Evidence map›Paper›PMID 26167642›Full record

ArticleNature methods2015

Imaging G protein-coupled receptors while quantifying their ligand-binding free-energy landscape.

David Alsteens, Moritz Pfreundschuh, Cheng Zhang, Patrizia M Spoerri, Shaun R Coughlin, Brian K Kobilka, Daniel J Müller

Open access · greenAbstract read
In one paragraph

Article in Nature methods, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
10.1field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

31 citing papers in PubMed, 120 citations in OpenAlex.

  1. Single-Molecule Force Spectroscopy: Experiments, Analysis, and Simulations.Methods in molecular biology (Clifton, N.J.) · 2027
    Article
  2. Article
  3. Factors modulating the assembly of human βNature structural & molecular biology · 2026
    Article
  4. Review
  5. Membrane mimetic-dependence of GPCR energy landscapes.Structure (London, England : 1993) · 2024
    Article
  6. Article
  7. Membrane Mimetic-Dependence of GPCR Energy Landscapes.bioRxiv : the preprint server for biology · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Array atomic force microscopy for real-time multiparametric analysis.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  20. Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 2 countries.

David Alsteens *Department of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zurich, Basel, Switzerland.
Moritz Pfreundschuh *Department of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zurich, Basel, Switzerland.
Cheng ZhangDepartment of Cellular Physiology and Medicine, Stanford University School of Medicine, Stanford, California, USA.
Patrizia M SpoerriDepartment of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zurich, Basel, Switzerland.
Shaun R CoughlinCardiovascular Research Institute, University of California, San Francisco, San Francisco, California, USA.
Brian K KobilkaDepartment of Cellular Physiology and Medicine, Stanford University School of Medicine, Stanford, California, USA.
Daniel J MüllerDepartment of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zurich, Basel, Switzerland.
Board of the Swiss Federal Institutes of Technology · CHStanford University · USUniversity of California, San Francisco · USUniversity of Pittsburgh · US

Funding

Structural Basis of Protease-Activated Receptor FunctionR01HL121387 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI COUGHLIN, SHAUN R., KOBILKA, BRIAN K · 2014 to 2017
$2.9M
NHLBI NIH HHS R01 HL121387
6 · The paper itself

Abstract

Imaging native membrane receptors and testing how they interact with ligands is of fundamental interest in the life sciences but has proven remarkably difficult to accomplish. Here, we introduce an approach that uses force-distance curve-based atomic force microscopy to simultaneously image single native G protein-coupled receptors in membranes and quantify their dynamic binding strength to native and synthetic ligands. We measured kinetic and thermodynamic parameters for individual protease-activated receptor-1 (PAR1) molecules in the absence and presence of antagonists, and these measurements enabled us to describe PAR1's ligand-binding free-energy landscape with high accuracy. Our nanoscopic method opens an avenue to directly image and characterize ligand binding of native membrane receptors.

Indexed as

Models, ChemicalBinding SitesComputer SimulationEnergy TransferHumansKineticsLigandsLipid BilayersMicroscopy, Atomic ForceMolecular ImagingProtein BindingReceptor, PAR-1Stress, MechanicalLigandsLipid BilayersReceptor, PAR-1

Identifiers

PMID26167642
PMCPMC5087271
OpenAlexW1827896143

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.