Evidence map›Paper›PMID 22063273›Full record

ArticleBiochimica et biophysica acta2012

Rotational and hinge dynamics of discoidal high density lipoproteins probed by interchain disulfide bond formation.

Ling Li, Songlin Li, Martin K Jones, Jere P Segrest

Abstract read
In one paragraph

Article in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

17 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Molecular dynamics simulations of lipid nanodiscs.Biochimica et biophysica acta. Biomembranes · 2018
    Article
  4. Article
  5. 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
  6. Article
  7. ApoA1 and ApoA1-specific self-antibodies in cardiovascular disease.Laboratory investigation; a journal of technical methods and pathology · 2016
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
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  17. 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

4 authors at 1 institution in 1 country.

Ling LiDepartment of Medicine and Atherosclerosis Research Unit, University of Alabama at Birmingham, Birmingham, AL 35294, USA. lil@umn.edu
Songlin Li
Martin K Jones
Jere P Segrest
University 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
Protective Mechanisms of Statins in Alzheimer's DiseaseR01AG031846 · NIA · UNIVERSITY OF MINNESOTA · PI LI, LING · 2008 to 2012
$1.5M
NHLBI NIH HHS P01 HL034343NHLBI NIH HHS P01 HL34343NIA NIH HHS R01 AG031846
6 · The paper itself

Abstract

To develop a detailed double belt model for discoidal HDL, we previously scored inter-helical salt bridges between all possible registries of two stacked antiparallel amphipathic helical rings of apolipoprotein (apo) A-I. The top score was the antiparallel apposition of helix 5 with 5 followed closely by appositions of helix 5 with 4 and helix 5 with 6. The rationale for the current study is that, for each of the optimal scores, a pair of identical residues can be identified in juxtaposition directly on the contact edge between the two antiparallel helical belts of apoA-I. Further, these residues are always in the '9th position' in one of the eighteen 11-mer repeats that make up the lipid-associating domain of apoA-I. To illustrate our terminology, 129j (LL5/5) refers to the juxtaposition of the Cα atoms of G129 (in a '9th position') in the pairwise helix 5 domains. We reasoned that if identical residues in the double belt juxtapositions were mutated to a cysteine and kept under reducing conditions during disc formation, we would have a precise method for determining registration in discoidal HDL by formation of a disulfide-linked apoA-I homodimer. Using this approach, we conclude that 129j (LL5/5) is the major rotamer orientation for double belt HDL and propose that the small ubiquitous gap between the pairwise helix 5 portions of the double belt in larger HDL discoidal particles is significantly dynamic to hinge off the disc edge under certain conditions, e.g., in smaller particles or perhaps following binding of the enzyme LCAT. This article is part of a Special Issue entitled Advances in High Density Lipoprotein Formation and Metabolism: A Tribute to John F. Oram (1945-2010).

Indexed as

Amino Acid SubstitutionApolipoprotein A-ICystineDimyristoylphosphatidylcholineHumansLipoproteinsMolecular Dynamics SimulationMutagenesis, Site-DirectedProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiaryRNA-Binding ProteinsAPOA1 protein, humanApolipoprotein A-ICystineDimyristoylphosphatidylcholinediscoidal lipoproteinshigh density lipoprotein binding proteinLipoproteinsRNA-Binding Proteins

Identifiers

PMID22063273
PMCPMC3666556
OpenAlexW2020331655

What OpenQuestion holds

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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.