Evidence map›Paper›PMID 39943784›Full record

ReviewBiochemistry2025

How Ligands Achieve Biased Signaling toward Arrestins.

Qianru Jiang, Tao Che

Abstract readReview
In one paragraph

Review in Biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Review
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

2 authors.

Qianru JiangCenter for Clinical Pharmacology, Department of Anesthesiology, Washington University Medical School, Saint Louis, Missouri 63110, United States.
Tao CheCenter for Clinical Pharmacology, Department of Anesthesiology, Washington University Medical School, Saint Louis, Missouri 63110, United States.ORCID 0000-0002-1620-3027

Funding

Mechanisms and Regulations of kappa Opioid Receptor SignalingR01DA058020 · NIDA · WASHINGTON UNIVERSITY · PI Tao Che · 2024 to 2026
$1.4M
NIDA NIH HHS R01 DA058020
6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) mediate the effects of various endogenous and extracellular stimuli through multiple transducers, including heterotrimeric G proteins, GPCR kinases (GRKs), and arrestins. Biased signaling, which preferentially activates certain G protein or GRK/arrestin signaling pathways, provides great opportunities for developing drugs with enhanced therapeutic efficacy and minimized side effects. In this Review, we review studies addressing the structural dynamics of GPCRs bound to balanced and biased ligands and current consensus on how ligand-receptor interactions determine signaling outcomes. We also examine the conformational changes in GPCRs when in complex with G proteins, arrestins, and GRKs, highlighting a more profound impact of signal transducers on receptor rearrangements compared with biased ligands. This evidence supports the idea that biased signaling can be achieved through the promotion of multiple conformational states by biased agonists and the stabilization of specific active conformations by individual signal transducers.

Indexed as

ArrestinsReceptors, G-Protein-CoupledSignal TransductionAnimalsG-Protein-Coupled Receptor KinasesHumansLigandsProtein ConformationArrestinsG-Protein-Coupled Receptor KinasesLigandsReceptors, G-Protein-Coupledarrestinbiased ligandbiased signalingGPCRGPCR kinase

Identifiers

PMID39943784
PMCPMC11936672

What OpenQuestion holds

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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.