ArticleNature communications2019
Rearrangement of the transmembrane domain interfaces associated with the activation of a GPCR hetero-oligomer.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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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
38 citing papers in PubMed.
- Normalization of network activity in an epilepsy model with a constitutively active GABBR2 variant.Brain : a journal of neurology · 2026Article
- Functional and structural basis of a negative allostery within GABANature communications · 2026Article
- Allosteric activation of the glutamate receptor mGlu2 by the serotonin receptor 5-HTNature communications · 2026Article
- GABA-independent activation of GABANature communications · 2025Article
- Structural Basis of GABAAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Identification of Orthosteric GABAACS omega · 2025Article
- Single-molecule localization microscopy as a tool to quantify di/oligomerization of receptor tyrosine kinases and G protein-coupled receptors.Molecular pharmacology · 2025Review
- Presynaptic hyperexcitability reversed by positive allosteric modulation of a GABABR epilepsy variant.Brain : a journal of neurology · 2025Article
- Structural basis of orientated asymmetry in a mGlu heterodimer.Nature communications · 2024Article
- Impact of aging on the GABAbioRxiv : the preprint server for biology · 2024Article
- Absence of calcium-sensing receptor basal activity due to inter-subunit disulfide bridges.Communications biology · 2024Article
- G protein-coupled receptors (GPCRs): advances in structures, mechanisms, and drug discovery.Signal transduction and targeted therapy · 2024Review
- Extracellular calcium functions as a molecular glue for transmembrane helices to activate the scramblase Xkr4.Nature communications · 2023Article
- Protein overexpression can induce the elongation of cell membrane nanodomains.Biophysical journal · 2023Article
- Filamin A organizes γ‑aminobutyric acid type B receptors at the plasma membrane.Nature communications · 2023Article
- Characterization of aFrontiers in molecular neuroscience · 2023Article
- Oligomerization of the heteromeric γ-aminobutyric acid receptor GABAScientific reports · 2022Article
- Biased signaling due to oligomerization of the G protein-coupled platelet-activating factor receptor.Nature communications · 2022Article
- Myocardial TRPC6-mediated ZnNature communications · 2022Article
- Functional Assessment of Calcium-Sensing Receptor Variants Confirms Familial Hypocalciuric Hypercalcemia.Journal of the Endocrine Society · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
Abstract
G protein-coupled receptors (GPCRs) can integrate extracellular signals via allosteric interactions within dimers and higher-order oligomers. However, the structural bases of these interactions remain unclear. Here, we use the GABA
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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.