Evidence map›Paper›PMID 22579246›Full record

ArticleStructure (London, England : 1993)2012

The structure of dimeric apolipoprotein A-IV and its mechanism of self-association.

Xiaodi Deng, Jamie Morris, James Dressmen, Matthew R Tubb, Patrick Tso, W Gray Jerome, W Sean Davidson, Thomas B Thompson

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

29 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Biomedicines · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Pleiotropic roles of late embryogenesis abundant proteins ofComputational and structural biotechnology journal · 2021
    Review
  10. Article
  11. Article
  12. GROWTH POLE RING protein forms a 200-nm-diameter ring structure essential for polar growth and rod shape inProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  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

8 authors at 2 institutions in 1 country.

Xiaodi DengDepartment of Molecular Genetics, Biochemistry, and Microbiology, College of Medicine, University of Cincinnati, OH 45267, USA.
Jamie Morris
James Dressmen
Matthew R Tubb
Patrick Tso
W Gray Jerome
W Sean Davidson
Thomas B Thompson
University of Cincinnati · USVanderbilt University Medical Center · US

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI MATTHEW J TYSKA · 1995 to 2026
$172.8M
Translational Analysis CoreP30DK058404 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI RICHARD M. PEEK · 2002 to 2026
$29.9M
Vanderbilt Diabetes Research CenterP30DK020593 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI OWEN P MCGUINNESS · 2012 to 2026
$29.3M
TRANSGENIC MOUSE/ ES CELL SHARES RESOURCESP60DK020593 · NIDDK · VANDERBILT UNIVERSITY · PI MCGUINNESS, OWEN P · 1986 to 2011
$28.1M
TRAINING IN CARDIOVASCULAR BIOLOGYT32HL007382 · NHLBI · UNIVERSITY OF CINCINNATI · PI SCHWARTZ, ARNOLD · 1985 to 2012
$5.9M
Apolipoprotein A-I structure in high density lipoproteinsR01HL067093 · NHLBI · UNIVERSITY OF CINCINNATI · PI DAVIDSON, W SEAN · 2002 to 2016
$4.3M
A high-resolution structural approach to understanding HDL biogenesisR01GM098458 · NIGMS · UNIVERSITY OF CINCINNATI · PI DAVIDSON, W SEAN · 2011 to 2014
$1.2M
GENDER DIFFERENCES IN FAMILIAL RISKR01HL048148 · NHLBI · VIRGINIA COMMONWEALTH UNIVERSITY · PI EAVES, LINDON J · 1993 to 1995
–
NCI NIH HHS CA68485NCI NIH HHS P30 CA068485NHLBI NIH HHS HL48148NHLBI NIH HHS HL67093NHLBI NIH HHS R01 HL067093NHLBI NIH HHS T32 HL007382NIDDK NIH HHS DK20593NIDDK NIH HHS DK58404NIDDK NIH HHS P30 DK020593NIDDK NIH HHS P30 DK058404NIDDK NIH HHS P60 DK020593NIGMS NIH HHS R01 GM098458
6 · The paper itself

Abstract

Apolipoproteins are key structural elements of lipoproteins and critical mediators of lipid metabolism. Their detergent-like properties allow them to emulsify lipid or exist in a soluble lipid-free form in various states of self-association. Unfortunately, these traits have hampered high-resolution structural studies needed to understand the biogenesis of cardioprotective high-density lipoproteins (HDLs). We derived a crystal structure of the core domain of human apolipoprotein (apo)A-IV, an HDL component and important mediator of lipid absorption. The structure at 2.4 Å depicts two linearly connected 4-helix bundles participating in a helix swapping arrangement that offers a clear explanation for how the protein self-associates as well as clues to the structure of its monomeric form. This also provides a logical basis for antiparallel arrangements recently described for lipid-containing particles. Furthermore, we propose a "swinging door" model for apoA-IV lipid association.

Indexed as

Protein Structure, SecondaryApolipoproteins ABinding SitesCrystallography, X-RayDimerizationHumansLipid MetabolismModels, Molecularapolipoprotein A-IVApolipoproteins A

Identifiers

PMID22579246
PMCPMC3354570
OpenAlexW2143836021

What OpenQuestion holds

Textmetadata
LicenceTDM
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.