Agency
National Institute of Health (NIH)
Institute
National Institute of Neurological Disorders and Stroke (NINDS)
Type
Research Project (R01)
Project #
2R01NS016577-17A2
Application #
2624836
Study Section
Physical Biochemistry Study Section (PB)
Program Officer
Baughman, Robert W
Project Start
1980-07-01
Project End
2001-03-31
Budget Start
1998-04-01
Budget End
1999-03-31
Support Year
17
Fiscal Year
1998
Total Cost
Indirect Cost
Name
Mayo Clinic, Jacksonville
Department
Type
DUNS #
153223151
City
Jacksonville
State
FL
Country
United States
Zip Code
32224
Venkatasubban, Kunisi S; Johnson, Joseph L; Thomas, Jamie L et al. (2018) Decarbamoylation of acetylcholinesterases is markedly slowed as carbamoyl groups increase in size. Arch Biochem Biophys 655:67-74
Beri, Veena; Auletta, Jeffrey T; Maharvi, Ghulam M et al. (2013) Hydrolysis of low concentrations of the acetylthiocholine analogs acetyl(homo)thiocholine and acetyl(nor)thiocholine by acetylcholinesterase may be limited by selective gating at the enzyme peripheral site. Chem Biol Interact 203:38-43
Dvir, Hay; Silman, Israel; Harel, Michal et al. (2010) Acetylcholinesterase: from 3D structure to function. Chem Biol Interact 187:10-22
Auletta, Jeffrey T; Johnson, Joseph L; Rosenberry, Terrone L (2010) Molecular basis of inhibition of substrate hydrolysis by a ligand bound to the peripheral site of acetylcholinesterase. Chem Biol Interact 187:135-41
Rosenberry, Terrone L; Sonoda, Leilani K; Dekat, Sarah E et al. (2008) Monitoring the reaction of carbachol with acetylcholinesterase by thioflavin T fluorescence and acetylthiocholine hydrolysis. Chem Biol Interact 175:235-41
Rosenberry, Terrone L; Sonoda, Leilani K; Dekat, Sarah E et al. (2008) Analysis of the reaction of carbachol with acetylcholinesterase using thioflavin T as a coupled fluorescence reporter. Biochemistry 47:13056-63
Harel, Michal; Sonoda, Leilani K; Silman, Israel et al. (2008) Crystal structure of thioflavin T bound to the peripheral site of Torpedo californica acetylcholinesterase reveals how thioflavin T acts as a sensitive fluorescent reporter of ligand binding to the acylation site. J Am Chem Soc 130:7856-61
Johnson, Joseph L; Cusack, Bernadette; Davies, Matthew P et al. (2003) Unmasking tandem site interaction in human acetylcholinesterase. Substrate activation with a cationic acetanilide substrate. Biochemistry 42:5438-52
Dvir, H; Wong, D M; Harel, M et al. (2002) 3D structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 A resolution: kinetic and molecular dynamic correlates. Biochemistry 41:2970-81
De Ferrari, G V; Mallender, W D; Inestrosa, N C et al. (2001) Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and acylation sites. J Biol Chem 276:23282-7

Showing the most recent 10 out of 46 publications