ReviewCommunications biology2026
Strategic advances for cryo-EM structural studies of small (<100 kDa) GPCRs.
Review in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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.
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.
Who cites it
2 citing papers in PubMed.
- A novel fusion tool to enable G protein-coupled receptor structure determination.Acta crystallographica. Section D, Structural biology · 2026Article
- GPCR signaling systems facilitate precision interventions for multi-oncology therapy.Frontiers in systems biology · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Membrane proteins constitute ~25-30% of the human proteome, with G protein-coupled receptors (GPCRs) representing the largest family and targets of ~35% of FDA-approved drugs. While cryo-electron microscopy (cryo-EM) has transformed GPCR structural biology, resolving small GPCR complexes, particularly those in the apo and inactive states, remains challenging due to their limited size and conformational flexibility. This limitation is significant, as many therapeutics act by stabilizing inactive GPCR conformations. In this review, we discuss the key obstacles to visualizing apo/inactive GPCRs by cryo-EM, summarize fusion and target-binding strategies that have enabled their structural determination, outline practical considerations for fiducial design, and highlight emerging AI-driven approaches likely to further expand the scope of GPCR structural studies.
Indexed as
Identifiers
What Socratic holds
Registered trials
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 Socratic graph.