Evidence map›Paper›PMID 32127399›Full record

ArticleThe Journal of biological chemistry2020

An RNA aptamer with potent affinity for a toxic dimer of amyloid β42 has potential utility for histochemical studies of Alzheimer's disease.

Kazuma Murakami, Yayoi Obata, Asa Sekikawa, Haruka Ueda, Naotaka Izuo, Tatsuya Awano, Keiji Takabe, Takahiko Shimizu, Kazuhiro Irie

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

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  8. Emerging Perspectives on Prime Editor Delivery to the Brain.Pharmaceuticals (Basel, Switzerland) · 2024
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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

9 authors at 2 institutions in 1 country.

Kazuma MurakamiDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan murakami.kazuma.4v@kyoto-u.ac.jp.ORCID 0000-0003-3152-1784
Yayoi ObataDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan.
Asa SekikawaDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan.
Haruka UedaDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan.
Naotaka IzuoDepartment of Endocrinology, Hematology and Gerontology, Graduate School of Medicine, Chiba University, Chiba, 260-8670, Japan.
Tatsuya AwanoDivision of Forest and Biomaterials Sciences, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan.
Keiji TakabeDivision of Forest and Biomaterials Sciences, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan.
Takahiko ShimizuDepartment of Endocrinology, Hematology and Gerontology, Graduate School of Medicine, Chiba University, Chiba, 260-8670, Japan.
Kazuhiro IrieDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan irie.kazuhiro.2z@kyoto-u.ac.jp.ORCID 0000-0001-7109-8568
Kyoto University · JPChiba University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oligomers of β-amyloid 42 (Aβ42), rather than fibrils, drive the pathogenesis of Alzheimer's disease (AD). In particular, toxic oligomeric species called protofibrils (PFs) have attracted significant attention. Herein, we report RNA aptamers with higher affinity toward PFs derived from a toxic Aβ42 dimer than toward fibrils produced from WT Aβ42 or from a toxic, conformationally constrained Aβ42 variant, E22P-Aβ42. We obtained these RNA aptamers by using the preincubated dimer model of E22P-Aβ42, which dimerized via a linker located at Val-40, as the target of

Indexed as

Disease Models, AnimalAlzheimer DiseaseAmyloid beta-PeptidesAnimalsAptamers, NucleotideHumansImmunohistochemistryMicePeptide FragmentsPlaque, AmyloidAmyloid beta-Peptidesamyloid beta-protein (1-42)Aptamers, NucleotidePeptide FragmentsaggregationAlzheimer diseaseamyloid-beta (AB)aptamercircular dichroism (CD)G-quadrupleximmunohistochemistryoligomerRNAtransgenic mice

Identifiers

PMID32127399
PMCPMC7152766
OpenAlexW3009638976

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.