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Items: 5

1.

Salmeterol's extreme β2 selectivity is due to residues in both extracellular loops and transmembrane domains.

Baker JG, Proudman RG, Hill SJ.

Mol Pharmacol. 2015 Jan;87(1):103-20. doi: 10.1124/mol.114.095364. Epub 2014 Oct 16.

PMID:
25324048
2.

Identification of key residues in transmembrane 4 responsible for the secondary, low-affinity conformation of the human β1-adrenoceptor.

Baker JG, Proudman RG, Hill SJ.

Mol Pharmacol. 2014 May;85(5):811-29. doi: 10.1124/mol.114.091587. Epub 2014 Mar 7.

3.

Impact of polymorphic variants on the molecular pharmacology of the two-agonist conformations of the human β1-adrenoceptor.

Baker JG, Proudman RG, Hill SJ.

PLoS One. 2013 Nov 8;8(11):e77582. doi: 10.1371/journal.pone.0077582. eCollection 2013.

4.

The pharmacological effects of the thermostabilising (m23) mutations and intra and extracellular (β36) deletions essential for crystallisation of the turkey β-adrenoceptor.

Baker JG, Proudman RG, Tate CG.

Naunyn Schmiedebergs Arch Pharmacol. 2011 Jul;384(1):71-91. doi: 10.1007/s00210-011-0648-4. Epub 2011 May 6.

5.

Role of key transmembrane residues in agonist and antagonist actions at the two conformations of the human beta1-adrenoceptor.

Baker JG, Proudman RG, Hawley NC, Fischer PM, Hill SJ.

Mol Pharmacol. 2008 Nov;74(5):1246-60. doi: 10.1124/mol.108.048371. Epub 2008 Aug 7.

PMID:
18687809

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