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My research concerns the enzyme acetylcholinesterase (AChE), which terminates impulse transmission at cholinergic synapses by hydrolyzing the neurotransmitter, acetylcholine (ACh). AChE is a rapid enzyme that occurs in multiple forms differing in structure and modes of attachment to the cell surface. They are generated by alternative splicing, which leads to differential posttranslational modification producing several modes of membrane-anchoring. My work deals with the structure of AChE, its mechanism, its anchoring and localization, and with regulation of its folding and assembly.
Most of our work employs a dimeric form of AChE from the electric organ of Torpedo californica. This form belongs to a family of membrane proteins, the GPI-proteins; they are anchored to the outer face of the plasma membrane by a single residue of phosphatidylinositol (PI), covalently attached, via an oligoglycan (G) extension, at the COOH-terminus. With Mike Ferguson and Steve Homans (University of Dundee), we have determined the structure of the anchoring domain.
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JOURNAL OF MOLECULAR NEUROSCIENCEno. SUPnan (2012): S4-S4
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Structural Proteomics and Its Impact on the Life Sciencespp.505-537, (2008)
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