ArticleAnnals of the New York Academy of Sciences2014
New functions and signaling mechanisms for the class of adhesion G protein-coupled receptors.
Article in Annals of the New York Academy of Sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 32 citations in OpenAlex.
- The atypical adhesion GPCR ADGRA1 controls hippocampal inhibitory circuit function.Cell reports · 2026Article
- GPR126 is a specifier of blood-brain barrier formation in the mouse central nervous system.The Journal of clinical investigation · 2024Article
- The adhesion GPCR GPR116/ADGRF5 has a dual function in pancreatic islets regulating somatostatin release and islet development.Communications biology · 2024Article
- A screen of pharmacologically active compounds to identify modulators of the Adgrg6/Gpr126 signalling pathway in zebrafish embryos.Basic & clinical pharmacology & toxicology · 2023Article
- Transcriptomic Response of Differentiating Porcine Myotubes to Thermal Stress and Donor Piglet Age.International journal of molecular sciences · 2023Article
- The adhesion GPCRs CELSR1-3 and LPHN3 engage G proteins via distinct activation mechanisms.Cell reports · 2023Article
- The adhesion GPCR Adgrg6 (Gpr126): Insights from the zebrafish model.Genesis (New York, N.Y. : 2000) · 2021Review
- Article
- The polymicrogyria-associated GPR56 promoter preferentially drives gene expression in developing GABAergic neurons in common marmosets.Scientific reports · 2020Article
- In vivo identification of small molecules mediating Gpr126/Adgrg6 signaling during Schwann cell development.Annals of the New York Academy of Sciences · 2019Article
- The Adhesion G-Protein-Coupled Receptor, GPR56/ADGRG1, Inhibits Cell-Extracellular Matrix Signaling to Prevent Metastatic Melanoma Growth.Frontiers in oncology · 2018Article
- High expression of GPR116 indicates poor survival outcome and promotes tumor progression in colorectal carcinoma.Oncotarget · 2017Article
- Disease-associated extracellular loop mutations in the adhesion G protein-coupled receptor G1 (ADGRG1; GPR56) differentially regulate downstream signaling.The Journal of biological chemistry · 2017Article
- Extracellular cues influencing oligodendrocyte differentiation and (re)myelination.Experimental neurology · 2016Review
- Truncating Mutations in the Adhesion G Protein-Coupled Receptor G2 Gene ADGRG2 Cause an X-Linked Congenital Bilateral Absence of Vas Deferens.American journal of human genetics · 2016Article
- Adhesion G Protein-Coupled Receptors: From In Vitro Pharmacology to In Vivo Mechanisms.Molecular pharmacology · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
32 authors at 20 institutions in 11 countries.
Funding
Abstract
The class of adhesion G protein-coupled receptors (aGPCRs), with 33 human homologs, is the second largest family of GPCRs. In addition to a seven-transmembrane α-helix-a structural feature of all GPCRs-the class of aGPCRs is characterized by the presence of a large N-terminal extracellular region. In addition, all aGPCRs but one (GPR123) contain a GPCR autoproteolysis-inducing (GAIN) domain that mediates autoproteolytic cleavage at the GPCR autoproteolysis site motif to generate N- and a C-terminal fragments (NTF and CTF, respectively) during protein maturation. Subsequently, the NTF and CTF are associated noncovalently as a heterodimer at the plasma membrane. While the biological function of the GAIN domain-mediated autocleavage is not fully understood, mounting evidence suggests that the NTF and CTF possess distinct biological activities in addition to their function as a receptor unit. We discuss recent advances in understanding the biological functions, signaling mechanisms, and disease associations of the aGPCRs.
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.