Negative cooperativity across β 1 ‐adrenoceptor homodimers provides insights into the nature of the secondary low‐affinity CGP 12177 β1‐adrenoceptor binding conformation-Reference-Cited by-同舟云学术

Negative cooperativity across β 1 ‐adrenoceptor homodimers provides insights into the nature of the secondary low‐affinity CGP 12177 β1‐adrenoceptor binding conformation

Published:2015-04-02 Issue:7 Volume:29 Page:2859-2871
ISSN:0892-6638
Container-title:The FASEB Journal
language:en
Short-container-title:FASEB j.

Author:

Gherbi Karolina¹,May Lauren T.¹,Baker Jillian G.¹,Briddon Stephen J.¹,Hill Stephen J.¹

Affiliation:

1. Cell Signalling Research GroupSchool of Life Sciences, University of NottinghamNottinghamUnited Kingdom

Funder

Medical Research Council

Publisher

Wiley

Subject

Genetics,Molecular Biology,Biochemistry,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1096/fj.14-265199

Reference36 articles.

1. Abolition of (-)-CGP 12177-evoked cardiostimulation in double ? 1 /? 2 -adrenoceptor knockout mice. Obligatory role of ? 1 -adrenoceptors for putative ? 4 -adrenoceptor pharmacology

2. (-)-CGP 12177 increases contractile force and hastens relaxation of human myocardial preparations through a propranolol-resistant state of the β1-adrenoceptor

3. The low-affinity site of the β1-adrenoceptor and its relevance to cardiovascular pharmacology

4. Anomalous Behavior of CGP 12177A ON β2-Adrenergic Receptors

5. The putative β4-adrenergic receptor is a novel state of the β1-adrenergic receptor

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