| Year |
Citation |
Score |
| 2018 |
Quinn DM. Resurrection Biology: Aged Acetylcholinesterase Brought Back to Life. Journal of Medicinal Chemistry. 61: 7032-7033. PMID 30110162 DOI: 10.1021/Acs.Jmedchem.8B01122 |
0.389 |
|
| 2017 |
Ranasinghe C, Guo Q, Sapienza PJ, Lee AL, Quinn DM, Cheatum CM, Kohen A. Protein Mass Effects on Formate Dehydrogenase. Journal of the American Chemical Society. PMID 29083897 DOI: 10.1021/Jacs.7B08359 |
0.331 |
|
| 2017 |
Quinn DM, Topczewski J, Yasapala N, Lodge A. Why is Aged Acetylcholinesterase So Difficult to Reactivate? Molecules (Basel, Switzerland). 22. PMID 28869561 DOI: 10.3390/Molecules22091464 |
0.726 |
|
| 2017 |
Karunaratne K, Luedtke N, Quinn DM, Kohen A. Flavin-dependent thymidylate synthase: N5 of flavin as a Methylene carrier. Archives of Biochemistry and Biophysics. PMID 28821425 DOI: 10.1016/J.Abb.2017.08.011 |
0.362 |
|
| 2015 |
Morrill JA, Topczewski JJ, Lodge AM, Yasapala N, Quinn DM. Development of quantitative structure activity relationships for the binding affinity of methoxypyridinium cations for human acetylcholinesterase. Journal of Molecular Graphics & Modelling. 62: 181-189. PMID 26454505 DOI: 10.1016/J.Jmgm.2015.09.016 |
0.707 |
|
| 2013 |
Topczewski JJ, Lodge AM, Yasapala SN, Payne MK, Keshavarzi PM, Quinn DM. Reversible inhibition of human acetylcholinesterase by methoxypyridinium species. Bioorganic & Medicinal Chemistry Letters. 23: 5786-9. PMID 24076173 DOI: 10.1016/J.Bmcl.2013.09.008 |
0.709 |
|
| 2013 |
Topczewski JJ, Quinn DM. Kinetic assessment of N-methyl-2-methoxypyridinium species as phosphonate anion methylating agents. Organic Letters. 15: 1084-7. PMID 23410111 DOI: 10.1021/Ol400054M |
0.406 |
|
| 2010 |
Tormos JR, Wiley KL, Wang Y, Fournier D, Masson P, Nachon F, Quinn DM. Accumulation of tetrahedral intermediates in cholinesterase catalysis: a secondary isotope effect study. Journal of the American Chemical Society. 132: 17751-9. PMID 21105647 DOI: 10.1021/Ja104496Q |
0.404 |
|
| 2010 |
Wiley KL, Tormos JR, Quinn DM. A secondary isotope effect study of equine serum butyrylcholinesterase-catalyzed hydrolysis of acetylthiocholine. Chemico-Biological Interactions. 187: 124-7. PMID 20493178 DOI: 10.1016/J.Cbi.2010.05.007 |
0.352 |
|
| 2005 |
Tormos JR, Wiley KL, Seravalli J, Nachon F, Masson P, Nicolet Y, Quinn DM. The reactant state for substrate-activated turnover of acetylthiocholine by butyrylcholinesterase is a tetrahedral intermediate. Journal of the American Chemical Society. 127: 14538-9. PMID 16231883 DOI: 10.1021/Ja052401Q |
0.408 |
|
| 2002 |
Sikorski RS, Malany S, Seravalli J, Quinn DM. Computational study of substrate isotope effect probes of transition state structure for acetylcholinesterase catalysis Nukleonika. 47: S9-S12. |
0.691 |
|
| 2000 |
Liang Y, Medhekar R, Brockman HL, Quinn DM, Hui DY. 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. PMID 10811659 DOI: 10.1074/Jbc.M003187200 |
0.317 |
|
| 2000 |
Malany S, Sawai M, Sikorski RS, Seravalli J, Quinn DM, Radi? Z, Taylor P, Kronman C, Velan B, Shafferman A. 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. DOI: 10.1021/Ja9933590 |
0.724 |
|
| 2000 |
Quinn DM, Feaster SR, Nair HK, Baker NA, Radi? Z, Taylor P. Delineation and decomposition of energies involved in quaternary ammonium binding in the active site of acetylcholinesterase Journal of the American Chemical Society. 122: 2975-2980. DOI: 10.1021/Ja9933588 |
0.582 |
|
| 1999 |
