Daniel M. Quinn

Affiliations: 
Chemistry University of Iowa, Iowa City, IA 
Area:
reaction dynamics of hydrolytic enzymes
Website:
http://www.chem.uiowa.edu/people/daniel-m-quinn
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"Daniel M. Quinn"
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Parents

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Richard L. Schowen grad student 1977 University of Kansas
 (Approaches to Transition-state Structure for Various Enzyme-catalyzed Acyl Transfers)
Eugene H. Cordes post-doc 1978-1980 Indiana University
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Publications

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Quinn DM, Topczewski J, Yasapala N, et al. (2017) Why is Aged Acetylcholinesterase So Difficult to Reactivate? Molecules (Basel, Switzerland). 22
Morrill JA, Topczewski JJ, Lodge AM, et al. (2015) Development of quantitative structure activity relationships for the binding affinity of methoxypyridinium cations for human acetylcholinesterase. Journal of Molecular Graphics & Modelling. 62: 181-189
Topczewski JJ, Lodge AM, Yasapala SN, et al. (2013) Reversible inhibition of human acetylcholinesterase by methoxypyridinium species. Bioorganic & Medicinal Chemistry Letters. 23: 5786-9
Topczewski JJ, Quinn DM. (2013) Kinetic assessment of N-methyl-2-methoxypyridinium species as phosphonate anion methylating agents. Organic Letters. 15: 1084-7
Tormos JR, Wiley KL, Wang Y, et al. (2010) Accumulation of tetrahedral intermediates in cholinesterase catalysis: a secondary isotope effect study. Journal of the American Chemical Society. 132: 17751-9
Wiley KL, Tormos JR, Quinn DM. (2010) A secondary isotope effect study of equine serum butyrylcholinesterase-catalyzed hydrolysis of acetylthiocholine. Chemico-Biological Interactions. 187: 124-7
Tormos JR, Wiley KL, Seravalli J, et al. (2005) The reactant state for substrate-activated turnover of acetylthiocholine by butyrylcholinesterase is a tetrahedral intermediate. Journal of the American Chemical Society. 127: 14538-9
Sikorski RS, Malany S, Seravalli J, et al. (2002) Computational study of substrate isotope effect probes of transition state structure for acetylcholinesterase catalysis Nukleonika. 47: S9-S12
Liang Y, Medhekar R, Brockman HL, et al. (2000) Importance of arginines 63 and 423 in modulating the bile salt-dependent and bile salt-independent hydrolytic activities of rat carboxyl ester lipase. The Journal of Biological Chemistry. 275: 24040-6
Malany S, Sawai M, Sikorski RS, et al. (2000) Transition state structure and rate determination for the acylation stage of acetylcholinesterase catalyzed hydrolysis of (acetylthio)choline Journal of the American Chemical Society. 122: 2981-2987
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