ReviewEndocrine-related cancer2026
RET receptor tyrosine kinase architecture, assemblies, and activation.
Review in Endocrine-related cancer, 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.
- RETurn of the Gene. Post scriptum.Endocrine-related cancer · 2026Article
- A long-chain heparan sulfate capture mechanism directs paracrine GDNF-GFRα1 signalling through RET.bioRxiv : the preprint server for biology · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Among the 58 human receptor tyrosine kinases that are known, only the RET (REarrangement during Transfection) receptor contains cadherin-like domains in its extracellular portion. This multidomain extracellular module contains a binding site for a family of five related heterodimeric ligands. Each heterodimer comprises a secreted glial cell line-derived neurotrophic factor (GDNF) family ligand (GFL) and a membrane-anchored co-receptor GFR⍺ (GDNF family receptor alpha). Once a GFL-GFR⍺ ligand is bound to RET, this stimulates the activation of the receptor through tyrosine-based autophosphorylation. This mini review explores how the shape and architecture of RET encode a flexible GFL-GFR⍺-binding site, summarising recent progress in understanding RET structure. It then discusses current views on how distinct assemblies of GFL-GFR⍺-RET receptor complexes are able to activate the intrinsic RET tyrosine kinase function to relay intracellular signals.
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.