Evidence map›Paper›PMID 39940966›Full record

ReviewInternational journal of molecular sciences2025

Multimer Detection System: A Universal Assay System for Differentiating Protein Oligomers from Monomers.

Angelo Moscoso Jamerlan, Kyu Hwan Shim, Niti Sharma, Seong Soo A An

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
  2. Observational
  3. Article
  4. Article
  5. Review
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

4 authors.

Angelo Moscoso JamerlanDepartment of Bionano Technology, Gachon Medical Research Institute, Gachon University, Seongnam-si 13120, Republic of Korea.ORCID 0000-0002-5669-8386
Kyu Hwan ShimDepartment of Bionano Technology, Gachon Medical Research Institute, Gachon University, Seongnam-si 13120, Republic of Korea.ORCID 0000-0001-5402-337X
Niti SharmaDepartment of Bionano Technology, Gachon Medical Research Institute, Gachon University, Seongnam-si 13120, Republic of Korea.ORCID 0000-0001-6720-257X
Seong Soo A AnDepartment of Bionano Technology, Gachon Medical Research Institute, Gachon University, Seongnam-si 13120, Republic of Korea.ORCID 0000-0002-8123-6183

Funding

National Research Foundation of Korea 2021R1A6A1A03038996National Research Foundation of Korea RS-2023-00251396
6 · The paper itself

Abstract

Depositions of protein aggregates are typical pathological hallmarks of various neurodegenerative diseases (NDs). For example, amyloid-beta (Aβ) and tau aggregates are present in the brain and plasma of patients with Alzheimer's disease (AD); α-synuclein in Parkinson's disease (PD), dementia with Lewy bodies (DLB), and multiple system atrophy (MSA); mutant huntingtin protein (Htt) in Huntington's disease (HD); and DNA-binding protein 43 kD (TDP-43) in amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and limbic-predominant age-related TDP-43 encephalopathy (LATE). The same misfolded proteins can be present in multiple diseases in the form of mixed proteinopathies. Since there is no cure for all these diseases, understanding the mechanisms of protein aggregation becomes imperative in modern medicine, especially for developing diagnostics and therapeutics. A Multimer Detection System (MDS) was designed to distinguish and quantify the multimeric/oligomeric forms from the monomeric form of aggregated proteins. As the unique epitope of the monomer is already occupied by capturing or detecting antibodies, the aggregated proteins with multiple epitopes would be accessible to both capturing and detecting antibodies simultaneously, and signals will be generated from the oligomers rather than the monomers. Hence, MDS could present a simple solution for measuring various conformations of aggregated proteins with high sensitivity and specificity, which may help to explore diagnostic and treatment strategies for developing anti-aggregation therapeutics.

Indexed as

Neurodegenerative DiseasesProtein Aggregation, PathologicalProtein Multimerizationalpha-SynucleinAmyloid beta-PeptidesDNA-Binding ProteinsHumansProtein Aggregatestau Proteinsalpha-SynucleinAmyloid beta-PeptidesDNA-Binding ProteinsProtein Aggregatestau Proteinsmultimer detection systemneurodegenerative diseaseoligomerizationprotein aggregates

Identifiers

PMID39940966
PMCPMC11818661

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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.