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Receptor Mechanisms and Signaling
Research Guide

What is Receptor Mechanisms and Signaling?

Receptor mechanisms and signaling refer to the molecular processes by which cell surface or intracellular receptors detect extracellular ligands, undergo conformational changes, and transduce signals into cellular responses through associated proteins such as G proteins or nuclear receptors.

The field encompasses over 106,510 works analyzing ligand binding, receptor activation, and downstream signaling pathways. Key studies include structural determination of G protein-coupled receptors like rhodopsin and computational tools for ligand-receptor characterization. Research spans enzymatic assays, vasoconstrictor discovery, and nuclear receptor superfamilies, with applications in pharmacology and disease.

106.5K
Papers
N/A
5yr Growth
2.9M
Total Citations

Research Sub-Topics

Why It Matters

Receptor mechanisms and signaling underpin drug development targeting GPCRs, which mediate responses to ligands like endothelin discovered by Yanagisawa et al. (1988) in "A novel potent vasoconstrictor peptide produced by vascular endothelial cells," influencing vascular tone and hypertension therapies. Palczewski et al. (2000) in "Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor" provided the first GPCR structure, enabling docking methods refined by Friesner et al. (2006) in "Extra Precision Glide:  Docking and Scoring Incorporating a Model of Hydrophobic Enclosure for Protein−Ligand Complexes," which improved binding affinity predictions for over 6,630 citations' worth of protein-ligand complexes. Recent structural insights into SARS-CoV-2 binding to ACE2 by Yan et al. (2020) in "Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2" directly informed COVID-19 interventions, while nuclear receptor work by Mangelsdorf et al. (1995) in "The nuclear receptor superfamily: The second decade" supports endocrine therapies.

Reading Guide

Where to Start

"Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor" by Palczewski et al. (2000), as it provides the foundational atomic structure of a GPCR, essential for understanding receptor mechanisms before advancing to signaling complexity.

Key Papers Explained

Palczewski et al. (2000) in "Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor" established GPCR architecture, enabling Friesner et al. (2006) in "Extra Precision Glide:  Docking and Scoring Incorporating a Model of Hydrophobic Enclosure for Protein−Ligand Complexes" to develop docking tools incorporating hydrophobic enclosure for binding predictions. Munson and Rodbard (1980) in "LIGAND: A versatile computerized approach for characterization of ligand-binding systems" provided quantitative analysis methods that complement these structures. Yanagisawa et al. (1988) in "A novel potent vasoconstrictor peptide produced by vascular endothelial cells" exemplified functional signaling via GPCR-like endothelin receptors, while Mangelsdorf et al. (1995) in "The nuclear receptor superfamily: The second decade" extended mechanisms to intracellular receptors.

Paper Timeline

100%
graph LR P0["Relationship between the inhibit...
1973 · 12.8K cites"] P1["Enzymatic Determination of Total...
1974 · 9.1K cites"] P2["LIGAND: A versatile computerized...
1980 · 8.5K cites"] P3["Validation of open : closed arm ...
1985 · 5.7K cites"] P4["A novel potent vasoconstrictor p...
1988 · 10.7K cites"] P5["The nuclear receptor superfamily...
1995 · 6.9K cites"] P6["Extra Precision Glide: Docking ...
2006 · 6.6K cites"] P0 --> P1 P1 --> P2 P2 --> P3 P3 --> P4 P4 --> P5 P5 --> P6 style P0 fill:#DC5238,stroke:#c4452e,stroke-width:2px
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Most-cited paper highlighted in red. Papers ordered chronologically.

Advanced Directions

Recent preprints focus on GPCR biased signaling, such as "Ligand-specific activation trajectories dictate GPCR signalling in cells" and "The molecular basis of μ-opioid receptor signaling plasticity," using cryo-EM to map intermediate states and plasticity. News highlights allosteric modulators in "Designing allosteric modulators to change GPCR G protein subtype selectivity" and peptide ligand mechanisms in "Structural insights into GPCR signaling activated by peptide ligands: from molecular mechanism to therapeutic application."

Papers at a Glance

In the News

Code & Tools

Recent Preprints

Ligand-specific activation trajectories dictate GPCR signalling in cells

Jan 2026 nature.com Preprint

Activation of cell surface receptors by extracellular ligands is the hallmark of cell–cell communication and controls most physiological functions in humans. GPCRs are the largest class of such rec...

