Evidence mapPaperPMID 16636271Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Apolipoprotein B is conformationally flexible but anchored at a triolein/water interface: a possible model for lipoprotein surfaces.

Libo Wang, Mary T Walsh, Donald M Small

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

26 citing papers in PubMed, 52 citations in OpenAlex.

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  13. Lipids and HCV.Seminars in immunopathology · 2013
    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 2 institutions in 1 country.

Libo WangDepartment of Physiology and Biophysics, Boston University School of Medicine, Boston, MA 02118, USA.
Mary T Walsh
Donald M Small
Boston University · USUniversity of California, San Francisco · US

Funding

STRUCTURE AND INTERACTIONS OF COMPLEX POLAR LIPIDSP01HL026335 · BOSTON UNIVERSITY MEDICAL CAMPUS · 1985 to 2005
$13.0M
NHLBI NIH HHS 2P01 HL26335-21NHLBI NIH HHS P01 HL026335
6 · The paper itself

Abstract

Apolipoprotein B (apoB) is one of a unique group of proteins that form and bind to fat droplets, stabilize the emulsified fat, and direct their metabolism. ApoB, secreted on lipoproteins (emulsions), remains bound during lipid metabolism yet exhibits conformational flexibility. It has amphipathic beta-strand (AbetaS)-rich domains and amphipathic alpha-helix (AalphaH)-rich domains. We showed that two consensus AbetaS peptides of apoB bound strongly to hydrophobic interfaces [triolein/water (TO/W) and dodecane/water], were elastic, and were not pushed off the interface when the surface was compressed. In contrast, an AalphaH peptide modeling helical parts of apoB was forced off the TO/W interface by compression and readsorbed when the interface was expanded. In this report, the surface behavior of apoB-100 was studied at the TO/W interface. Solubilized apoB lowered the interfacial tension of TO/W in a concentration-dependent fashion. At equilibrium tension, if the surface was compressed, part of apoB was pushed off but quickly readsorbed when the surface was expanded. Even when the surface area was compressed by approximately 55%, part of the apoB molecule remained bound. The maximum surface pressure that apoB could withstand without being partially ejected was 13 mN/m. ApoB showed high elasticity at the TO/W interface. Based on studies of the consensus AbetaS and AalphaH peptides, we suggest that AbetaSs anchor apoB and are its nonexchangeable motif, whereas its conformational flexibility arises from both the elastic nature of the AbetaS and the ability of AalphaH domains of the molecule to desorb and readsorb rapidly in response to surface pressure changes.

Indexed as

AdsorptionAnimalsApolipoproteins BElasticityHumansLipoproteins, LDLModels, MolecularPeptidesSurface PropertiesTrioleinWaterApolipoproteins BLipoproteins, LDLPeptidesTrioleinWater

Identifiers

PMID16636271
PMCPMC1458986
OpenAlexW2124877134

What Socratic 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 Socratic graph.