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. (2018) Resurrection Biology: Aged Acetylcholinesterase Brought Back to Life. Journal of Medicinal Chemistry. 61: 7032-7033
Ranasinghe C, Guo Q, Sapienza PJ, et al. (2017) Protein Mass Effects on Formate Dehydrogenase. Journal of the American Chemical Society
Quinn DM, Topczewski J, Yasapala N, et al. (2017) Why is Aged Acetylcholinesterase So Difficult to Reactivate? Molecules (Basel, Switzerland). 22
Karunaratne K, Luedtke N, Quinn DM, et al. (2017) Flavin-dependent thymidylate synthase: N5 of flavin as a Methylene carrier. Archives of Biochemistry and Biophysics
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
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