Evidence map›Paper›PMID 35385593›Full record

ArticleAngewandte Chemie (International ed. in English)2022

Structure-Based Evolution of G Protein-Biased μ-Opioid Receptor Agonists.

Haoqing Wang, Florian Hetzer, Weijiao Huang, Qianhui Qu, Justin Meyerowitz, Jonas Kaindl, Harald Hübner, Georgios Skiniotis, Brian K Kobilka, Peter Gmeiner

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed, 2 pooled it
6.4field-weighted citation impact, top 2% 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

50 citing papers in PubMed, 2 syntheses or guidelines pooled it, 61 citations in OpenAlex.

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  18. Rational Design Biased Compounds against μ‑Opioid Receptor.ACS pharmacology & translational science · 2025
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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

10 authors at 3 institutions in 3 countries.

Haoqing WangDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA, USA.
Florian HetzerDepartment of Chemistry and Pharmacy, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nikolaus-Fiebiger-Strasse 10, 91058, Erlangen, Germany.
Weijiao HuangDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA, USA.
Qianhui QuDepartment of Molecular and Cellular Physiology, Department of Structural Biology, Stanford University School of Medicine, Stanford, CA, USA.
Justin MeyerowitzDepartment of Molecular and Cellular Physiology, Department of Structural Biology, Stanford University School of Medicine, Stanford, CA, USA.
Jonas KaindlDepartment of Chemistry and Pharmacy, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nikolaus-Fiebiger-Strasse 10, 91058, Erlangen, Germany.
Harald HübnerDepartment of Chemistry and Pharmacy, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nikolaus-Fiebiger-Strasse 10, 91058, Erlangen, Germany.
Georgios SkiniotisDepartment of Molecular and Cellular Physiology, Department of Structural Biology, Stanford University School of Medicine, Stanford, CA, USA.
Brian K KobilkaDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA, USA.
Peter GmeinerDepartment of Chemistry and Pharmacy, Friedrich-Alexander-Universität Erlangen-Nürnberg, Nikolaus-Fiebiger-Strasse 10, 91058, Erlangen, Germany.ORCID 0000-0002-4127-197X
Stanford University · USFriedrich-Alexander-Universität Erlangen-Nürnberg · DEFudan University · CN

Funding

Research in Anesthesia Training Program (ReAP)T32GM089626 · NIGMS · STANFORD UNIVERSITY · PI Vivianne L Tawfik · 2010 to 2026
$5.2M
Structural Basis of Opioid Receptor FunctionR37DA036246 · NIDA · STANFORD UNIVERSITY · PI KOBILKA, BRIAN K · 2013 to 2020
$4.2M
NIDA NIH HHS R37 DA036246NIGMS NIH HHS T32 GM089626
6 · The paper itself

Abstract

The μ-opioid receptor (μOR) is the major target for opioid analgesics. Activation of μOR initiates signaling through G protein pathways as well as through β-arrestin recruitment. μOR agonists that are biased towards G protein signaling pathways demonstrate diminished side effects. PZM21, discovered by computational docking, is a G protein biased μOR agonist. Here we report the cryoEM structure of PZM21 bound μOR in complex with G

Indexed as

GTP-Binding ProteinsReceptors, Opioid, muAnalgesics, Opioidbeta-ArrestinsSignal TransductionAnalgesics, Opioidbeta-ArrestinsGTP-Binding ProteinsReceptors, Opioid, mucryoEM StructureDrug DiscoveryGPCRsMedicinal ChemistryOpioids

Identifiers

PMID35385593
PMCPMC9322534
OpenAlexW4224274219

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.