Structures of Human Acetylcholinesterase Bound to Dihydrotanshinone I and Territrem B Show Peripheral Site Flexibility-Reference-Cited by-同舟云学术

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Structures of Human Acetylcholinesterase Bound to Dihydrotanshinone I and Territrem B Show Peripheral Site Flexibility

Published:2013-09-30 Issue:11 Volume:4 Page:1091-1096
ISSN:1948-5875
Container-title:ACS Medicinal Chemistry Letters
language:en
Short-container-title:ACS Med. Chem. Lett.

Author:

Cheung Jonah¹,Gary Ebony N.¹,Shiomi Kazuro²,Rosenberry Terrone L.³

Affiliation:

1. New York Structural Biology Center, New York, New York 10027, United States

2. Kitasato Institute for Life Sciences, Kitasato University, Tokyo 108-8641, Japan

3. Departments of Neuroscience and Pharmacology, Mayo Clinic Florida, Jacksonville, Florida 32224, United States

Publisher

American Chemical Society (ACS)

Subject

Organic Chemistry,Drug Discovery,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ml400304w

Reference36 articles.

1. Quantitative simulation of endplate currents at neuromuscular junctions based on the reaction of acetylcholine with acetylcholine receptor and acetylcholinesterase

2. Anticholinesterases: Medical Applications of Neurochemical Principles

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

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