Crystal Structure of Human Butyrylcholinesterase and of Its Complexes with Substrate and Products
Top Cited Papers
Open Access
- 1 October 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (42) , 41141-41147
- https://doi.org/10.1074/jbc.m210241200
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- Does “Butyrylization” of Acetylcholinesterase through Substitution of the Six Divergent Aromatic Amino Acids in the Active Center Gorge Generate an Enzyme Mimic of Butyrylcholinesterase?Biochemistry, 2001
- Crystal Structure of Mouse AcetylcholinesteraseJournal of Biological Chemistry, 1999
- Substrate Binding to the Peripheral Site of Acetylcholinesterase Initiates Enzymatic Catalysis. Substrate Inhibition Arises as a Secondary EffectBiochemistry, 1998
- Trp82 and Tyr332 Are Involved in Two Quaternary Ammonium Binding Domains of Human Butyrylcholinesterase as Revealed by Photoaffinity Labeling with [3H]DDFBiochemistry, 1998
- Role of Aspartate 70 and Tryptophan 82 in Binding of Succinyldithiocholine to Human ButyrylcholinesteraseBiochemistry, 1997
- Acetylcholinesterase inhibition by fasciculin: Crystal structure of the complexCell, 1995
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitorsBiochemistry, 1993
- Protein structure refinement: Streptomyces griseus serine protease A at 1.8 Å resolutionJournal of Molecular Biology, 1979
- Dealkylation and Loss of Capacity for Reactivation of Cholinesterase Inhibited by SarinScience, 1966