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Research ArticleArticle

Salmeterol’s Extreme β2 Selectivity Is Due to Residues in Both Extracellular Loops and Transmembrane Domains

Jillian G. Baker, Richard G. W. Proudman and Stephen J. Hill
Molecular Pharmacology January 2015, 87 (1) 103-120; DOI: https://doi.org/10.1124/mol.114.095364

Article Information

vol. 87 no. 1 103-120
DOI 
https://doi.org/10.1124/mol.114.095364
PubMed 
25324048
Published By 
American Society for Pharmacology and Experimental Therapeutics
Print ISSN 
0026-895X
Online ISSN 
1521-0111
History 
  • Received August 12, 2014
  • Accepted October 16, 2014
  • Published online November 20, 2014.

Article Versions

Copyright & Usage 
Copyright © 2014 by The American Society for Pharmacology and Experimental Therapeutics

Author Information

  1. Jillian G. Baker,
  2. Richard G. W. Proudman, and
  3. Stephen J. Hill
  1. Cell Signalling, School of Life Sciences, Queen’s Medical Centre, University of Nottingham, Nottingham, United Kingdom
  1. Address correspondence to:
    Dr. Jillian G. Baker, Cell Signalling, School of Life Sciences, C Floor Medical School, University of Nottingham, Queen’s Medical Centre, Nottingham, NG7 2UH, United Kingdom. E-mail: jillian.baker{at}nottingham.ac.uk
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Identification of Salmeterol’s High-Affinity Binding Sites

Jillian G. Baker, Richard G. W. Proudman and Stephen J. Hill
Molecular Pharmacology January 1, 2015, 87 (1) 103-120; DOI: https://doi.org/10.1124/mol.114.095364
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