Biophysical Fragment Screening of the β1-Adrenergic Receptor: Identification of High Affinity Arylpiperazine Leads Using Structure-Based Drug Design-Reference-Cited by-同舟云学术

Biophysical Fragment Screening of the β1-Adrenergic Receptor: Identification of High Affinity Arylpiperazine Leads Using Structure-Based Drug Design

Published:2013-04-09 Issue:9 Volume:56 Page:3446-3455
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Christopher John A.¹,Brown Jason¹,Doré Andrew S.¹,Errey James C.¹,Koglin Markus¹,Marshall Fiona H.¹,Myszka David G.²,Rich Rebecca L.²,Tate Christopher G.³,Tehan Benjamin¹,Warne Tony³,Congreve Miles¹

Affiliation:

1. Heptares Therapeutics Ltd., BioPark, Welwyn Garden City, Hertfordshire, AL7 3AX, U.K.

2. Biosensor Tools LLC, Salt Lake City, Utah 84103, United States

3. MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge CB2 0QH, U.K.

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/jm400140q

Reference77 articles.

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3. Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor

4. Crystal structure of the human β2 adrenergic G-protein-coupled receptor

5. High-Resolution Crystal Structure of an Engineered Human β 2 -Adrenergic G Protein–Coupled Receptor

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