Cage amines as the stopper inhibitors of cholinesterases

scientific article published on September 1, 2003

Cage amines as the stopper inhibitors of cholinesterases is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1016/S0960-894X(03)00599-7
P953full work available at URLhttps://api.elsevier.com/content/article/PII:S0960894X03005997?httpAccept=text/xml
https://api.elsevier.com/content/article/PII:S0960894X03005997?httpAccept=text/plain
P698PubMed publication ID14611850

P2093author name stringGialih Lin
Hou-Jen Tsai
Yi-Hon Tsai
P2860cites workJournal of Pharmacology and Experimental TherapeuticsQ1500272
Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesteraseQ24561371
A new and rapid colorimetric determination of acetylcholinesterase activityQ26778487
"Back door" opening implied by the crystal structure of a carbamoylated acetylcholinesteraseQ27618113
Conformational flexibility of the acetylcholinesterase tetramer suggested by x-ray crystallographyQ27619980
Atomic Structure of Acetylcholinesterase from Torpedo californica : A Prototypic Acetylcholine-Binding ProteinQ28247386
Phenserine and ring C hetero-analogues: drug candidates for the treatment of Alzheimer's diseaseQ40616325
Methyl analogues of the experimental Alzheimer drug phenserine: synthesis and structure/activity relationships for acetyl- and butyrylcholinesterase inhibitory actionQ43799625
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitorsQ46263827
Highly potent, selective, and low cost bis-tetrahydroaminacrine inhibitors of acetylcholinesterase. Steps toward novel drugs for treating Alzheimer's diseaseQ48913512
The X-ray Structure of a Transition State Analog Complex Reveals the Molecular Origins of the Catalytic Power and Substrate Specificity of AcetylcholinesteraseQ57998549
Molecular recognition in acetylcholinesterase catalysis: free-energy correlations for substrate turnover and inhibition by trifluoro ketone transition-state analogsQ72061964
Differences in active site gorge dimensions of cholinesterases revealed by binding of inhibitors to human butyrylcholinesteraseQ73940207
Interaction between the peripheral site residues of human butyrylcholinesterase, D70 and Y332, in binding and hydrolysis of substratesQ78122923
P433issue17
P407language of work or nameEnglishQ1860
P921main subjectpharmaceutical scienceQ7180763
biochemistryQ7094
organic chemistryQ11351
molecular medicineQ3523816
P304page(s)2887-2890
P577publication date2003-09-01
P1433published inBioorganic & Medicinal Chemistry LettersQ2709483
P1476titleCage amines as the stopper inhibitors of cholinesterases
P478volume13

Reverse relations

cites work (P2860)
Q47220501Molecular docking of different inhibitors and activators to butyrylcholinesterase
Q45222504Ortho effects in quantitative structure-activity relationships for acetylcholinesterase inhibition by aryl carbamates
Q43210299Stereoselective inhibition of butyrylcholinesterase by enantiomers of exo- and endo-2-norbornyl-N-n-butylcarbamates
Q45983116Synthesis of enantiomers of exo-2-norbornyl-N-n-butylcarbamate and endo-2-norbornyl-N-n-butylcarbamate for stereoselective inhibition of acetylcholinesterase.

Search more.