Evidence map›Paper›PMID 21914797›Full record

ArticleThe Journal of biological chemistry2011

Crystal structure of C-terminal truncated apolipoprotein A-I reveals the assembly of high density lipoprotein (HDL) by dimerization.

Xiaohu Mei, David Atkinson

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 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed
11.5field-weighted citation impact, top 1% 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

110 citing papers in PubMed, 196 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Foam fractionation studies of recombinant human apolipoprotein A-I.Biochimica et biophysica acta. Biomembranes · 2024
    Article
  9. Article
  10. Article
  11. Molecular dynamics simulation of apolipoprotein E3 lipid nanodiscs.Biochimica et biophysica acta. Biomembranes · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. HDL Structure.Advances in experimental medicine and biology · 2022
    Article
  20. Review

50 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

2 authors at 1 institution in 1 country.

Xiaohu MeiDepartment of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts 02118.
David AtkinsonDepartment of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts 02118. Electronic address: atkinson@bu.edu.
Boston University · US

Funding

STRUCTURE AND INTERACTIONS OF COMPLEX POLAR LIPIDSP01HL026335 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI CARRAWAY, MARGARETHA · 1985 to 2010
$23.1M
Apolipoprotein A-l and HDL: Structure, Formation and FunctionR01HL116518 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI ATKINSON, DAVID · 2014 to 2017
$2.2M
NHLBI NIH HHS P01 HL026335NHLBI NIH HHS P01-HL026335NHLBI NIH HHS R01 HL116518
6 · The paper itself

Abstract

Apolipoprotein A-I (apoA-I) plays important structural and functional roles in plasma high density lipoprotein (HDL) that is responsible for reverse cholesterol transport. However, a molecular understanding of HDL assembly and function remains enigmatic. The 2.2-Å crystal structure of Δ(185-243)apoA-I reported here shows that it forms a half-circle dimer. The backbone of the dimer consists of two elongated antiparallel proline-kinked helices (five AB tandem repeats). The N-terminal domain of each molecule forms a four-helix bundle with the helical C-terminal region of the symmetry-related partner. The central region forms a flexible domain with two antiparallel helices connecting the bundles at each end. The two-domain dimer structure based on helical repeats suggests the role of apoA-I in the formation of discoidal HDL particles. Furthermore, the structure suggests the possible interaction with lecithin-cholesterol acyltransferase and may shed light on the molecular details of the effect of the Milano, Paris, and Fin mutations.

Indexed as

Apolipoprotein A-IAtherosclerosisCholesterolCrystallizationCrystallography, X-RayDimerizationHumansLecithinsLipoproteins, HDLMutationPhosphatidylcholine-Sterol O-AcyltransferaseProtein Structure, TertiarySaltsSurface PropertiesApolipoprotein A-ICholesterolLecithinsLipoproteins, HDLPhosphatidylcholine-Sterol O-AcyltransferaseSalts

Identifiers

PMID21914797
PMCPMC3207425
OpenAlexW2051560414

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.