scholarly article | Q13442814 |
P2093 | author name string | Gialih Lin | |
Hou-Jen Tsai | |||
Yi-Hon Tsai | |||
P2860 | cites work | Journal of Pharmacology and Experimental Therapeutics | Q1500272 |
Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase | Q24561371 | ||
A new and rapid colorimetric determination of acetylcholinesterase activity | Q26778487 | ||
"Back door" opening implied by the crystal structure of a carbamoylated acetylcholinesterase | Q27618113 | ||
Conformational flexibility of the acetylcholinesterase tetramer suggested by x-ray crystallography | Q27619980 | ||
Atomic Structure of Acetylcholinesterase from Torpedo californica : A Prototypic Acetylcholine-Binding Protein | Q28247386 | ||
Phenserine and ring C hetero-analogues: drug candidates for the treatment of Alzheimer's disease | Q40616325 | ||
Methyl analogues of the experimental Alzheimer drug phenserine: synthesis and structure/activity relationships for acetyl- and butyrylcholinesterase inhibitory action | Q43799625 | ||
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors | Q46263827 | ||
Highly potent, selective, and low cost bis-tetrahydroaminacrine inhibitors of acetylcholinesterase. Steps toward novel drugs for treating Alzheimer's disease | Q48913512 | ||
The X-ray Structure of a Transition State Analog Complex Reveals the Molecular Origins of the Catalytic Power and Substrate Specificity of Acetylcholinesterase | Q57998549 | ||
Molecular recognition in acetylcholinesterase catalysis: free-energy correlations for substrate turnover and inhibition by trifluoro ketone transition-state analogs | Q72061964 | ||
Differences in active site gorge dimensions of cholinesterases revealed by binding of inhibitors to human butyrylcholinesterase | Q73940207 | ||
Interaction between the peripheral site residues of human butyrylcholinesterase, D70 and Y332, in binding and hydrolysis of substrates | Q78122923 | ||
P433 | issue | 17 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | pharmaceutical science | Q7180763 |
biochemistry | Q7094 | ||
organic chemistry | Q11351 | ||
molecular medicine | Q3523816 | ||
P304 | page(s) | 2887-2890 | |
P577 | publication date | 2003-09-01 | |
P1433 | published in | Bioorganic & Medicinal Chemistry Letters | Q2709483 |
P1476 | title | Cage amines as the stopper inhibitors of cholinesterases | |
P478 | volume | 13 |
Q47220501 | Molecular docking of different inhibitors and activators to butyrylcholinesterase |
Q45222504 | Ortho effects in quantitative structure-activity relationships for acetylcholinesterase inhibition by aryl carbamates |
Q43210299 | Stereoselective inhibition of butyrylcholinesterase by enantiomers of exo- and endo-2-norbornyl-N-n-butylcarbamates |
Q45983116 | Synthesis of enantiomers of exo-2-norbornyl-N-n-butylcarbamate and endo-2-norbornyl-N-n-butylcarbamate for stereoselective inhibition of acetylcholinesterase. |
Search more.