Evidence map›Paper›PMID 19542224›Full record

ArticleThe Journal of biological chemistry2009

The first draft of the endostatin interaction network.

Clément Faye, Emilie Chautard, Bjorn R Olsen, Sylvie Ricard-Blum

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

36 citing papers in PubMed, 85 citations in OpenAlex.

  1. Trial
  2. Review
  3. Expression of Recombinant Collagen Domains and Matrikines in Eukaryotic Cells.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  4. Review
  5. Review
  6. Article
  7. Proteolysis: a key post-translational modification regulating proteoglycans.American journal of physiology. Cell physiology · 2022
    Review
  8. Article
  9. Prokaryotic Collagen-Like Proteins as Novel Biomaterials.Frontiers in bioengineering and biotechnology · 2022
    Review
  10. The Heparanase Regulatory Network in Health and Disease.International journal of molecular sciences · 2021
    Review
  11. Article
  12. Glycosaminoglycan-Protein Interactions: The First Draft of the Glycosaminoglycan Interactome.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2021
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Glycosaminoglycanomics: where we are.Glycoconjugate journal · 2017
    Review
  19. Article
  20. 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

4 authors at 3 institutions in 2 countries.

Clément FayeInstitut de Biologie et Chimie des Protéines, UMR 5086 CNRS, University Lyon 1, IFR 128 Biosciences Gerland Lyon Sud, 7 passage du Vercors, 69367 Lyon Cedex 07, France.
Emilie ChautardInstitut de Biologie et Chimie des Protéines, UMR 5086 CNRS, University Lyon 1, IFR 128 Biosciences Gerland Lyon Sud, 7 passage du Vercors, 69367 Lyon Cedex 07, France.
Bjorn R OlsenDepartment of Developmental Biology, Harvard School of Dental Medicine and Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115.
Sylvie Ricard-BlumInstitut de Biologie et Chimie des Protéines, UMR 5086 CNRS, University Lyon 1, IFR 128 Biosciences Gerland Lyon Sud, 7 passage du Vercors, 69367 Lyon Cedex 07, France.
Institut de Biologie et de Chimie des Protéines · FRCentre National de la Recherche Scientifique · FRHarvard University · US

Funding

PHS HHS 36820
6 · The paper itself

Abstract

Endostatin is a C-terminal proteolytic fragment of collagen XVIII that is localized in vascular basement membrane zones in various organs. It binds to heparin/heparan sulfate and to a number of proteins, but its molecular mechanisms of action are not fully elucidated. We have used surface plasmon resonance (SPR) arrays to identify new partners of endostatin, and to give further insights on its molecular mechanism of action. New partners of endostatin include glycosaminoglycans (chondroitin and dermatan sulfate), matricellular proteins (thrombospondin-1 and SPARC), collagens (I, IV, and VI), the amyloid peptide Abeta-(1-42), and transglutaminase-2. The biological functions of the endostatin network involve a number of extracellular proteins containing epidermal growth factor and epidermal growth factor-like domains, and able to bind calcium. Depending on the trigger event, and on the availability of its members in a given tissue at a given time, the endostatin network might be involved either in the control of angiogenesis, and tumor growth, or in neurogenesis and neurodegenerative diseases.

Indexed as

Protein Interaction MappingAnimalsDatabases, ProteinEndostatinsEpidermal Growth FactorHumansLamininModels, BiologicalNeovascularization, PathologicNeurodegenerative DiseasesProtein BindingProtein Structure, TertiarySurface Plasmon ResonanceTime FactorsEndostatinsEpidermal Growth FactorLamininlaminin 1

Identifiers

PMID19542224
PMCPMC2755928
OpenAlexW1979909621

What OpenQuestion holds

Textmetadata
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.