Evidence for Subdomain Flexibility in Drosophila melanogaster Acetylcholinesterase-Reference-Cited by-同舟云学术

Evidence for Subdomain Flexibility in Drosophila melanogaster Acetylcholinesterase

Published:2008-04-26 Issue:20 Volume:47 Page:5599-5607
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Stojan Jure¹,Ladurantie Caroline¹,Siadat Omid Ranei¹,Paquereau Laurent¹,Fournier Didier¹

Affiliation:

1. Institute of Biochemistry, Faculty of Medicine, University of Ljubljana, Vrazov trg 2, 1000 Ljubljana, Slovenia, and IPBS-CNRS, 205 Route de Narbonne, Toulouse, France

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi7025479

Reference47 articles.

1. Atomic Structure of Acetylcholinesterase from Torpedo californica : A Prototypic Acetylcholine-Binding Protein

2. Acetylthiocholine Binds to Asp74 at the Peripheral Site of Human Acetylcholinesterase as the First Step in the Catalytic Pathway

3. Inhibition of Drosophila melanogaster acetylcholinesterase by high concentrations of substrate

4. Structural insights into substrate traffic and inhibition in acetylcholinesterase

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