scholarly journals Correction to “Sodium Ion Binding Pocket Mutations and Adenosine A2A Receptor Function”

2019 ◽  
Vol 95 (4) ◽  
pp. 462-462
Keyword(s):  
Binding Pocket ◽  
Adenosine A2a Receptor ◽  
Sodium Ion ◽  
Ion Binding ◽  
Receptor Function ◽  
A2a Receptor ◽  
Adenosine A2a

scholarly journals Sodium Ion Binding Pocket Mutations and Adenosine A2A Receptor Function

2014 ◽  
Vol 87 (2) ◽  
pp. 305-313 ◽  
Author(s):  
Arnault Massink ◽  
Hugo Gutiérrez-de-Terán ◽  
Eelke B. Lenselink ◽  
Natalia V. Ortiz Zacarías ◽  
Lizi Xia ◽  
...  
Keyword(s):  
Binding Pocket ◽  
Adenosine A2a Receptor ◽  
Sodium Ion ◽  
Ion Binding ◽  
Receptor Function ◽  
A2a Receptor ◽  
Adenosine A2a

scholarly journals P3-214: ADENOSINE A2A RECEPTOR ACTIVATION ATTENUATES NMDA RECEPTOR FUNCTION IN ALZHEIMER DISEASE

2019 ◽  
Vol 15 ◽  
pp. P1012-P1012
Author(s):  
Gemma Navarro Brugal ◽  
David Aguinaga ◽  
Irene Reyes ◽  
Iu Raïch ◽  
Anna Del Ser ◽  
...  
Keyword(s):  
Nmda Receptor ◽  
Alzheimer Disease ◽  
Receptor Activation ◽  
Adenosine A2a Receptor ◽  
Receptor Function ◽  
A2a Receptor ◽  
Nmda Receptor Function ◽  
Adenosine A2a

5′-Substituted Amiloride Derivatives as Allosteric Modulators Binding in the Sodium Ion Pocket of the Adenosine A2A Receptor

2016 ◽  
Vol 59 (10) ◽  
pp. 4769-4777 ◽  
Author(s):  
Arnault Massink ◽  
Julien Louvel ◽  
Ilze Adlere ◽  
Corine van Veen ◽  
Berend J. H. Huisman ◽  
...  
Keyword(s):  
Adenosine A2a Receptor ◽  
Sodium Ion ◽  
Allosteric Modulators ◽  
A2a Receptor ◽  
Amiloride Derivatives ◽  
Adenosine A2a

scholarly journals The caffeine-binding adenosine A2A receptor induces age-like HPA-axis dysfunction by targeting glucocorticoid receptor function

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Vânia L. Batalha ◽  
Diana G. Ferreira ◽  
Joana E. Coelho ◽  
Jorge S. Valadas ◽  
Rui Gomes ◽  
...  
Keyword(s):  
Glucocorticoid Receptor ◽  
Hpa Axis ◽  
Adenosine A2a Receptor ◽  
Receptor Function ◽  
A2a Receptor ◽  
Adenosine A2a

Influence of CGS 21680, a selective adenosine A2A receptor agonist, on NMDA receptor function and expression in the brain of Huntington's disease mice

2010 ◽  
Vol 1323 ◽  
pp. 184-191 ◽  
Author(s):  
Antonella Ferrante ◽  
Alberto Martire ◽  
Monica Armida ◽  
Valentina Chiodi ◽  
Antonella Pézzola ◽  
...  
Keyword(s):  
Nmda Receptor ◽  
Huntington's Disease ◽  
Receptor Agonist ◽  
Adenosine A2a Receptor ◽  
Receptor Function ◽  
Cgs 21680 ◽  
A2a Receptor ◽  
Nmda Receptor Function ◽  
Adenosine A2a ◽  
The Brain

Blunted adenosine A2a receptor function in platelets in patients with major depression

2001 ◽  
Vol 11 (2) ◽  
pp. 183-186 ◽  
Author(s):  
Michael Berk ◽  
Helene Plein ◽  
Dulcie Ferreira ◽  
Brian Jersky
Keyword(s):  
Major Depression ◽  
Adenosine A2a Receptor ◽  
Receptor Function ◽  
A2a Receptor ◽  
Adenosine A2a

scholarly journals Cryo-EM structure of the adenosine A2A receptor coupled to an engineered heterotrimeric G protein

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Javier García-Nafría ◽  
Yang Lee ◽  
Xiaochen Bai ◽  
Byron Carpenter ◽  
Christopher G Tate
Keyword(s):  
G Protein ◽  
Binding Pocket ◽  
Adenosine A2a Receptor ◽  
Intracellular Loop ◽  
Heterotrimeric G Protein ◽  
A2a Receptor ◽  
Density Map ◽  
Adenosine A2a ◽  
G Protein Coupled ◽  
Comparable Quality

The adenosine A2A receptor (A2AR) is a prototypical G protein-coupled receptor (GPCR) that couples to the heterotrimeric G protein GS. Here, we determine the structure by electron cryo-microscopy (cryo-EM) of A2AR at pH 7.5 bound to the small molecule agonist NECA and coupled to an engineered heterotrimeric G protein, which contains mini-GS, the βγ subunits and nanobody Nb35. Most regions of the complex have a resolution of ~3.8 Å or better. Comparison with the 3.4 Å resolution crystal structure shows that the receptor and mini-GS are virtually identical and that the density of the side chains and ligand are of comparable quality. However, the cryo-EM density map also indicates regions that are flexible in comparison to the crystal structures, which unexpectedly includes regions in the ligand binding pocket. In addition, an interaction between intracellular loop 1 of the receptor and the β subunit of the G protein was observed.

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