Evidence map›Paper›PMID 19901993›Full record

ArticlePloS one2009

RNA aptamers generated against oligomeric Abeta40 recognize common amyloid aptatopes with low specificity but high sensitivity.

Farid Rahimi, Kazuma Murakami, Jamie L Summers, Chi-Hong B Chen, Gal Bitan

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

33 citing papers in PubMed, 65 citations in OpenAlex.

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  14. Aptamer Applications in Neuroscience.Pharmaceuticals (Basel, Switzerland) · 2021
    Review
  15. Article
  16. Article
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  18. Article
  19. Updates on Aptamer Research.International journal of molecular sciences · 2019
    Review
  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

5 authors at 1 institution in 1 country.

Farid RahimiDepartment of Neurology, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, California, USA.
Kazuma Murakami
Jamie L Summers
Chi-Hong B Chen
Gal Bitan
University of California, Los Angeles · US

Funding

Novel Specific Ligands for ABeta OligomersR21AG030709 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BITAN, GAL · 2007 to 2008
$357k
NIA NIH HHS AG030709NIA NIH HHS R21 AG030709
6 · The paper itself

Abstract

Aptamers are useful molecular recognition tools in research, diagnostics, and therapy. Despite promising results in other fields, aptamer use has remained scarce in amyloid research, including Alzheimer's disease (AD). AD is a progressive neurodegenerative disease believed to be caused by neurotoxic amyloid beta-protein (Abeta) oligomers. Abeta oligomers therefore are an attractive target for development of diagnostic and therapeutic reagents. We used covalently-stabilized oligomers of the 40-residue form of Abeta (Abeta40) for aptamer selection. Despite gradually increasing the stringency of selection conditions, the selected aptamers did not recognize Abeta40 oligomers but reacted with fibrils of Abeta40, Abeta42, and several other amyloidogenic proteins. Aptamer reactivity with amyloid fibrils showed some degree of protein-sequence dependency. Significant fibril binding also was found for the naïve library and could not be eliminated by counter-selection using Abeta40 fibrils, suggesting that aptamer binding to amyloid fibrils was RNA-sequence-independent. Aptamer binding depended on fibrillogenesis and showed a lag phase. Interestingly, aptamers detected fibril formation with > or =15-fold higher sensitivity than thioflavin T (ThT), revealing substantial beta-sheet and fibril formation undetected by ThT. The data suggest that under physiologic conditions, aptamers for oligomeric forms of amyloidogenic proteins cannot be selected due to high, non-specific affinity of oligonucleotides for amyloid fibrils. Nevertheless, the high sensitivity, whereby aptamers detect beta-sheet formation, suggests that they can serve as superior amyloid recognition tools.

Indexed as

Alzheimer DiseaseAmyloidAmyloid beta-PeptidesAptamers, NucleotideBenzothiazolesDensitometryDimerizationDNA, Single-StrandedHumansLigandsPeptide FragmentsProtein BindingProtein FoldingProtein Structure, SecondaryThiazolesAmyloidAmyloid beta-Peptidesamyloid beta-protein (1-40)Aptamers, NucleotideBenzothiazolesDNA, Single-StrandedLigandsPeptide FragmentsThiazolesthioflavin T

Identifiers

PMID19901993
PMCPMC2770325
OpenAlexW2103585077

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.