ArticleScience (New York, N.Y.)2022
Cryo-EM structure of human GPR158 receptor coupled to the RGS7-Gβ5 signaling complex.
Article in Science (New York, N.Y.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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
31 citing papers in PubMed, 60 citations in OpenAlex.
- Structural basis for modulation of group III mGlu receptors by transsynaptic interactions.Science advances · 2026Article
- Non-canonical pore architecture underlies constitutive gating of human retinal TRPM1.Nature communications · 2026Article
- Olfactory-gustatory cross-modal integration: mechanisms of aroma-induced sweetness enhancement, sensory evaluation methodologies, neuroimaging evidence and advances in influencing factors.Journal of advanced research · 2026Review
- CryoEM structure of mGlu6 captures receptor activation prior to G protein coupling.Nature communications · 2026Article
- Targeting mGlyR with nanobodies for depression.Nature communications · 2026Article
- Constitutively active orphan G protein-coupled receptors through the lenses of cryo-electron microscopy.The Journal of biological chemistry · 2025Review
- Cerebrospinal fluid quantitative proteomic reveals potential mechanisms and biomarker candidates of children with bacterial meningitis complicated by neurological complications.Clinical proteomics · 2025Article
- Gnb5 is a negative regulator of the BACE1-mediated Aβ generation and ameliorates cognitive deficits in a mouse model of Alzheimer's disease.PLoS biology · 2025Article
- The Conformational Equilibria of a Human GPCR Compared between Lipid Vesicles and Aqueous Solutions by IntegrativeJournal of the American Chemical Society · 2025Article
- Molecular architecture of human LYCHOS involved in lysosomal cholesterol signaling.Nature structural & molecular biology · 2025Article
- Trilobatin, a Naturally Occurring GPR158 Ligand, Alleviates Depressive-like Behavior by Promoting Mitophagy.Journal of agricultural and food chemistry · 2025Article
- Osteocalcin and GPR158: linking bone and brain function.Frontiers in cell and developmental biology · 2025Review
- Native MS-guided lipidomics to define endogenous lipid microenvironments of eukaryotic receptors and transporters.Nature protocols · 2025Article
- Molecular insights into the activation mechanism of GPR156 in maintaining auditory function.Nature communications · 2024Article
- Cryo-EM structure of human class C orphan GPCR GPR179 involved in visual processing.Nature communications · 2024Article
- Article
- Emerging modes of regulation of neuromodulatory G protein-coupled receptors.Trends in neurosciences · 2024Review
- GRK2 kinases in the primary cilium initiate SMOOTHENED-PKA signaling in the Hedgehog cascade.PLoS biology · 2024Article
- The binding mechanism of an anti-multiple myeloma antibody to the human GPRC5D homodimer.Nature communications · 2024Article
- Constitutive activation mechanism of a class C GPCR.Nature structural & molecular biology · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 4 institutions in 3 countries.
Funding
Abstract
GPR158 is an orphan G protein–coupled receptor (GPCR) highly expressed in the brain, where it controls synapse formation and function. GPR158 has also been implicated in depression, carcinogenesis, and cognition. However, the structural organization and signaling mechanisms of GPR158 are largely unknown. We used single-particle cryo–electron microscopy (cryo-EM) to determine the structures of human GPR158 alone and bound to an RGS signaling complex. The structures reveal a homodimeric organization stabilized by a pair of phospholipids and the presence of an extracellular Cache domain, an unusual ligand-binding domain in GPCRs. We further demonstrate the structural basis of GPR158 coupling to RGS7-Gβ5. Together, these results provide insights into the unusual biology of orphan receptors and the formation of GPCR-RGS complexes.
Indexed as
Identifiers
What OpenQuestion 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 OpenQuestion graph.