Modeling Anesthetic Binding Sites within the Glycine Alpha One Receptor Based on Prokaryotic Ion Channel Templates: The Problem with TM4-Reference-Cited by-同舟云学术

Modeling Anesthetic Binding Sites within the Glycine Alpha One Receptor Based on Prokaryotic Ion Channel Templates: The Problem with TM4

Published:2010-11-30 Issue:12 Volume:50 Page:2248-2255
ISSN:1549-9596
Container-title:Journal of Chemical Information and Modeling
language:en
Short-container-title:J. Chem. Inf. Model.

Author:

Bertaccini Edward J.¹,Wallner Björn¹,Trudell James R.¹,Lindahl Erik¹

Affiliation:

1. Department of Anesthesia, Stanford University School of Medicine and Beckman Center for Molecular and Genetic Medicine, Stanford, California, United States, Department of Veterans Affairs, Palo Alto VA Health Care System, Palo Alto, California, United States, and Department of Biochemistry and Biophysics, Stockholm Bioinformatics Center and Center for Biomembrane Research, Stockholm University, Stockholm, Sweden

Publisher

American Chemical Society (ACS)

Subject

Library and Information Sciences,Computer Science Applications,General Chemical Engineering,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ci100266c

Reference37 articles.

1. Refined Structure of the Nicotinic Acetylcholine Receptor at 4Å Resolution

2. Normal-Mode Analysis of the Glycine Alpha1 Receptor by Three Separate Methods

3. The Common Chemical Motifs Within Anesthetic Binding Sites

4. Homology Modeling of a Human Glycine Alpha 1 Receptor Reveals a Plausible Anesthetic Binding Site

5. Predicting the transmembrane secondary structure of ligand-gated ion channels

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