Evidence map›Paper›PMID 23230082›Full record

ReviewJournal of lipid research2013

New insights into the determination of HDL structure by apolipoproteins: Thematic review series: high density lipoprotein structure, function, and metabolism.

Michael C Phillips

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of lipid research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

97 citing papers in PubMed, 170 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Observational
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. International journal of molecular sciences · 2025
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

37 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Michael C PhillipsLipid Research Group, Division of Gastroenterology, Hepatology and Nutrition, The Children's Hospital of Philadelphia, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA. Electronic address: phillipsmi@email.chop.edu.
Philadelphia University · US

Funding

TISSUE CULTURE CORE LABORATORYP01HL022633 · NHLBI · MCP HAHNEMANN UNIVERSITY · PI LUND-KATZ, SISSEL · 1985 to 2013
$26.1M
STRUCTURAL BASIS OF THE INTERACTIONS OF APOLIPOPROTEIN ER01HL056083 · NHLBI · MCP HAHNEMANN UNIVERSITY · PI LUND-KATZ, SISSEL · 1997 to 2013
$5.0M
NHLBI NIH HHS HL-22633NHLBI NIH HHS HL-56083NHLBI NIH HHS P01 HL022633NHLBI NIH HHS R01 HL056083
6 · The paper itself

Abstract

Apolipoprotein (apo)A-I is the principal protein component of HDL, and because of its conformational adaptability, it can stabilize all HDL subclasses. The amphipathic α-helix is the structural motif that enables apoA-I to achieve this functionality. In the lipid-free state, the helical segments unfold and refold in seconds and are located in the N-terminal two thirds of the molecule where they are loosely packed as a dynamic, four-helix bundle. The C-terminal third of the protein forms an intrinsically disordered domain that mediates initial binding to phospholipid surfaces, which occurs with coupled α-helix formation. The lipid affinity of apoA-I confers detergent-like properties; it can solubilize vesicular phospholipids to create discoidal HDL particles with diameters of approximately 10 nm. Such particles contain a segment of phospholipid bilayer and are stabilized by two apoA-I molecules that are arranged in an anti-parallel, double-belt conformation around the edge of the disc, shielding the hydrophobic phospholipid acyl chains from exposure to water. The apoA-I molecules are in a highly dynamic state, and they stabilize discoidal particles of different sizes by certain segments forming loops that detach reversibly from the particle surface. The flexible apoA-I molecule adapts to the surface of spherical HDL particles by bending and forming a stabilizing trefoil scaffold structure. The above characteristics of apoA-I enable it to partner with ABCA1 in mediating efflux of cellular phospholipid and cholesterol and formation of a heterogeneous population of nascent HDL particles. Novel insights into the structure-function relationships of apoA-I should help reveal mechanisms by which HDL subclass distribution can be manipulated.

Indexed as

ApolipoproteinsHumansLipoproteins, HDLModels, MolecularProtein ConformationApolipoproteinsLipoproteins, HDLamphipathic α-helixapoA-IapoEATP binding cassette transporter A1cholesterolhelix bundlelipoproteinmembrane solubilizationphospholipid

Identifiers

PMID23230082
PMCPMC3708355
OpenAlexW2021267305

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.