Evidence map›Paper›PMID 18417335›Full record

ArticleMatrix biology : journal of the International Society for Matrix Biology2008

Assay to mechanically tune and optically probe fibrillar fibronectin conformations from fully relaxed to breakage.

William C Little, Michael L Smith, Urs Ebneter, Viola Vogel

Open access · greenAbstract read
In one paragraph

Article in Matrix biology : journal of the International Society for Matrix Biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

52 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
  2. Measuring the biomechanical properties of cell-derived fibronectin fibrils.Biomechanics and modeling in mechanobiology · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. The Janus Role of Adhesion in Chondrogenesis.International journal of molecular sciences · 2020
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

4 authors at 1 institution in 1 country.

William C LittleDepartment of Materials, ETH Zurich, CH-8093, Zürich, Switzerland.
Michael L Smith
Urs Ebneter
Viola Vogel
ETH Zurich · CH

Funding

Nanomedicine development center for mechanobiologyPN2EY016586 · NEI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI DUSTIN, MICHAEL LORAN · 2005 to 2014
$23.0M
NEI NIH HHS PN2 EY016586
6 · The paper itself

Abstract

In response to growing needs for quantitative biochemical and cellular assays that address whether the extracellular matrix (ECM) acts as a mechanochemical signal converter to co-regulate cellular mechanotransduction processes, a new assay is presented where plasma fibronectin fibers are manually deposited onto elastic sheets, while force-induced changes in protein conformation are monitored by fluorescence resonance energy transfer (FRET). Fully relaxed assay fibers can be stretched at least 5-6 fold, which involves Fn domain unfolding, before the fibers break. In native fibroblast ECM, this full range of stretch-regulated conformations coexists in every field of view confirming that the assay fibers are physiologically relevant model systems. Since alterations of protein function will directly correlate with their extension in response to force, the FRET vs. strain curves presented herein enable the mapping of fibronectin strain distributions in 2D and 3D cell cultures with high spatial resolution. Finally, cryptic sites for fibronectin's N-terminal 70-kD fragment were found to be exposed at relatively low strain, demonstrating the assay's potential to analyze stretch-regulated protein-protein interactions.

Indexed as

AnimalsElasticityEndothelial CellsExtracellular MatrixFibroblastsFibronectinsFluorescence Resonance Energy TransferFluorescent DyesHumansMechanotransduction, CellularMiceMicroscopy, Atomic ForceMicroscopy, FluorescenceNIH 3T3 CellsPeptide FragmentsProtein Conformationfibroblast motility-stimulating factorFibronectinsFluorescent DyesPeptide FragmentsSilicones

Identifiers

PMID18417335
PMCPMC5615104
OpenAlexW2045981338

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.