Evidence map›Paper›PMID 31745115›Full record

ArticleScientific reports2019

DDR1 autophosphorylation is a result of aggregation into dense clusters.

David S Corcoran, Victoria Juskaite, Yuewei Xu, Frederik Görlitz, Yuriy Alexandrov, Christopher Dunsby, Paul M W French, Birgit Leitinger

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
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  5. Discoid Domain Receptors Signaling in Macrophages-Mediated Diseases.International journal of general medicine · 2025
    Review
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  20. Two-step release of kinase autoinhibition in discoidin domain receptor 1.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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

8 authors at 2 institutions in 2 countries.

David S CorcoranNational Heart and Lung Institute, Imperial College London, London, SW7 2AZ, UK.
Victoria JuskaiteNational Heart and Lung Institute, Imperial College London, London, SW7 2AZ, UK.
Yuewei XuNational Heart and Lung Institute, Imperial College London, London, SW7 2AZ, UK.
Frederik GörlitzPhotonics Group, Physics Department, Imperial College London, London, SW7 2AZ, UK.
Yuriy AlexandrovPhotonics Group, Physics Department, Imperial College London, London, SW7 2AZ, UK.
Christopher DunsbyPhotonics Group, Physics Department, Imperial College London, London, SW7 2AZ, UK.
Paul M W FrenchPhotonics Group, Physics Department, Imperial College London, London, SW7 2AZ, UK.
Birgit LeitingerNational Heart and Lung Institute, Imperial College London, London, SW7 2AZ, UK. b.leitinger@imperial.ac.uk.
Imperial College London · GBThe Francis Crick Institute · GB

Funding

Medical Research Council MR/K015834/1
6 · The paper itself

Abstract

The collagen receptor DDR1 is a receptor tyrosine kinase that promotes progression of a wide range of human disorders. Little is known about how ligand binding triggers DDR1 kinase activity. We previously reported that collagen induces DDR1 activation through lateral dimer association and phosphorylation between dimers, a process that requires specific transmembrane association. Here we demonstrate ligand-induced DDR1 clustering by widefield and super-resolution imaging and provide evidence for a mechanism whereby DDR1 kinase activity is determined by its molecular density. Ligand binding resulted in initial DDR1 reorganisation into morphologically distinct clusters with unphosphorylated DDR1. Further compaction over time led to clusters with highly aggregated and phosphorylated DDR1. Ligand-induced DDR1 clustering was abolished by transmembrane mutations but did not require kinase activity. Our results significantly advance our understanding of the molecular events underpinning ligand-induced DDR1 kinase activity and provide an explanation for the unusually slow DDR1 activation kinetics.

Indexed as

Protein MultimerizationCollagenDiscoidin Domain Receptor 1HEK293 CellsHumansMutationPhosphorylationCollagenDDR1 protein, humanDiscoidin Domain Receptor 1

Identifiers

PMID31745115
PMCPMC6863838
OpenAlexW2991130173

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.