The molecular basis of μ-opioid receptor signaling plasticity

Nov 2025 nature.com Preprint

Activation of the μ-opioid receptor (μOR) alleviates pain but also elicits adverse effects through diverse G proteins and β-arrestins. The structural details of μOR complexes with Gzand β-arrestins...

Designing allosteric modulators to change GPCR G protein subtype selectivity

Oct 2025 nature.com Preprint

G-protein-coupled receptors (GPCRs) convert extracellular signals into intracellular responses by signalling through 16 subtypes of Gα proteins and two β-arrestin proteins. Biased compounds—molecul...

Non-equilibrium snapshots of ligand efficacy at the μ-opioid receptor

Dec 2025 nature.com Preprint

Distinct ligands for the same G-protein coupled receptor (GPCR) activate intracellular signaling partners to varying extents, but the molecular mechanisms driving these differences remain elusive. ...

Structural and dynamic insights into the biased signaling mechanism of the human kappa opioid receptor

Oct 2025 nature.com Preprint

The κ-opioid receptor (KOR) is a member of the G protein-coupled receptor (GPCR) family, modulating cellular responses through transducers such as G proteins and β-arrestins. G-protein-biased KOR a...

Latest Developments

Recent developments in Receptor Mechanisms and Signaling research include the upcoming Gordon Research Conference in February 2026 focusing on photosensory receptors and signal transduction, highlighting cutting-edge research in photoreceptors and optogenetics (GRC Conference). Additionally, advances in understanding GPCR signaling, including ligand-specific activation trajectories and biased signaling, are being actively studied, with recent publications exploring structural and mechanistic insights into GPCR function and therapeutic targeting (Nature, 2026, Science Direct).

Frequently Asked Questions

What is the relationship between inhibition constant KI and I50 in receptor assays?

Cheng and Prusoff (1973) in "Relationship between the inhibition constant (KI) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction" derived the formula KI = I50 / (1 + [S]/Km), correcting for substrate concentration effects in ligand-binding studies. This equation standardizes inhibitor potency measurements across enzymatic reactions involving receptors. It has been cited 12,805 times for accurate pharmacological analysis.

How do GPCRs transduce signals from ligands?

GPCRs like rhodopsin feature seven transmembrane α-helices that bind ligands and activate G proteins, as shown in the crystal structure by Palczewski et al. (2000) in "Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor." Ligand binding induces conformational changes propagating signals intracellularly. This mechanism applies to diverse stimuli and has 5,575 citations.

What methods characterize ligand-binding systems?

Munson and Rodbard (1980) developed LIGAND, a computerized approach for analyzing ligand-receptor interactions through nonlinear least-squares fitting of binding data, cited 8,490 times. It handles complex models including multiple ligands and sites. The tool remains foundational for quantitative receptor studies.

What defines the nuclear receptor superfamily?

Mangelsdorf et al. (1995) in "The nuclear receptor superfamily: The second decade" cataloged over 50 members regulating gene expression via ligand binding, with 6,937 citations. These receptors control development, metabolism, and reproduction. Advances revealed structural homologies across species.

How was endothelin discovered as a vasoconstrictor?

Yanagisawa et al. (1988) in "A novel potent vasoconstrictor peptide produced by vascular endothelial cells" identified endothelin-1 from porcine aortic endothelium, exhibiting potent vasoconstriction via receptor signaling. The peptide has 21 amino acids and marked potency. It has 10,748 citations and reshaped vascular biology.

What structural insights exist for SARS-CoV-2 receptor binding?

Yan et al. (2020) in "Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2" resolved the spike-ACE2 complex at atomic resolution, revealing key contacts for viral entry. This informed neutralizing antibody design. The work received 5,531 citations amid the pandemic.

Open Research Questions

  • ? How do ligand-specific activation trajectories determine GPCR signaling outcomes in cells?
  • ? What structural features underlie μ-opioid receptor signaling plasticity with Gz and β-arrestins?
  • ? How can allosteric modulators alter GPCR selectivity for specific G protein subtypes?
  • ? What non-equilibrium intermediates capture ligand efficacy differences at the μ-opioid receptor?
  • ? What dynamic mechanisms drive biased signaling in the human kappa opioid receptor?

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