Malany S, Baker N, Verweyst M, Medhekar R, Quinn DM, Velan B, Kronman C, Shafferman A. Theoretical and experimental investigations of electrostatic effects on acetylcholinesterase catalysis and inhibition. Chemico-Biological Interactions. 119: 99-110. PMID 10421443 DOI: 10.1016/S0009-2797(99)00018-6 |
0.578 |
|
| 1998 |
Savle PS, Medhekar RA, Kelley EL, May JG, Watkins SF, Fronczek FR, Quinn DM, Gandour RD. Change in the mode of inhibition of acetylcholinesterase by (4-nitrophenyl)sulfonoxyl derivatives of conformationally constrained choline analogues. Chemical Research in Toxicology. 11: 19-25. PMID 9477222 DOI: 10.1021/Tx970019O |
0.322 |
|
| 1997 |
Feaster SR, Quinn DM. Mechanism-based inhibitors of mammalian cholesterol esterase. Methods in Enzymology. 286: 231-52. PMID 9309653 DOI: 10.1016/S0076-6879(97)86013-2 |
0.416 |
|
| 1997 |
Radi? Z, Kirchhoff PD, Quinn DM, McCammon JA, Taylor P. Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase. Distinctions between active center ligands and fasciculin. The Journal of Biological Chemistry. 272: 23265-77. PMID 9287336 DOI: 10.1074/Jbc.272.37.23265 |
0.45 |
|
| 1997 |
Saxena A, Maxwell DM, Quinn DM, Radi? Z, Taylor P, Doctor BP. Mutant acetylcholinesterases as potential detoxification agents for organophosphate poisoning. Biochemical Pharmacology. 54: 269-74. PMID 9271331 DOI: 10.1016/S0006-2952(97)00180-9 |
0.397 |
|
| 1996 |
Feaster SR, Lee K, Baker N, Hui DY, Quinn DM. Molecular recognition by cholesterol esterase of active site ligands: structure-reactivity effects for inhibition by aryl carbamates and subsequent carbamylenzyme turnover. Biochemistry. 35: 16723-34. PMID 8988009 DOI: 10.1021/Bi961677V |
0.624 |
|
| 1996 |
Hosea NA, Radi? Z, Tsigelny I, Berman HA, Quinn DM, Taylor P. Aspartate 74 as a primary determinant in acetylcholinesterase governing specificity to cationic organophosphonates. Biochemistry. 35: 10995-1004. PMID 8718893 DOI: 10.1021/Bi9611220 |
0.362 |
|
| 1996 |
Harel M, Quinn DM, Nair HK, Silman I, Sussman JL. The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase Journal of the American Chemical Society. 118: 2340-2346. DOI: 10.1021/Ja952232H |
0.41 |
|
| 1995 |
Ashani Y, Radi? Z, Tsigelny I, Vellom DC, Pickering NA, Quinn DM, Doctor BP, Taylor P. Amino acid residues controlling reactivation of organophosphonyl conjugates of acetylcholinesterase by mono- and bisquaternary oximes. The Journal of Biological Chemistry. 270: 6370-80. PMID 7890775 DOI: 10.1074/Jbc.270.11.6370 |
0.374 |
|
| 1995 |
Radi? Z, Quinn DM, Vellom DC, Camp S, Taylor P. Allosteric control of acetylcholinesterase catalysis by fasciculin. The Journal of Biological Chemistry. 270: 20391-9. PMID 7657613 DOI: 10.1074/Jbc.270.35.20391 |
0.419 |
|
| 1994 |
Nair HK, Seravalli J, Arbuckle T, Quinn DM. Molecular recognition in acetylcholinesterase catalysis: free-energy correlations for substrate turnover and inhibition by trifluoro ketone transition-state analogs. Biochemistry. 33: 8566-76. PMID 8031791 DOI: 10.1021/Bi00194A023 |
0.404 |
|
| 1994 |
Saxena A, Qian N, Kovach IM, Kozikowski AP, Pang YP, Vellom DC, Radi? Z, Quinn D, Taylor P, Doctor BP. Identification of amino acid residues involved in the binding of Huperzine A to cholinesterases. Protein Science : a Publication of the Protein Society. 3: 1770-8. PMID 7849595 DOI: 10.1002/Pro.5560031017 |
0.363 |
|
| 1993 |
Selwood T, Feaster SR, States MJ, Pryor AN, Quinn DM. Parallel mechanisms in acetylcholinesterase-catalyzed hydrolysis of choline esters Journal of the American Chemical Society. 115: 10477-10482. DOI: 10.1021/Ja00076A002 |
