Evidence map›Paper›PMID 32483378›Full record

ArticleNature chemical biology2020

An allosteric modulator binds to a conformational hub in the β

Xiangyu Liu, Jonas Kaindl, Magdalena Korczynska, Anne Stößel, Daniela Dengler, Markus Stanek, Harald Hübner, Mary J Clark, Jake Mahoney, Rachel Ann Matt and 6 more

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

62 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Biased Allosteric Modulation in GPCR Drug Discovery.Handbook of experimental pharmacology · 2026
    Review
  11. Structural Perspectives on Biased Allostery of GPCR Signaling.Handbook of experimental pharmacology · 2026
    Review
  12. Article
  13. A biased allosteric modulator functions as a molecular glue to induce βbioRxiv : the preprint server for biology · 2025
    Article
  14. Review
  15. Article
  16. Article
  17. Gut-heart axis: cardiac remodeling and heart failure in the context of inflammatory bowel disease and dysbiosis.American journal of physiology. Gastrointestinal and liver physiology · 2025
    Review
  18. Implication of Central βArchiv der Pharmazie · 2025
    Review
  19. Review
  20. Article

2 more citing papers are in PubMed but not listed here.

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

16 authors at 6 institutions in 4 countries.

Xiangyu Liu *School of Pharmaceutical Sciences, Tsinghua University, Beijing, China.ORCID http://orcid.org/0000-0003-3178-9238
Jonas Kaindl *Department of Chemistry and Pharmacy, Medicinal Chemistry, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.ORCID http://orcid.org/0000-0002-8310-5398
Magdalena KorczynskaDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA, USA.
Anne StößelDepartment of Chemistry and Pharmacy, Medicinal Chemistry, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.
Daniela DenglerDepartment of Chemistry and Pharmacy, Medicinal Chemistry, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.
Markus StanekDepartment of Chemistry and Pharmacy, Medicinal Chemistry, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.
Harald HübnerDepartment of Chemistry and Pharmacy, Medicinal Chemistry, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.
Mary J ClarkDepartment of Pharmacology, University of California San Diego School of Medicine, La Jolla, CA, USA.ORCID http://orcid.org/0000-0003-1176-5626
Jake MahoneyDepartment of Pharmacology, University of California San Diego School of Medicine, La Jolla, CA, USA.
Rachel Ann MattDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA, USA.ORCID http://orcid.org/0000-0002-9944-8897
Xinyu XuBeijing Advanced Innovation Center for Structural Biology, Tsinghua University, Beijing, China.
Kunio HirataAdvanced Photon Technology Division, Research Infrastructure Group, SR Life Science Instrumentation Unit, RIKEN/SPring-8 Center Sayo-gun, Hyogo, Japan.ORCID http://orcid.org/0000-0002-1491-6509
Brian K ShoichetDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA, USA.ORCID http://orcid.org/0000-0002-6098-7367
Roger K SunaharaDepartment of Pharmacology, University of California San Diego School of Medicine, La Jolla, CA, USA. rsunahara@ucsd.edu.ORCID http://orcid.org/0000-0003-1702-8619
Brian K KobilkaBeijing Advanced Innovation Center for Structural Biology, Tsinghua University, Beijing, China. kobilka@stanford.edu.ORCID http://orcid.org/0000-0001-5958-3990
Peter GmeinerDepartment of Chemistry and Pharmacy, Medicinal Chemistry, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany. peter.gmeiner@fau.de.ORCID http://orcid.org/0000-0002-4127-197X
Friedrich-Alexander-Universität Erlangen-Nürnberg · DEBeijing Advanced Sciences and Innovation Center · CNUniversity of California San Diego · USUniversity of California, San Francisco · USJapan Science and Technology Agency · JPStanford University · US

Funding

Development and Testing of New Computational Methods for Ligand Discovery and MechanismR35GM122481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Brian K Shoichet · 2017 to 2026
$8.5M
Structure-based discovery of allosteric ligands for G Protein Coupled ReceptorsU19GM106990 · NIGMS · STANFORD UNIVERSITY · PI KOBILKA, BRIAN K · 2013 to 2017
$6.3M
NIGMS NIH HHS R35 GM122481NIGMS NIH HHS U19 GM106990
6 · The paper itself

Abstract

Most drugs acting on G-protein-coupled receptors target the orthosteric binding pocket where the native hormone or neurotransmitter binds. There is much interest in finding allosteric ligands for these targets because they modulate physiologic signaling and promise to be more selective than orthosteric ligands. Here we describe a newly developed allosteric modulator of the β

Indexed as

Adrenergic beta-2 Receptor AgonistsAdrenergic beta-AntagonistsAllosteric RegulationAllosteric SiteAlprenololHEK293 CellsHumansKineticsLigandsMolecular Docking SimulationMolecular Dynamics SimulationNorepinephrineProtein BindingProtein Interaction Domains and MotifsProtein Structure, SecondaryReceptors, Adrenergic, beta-2Adrenergic beta-2 Receptor AgonistsAdrenergic beta-AntagonistsAlprenololLigandsNorepinephrineReceptors, Adrenergic, beta-2Salmeterol XinafoateWater

Identifiers

PMID32483378
PMCPMC7816728
OpenAlexW3032032492

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.