ArticleScientific reports2024
A single-domain antibody library based on a stability-engineered human VH3 scaffold.
Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
7 citing papers in PubMed.
- A side-by-side biophysical comparison of five single-domain antibody scaffolds used for synthetic display libraries.The Journal of biological chemistry · 2026Article
- Novel recombinant VH43 antibody fragment potentiates the antibacterial activity of cephalosporins against Enterococcus faecium.Archives of microbiology · 2026Article
- Nanobodies in biomedicine: from molecular characteristics to fabrication and clinical translation.Military Medical Research · 2026Review
- De novo design of epitope-specific antibodies via a structure-driven computational workflow.Nature communications · 2025Article
- Insights into the recognition mechanism of shark-derived single-domain antibodies with high affinity and specificity targeting fluoroquinolones.Marine life science & technology · 2025Article
- Development of Anti-CEA CMolecular imaging and biology · 2025Article
- Addressing challenging impurities in fusion proteins: A comprehensive review and cost-effective strategy for HCP and low molecular weight species control.Biotechnology progressReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Using conventional immunoglobulin G (IgG) molecules as therapeutic agents presents several well-known disadvantages owing to their large size and structural complexity, negatively impacting development and production efficiency. Single-domain antibodies (sdAbs) are the smallest functional antibody format (~ 15 kDa) and represent a viable alternative to IgG in many applications. However, unlike natural single-domain antibodies, such as camelid V
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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.