ArticleChemistryOpen2019
Solution-Based Determination of Dissociation Constants for the Binding of Aβ42 to Antibodies.
Article in ChemistryOpen, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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.
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.
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Who cites it
8 citing papers in PubMed, 8 citations in OpenAlex.
- Pharmaceutical Stability of Romiplostim: In-use Functional Study Using Microscale Thermophoresis New Strategy and Elisa.Pharmaceutical research · 2026Article
- Article
- Antibody Aggregation: A Problem Within the Biopharmaceutical Industry and Its Role in AL Amyloidosis Disease.The protein journal · 2025Review
- Viral S protein histochemistry reveals few potential SARS-CoV-2 entry sites in human ocular tissues.Scientific reports · 2021Article
- A Probeless Capacitive Biosensor for Direct Detection of Amyloid Beta 1-42 in Human Serum Based on an Interdigitated Chain-Shaped Electrode.Micromachines · 2020Article
- Halogenation of theChemistryOpen · 2020Article
- Solution-Based Determination of Dissociation Constants for the Binding of Aβ42 to Antibodies.ChemistryOpen · 2019Article
- Quantitative systems pharmacology-based exploration of relevant anti-amyloid therapy challenges in clinical practice.Alzheimer's & dementia (New York, N. Y.)Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid β-peptides (Aβ) play a major role in the pathogenesis of Alzheimer's disease. Therefore, numerous monoclonal antibodies against Aβ have been developed for basic and clinical research. The present study applied fluorescence based analytical ultracentrifugation and microscale thermophoresis to characterize the interaction between Aβ42 monomers and three popular, commercially available antibodies, namely 6E10, 4G8 and 12F4. Both methods allowed us to analyze the interactions at low nanomolar concentrations of analytes close to their dissociation constants (
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Registered trials
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.