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Qianyi Luo, Ph.D. - Publications

Affiliations: 
Biochemistry & Molecular Biology University of Kansas, Lawrence, KS, United States 
Area:
Iron uptake
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6 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
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  0.711
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  0.753
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  0.741
2011 Olucha J, Ouellette AN, Luo Q, Lamb AL. PH dependence of catalysis by pseudomonas aeruginosa isochorismate - Pyruvate lyase: Implications for transition state stabilization and the role of lysine 42 Biochemistry. 50: 7198-7207. PMID 21751784 DOI: 10.1021/Bi200599J  0.725
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  0.748
2009 Luo Q, Olucha J, Lamb AL. Structure-function analyses of isochorismate-pyruvate lyase from Pseudomonas aeruginosa suggest differing catalytic mechanisms for the two pericyclic reactions of this bifunctional enzyme Biochemistry. 48: 5239-5245. PMID 19432488 DOI: 10.1021/Bi900456E  0.718
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