Evidence map›Paper›PMID 33484636›Full record

ArticleStructure (London, England : 1993)2021

A two-site flexible clamp mechanism for RET-GDNF-GFRα1 assembly reveals both conformational adaptation and strict geometric spacing.

Sarah E Adams, Andrew G Purkiss, Phillip P Knowles, Andrea Nans, David C Briggs, Annabel Borg, Christopher P Earl, Kerry M Goodman, Agata Nawrotek, Aaron J Borg and 4 more

Open access · hybridAbstract readComparative Study
PubMed Full text at PMC Publisher
In one paragraph

Article in Structure (London, England : 1993), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.5field-weighted citation impact, top 39% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. RET receptor signaling: Function in development, metabolic disease, and cancer.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2022
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

14 authors at 1 institution in 1 country.

Sarah E AdamsSignalling and Structural Biology Laboratory, Francis Crick Institute, NW1 1AT London, UK.
Andrew G PurkissStructural Biology Science Technology Platform, Francis Crick Institute, NW1 1AT London, UK.
Phillip P KnowlesSignalling and Structural Biology Laboratory, Francis Crick Institute, NW1 1AT London, UK.
Andrea NansStructural Biology Science Technology Platform, Francis Crick Institute, NW1 1AT London, UK.
David C BriggsSignalling and Structural Biology Laboratory, Francis Crick Institute, NW1 1AT London, UK.
Annabel BorgStructural Biology Science Technology Platform, Francis Crick Institute, NW1 1AT London, UK.
Christopher P EarlSignalling and Structural Biology Laboratory, Francis Crick Institute, NW1 1AT London, UK.
Kerry M GoodmanSignalling and Structural Biology Laboratory, Francis Crick Institute, NW1 1AT London, UK.
Agata NawrotekSignalling and Structural Biology Laboratory, Francis Crick Institute, NW1 1AT London, UK.
Aaron J BorgMass Spectrometry Science Technology Platform, Francis Crick Institute, NW1 1AT London, UK.
Pauline B McIntoshStructural Biology of Cells and Viruses Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Francesca M HoughtonSignalling and Structural Biology Laboratory, Francis Crick Institute, NW1 1AT London, UK.
Svend KjærStructural Biology Science Technology Platform, Francis Crick Institute, NW1 1AT London, UK.
Neil Q McDonaldSignalling and Structural Biology Laboratory, Francis Crick Institute, NW1 1AT London, UK; Institute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck College, Malet Street, London WC1E 7HX, UK. Electronic address: neil.mcdonald@crick.ac.uk.
The Francis Crick Institute · GB

Funding

Wellcome Trust FC001115
6 · The paper itself

Abstract

RET receptor tyrosine kinase plays vital developmental and neuroprotective roles in metazoans. GDNF family ligands (GFLs) when bound to cognate GFRα co-receptors recognize and activate RET stimulating its cytoplasmic kinase function. The principles for RET ligand-co-receptor recognition are incompletely understood. Here, we report a crystal structure of the cadherin-like module (CLD1-4) from zebrafish RET revealing interdomain flexibility between CLD2 and CLD3. Comparison with a cryo-electron microscopy structure of a ligand-engaged zebrafish RET

Indexed as

AnimalsCadherinsCryoelectron MicroscopyCrystallography, X-RayGlial Cell Line-Derived Neurotrophic FactorGlial Cell Line-Derived Neurotrophic Factor ReceptorsModels, MolecularMultiprotein ComplexesProtein BindingProtein ConformationProtein DomainsProto-Oncogene Proteins c-retZebrafishZebrafish ProteinsCadherinsgdnfa protein, zebrafishgfra1a protein, zebrafishGlial Cell Line-Derived Neurotrophic FactorGlial Cell Line-Derived Neurotrophic Factor ReceptorsMultiprotein ComplexesProto-Oncogene Proteins c-retRet protein, zebrafishZebrafish Proteinsco-receptorcryo-EMcystine knotGDNF family ligandsglycosylationligand recognitionreceptor tyrosine kinaseRETX-ray crystallography

Identifiers

PMID33484636
PMCPMC8266384
OpenAlexW3123054214

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.