Evidence map›Paper›PMID 15533920›Full record

ArticleBiophysical journal2005

Nanoscale features of fibronectin fibrillogenesis depend on protein-substrate interaction and cytoskeleton structure.

Tilo Pompe, Lars Renner, Carsten Werner

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.7field-weighted citation impact, top 19% 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

11 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Cell-material interactions on biphasic polyurethane matrix.Journal of biomedical materials research. Part A · 2013
    Article
  4. Article
  5. Review
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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.

Tilo PompeInstitute of Polymer Research Dresden and Max Bergmann Center of Biomaterials Dresden, 01069 Dresden, Germany. pompe-tilo@ipfdd.de
Lars Renner
Carsten Werner
Max Bergmann Zentrum für Biomaterialien · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell-reorganized fibronectin layers on polymer films providing a gradation of the binding strength between protein and substrate were analyzed by combined fluorescence and scanning force microscopy. The nanoscale fibronectin patterns exhibited paired parallel fibrils with characteristic spacings of 156, 233, 304, and 373 nm. These spacings depend on the interaction of fibronectin with the substrate: at enhanced fibronectin-substrate anchorage the cells form larger stress fibers, which are assembled by alpha-actinin cross-linked pairs of actin filaments subunits at the focal adhesions. A ubiquitous repeating unit of approximately 71 nm was found within these characteristic distances. We conclude that the dimensions of the actin stress fibers reflect the binding strength of fibronectin to the polymer substrate and act--in turn--as a template for the reorganization of fibronectin into surface-bound nanofibrils with characteristic spacings. This explanation was confirmed by data showing the alpha-actinin/fibronectin colocalization.

Indexed as

ActininActinsAdsorptionCell AdhesionCross-Linking ReagentsCytoskeletonEndothelial CellsFibronectinsFocal AdhesionsHumansImage Processing, Computer-AssistedMicroscopy, Atomic ForceMicroscopy, ConfocalMicroscopy, FluorescencePolymersProtein BindingActininActinsCross-Linking ReagentsFibronectinsPolymers

Identifiers

PMID15533920
PMCPMC1305030
OpenAlexW2018708785

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.