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Suzanne Bon

Researcher at École Normale Supérieure

Publications -  94
Citations -  5996

Suzanne Bon is an academic researcher from École Normale Supérieure. The author has contributed to research in topics: Acetylcholinesterase & Electrophorus. The author has an hindex of 43, co-authored 94 publications receiving 5883 citations. Previous affiliations of Suzanne Bon include Centre national de la recherche scientifique & French Institute of Health and Medical Research.

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Molecular and cellular biology of cholinesterases

TL;DR: In this article, the authors propose a method to identify the root cause of a problem.Abbreviations: [2]... ].., [3]
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Conversion of acetylcholinesterase to butyrylcholinesterase: modeling and mutagenesis.

TL;DR: Modeling showed that two conserved aromatic residues that line the active-site gorge in AcChoEase may prevent entrance of butyrylcholine into the acyl-binding pocket in Bt ChoEase, and showed a double mutant that hydrolyzed butyRYlthiocholine almost as well as acetylth Antiocholine.
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Asymmetric and globular forms of acetylcholinesterase in mammals and birds.

TL;DR: The nomenclature introduced is very probably valid for the main AcChoE molecular forms, at least in vertebrates, and should help to clarify structural relationships and homologies among them, and does not claim to represent entirely the complex polymorphism of Ac ChoE.
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Mutation in the Human Acetylcholinesterase-Associated Collagen Gene, COLQ, Is Responsible for Congenital Myasthenic Syndrome with End-Plate Acetylcholinesterase Deficiency (Type Ic)

TL;DR: A large family comprising 11 siblings, 6 of whom are affected by a mild form of CMS-Ic, is studied, finding that the patients present a homozygous missense mutation, Y431S, in the conserved C-terminal domain of COLQ, thought to disturb the attachment of collagen-tailed AChE to the NMJ, thus constituting the first genetic defect causing CMS- Ic.
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Affinity chromatography of acetylcholinesterase. The importance of hydrophobic interactions.

TL;DR: An easily prepared affinity column for acetylcholinesterase is described, which may be operated at ionic strength high enough to prevent aggregation of the asymmetric forms of the enzyme.