Evidence map›Paper›PMID 21539780›Full record

ArticleBiophysical journal2011

Physical determinants of β-barrel membrane protein folding in lipid vesicles.

Alison H Dewald, Jacqueline C Hodges, Linda Columbus

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

21 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. A fluorescent reporter and single-turnover kinetics reveal insight into BAM complex function.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  10. Transmembrane β-barrels: Evolution, folding and energetics.Biochimica et biophysica acta. Biomembranes · 2017
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Solution NMR resonance assignment strategies for β-barrel membrane proteins.Protein science : a publication of the Protein Society · 2013
    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

3 authors at 1 institution in 1 country.

Alison H DewaldDepartment of Chemistry, University of Virginia, Charlottesville, Virginia, USA.
Jacqueline C Hodges
Linda Columbus
University of Virginia · US

Funding

Structure and dynamics of bacterial membrane protein - receptor interactionsR01GM087828 · NIGMS · UNIVERSITY OF VIRGINIA · PI COLUMBUS, LINDA M · 2009 to 2018
$2.7M
NIGMS NIH HHS R01 GM087828NIGMS NIH HHS R01GM087828
6 · The paper itself

Abstract

The spontaneous folding of two Neisseria outer membrane proteins, opacity-associated (Opa)(60) and Opa(50) into lipid vesicles was investigated by systematically varying bulk and membrane properties. Centrifugal fractionation coupled with sodium dodecyl sulfate polyacrylamide gel electrophoresis mobility assays enabled the discrimination of aggregate, unfolded membrane-associated, and folded membrane-inserted protein states as well as the influence of pH, ionic strength, membrane surface potential, lipid saturation, and urea on each. Protein aggregation was reduced with increasing lipid chain length, basic pH, low salt, the incorporation of negatively charged guest lipids, or by the addition of urea to the folding reaction. Insertion from the membrane-associated form was improved in shorter chain lipids, with more basic pH and low ionic strength; it is hindered by unsaturated or ether-linked lipids. The isolation of the physical determinants of insertion suggests that the membrane surface and dipole potentials are driving forces for outer membrane protein insertion and folding into lipid bilayers.

Indexed as

Protein FoldingBacterial Outer Membrane ProteinsCarbonCentrifugationChemical FractionationElectrophoresis, Polyacrylamide GelFatty Acids, UnsaturatedHydrogen-Ion ConcentrationKineticsLipid BilayersLipidsOsmolar ConcentrationProtein Structure, QuaternaryProtein Structure, SecondarySurface PropertiesUreaBacterial Outer Membrane ProteinsCarbonFatty Acids, UnsaturatedLipid BilayersLipidsOMPA outer membrane proteinsOpa protein, NeisseriaUrea

Identifiers

PMID21539780
PMCPMC3149260
OpenAlexW1987024731

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.