Evidence map›Paper›PMID 27374357›Full record

ArticleScientific reports2016

Monoclonal antibody with conformational specificity for a toxic conformer of amyloid β42 and its application toward the Alzheimer's disease diagnosis.

Kazuma Murakami, Maki Tokuda, Takashi Suzuki, Yumi Irie, Mizuho Hanaki, Naotaka Izuo, Yoko Monobe, Ken-Ichi Akagi, Ryotaro Ishii, Harutsugu Tatebe and 5 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

23 citing papers in PubMed, 58 citations in OpenAlex.

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  7. An ultra-sensitive immunoassay detects and quantifies soluble Aβ oligomers in human plasma.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2022
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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

15 authors at 6 institutions in 1 country.

Kazuma MurakamiDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto, Japan.
Maki TokudaDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto, Japan.
Takashi SuzukiDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto, Japan.
Yumi IrieDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto, Japan.
Mizuho HanakiDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto, Japan.
Naotaka IzuoDepartment of Advanced Aging Medicine, Chiba University Graduate School of Medicine, Chiba, Japan.
Yoko MonobeNational Institute of Biomedical Innovation, Health and Nutrition, Osaka, Japan.
Ken-Ichi AkagiNational Institute of Biomedical Innovation, Health and Nutrition, Osaka, Japan.
Ryotaro IshiiDepartment of Neurology, Kyoto Prefectural University of Medicine, Kyoto, Japan.
Harutsugu TatebeDepartment of Neurology, Kyoto Prefectural University of Medicine, Kyoto, Japan.
Takahiko TokudaDepartment of Neurology, Kyoto Prefectural University of Medicine, Kyoto, Japan.
Masahiro MaedaImmuno-Biological Laboratories Co, Ltd., Gunma, Japan.
Toshiaki KumeDepartment of Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan.
Takahiko ShimizuDepartment of Advanced Aging Medicine, Chiba University Graduate School of Medicine, Chiba, Japan.
Kazuhiro IrieDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto, Japan.
Kyoto University · JPKyoto Prefectural University of Medicine · JPChiba University · JPNational Institute of Biomedical Innovation, Health and Nutrition · JPKyoto Pharmaceutical University · JPMedical & Biological Laboratories (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloid β-protein (Aβ42) oligomerization is an early event in Alzheimer's disease (AD). Current diagnostic methods using sequence-specific antibodies against less toxic fibrillar and monomeric Aβ42 run the risk of overdiagnosis. Hence, conformation-specific antibodies against neurotoxic Aβ42 oligomers have garnered much attention for developing more accurate diagnostics. Antibody 24B3, highly specific for the toxic Aβ42 conformer that has a turn at Glu22 and Asp23, recognizes a putative Aβ42 dimer, which forms stable and neurotoxic oligomers more potently than the monomer. 24B3 significantly rescues Aβ42-induced neurotoxicity, whereas sequence-specific antibodies such as 4G8 and 82E1, which recognizes the N-terminus, do not. The ratio of toxic to total Aβ42 in the cerebrospinal fluid of AD patients is significantly higher than in control subjects as measured by sandwich ELISA using antibodies 24B3 and 82E1. Thus, 24B3 may be useful for AD diagnosis and therapy.

Indexed as

AgedAged, 80 and overAlzheimer DiseaseAmyloid beta-PeptidesAnimalsAntibodies, MonoclonalCase-Control StudiesCell Line, TumorCells, CulturedFemaleHumansMaleMolecular ConformationNeuronsPeptide FragmentsRats, WistarAmyloid beta-Peptidesamyloid beta-protein (1-42)Antibodies, MonoclonalPeptide Fragments

Identifiers

PMID27374357
PMCPMC4931470
OpenAlexW2472226915

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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.