0.317 |
|
| 1992 |
Shin HC, Quinn DM. Interaction of lipoprotein lipase with p-nitrophenyl N-alkylcarbamates: kinetics, mechanism, and analogy to the acylenzyme mechanism. Biochemistry. 31: 811-8. PMID 1731939 DOI: 10.1021/Bi00118A025 |
0.371 |
|
| 1992 |
Lee BH, Stelly TC, Colucci WJ, Garcia JG, Gandour RD, Quinn DM. Inhibition of acetylcholinesterase by hemicholiniums, conformationally constrained choline analogues. Evaluation of aryl and alkyl substituents. Comparisons with choline and (3-hydroxyphenyl)trimethylammonium. Chemical Research in Toxicology. 5: 411-8. PMID 1504265 DOI: 10.1021/Tx00027A015 |
0.354 |
|
| 1992 |
Pryor AN, Selwood T, Leu LS, Andracki MA, Lee BH, Rao M, Rosenberry T, Doctor BP, Silman I, Quinn DM. Simple general acid-base catalysis of physiological acetylcholinesterase reactions Journal of the American Chemical Society. 114: 3896-3900. DOI: 10.1021/Ja00036A043 |
0.391 |
|
| 1991 |
Sutton LD, Froelich S, Hendrickson HS, Quinn DM. Cholesterol esterase catalyzed hydrolysis of mixed micellar thiophosphatidylcholines: a possible charge-relay mechanism. Biochemistry. 30: 5888-93. PMID 2043629 DOI: 10.1021/Bi00238A012 |
0.421 |
|
| 1990 |
Acheson SA, Quinn DM. Anatomy of acetylcholinesterase catalysis: reaction dynamics analogy for human erythrocyte and electric eel enzymes. Biochimica Et Biophysica Acta. 1040: 199-205. PMID 2400771 DOI: 10.1016/0167-4838(90)90076-R |
0.435 |
|
| 1990 |
Yuan W, Quinn DM, Sigler PB, Gelb MH. Kinetic and inhibition studies of phospholipase A2 with short-chain substrates and inhibitors. Biochemistry. 29: 6082-94. PMID 2383571 DOI: 10.1021/Bi00477A028 |
0.386 |
|
| 1990 |
Sutton LD, Lantz JL, Eibes T, Quinn DM. Dimensional mapping of the active site of cholesterol esterase with alkylboronic acid inhibitors. Biochimica Et Biophysica Acta. 1041: 79-82. PMID 2223850 DOI: 10.1016/0167-4838(90)90125-Y |
0.423 |
|
| 1990 |
Quinn DM, Sutton LD, Stout JS, Calogeropoulou T, Wiemer DF, Hendrickson HS. Phospholipase A1 activity and catalytic mechanism of pancreatic cholesterol esterase Phosphorus Sulfur and Silicon and the Related Elements. 51: 43-46. DOI: 10.1080/10426509008544196 |
0.358 |
|
| 1990 |
Sutton LD, Quinn DM. Modulation by organic cosolvent of microscopic compositions of virtual transition states in the acylation stage of cholesterol esterase catalyzed hydrolysis of short-chain p-nitrophenyl esters Journal of the American Chemical Society. 112: 8404-8408. DOI: 10.1021/Ja00179A026 |
0.323 |
|
| 1990 |
Sutton LD, Stout JS, Quinn DM. Dependence of transition-state structure on acyl chain length for cholesterol esterase catalyzed hydrolysis of lipid p-nitrophenyl esters Journal of the American Chemical Society. 112: 8398-8403. DOI: 10.1021/Ja00179A025 |
0.35 |
|
| 1988 |
Sohl J, Sutton LD, Burton DJ, Quinn DM. Haloketone transition state analog inhibitors of cholesterol esterase. Biochemical and Biophysical Research Communications. 151: 554-60. PMID 3348795 DOI: 10.1016/0006-291X(88)90630-4 |
0.434 |
|
| 1987 |
Barlow PN, Acheson SA, Swanson ML, Quinn DM. Acetylcholinesterase-catalyzed hydrolysis of anilides: Acylation reaction dynamics and intrinsic chemical transition-state structures Journal of the American Chemical Society. 109: 253-257. DOI: 10.1021/Ja00235A038 |
0.403 |
|
| 1987 |
Acheson SA, Barlow PN, Lee GC, Swanson ML, Quinn DM. Effect of reactivity on virtual transition-state structure for the acylation stage of acetylcholinesterase-catalyzed hydrolysis of aryl esters and anilides Journal of the American Chemical Society. 109: 246-252. DOI: 10.1021/Ja00235A037 |
