Evidence map›Paper›PMID 16581834›Full record

ArticleBiophysical journal2006

Novel changes in discoidal high density lipoprotein morphology: a molecular dynamics study.

Andrea Catte, James C Patterson, Martin K Jones, W Gray Jerome, Denys Bashtovyy, Zhengchang Su, Feifei Gu, Jianguo Chen, Marcela P Aliste, Stephen C Harvey and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

42 citing papers in PubMed, 92 citations in OpenAlex.

  1. Molecular dynamics simulations of lipid nanodiscs.Biochimica et biophysica acta. Biomembranes · 2018
    Article
  2. IgG Antibody 3D Structures and Dynamics.Antibodies (Basel, Switzerland) · 2018
    Review
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  18. Lipid simulations: a perspective on lipids in action.Cold Spring Harbor perspectives in biology · 2011
    Review
  19. Article
  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

13 authors at 4 institutions in 1 country.

Andrea CatteDepartment of Medicine, and Center for Computational and Structural Biology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
James C Patterson
Martin K Jones
W Gray Jerome
Denys Bashtovyy
Zhengchang Su
Feifei Gu
Jianguo Chen
Marcela P Aliste
Stephen C Harvey
Ling Li
Gilbert Weinstein
Jere P Segrest
University of Alabama at Birmingham · USGeorgia Institute of Technology · USUniversity of Georgia · USVanderbilt University Medical Center · US

Funding

SYNTHETIC PEPTIDE STUDIES OF THE AMPHIPATHIC HELIXP01HL034343 · NHLBI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI SEGREST, JERE P · 1985 to 2012
$18.8M
NHLBI NIH HHS HL-34343NHLBI NIH HHS P01 HL034343
6 · The paper itself

Abstract

ApoA-I is a uniquely flexible lipid-scavenging protein capable of incorporating phospholipids into stable particles. Here we report molecular dynamics simulations on a series of progressively smaller discoidal high density lipoprotein particles produced by incremental removal of palmitoyloleoylphosphatidylcholine via four different pathways. The starting model contained 160 palmitoyloleoylphosphatidylcholines and a belt of two antiparallel amphipathic helical lipid-associating domains of apolipoprotein (apo) A-I. The results are particularly compelling. After a few nanoseconds of molecular dynamics simulation, independent of the starting particle and method of size reduction, all simulated double belts of the four lipidated apoA-I particles have helical domains that impressively approximate the x-ray crystal structure of lipid-free apoA-I, particularly between residues 88 and 186. These results provide atomic resolution models for two of the particles produced by in vitro reconstitution of nascent high density lipoprotein particles. These particles, measuring 95 angstroms and 78 angstroms by nondenaturing gradient gel electrophoresis, correspond in composition and in size/shape (by negative stain electron microscopy) to the simulated particles with molar ratios of 100:2 and 50:2, respectively. The lipids of the 100:2 particle family form minimal surfaces at their monolayer-monolayer interface, whereas the 50:2 particle family displays a lipid pocket capable of binding a dynamic range of phospholipid molecules.

Indexed as

Models, ChemicalModels, MolecularApolipoprotein A-IComputer SimulationCrystallographyLipoproteins, HDLMotionProtein ConformationApolipoprotein A-ILipoproteins, HDL

Identifiers

PMID16581834
PMCPMC1471865
OpenAlexW2043242227

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.