Evidence map›Paper›PMID 22150513›Full record

ArticleThe Biochemical journal2012

Folded functional lipid-poor apolipoprotein A-I obtained by heating of high-density lipoproteins: relevance to high-density lipoprotein biogenesis.

Shobini Jayaraman, Giorgio Cavigiolio, Olga Gursky

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2012. 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
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

21 citing papers in PubMed, 29 citations in OpenAlex.

  1. Trial
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  10. High-Density Lipoproteins for Therapeutic Delivery Systems.Journal of materials chemistry. B · 2016
    Article
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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.

Shobini JayaramanDepartment of Physiology and Biophysics, Boston University School of Medicine, MA 02118, USA. shobini@bu.edu
Giorgio Cavigiolio
Olga Gursky
Boston University · USChildren’s Institute · US

Funding

STRUCTURE AND INTERACTIONS OF COMPLEX POLAR LIPIDSP01HL026335 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI CARRAWAY, MARGARETHA · 1985 to 2010
$23.1M
Structural Thermodynamics of Human Apolipoprotein C-1R01GM067260 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI GURSKY, OLGA · 2003 to 2024
$7.4M
Impact of self-association on structure and function of apolipoprotein A-IR01HL113059 · NHLBI · CHILDREN'S HOSPITAL & RES CTR AT OAKLAND · PI CAVIGIOLIO, GIORGIO · 2012 to 2016
$2.0M
NHLBI NIH HHS HL026335NHLBI NIH HHS P01 HL026335NHLBI NIH HHS R01 HL113059NIGMS NIH HHS R01 GM067260
6 · The paper itself

Abstract

HDL (high-density lipoproteins) remove cell cholesterol and protect from atherosclerosis. The major HDL protein is apoA-I (apolipoprotein A-I). Most plasma apoA-I circulates in lipoproteins, yet ~5% forms monomeric lipid-poor/free species. This metabolically active species is a primary cholesterol acceptor and is central to HDL biogenesis. Structural properties of lipid-poor apoA-I are unclear due to difficulties in isolating this transient species. We used thermal denaturation of human HDL to produce lipid-poor apoA-I. Analysis of the isolated lipid-poor fraction showed a protein/lipid weight ratio of 3:1, with apoA-I, PC (phosphatidylcholine) and CE (cholesterol ester) at approximate molar ratios of 1:8:1. Compared with lipid-free apoA-I, lipid-poor apoA-I showed slightly altered secondary structure and aromatic packing, reduced thermodynamic stability, lower self-associating propensity, increased adsorption to phospholipid surface and comparable ability to remodel phospholipids and form reconstituted HDL. Lipid-poor apoA-I can be formed by heating of either plasma or reconstituted HDL. We propose the first structural model of lipid-poor apoA-I which corroborates its distinct biophysical properties and postulates the lipid-induced ordering of the labile C-terminal region. In summary, HDL heating produces folded functional monomolecular lipid-poor apoA-I that is distinct from lipid-free apoA-I. Increased adsorption to phospholipid surface and reduced C-terminal disorder may help direct lipid-poor apoA-I towards HDL biogenesis.

Indexed as

Apolipoprotein A-ICircular DichroismHumansLipoproteins, HDLProtein DenaturationProtein Structure, SecondaryApolipoprotein A-ILipoproteins, HDL

Identifiers

PMID22150513
PMCPMC3857142
OpenAlexW2082763038

What OpenQuestion holds

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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.