Evidence map›Paper›PMID 19900459›Full record

ArticleJournal of molecular biology2010

Inhibition of collagen fibrillogenesis by cells expressing soluble extracellular domains of DDR1 and DDR2.

Lisa A Flynn, Angela R Blissett, Edward P Calomeni, Gunjan Agarwal

Abstract read
In one paragraph

Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

39 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Collagen in Fibrotic Diseases.Sub-cellular biochemistry · 2026
    Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Identification of a novel homozygous mutation in theIranian journal of basic medical sciences · 2021
    Article
  16. Review
  17. Article
  18. Article
  19. Discoidin domain receptors: Micro insights into macro assemblies.Biochimica et biophysica acta. Molecular cell research · 2019
    Review
  20. Modulation of biomimetic mineralization of collagen by soluble ectodomain of discoidin domain receptor 2.Materials science & engineering. C, Materials for biological applications · 2019
    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

4 authors at 2 institutions in 1 country.

Lisa A FlynnDavis Heart and Lung Research Institute, 473 West 12th Avenue, Columbus, OH 43210, USA.
Angela R Blissett
Edward P Calomeni
Gunjan Agarwal
Lung Institute · USThe Ohio State University · US

Funding

Myocardial matrix remodeling by DDRsK25HL081442 · NHLBI · OHIO STATE UNIVERSITY · PI AGARWAL, GUNJAN · 2005 to 2009
$716k
NHLBI NIH HHS K25 HL081442NHLBI NIH HHS K25 HL81442-03
6 · The paper itself

Abstract

Collagen fiber assembly affects many physiological processes and is tightly controlled by collagen-binding proteins. However, to what extent membrane-bound versus cell-secreted collagen-binding proteins affect collagen fibrillogenesis is not well understood. In our previous studies, we had demonstrated that the membrane-anchored extracellular domain (ECD) of the collagen receptor discoidin domain receptor 2 (DDR2) inhibits fibrillogenesis of collagen endogenously secreted by the cells. These results led to a novel functional role of the DDR2 ECD. However, since soluble forms of DDR1 and DDR2 containing its ECD are known to naturally exist in the extracellular matrix, in this work we investigated if these soluble DDR ECDs may have a functional role in modulating collagen fibrillogenesis. For this purpose, we created mouse osteoblast cell lines stably secreting DDR1 or DDR2 ECD as soluble proteins. Transmission electron microscopy, fluorescence microscopy, and hydroxyproline assays were used to demonstrate that DDR ECD expression reduced the rate and quantity of collagen deposition and induced significant changes in fiber morphology and matrix mineralization. Collectively, our studies advance our understanding of DDR receptors as powerful regulators of collagen deposition in the ECM and elucidate their multifaceted role in ECM remodeling.

Indexed as

3T3 CellsAnimalsBase SequenceCollagenDiscoidin Domain Receptor 1Discoidin Domain ReceptorsDNA PrimersExtracellular MatrixHydroxyprolineKineticsMiceMicroscopy, Electron, TransmissionMicroscopy, FluorescenceOsteoblastsProtein MultimerizationProtein Structure, TertiaryCollagenDdr1 protein, mouseDiscoidin Domain Receptor 1Discoidin Domain ReceptorsDNA PrimersHydroxyprolineReceptor Protein-Tyrosine KinasesReceptors, MitogenRecombinant Proteins

Identifiers

PMID19900459
PMCPMC2813395
OpenAlexW2045681515

What OpenQuestion holds

Textmetadata
LicenceTDM
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.