Evidence map›Paper›PMID 18711207›Full record

ArticleJournal of lipid research2009

Structural and dynamic interfacial properties of the lipoprotein initiating domain of apolipoprotein B.

Aubrey S Ledford, Victoria A Cook, Gregory S Shelness, Richard B Weinberg

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.8field-weighted citation impact, top 22% 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

12 citing papers in PubMed, 17 citations in OpenAlex.

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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

4 authors at 1 institution in 4 countries.

Aubrey S LedfordDepartment of Pathology, Wake Forest University School of Medicine, Winston-Salem, NC 27157, USA.
Victoria A Cook
Gregory S Shelness
Richard B Weinberg
Wake Forest University · US

Funding

TISSUE CULTURE COREP01HL049373 · NHLBI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI SHELNESS, GREGORY S · 1993 to 2012
$23.8M
STRUCTURE AND LIPID BINDING OF HUMAN APOLIPOPROTEINR01HL030897 · NHLBI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI WEINBERG, RICHARD B · 1987 to 2010
$2.9M
STRUCTURE AND LIPID BINDING OF HUMAN APOLIPOPROTEIN A-IVR23HL030897 · NHLBI · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI WEINBERG, RICHARD B · 1985 to 1986
–
NHLBI NIH HHS HL30897NHLBI NIH HHS HL49373NHLBI NIH HHS P01 HL049373NHLBI NIH HHS R01 HL030897
6 · The paper itself

Abstract

To better understand the earliest steps in the assembly of triglyceride (TG)-rich lipoproteins, we compared the biophysical and interfacial properties of two closely related apolipoprotein B (apoB) truncation mutants, one of which contains the complete lipoprotein initiating domain (apoB20.1; residues 1-912), and one of which, by virtue of a 50 amino acid C-terminal truncation, is incapable of forming nascent lipoproteins (apoB19; residues 1-862). Spectroscopic studies detected no major differences in secondary structure, and only minor differences in conformation and thermodynamic stability, between the two truncation mutants. Monolayer studies revealed that both apoB19 and apoB20.1 bound to and penetrated egg phosphatidylcholine (EPC) monolayers; however, the interfacial exclusion pressure of apoB20.1 was higher than apoB19 (25.1 mN/m vs. 22.8 mN/m). Oil drop tensiometry revealed that both proteins bound rapidly to the hydrophobic triolein/water interface, reducing interfacial tension by approximately 20 mN/m. However, when triolein drops were first coated with phospholipids (PL), apoB20.1 bound with faster kinetics than apoB19 and also displayed greater interfacial elasticity (26.9 +/- 0.8 mN/m vs. 22.9 +/- 0.8 mN/m). These data establish that the transition of apoB to assembly competence is accompanied by increases in surface activity and elasticity, but not by significant changes in global structure.

Indexed as

AdsorptionAmino Acid SequenceAnimalsApolipoproteins BChickensCircular DichroismLipoproteinsModels, BiologicalMolecular ConformationMolecular Sequence DataSpectrometry, FluorescenceSpectrophotometryThermodynamicsTrioleinWaterApolipoproteins BLipoproteinsTrioleinWater

Identifiers

PMID18711207
PMCPMC2602867
OpenAlexW2111992715

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.