Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structure-Based Design of Potent and Selective Ligands at the Four Adenosine Receptors.

Molecules (Basel, Switzerland) - 10 Nov 2017

Jespers Willem, Oliveira Ana, Prieto-Díaz Rubén, Majellaro María, Åqvist Johan, Sotelo Eddy, Gutiérrez-de-Terán Hugo

Abstract excerpt

The four receptors that signal for adenosine, A₁, A2A, A2B and A₃ ARs, belong to the superfamily of G protein-coupled receptors (GPCRs). They mediate a number of (patho)physiological functions and have attracted the interest of the biopharmaceutical sector for decades as potential drug targets. The many crystal structures of the A2A, and lately the A₁ ARs, allow for the use of advanced computational,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Thermodynamics
Share to Ligands
Share to Molecular Dynamics Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Stereoisomerism

Share to Xanthines

Source

Open in PubMed Open full text

Identifiers

PMID: 29125553
DOI: 10.3390/molecules22111945
PMCID: PMC6150288

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure-Based Design of Potent and Selective Ligands at the Four Adenosine Receptors.PMID 29125553Read ↗

Deciphering conformational selectivity in the A <sub>2A</sub> adenosine G protein-coupled receptor by Free Energy simulationsSemantic proximity Read ↗

Structural Mapping of Adenosine Receptor Mutations: Ligand Binding and Signaling Mechanisms.Semantic proximity Read ↗

Structural and energetic effects of A2A adenosine receptor mutations on agonist and antagonist binding.Semantic proximity Read ↗

Crystal structure of adenosine A2A receptor in complex with clinical candidate Etrumadenant reveals novel antagonist interactionSemantic proximity Read ↗

A pan-positive allosteric modulator that mediates sustainable GPCR activationSemantic proximity Read ↗

Thermostabilisation of an agonist-bound conformation of the human adenosine A(2A) receptor.Semantic proximity Read ↗

Scanning mutagenesis in a yeast system delineates the role of the NPxxY(x)(5,6)F motif and helix 8 of the adenosine A(2B) receptor in G protein coupling.Semantic proximity Read ↗

Structure-Guided Design of Partial Agonists at an Opioid ReceptorSemantic proximity Read ↗

Mechanistic insights from resolving ligand-dependent kinetics of conformational changes at ATP-gated P2X1R ion channels.Semantic proximity Read ↗

Dynamic behavior of the active and inactive states of the adenosine A(2A) receptor.Semantic proximity Read ↗

Structural insights into the allosteric inhibition of P2X4 receptorsSemantic proximity Read ↗

The second extracellular loop of GPCRs determines subtype-selectivity and controls efficacy as evidenced by loop exchange study at A2 adenosine receptors.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.