Evidence map›Paper›PMID 20923646›Full record

ArticleBiophysical journal2010

Quantitative experimental assessment of macromolecular crowding effects at membrane surfaces.

Rania Leventis, John R Silvius

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. 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
1.1field-weighted citation impact, top 25% 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, 22 citations in OpenAlex.

  1. Review
  2. Engineered molecular sensors for quantifying cell surface crowding.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  3. Article
  4. Article
  5. Membrane fission by protein crowding.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Entropic tension in crowded membranes.PLoS computational biology · 2012
    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 1 country.

Rania LeventisDepartment of Biochemistry, McGill University, Montréal, Québec, Canada.
John R Silvius
McGill University · CA

Funding

Canadian Institutes of Health Research MOP-7776
6 · The paper itself

Abstract

We examined how crowding of the surfaces of lipid vesicles with either grafted polyethyleneglycol (PEG) chains or bilayer-anchored protein molecules affects the binding of soluble proteins to the vesicle surface. Escherichia coli dihydrofolate reductase (DHFR, 18 kDa) or a larger fusion protein, NusA-DHFR (72 kDa), binds reversibly but with high affinity to a methotrexate-modified lipid (MTX-PE) incorporated into large unilamellar vesicles. Incorporation of phosphatidylethanolamine-PEG5000 into the vesicles strongly decreases the affinity of binding of both proteins, to a degree that varies roughly exponentially with the lateral density of the PEG chains. Covalently coupling maltose-binding protein (MBP) to the vesicle surfaces also strongly decreases the affinity of binding of NusDHFR or DHFR, to a degree that likewise varies roughly exponentially with the surface density of anchored MBP. Surface-coupled MBP strongly decreases the rate of binding of NusDHFR to MTX-PE-incorporating vesicles but does not affect the rate of NusDHFR dissociation. The large magnitudes of these effects (easily exceeding an order of magnitude for moderate degrees of surface crowding) support previous theoretical analyses and suggest that surface-crowding effects can markedly influence a variety of important aspects of protein behavior in membranes.

Indexed as

Membranes, ArtificialEscherichia coliFluorescenceKineticsLipid BilayersMacromolecular SubstancesMethotrexatePhosphatidylethanolaminesPolyethylene GlycolsProtein BindingRecombinant Fusion ProteinsSurface PropertiesTetrahydrofolate DehydrogenaseTime FactorsUnilamellar LiposomesLipid BilayersMacromolecular SubstancesMembranes, ArtificialMethotrexatephosphatidylethanolaminePhosphatidylethanolaminesPolyethylene GlycolsRecombinant Fusion ProteinsTetrahydrofolate DehydrogenaseUnilamellar Liposomes

Identifiers

PMID20923646
PMCPMC3042566
OpenAlexW1991291838

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.