Evidence map›Paper›PMID 21159667›Full record

ReviewJournal of lipid research2011

Sequence conservation of apolipoprotein A-I affords novel insights into HDL structure-function.

Denys Bashtovyy, Martin K Jones, G M Anantharamaiah, Jere P Segrest

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of lipid research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
5.7field-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

54 citing papers in PubMed, 84 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. HDL and Oxidation.Advances in experimental medicine and biology · 2022
    Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Molecular dynamics simulations of lipid nanodiscs.Biochimica et biophysica acta. Biomembranes · 2018
    Article
  17. Article
  18. Article
  19. Tertiary structure of apolipoprotein A-I in nascent high-density lipoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2018
    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

4 authors at 2 institutions in 2 countries.

Denys BashtovyyDepartment of Medicine, Atherosclerosis Research Unit, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Martin K Jones
G M Anantharamaiah
Jere P Segrest
Institute for Atherosclerosis Research · RUUniversity of Alabama at Birmingham · US

Funding

SYNTHETIC PEPTIDE STUDIES OF THE AMPHIPATHIC HELIXP01HL034343 · NHLBI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI SEGREST, JERE P · 1985 to 2012
$18.8M
Apo E mimetics reduce cholesterol and improve HDL functionR01HL090803 · NHLBI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI ANANTHARAMAIAH, G M · 2008 to 2011
$1.6M
NHLBI NIH HHS P01 HL034343NHLBI NIH HHS P01 HL-34343NHLBI NIH HHS R01 HL-090803NHLBI NIH HHS R01 HL090803
6 · The paper itself

Abstract

We performed alignment of apolipoprotein A-I (apoA-I) sequences from 31 species of animals. We found there is specific conservation of salt bridge-forming residues in the first 30 residues of apoA-I and general conservation of a variety of residue types in the central domain, helix 2/3 to helix 7/8. In the lipid-associating domain, helix 7 and helix 10 are the most and least conserved helixes, respectively. Furthermore, eight residues are completely conserved: P66, R83, P121, E191, and P220, and three of seven Tyr residues in human apoA-I, Y18, Y115, and Y192, are conserved. Residue Y18 appears to be important for assembly of HDL. E191-Y192 represents the only completely conserved pair of adjacent residues in apoA-I; Y192 is a preferred target for site-specific oxidative modification within atheroma, and molecular dynamic simulations suggest that the conserved pair E191-Y192 is in a solvent-exposed loop-helix-loop. Molecular dynamics testing of human apoA-I showed that M112 and M148 interact with Y115, a microenvironment unique to human apoA-I. Finally, conservation of Arg residues in the α11/3 helical wheel position 7 supports several possibilities: interactions with adjacent phospholipid molecules and/or oxidized lipids and/or binding of antioxidant enzymes through cation-π orbital interactions. We conclude that sequence alignment of apoA-I provides unique insights into apoA-I structure-function relationship.

Indexed as

Conserved SequenceAmino Acid SequenceAnimalsApolipoprotein A-IHumansLipoproteins, HDLMolecular Sequence DataProtein ConformationSequence AlignmentApolipoprotein A-ILipoproteins, HDL

Identifiers

PMID21159667
PMCPMC3035680
OpenAlexW2128583836

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.