Evidence map›Paper›PMID 20679346›Full record

ArticleThe Journal of biological chemistry2010

Influence of apolipoprotein (Apo) A-I structure on nascent high density lipoprotein (HDL) particle size distribution.

Charulatha Vedhachalam, Palaniappan Sevugan Chetty, Margaret Nickel, Padmaja Dhanasekaran, Sissel Lund-Katz, George H Rothblat, Michael C Phillips

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. 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
6.5field-weighted citation impact, top 3% 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, 46 citations in OpenAlex.

  1. Review
  2. Lipid Droplet Dynamics in Alcoholic Steatohepatitis.The American journal of pathology · 2026
    Review
  3. Foam fractionation studies of recombinant human apolipoprotein A-I.Biochimica et biophysica acta. Biomembranes · 2024
    Article
  4. Article
  5. Article
  6. Is ABCA1 a lipid transfer protein?Journal of lipid research · 2018
    Review
  7. ApoA1 and ApoA1-specific self-antibodies in cardiovascular disease.Laboratory investigation; a journal of technical methods and pathology · 2016
    Review
  8. Review
  9. Article
  10. Molecular mechanisms of cellular cholesterol efflux.The Journal of biological chemistry · 2014
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

7 authors at 3 institutions in 1 country.

Charulatha VedhachalamLipid Research Group, Gastroenterology, Hepatology, and Nutrition Division, Children's Hospital of Philadelphia, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-4318, USA.
Palaniappan Sevugan Chetty
Margaret Nickel
Padmaja Dhanasekaran
Sissel Lund-Katz
George H Rothblat
Michael C Phillips
Children's Hospital of Philadelphia · USPhiladelphia University · USUniversity of Pennsylvania · US

Funding

TISSUE CULTURE CORE LABORATORYP01HL022633 · NHLBI · MCP HAHNEMANN UNIVERSITY · PI ROTHBLAT, GEORGE H · 1985 to 2013
$26.1M
NHLBI NIH HHS HL22633NHLBI NIH HHS P01 HL022633
6 · The paper itself

Abstract

The principal protein of high density lipoprotein (HDL), apolipoprotein (apo) A-I, in the lipid-free state contains two tertiary structure domains comprising an N-terminal helix bundle and a less organized C-terminal domain. It is not known how the properties of these domains modulate the formation and size distribution of apoA-I-containing nascent HDL particles created by ATP-binding cassette transporter A1 (ABCA1)-mediated efflux of cellular phospholipid and cholesterol. To address this issue, proteins corresponding to the two domains of human apoA-I (residues 1-189 and 190-243) and mouse apoA-I (residues 1-186 and 187-240) together with some human/mouse domain hybrids were examined for their abilities to form HDL particles when incubated with either ABCA1-expressing cells or phospholipid multilamellar vesicles. Incubation of human apoA-I with cells gave rise to two sizes of HDL particles (hydrodynamic diameter, 8 and 10 nm), and removal or disruption of the C-terminal domain eliminated the formation of the smaller particle. Variations in apoA-I domain structure and physical properties exerted similar effects on the rates of formation and sizes of HDL particles created by either spontaneous solubilization of phospholipid multilamellar vesicles or the ABCA1-mediated efflux of cellular lipids. It follows that the sizes of nascent HDL particles are determined at the point at which cellular phospholipid and cholesterol are solubilized by apoA-I; apparently, this is the rate-determining step in the overall ABCA1-mediated cellular lipid efflux process. The stability of the apoA-I N-terminal helix bundle domain and the hydrophobicity of the C-terminal domain are important determinants of both nascent HDL particle size and their rate of formation.

Indexed as

Protein ConformationAnimalsApolipoprotein A-IATP Binding Cassette Transporter 1ATP-Binding Cassette TransportersCell LineCholesterolHumansLipoproteins, HDLMacrophagesMiceParticle SizeABCA1 protein, humanApolipoprotein A-IATP Binding Cassette Transporter 1ATP-Binding Cassette TransportersCholesterolLipoproteins, HDL

Identifiers

PMID20679346
PMCPMC2952197
OpenAlexW2037303704

What OpenQuestion holds

Textmetadata
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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.