Evidence map›Paper›PMID 27054174›Full record

ArticleData in brief2016

Data supporting beta-amyloid dimer structural transitions and protein-lipid interactions on asymmetric lipid bilayer surfaces using MD simulations on experimentally derived NMR protein structures.

Sara Y Cheng, George Chou, Creighton Buie, Mark W Vaughn, Campbell Compton, Kwan H Cheng

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Data in brief, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 32% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. 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

6 authors at 3 institutions in 1 country.

Sara Y ChengDepartment of Physics, University of Texas at Austin, Austin, TX 78712, USA.
George ChouDepartment of Chemical Engineering, Texas Tech University, Lubbock, TX 79409, USA.
Creighton BuieDepartment of Chemical Engineering, Texas Tech University, Lubbock, TX 79409, USA.
Mark W VaughnDepartment of Chemical Engineering, Texas Tech University, Lubbock, TX 79409, USA.
Campbell ComptonDepartment of Computer Science, Trinity University, San Antonio, TX 78212, USA.
Kwan H ChengDepartment of Physics, Texas Tech University, Lubbock, TX 79409, USA; Department of Physics and Astronomy, Trinity University, San Antonio, TX 78212, USA.
Texas Tech University · USTrinity University · USThe University of Texas at Austin · US

Funding

An Assessment of Multimodal Physics Lab Intervention Efficacy in STEM EducationRC1GM090897 · NIGMS · TEXAS TECH UNIVERSITY · PI CHENG, KWAN H KELVIN, THACKER, BETH · 2009 to 2010
$810k
NIGMS NIH HHS RC1 GM090897
6 · The paper itself

Abstract

This data article supports the research article entitled "Maximally Asymmetric Transbilayer Distribution of Anionic Lipids Alters the Structure and interaction with Lipids of an Amyloidogenic Protein Dimer Bound to the Membrane Surface" [1]. We describe supporting data on the binding kinetics, time evolution of secondary structure, and residue-contact maps of a surface-absorbed beta-amyloid dimer protein on different membrane surfaces. We further demonstrate the sorting of annular and non-annular regions of the protein/lipid bilayer simulation systems, and the correlation of lipid-number mismatch and surface area per lipid mismatch of asymmetric lipid membranes.

Indexed as

Asymmetric lipid membranesBeta-AmyloidProtein aggregationProtein–lipid interactionsProtein structure on surfaces

Identifiers

PMID27054174
PMCPMC4802547
OpenAlexW2297140904

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.