Evidence map›Paper›PMID 16326915›Full record

ArticleBiophysical journal2006

Self-assembly of actin scaffolds at ponticulin-containing supported phospholipid bilayers.

Benjamin R G Johnson, Richard J Bushby, John Colyer, Stephen D Evans

Erratum issuedAbstract readLetter
In one paragraph

Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Review
  2. Review
  3. Topography design in model membranes: Where biology meets physics.Experimental biology and medicine (Maywood, N.J.) · 2019
    Review
  4. The design of MACs (minimal actin cortices).Cytoskeleton (Hoboken, N.J.) · 2013
    Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors.

Benjamin R G Johnson
Richard J Bushby
John Colyer
Stephen D Evans

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phospholipid vesicles containing ponticulin have been used to form solid supported and tethered bilayer lipid membranes. The ponticulin serves as both a nucleation site for actin polymerization as well as a binding site for F-actin. Studies of F-actin binding to such bilayers have demonstrated the formation of an in vitro actin scaffold. The dissociation constant for the binding of F-actin filaments to a ponticulin-containing tethered bilayer was found to be 11 +/- 5 nM, indicative of high affinity binding.

Indexed as

ActinsAnimalsBinding SitesBiophysicsCarrier ProteinsDictyosteliumLipid BilayersLipidsMicrofilament ProteinsMicroscopy, Electron, TransmissionModels, BiologicalPhosphatidylcholinesPhospholipidsProtein BindingActinsCarrier ProteinsF-actin-binding proteinsLipid BilayersLipidsMicrofilament ProteinsPhosphatidylcholinesPhospholipids

Identifiers

PMID16326915
PMCPMC1367125

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.