title: Cholinesterase confabs and cousins: approaching forty years.
abstract: In the past four decades of cholinesterase (ChE) research, we have seen substantive evolution of the field from one centered around substrate and inhibitor kinetic profiles and compound characterizations to the analysis of ChE structure, first through the gene families and then by X-ray crystallographic determinations of the free enzymes and their complexes and conjugates. Indeed, these endeavors have been facilitated by recombinant DNA technologies, structure determinations and parallel studies in related proteins in the α/β-hydrolase fold family. This approach has not only contributed to a fundamental understanding of structure and function of a large family of hydrolase-like proteins possessing functions other than catalysis, but also has been used to develop new practical strategies for scavenging and antidotal activity in cases of organophosphate insecticide or nerve agent exposure.
authors.affiliation: Skaggs School of Pharmacy & Pharmaceutical Sciences, University of California, San Diego, 9500 Gilman Drive, Mail Code 0657, La Jolla, CA 92093, United States. pwtaylor@ucsd.edu
authors.forename: Palmer
authors.initials: P
authors.lastname: Taylor
authors.forename: Antonella
authors.initials: A
authors.lastname: De Jaco
authors.forename: Davide
authors.initials: D
authors.lastname: Comoletti
authors.forename: Meghan
authors.initials: M
authors.lastname: Miller
authors.forename: Shelley
authors.initials: S
authors.lastname: Camp
mesh_terms: D000818:Animals; D002802:Cholinesterases / Q000737:chemistry / Q000235:genetics / Q000266:history* / Q000378:metabolism; D049673:History, 20th Century; D049674:History, 21st Century; D006801:Humans; D008958:Models, Molecular; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000235:genetics / Q000266:history / Q000378:metabolism; D017510:Protein Folding; D017434:Protein Structure, Tertiary
chemical_list: D009419:Nerve Tissue Proteins; D002802:Cholinesterases