Allosteric Control of Acetylcholinesterase Catalysis by Fasciculin
Open Access
- 1 September 1995
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 270 (35) , 20391-20399
- https://doi.org/10.1074/jbc.270.35.20391
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- m-Alkyl, α,α,α-trifluoroacetophenones: A new class of potent transition state analog inhibitors of acetylcholinesteraseBioorganic & Medicinal Chemistry Letters, 1993
- Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitorsBiochemistry, 1993
- m-(N,N,N-Trimethylammonio)trifluoroacetophenone: a femtomolar inhibitor of acetylcholinesteraseJournal of the American Chemical Society, 1993
- Chimeric Human CholinesteraseJournal of Molecular Biology, 1993
- Amino acid residues controlling acetylcholinesterase and butyrylcholinesterase specificityBiochemistry, 1993
- Conversion of acetylcholinesterase to butyrylcholinesterase: modeling and mutagenesis.Proceedings of the National Academy of Sciences, 1992
- 1.9-A resolution structure of fasciculin 1, an anti-acetylcholinesterase toxin from green mamba snake venom.Journal of Biological Chemistry, 1992
- Current view on the structure-function relationship of postsynaptic neurotoxins from snake venomsPharmacology & Therapeutics, 1987
- Anticholinesterase toxinsPharmacology & Therapeutics, 1985
- A new and rapid colorimetric determination of acetylcholinesterase activityBiochemical Pharmacology, 1961