
0.691 |
|
2016 |
Meneely KM, Ronnebaum TA, Riley AP, Prisinzano TE, Lamb AL. Holo-structure and steady state kinetics of the thiazolinyl imine reductases for siderophore biosynthesis. Biochemistry. PMID 27601130 DOI: 10.1021/Acs.Biochem.6B00735 |
0.782 |
|
2016 |
Meneely KM, Sundlov JA, Gulick AM, Moran GR, Lamb AL. An Open and Shut Case: The Interaction of Magnesium with MST Enzymes. Journal of the American Chemical Society. PMID 27373320 DOI: 10.1021/Jacs.6B05134 |
0.696 |
|
2014 |
Meneely KM, Luo Q, Riley AP, Taylor B, Roy A, Stein RL, Prisinzano TE, Lamb AL. Expanding the results of a high throughput screen against an isochorismate-pyruvate lyase to enzymes of a similar scaffold or mechanism. Bioorganic & Medicinal Chemistry. 22: 5961-9. PMID 25282647 DOI: 10.1016/J.Bmc.2014.09.010 |
0.694 |
|
2013 |
Meneely KM, Luo Q, Lamb AL. Redesign of MST enzymes to target lyase activity instead promotes mutase and dehydratase activities Archives of Biochemistry and Biophysics. 539: 70-80. PMID 24055536 DOI: 10.1016/J.Abb.2013.09.007 |
0.74 |
|
2013 |
Meneely KM, Luo Q, Dhar P, Lamb AL. Lysine221 is the general base residue of the isochorismate synthase from Pseudomonas aeruginosa (PchA) in a reaction that is diffusion limited Archives of Biochemistry and Biophysics. 538: 49-56. PMID 23942051 DOI: 10.1016/J.Abb.2013.07.026 |
0.733 |
|
2012 |
Meneely KM, Lamb AL. Two structures of a thiazolinyl imine reductase from yersinia enterocolitica provide insight into catalysis and binding to the nonribosomal peptide synthetase module of HMWP1 Biochemistry. 51: 9002-9013. PMID 23066849 DOI: 10.1021/Bi3011016 |
0.719 |
|
2012 |
Olucha J, Meneely KM, Lamb AL. Modification of residue 42 of the active site loop with a lysine-mimetic side chain rescues isochorismate-pyruvate lyase activity in Pseudomonas aeruginosa PchB Biochemistry. 51: 7525-7532. PMID 22970849 DOI: 10.1021/Bi300472N |
0.765 |
|
2012 |
DeVore NM, Meneely KM, Bart AG, Stephens ES, Battaile KP, Scott EE. Structural comparison of cytochromes P450 2A6, 2A13, and 2E1 with pilocarpine. The Febs Journal. 279: 1621-31. PMID 22051186 DOI: 10.1111/J.1742-4658.2011.08412.X |
0.54 |
|
2011 |
Olucha J, Meneely KM, Chilton AS, Lamb AL. Two structures of an N-hydroxylating flavoprotein monooxygenase: Ornithine hydroxylase from Pseudomonas aeruginosa Journal of Biological Chemistry. 286: 31789-31798. PMID 21757711 DOI: 10.1074/Jbc.M111.265876 |
0.784 |
|
2011 |
Luo Q, Meneely KM, Lamb AL. Entropic and enthalpic components of catalysis in the mutase and lyase activities of pseudomonas aeruginosa PchB Journal of the American Chemical Society. 133: 7229-7233. PMID 21504201 DOI: 10.1021/Ja202091A |
0.718 |
|
2009 |
Zaitseva J, Meneely KM, Lamb AL. Structure of escherichia coli malate dehydrogenase at 1.45 Å resolution Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 65: 866-869. PMID 19724119 DOI: 10.1107/S1744309109032217 |
0.66 |
|
2009 |
Meneely KM, Barr EW, Bollinger JM, Lamb AL. Kinetic mechanism of ornithine hydroxylase (PvdA) from Pseudomonas aeruginosa: substrate triggering of O2 addition but not flavin reduction. Biochemistry. 48: 4371-6. PMID 19368334 DOI: 10.1021/Bi900442Z |
0.713 |
|
2008 |
Porubsky PR, Meneely KM, Scott EE. Structures of human cytochrome P-450 2E1. Insights into the binding of inhibitors and both small molecular weight and fatty acid substrates. The Journal of Biological Chemistry. 283: 33698-707. PMID 18818195 DOI: 10.1074/Jbc.M805999200 |
0.458 |
|
2007 |
Meneely KM, Lamb AL. Biochemical characterization of a flavin adenine dinculeotide-dependent monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests a novel reaction mechanism Biochemistry. 46: 11930-11937. PMID 17900176 DOI: 10.1021/Bi700932Q |
0.692 |
|
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