Evidence map›Paper›PMID 20386900›Full record

ArticleEuropean biophysics journal : EBJ2010

Adsorption of proteins on a lipid bilayer.

Vladimir P Zhdanov, Bengt Kasemo

Abstract read
PubMed Publisher
In one paragraph

Article in European biophysics journal : EBJ, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

2 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. 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

2 authors at 1 institution in 2 countries.

Vladimir P ZhdanovDepartment of Applied Physics, Chalmers University of Technology, 412 96 Göteborg, Sweden. zhdanov@catalysis.ru
Bengt Kasemo
Chalmers University of Technology · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In our analysis of protein adsorption on a lipid bilayer, the protein surface is considered to contain one or a few charged spots, and the bilayer contains a significant amount of lipids with oppositely charged head groups. After adsorption, a folded protein is assumed to change its shape slightly due to the electrostatic attraction, so that one of the spots forms a flat contact with the oppositely charged lipid heads of the lipid bilayer. With realistic parameters, this model predicts that the contribution of electrostatic interactions to the protein adsorption energy per charged amino acid-lipid pair is 16-25 kJ/mol. Thus, a few (four or five) pairs is sufficient for irreversible adsorption.

Indexed as

AdsorptionLipid BilayersProtein FoldingProteinsStatic ElectricityThermodynamicsLipid BilayersProteins

Identifiers

PMID20386900
OpenAlexW1997273795

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.