ArticleJournal of the American Chemical Society2025
Rational Design of a Foldon-Derived Heterotrimer Guided by Quantitative Native Mass Spectrometry.
Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- Mass spectrometry integrates protein design into structural biology method development.QRB discovery · 2026Review
- The mass spectrometric intact transition epitope mapping method supports protein engineering of foldon trimer variants.Scientific reports · 2025Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Designing stable hetero-oligomeric protein complexes with defined intersubunit stoichiometry remains a significant challenge. In this study, we report the design of a highly selective heterotrimeric assembly derived from the well-known foldon homotrimer. We generated an
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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.