Evidence map›Paper›PMID 21292766›Full record

ArticleThe Journal of biological chemistry2011

The low resolution structure of ApoA1 in spherical high density lipoprotein revealed by small angle neutron scattering.

Zhiping Wu, Valentin Gogonea, Xavier Lee, Roland P May, Vitaliy Pipich, Matthew A Wagner, Arundhati Undurti, Thomas C Tallant, Camelia Baleanu-Gogonea, Francesca Charlton and 4 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
6.8field-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

32 citing papers in PubMed, 59 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. HDL Structure.Advances in experimental medicine and biology · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. ApoA1 and ApoA1-specific self-antibodies in cardiovascular disease.Laboratory investigation; a journal of technical methods and pathology · 2016
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review
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

14 authors at 6 institutions in 5 countries.

Zhiping WuDepartment of Cell Biology, Center for Cardiovascular Diagnostics and Prevention, Cleveland Clinic, Cleveland, OH 44195, USA.
Valentin Gogonea
Xavier Lee
Roland P May
Vitaliy Pipich
Matthew A Wagner
Arundhati Undurti
Thomas C Tallant
Camelia Baleanu-Gogonea
Francesca Charlton
Alexander Ioffe
Joseph A DiDonato
Kerry-Anne Rye
Stanley L Hazen
Cleveland State University · USForschungszentrum Jülich · DECleveland Clinic · USInstitut Laue-Langevin · FRThe Heart Research Institute · AUThe University of Sydney · AU

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007250 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI HUANG, ALEX YEE-CHEN · 1985 to 2023
$33.4M
Structural Determinants Of Ceruloplasmin Inflammatory ActivityP01HL076491 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI PLOW, EDWARD FRANKLIN · 2004 to 2019
$27.3M
Regression of Atherosclerosis CoreP01HL098055 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI FISHER, EDWARD A · 2010 to 2014
$12.1M
REGULATION OF MONOCYTE 15-LIPOXYGENASE EXPRESSIONP01HL087018 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI MCINTYRE, THOMAS M · 2007 to 2011
$11.4M
NHLBI NIH HHS P01 HL076491NHLBI NIH HHS P01 HL076491-055328NHLBI NIH HHS P01 HL087018NHLBI NIH HHS P01 HL087018-02001NHLBI NIH HHS P01 HL098055NIGMS NIH HHS T32 GM007250
6 · The paper itself

Abstract

Spherical high density lipoprotein (sHDL), a key player in reverse cholesterol transport and the most abundant form of HDL, is associated with cardiovascular diseases. Small angle neutron scattering with contrast variation was used to determine the solution structure of protein and lipid components of reconstituted sHDL. Apolipoprotein A1, the major protein of sHDL, forms a hollow structure that cradles a central compact lipid core. Three apoA1 chains are arranged within the low resolution structure of the protein component as one of three possible global architectures: (i) a helical dimer with a hairpin (HdHp), (ii) three hairpins (3Hp), or (iii) an integrated trimer (iT) in which the three apoA1 monomers mutually associate over a portion of the sHDL surface. Cross-linking and mass spectrometry analyses help to discriminate among the three molecular models and are most consistent with the HdHp overall architecture of apoA1 within sHDL.

Indexed as

NeutronsScattering, Small AngleApolipoprotein A-IHumansLipoproteins, HDLMass SpectrometryProtein MultimerizationApolipoprotein A-ILipoproteins, HDL

Identifiers

PMID21292766
PMCPMC3069452
OpenAlexW2084842911

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.