Evidence map›Paper›PMID 19026087›Full record

ArticleThe Journal of chemical physics2008

The Alzheimer beta-amyloid (Abeta(1-39)) dimer in an implicit solvent.

Priya Anand, Fateh S Nandel, Ulrich H E Hansmann

Abstract read
In one paragraph

Article in The Journal of chemical physics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
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

22 citing papers in PubMed.

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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

3 authors.

Priya AnandDepartment of Biophysics, Panjab University, Chandigarh-160014, India. p.anand@daad-alumni.de
Fateh S Nandel
Ulrich H E Hansmann

Funding

Folding, Mis-Folding and Aggregation of Small ProteinsR01GM062838 · NIGMS · UNIVERSITY OF OKLAHOMA · PI HANSMANN, ULRICH H.E. · 2003 to 2012
$1.4M
NIGMS NIH HHS R01 GM062838
6 · The paper itself

Abstract

Oligomers of Abeta peptides are suspected as the underlying cause of Alzheimer disease. Knowledge of their structural properties could therefore lead to a deeper understanding of the mechanism behind the outbreak of this disease. As a step in this direction we have studied Abeta dimers by all-atom molecular dynamics simulations. Equilibrated structures at 300 K were clustered into different families with similar structural features. The dominant cluster has parallel N-terminals and a well defined segment Leu17-Ala21 that are stabilized by salt bridges between Lys28 of one chain and either Glu22 or Asp23 of the other chain. The formation of these salt bridges may be the limiting step in oligomerization and fibrillogenesis.

Indexed as

Protein MultimerizationAmino Acid SequenceAmyloid beta-PeptidesModels, MolecularMolecular Sequence DataProtein Structure, QuaternarySolventsTemperatureAmyloid beta-PeptidesSolvents

Identifiers

PMID19026087
PMCPMC5942451

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.