Evidence map›Paper›PMID 9398676›Full record

ArticleMolecular biology of the cell1997

Modulatory roles for integrin activation and the synergy site of fibronectin during matrix assembly.

J L Sechler, S A Corbett, J E Schwarzbauer

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

56 citing papers in PubMed, 159 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Fibronectin matrix assembly at a glance.Journal of cell science · 2025
    Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. EphA2 signaling within integrin adhesions regulates fibrillar adhesion elongation and fibronectin deposition.Matrix biology : journal of the International Society for Matrix Biology · 2021
    Article
  15. Structural insights into integrin αScience advances · 2021
    Article
  16. Review
  17. Article
  18. Article
  19. Controlling Fibronectin Fibrillogenesis Using Visible Light.Frontiers in molecular biosciences · 2020
    Article
  20. 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

3 authors at 1 institution in 1 country.

J L SechlerDepartment of Molecular Biology, Princeton University, Princeton, New Jersey 08544-1014, USA.
S A Corbett
J E Schwarzbauer
Princeton University · US

Funding

FUNCTIONAL ROLE OF FIBRONECTIN SUBUNIT HETEROGENEITYR01CA044627 · NCI · PRINCETON UNIVERSITY · PI SCHWARZBAUER, JEAN E · 1987 to 2009
$3.2M
NCI NIH HHS CA44627NCI NIH HHS R01 CA044627
6 · The paper itself

Abstract

Initiation of fibronectin (FN) matrix assembly is dependent on specific interactions between FN and cell surface integrin receptors. Here, we show that de novo FN matrix assembly exhibits a slow phase during initiation of fibrillogenesis followed by a more rapid growth phase. Mn2+, which acts by enhancing integrin function, increased the rate of FN fibril growth, but only after the initial lag phase. The RGD cell-binding sequence in type III repeat 10 is an absolute requirement for initiation by alpha5beta1 integrin. To investigate the role of the cell-binding synergy site in the adjacent repeat III9, a full-length recombinant FN containing a synergy mutation, FN(syn-), was tested for its ability to form fibrils. Mutation of this site drastically reduced FN assembly by CHOalpha5 cells. Only sparse short fibrils were formed even after prolonged incubation, indicating that FN(syn-) is defective in progression of the assembly process. These results show that the synergy site is essential for alpha5beta1-mediated accumulation of a FN matrix. However, the incorporation of FN(syn-) into fibrils and the deoxycholate-insoluble matrix could be stimulated by Mn2+. Therefore, exogenous activation of integrin receptors can overcome the requirement for FN's synergy site as well as modulate the rate of FN matrix formation.

Indexed as

AnimalsBinding SitesCHO CellsCricetinaeDeoxycholic AcidExtracellular MatrixFibronectinsHumansIntegrinsKineticsManganeseModels, BiologicalMutationOligopeptidesProtein BindingRatsarginyl-glycyl-aspartic acidDeoxycholic AcidFibronectinsIntegrinsManganeseOligopeptidesReceptors, VitronectinRecombinant ProteinsTetradecanoylphorbol Acetate

Identifiers

PMID9398676
PMCPMC25728
OpenAlexW2142634963

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.