Evidence map›Paper›PMID 22558151›Full record

ArticlePloS one2012

The influence of spin-labeled fluorene compounds on the assembly and toxicity of the aβ peptide.

Jitka Petrlova, Tamás Kálai, Izumi Maezawa, Robin Altman, Ghimire Harishchandra, Hyun-Seok Hong, Daniel A Bricarello, Atul N Parikh, Gary A Lorigan, Lee-Way Jin and 2 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 19 citations in OpenAlex.

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  7. Oligomerization Alters Binding Affinity Between Amyloid Beta and a Modulator of Peptide Aggregation.The journal of physical chemistry. C, Nanomaterials and interfaces · 2017
    Article
  8. A Metal-Free Method for Producing MRI Contrast at Amyloid-β.Journal of Alzheimer's disease : JAD · 2017
    Article
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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

12 authors at 3 institutions in 2 countries.

Jitka PetrlovaDepartment of Biochemistry and Molecular Medicine, University of California Davis, Davis, California, United States of America.
Tamás Kálai
Izumi Maezawa
Robin Altman
Ghimire Harishchandra
Hyun-Seok Hong
Daniel A Bricarello
Atul N Parikh
Gary A Lorigan
Lee-Way Jin
Kálmán Hideg
John C Voss
Miami University · USUniversity of California, Davis · USUniversity of Pecs · HU

Funding

The structural basis of apoE4's role in Alzheimer's DiseaseR01AG029246 · NIA · UNIVERSITY OF CALIFORNIA AT DAVIS · PI VOSS, JOHN CARL · 2007 to 2011
$1.3M
NIA NIH HHS R01 AG029246
6 · The paper itself

Abstract

backgroundThe deposition and oligomerization of amyloid β (Aβ) peptide plays a key role in the pathogenesis of Alzheimer's disease (AD). Aβ peptide arises from cleavage of the membrane-associated domain of the amyloid precursor protein (APP) by β and γ secretases. Several lines of evidence point to the soluble Aβ oligomer (AβO) as the primary neurotoxic species in the etiology of AD. Recently, we have demonstrated that a class of fluorene molecules specifically disrupts the AβO species. METHODOLOGY/PRINCIPAL

findingsTo achieve a better understanding of the mechanism of action of this disruptive ability, we extend the application of electron paramagnetic resonance (EPR) spectroscopy of site-directed spin labels in the Aβ peptide to investigate the binding and influence of fluorene compounds on AβO structure and dynamics. In addition, we have synthesized a spin-labeled fluorene (SLF) containing a pyrroline nitroxide group that provides both increased cell protection against AβO toxicity and a route to directly observe the binding of the fluorene to the AβO assembly. We also evaluate the ability of fluorenes to target multiple pathological processes involved in the neurodegenerative cascade, such as their ability to block AβO toxicity, scavenge free radicals and diminish the formation of intracellular AβO species.

conclusionsFluorene modified with pyrroline nitroxide may be especially useful in counteracting Aβ peptide toxicity, because they possess both antioxidant properties and the ability to disrupt AβO species.

Indexed as

Models, BiologicalSpin LabelsAlzheimer DiseaseAmyloid beta-PeptidesBlotting, WesternCell Line, TumorCircular DichroismElectron Spin Resonance SpectroscopyFluorenesFluorescent Antibody TechniqueFree Radical ScavengersHumansMicroscopy, Atomic ForceMolecular StructureNitrogen OxidesTetrazolium SaltsAmyloid beta-PeptidesfluoreneFluorenesFree Radical ScavengersNitrogen OxidesSpin LabelsTetrazolium SaltsThiazolesthiazolyl blue

Identifiers

PMID22558151
PMCPMC3340382
OpenAlexW2033911169

What OpenQuestion holds

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LicenceCC BY
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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.