Structural characterization of the asymmetric (17 + 13) S species of acetylcholinesterase from Torpedo. II. Component peptides obtained by selective proteolysis and disulfide bond reduction.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference20 articles.
1. Structural characterization of the asymmetric (17 + 13) S forms of acetylcholinesterase from Torpedo. I. Analysis of subunit composition.
2. Molecular forms of acetylcholinesterase from Torpedo californica: their relation to synaptic membranes
3. Torpedo marmorata Acetylcholinesterase; a Comparison with the Electrophorus electricus Enzyme. Molecular Forms, Subunits, Electron, Microscopy, Immunological Relationship
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1. Polyproline-rich peptides associated with Torpedo californica acetylcholinesterase tetramers;Chemico-Biological Interactions;2020-03
2. Tetrameric Mouse Acetylcholinesterase: Continuum Diffusion Rate Calculations by Solving the Steady-State Smoluchowski Equation Using Finite Element Methods;Biophysical Journal;2005-03
3. Conformational Flexibility of the Acetylcholinesterase Tetramer Suggested by X-ray Crystallography;Journal of Biological Chemistry;1999-10
4. A four-to-one association between peptide motifs: four C-terminal domains from cholinesterase assemble with one proline-rich attachment domain (PRAD) in the secretory pathway;The EMBO Journal;1998-11-02
5. At Least Two Receptors of Asymmetric Acetylcholinesterase Are Present at the Synaptic Basal Lamina ofTorpedoElectric Organ;Biochemical and Biophysical Research Communications;1998-09
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