The 2.1 Å Resolution Structure of Cyanopindolol-Bound β1-Adrenoceptor Identifies an Intramembrane Na+ Ion that Stabilises the Ligand-Free Receptor (Q27682443)

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English	The 2.1 Å Resolution Structure of Cyanopindolol-Bound β1-Adrenoceptor Identifies an Intramembrane Na+ Ion that Stabilises the Ligand-Free Receptor	scientific article

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12 March 2020

The 2.1 Å resolution structure of cyanopindolol-bound β1-adrenoceptor identifies an intramembrane Na+ ion that stabilises the ligand-free receptor (English)

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12 March 2020

Jennifer L Miller

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12 March 2020

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12 March 2020

Gebhard Schertler

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12 March 2020

Christopher G. Tate

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12 March 2020

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Rony Nehmé

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Patricia C Edwards

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12 March 2020

Andrew G W Leslie

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24 March 2014

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12 March 2020

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24 March 2014

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High-resolution crystal structure of human protease-activated receptor 1

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Crystal Structures of a Stabilized β1-Adrenoceptor Bound to the Biased Agonists Bucindolol and Carvedilol

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Mutational analysis of the conserved Asp2.50 and ERY motif reveals signaling bias of the urotensin II receptor

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Site-directed mutagenesis and continuous expression of human beta-adrenergic receptors. Identification of a conserved aspartate residue involved in agonist binding and receptor activation

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based on heuristic

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Metal-ligand geometry relevant to proteins and in proteins: sodium and potassium

1 reference

https://pubmed.ncbi.nlm.nih.gov/24663151

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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1 reference

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inferred from PubMed ID database lookup

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1 reference

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12 December 2020

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inferred from PubMed ID database lookup

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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10.1371/JOURNAL.PONE.0092727

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12 March 2020

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12 March 2020

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