ArticleQRB discovery2023
On the micelle formation of DNAJB6b.
Article in QRB discovery, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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
10 citing papers in PubMed, 9 citations in OpenAlex.
- Human chaperone DNAJB6b suppresses tau fibril formation through co-aggregation.Communications chemistry · 2026Article
- DNAJB6: A guardian against neurodegeneration.Neural regeneration research · 2026Article
- The chaperone DNAJB6b halts amyloid formation through association with transient Aβ oligomers.Physical chemistry chemical physics : PCCP · 2026Article
- Determining the Hydrodynamic Size of Lipid Nanoparticles by Fluorescent Universal Lipid Labeling for Microfluidic Diffusional Sizing (FULL-MDS).Methods in molecular biology (Clifton, N.J.) · 2026Article
- Effects of solution conditions on the self-assembly of the chaperone protein DNAJB6b.Communications chemistry · 2025Article
- On the self-assembly of αB-crystallin.Soft matter · 2025Article
- Air-Water Interfacial Adsorption of the Chaperone Protein DNAJB6b.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- The Role of α-Synuclein-DNAJB6b Coaggregation in Amyloid Suppression.ACS chemical neuroscience · 2025Article
- The low complexity linker of DNAJB6b is key to its anti-amyloid function.QRB discovery · 2025Article
- The Ability of DNAJB6b to Suppress Amyloid Formation Depends on the Chaperone Aggregation State.ACS chemical neuroscience · 2024Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human chaperone DNAJB6b increases the solubility of proteins involved in protein aggregation diseases and suppresses the nucleation of amyloid structures. Due to such favourable properties, DNAJB6b has gained increasing attention over the past decade. The understanding of how DNAJB6b operates on a molecular level may aid the design of inhibitors against amyloid formation. In this work, fundamental aspects of DNAJB6b self-assembly have been examined, providing a basis for future experimental designs and conclusions. The results imply the formation of large chaperone clusters in a concentration-dependent manner. Microfluidic diffusional sizing (MDS) was used to evaluate how DNAJB6b average hydrodynamic radius varies with concentration. We found that, in 20 mM sodium phosphate buffer, 0.2 mM EDTA, at pH 8.0 and room temperature, DNAJB6b displays a micellar behaviour, with a critical micelle concentration (CMC) of around 120 nM. The average hydrodynamic radius appears to be concentration independent between ∼10 μM and 100 μM, with a mean radius of about 12 nm. The CMC found by MDS is supported by native agarose gel electrophoresis and the size distribution appears bimodal in the DNAJB6b concentration range ∼100 nM to 4 μM.
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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 Socratic graph.