0.403 |
|
| 1987 |
Acheson SA, Dedopoulou D, Quinn DM. Simple general acid-base catalysis and virtual transition states for acetylcholinesterase-catalyzed hydrolysis of phenyl esters Journal of the American Chemical Society. 109: 239-245. DOI: 10.1021/Ja00235A036 |
0.364 |
|
| 1987 |
Quinn DM. Acetylcholinesterase: Enzyme structure, reaction dynamics, and virtual transition states Chemical Reviews. 87: 955-979. DOI: 10.1021/Cr00081A005 |
0.407 |
|
| 1986 |
Sutton LD, Stout JS, Hosie L, Spencer PS, Quinn DM. Phenyl-n-butylborinic acid is a potent transition state analog inhibitor of lipolytic enzymes. Biochemical and Biophysical Research Communications. 134: 386-92. PMID 3947331 DOI: 10.1016/0006-291X(86)90575-9 |
0.42 |
|
| 1985 |
Stout JS, Sutton LD, Quinn DM. Acylenzyme mechanism and solvent isotope effects for cholesterol esterase-catalyzed hydrolysis of p-nitrophenyl butyrate. Biochimica Et Biophysica Acta. 837: 6-12. PMID 4052438 DOI: 10.1016/0005-2760(85)90079-7 |
0.388 |
|
| 1985 |
Quinn DM. Solvent isotope effects for lipoprotein lipase catalyzed hydrolysis of water-soluble p-nitrophenyl esters. Biochemistry. 24: 3144-9. PMID 4027237 DOI: 10.1021/Bi00334A011 |
0.382 |
|
| 1985 |
Quinn DM. Diethyl-p-nitrophenyl phosphate: an active site titrant for lipoprotein lipase. Biochimica Et Biophysica Acta. 834: 267-71. PMID 3995064 DOI: 10.1016/0005-2760(85)90165-1 |
0.37 |
|
| 1984 |
Quinn DM, Swanson ML. Virtual transition state for the acylation step of acetylcholinesterase-catalyzed hydrolysis of o-nitrochloroacetanilide Journal of the American Chemical Society. 106: 1883-1884. DOI: 10.1021/Ja00318A080 |
0.343 |
|
| 1984 |
Stein RL, Fujihara H, Quinn DM, Fischer G, Kuellertz G, Barth A, Schowen RL. Transition-state structural features for anilide hydrolysis from. beta. -deuterium isotope effects Journal of the American Chemical Society. 106: 1457-1461. DOI: 10.1021/Ja00317A045 |
0.489 |
|
| 1984 |
Stein RL, Fujihara H, Quinn DM, Fischer G, Küllertz G, Barth A, Schowen RL. Transition-state structural features for anilide hydrolysis from β-deuterium isotope effects Journal of the American Chemical Society. 106: 1457-1461. |
0.5 |
|
| 1982 |
Quinn DM, Shirai K, Jackson RL, Harmony JA. Lipoprotein lipase catalyzed hydrolysis of water-soluble p-nitrophenyl esters. Inhibition by apolipoprotein C-II. Biochemistry. 21: 6872-9. PMID 7159570 DOI: 10.1021/Bi00269A038 |
0.337 |
|
| 1982 |
Kroon PA, Quinn DM, Cordes EH. A carbon-13 nuclear magnetic resonance study of aortic lesions and cholesteryl ester rich lipoproteins from atherosclerotic rabbits. Biochemistry. 21: 2745-53. PMID 7093219 DOI: 10.1021/Bi00540A026 |
0.516 |
|
| 1980 |
Quinn DM, Venkatasubban KS, Kise M, Schowen RL. Protonic reorganization and substrate structure in catalysis by amidohydrolases Journal of the American Chemical Society. 102: 5365-5369. DOI: 10.1021/Ja00536A041 |
0.558 |
|
| 1980 |
Quinn DM, Elrod JP, Ardis R, Friesen P, Schowen RL. Protonic reorganization in catalysis by serine proteases: Acylation by small substrates Journal of the American Chemical Society. 102: 5358-5365. DOI: 10.1021/Ja00536A040 |
0.561 |
|
| 1980 |
Elrod JP, Hogg JL, Quinn DM, Venkatasubban KS, Schowen RL. Protonic reorganization and substrate structure in catalysis by serine proteases Journal of the American Chemical Society. 102: 3917-3922. DOI: 10.1021/Ja00531A039 |
0.568 |
|
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