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

Conopeptide ρ-TIA defines a new allosteric site on the extracellular surface of the α1B-adrenoceptor.

The Journal of biological chemistry - 18 Jan 2013

Ragnarsson Lotten, Wang Ching-I Anderson, Andersson Åsa, Fajarningsih Dewi, Monks Thea, Brust Andreas, Rosengren K Johan, Lewis Richard J

Abstract excerpt

The G protein-coupled receptor (GPCR) superfamily is an important drug target that includes over 1000 membrane receptors that functionally couple extracellular stimuli to intracellular effectors. Despite the potential of extracellular surface (ECS) residues in GPCRs to interact with subtype-specific allosteric modulators, few ECS pharmacophores for class A receptors have been identified. Using the turkey...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Site
Share to Amino Acids

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cricetinae

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Structure, Secondary

Share to Receptors, Adrenergic, alpha-1

Share to Static Electricity

Share to Turkeys

Source

Open in PubMed Open full text

Identifiers

PMID: 23184947
DOI: 10.1074/jbc.M112.430785
PMCID: PMC3548491

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Conopeptide ρ-TIA defines a new allosteric site on the extracellular surface of the α1B-adrenoceptor.PMID 23184947Read ↗

Extracellular surface residues of the α1B-adrenoceptor critical for G protein-coupled receptor function.Semantic proximity Read ↗

Allosteric Modulation as a Unifying Mechanism for Receptor Function and Regulation.Semantic proximity Read ↗

A missense mutation in the seven-transmembrane domain of the human Ca2+ receptor converts a negative allosteric modulator into a positive allosteric modulator.Semantic proximity Read ↗

Role of the Second Extracellular Loop of the Adenosine A1 Receptor on Allosteric Modulator Binding, Signaling, and Cooperativity.Semantic proximity Read ↗

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

The G-protein coupled receptor family: actors with many faces.Semantic proximity Read ↗

Structural insight to mutation effects uncover a common allosteric site in class C GPCRs.Semantic proximity Read ↗

Orthosteric binding of ρ-Da1a, a natural peptide of snake venom interacting selectively with the α1A-adrenoceptor.Semantic proximity Read ↗

Pharmacogenomics of adrenoceptors.Semantic proximity Read ↗

GPCR-MAPS: high-resolution functional and allosteric mapping of G protein-coupled receptor activation and biasSemantic proximity Read ↗

Towards a structural understanding of allosteric drugs at the human calcium-sensing receptor.Semantic proximity Read ↗

Structural and functional roles of small group-conserved amino acids present on helix-H7 in the β(2)-adrenergic receptor.Semantic proximity Read ↗

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