ArticleJournal of molecular biology2023
Determinants of Developability and Evolvability of Synthetic Miniproteins as Ligand Scaffolds.
Article in Journal of molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed.
- From sequence to scaffold: Computational design of protein nanoparticle vaccines from AlphaFold2-predicted building blocks.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Artificial intelligence-driven framework for discovering synthetic binding protein-like scaffolds from the entire protein universe.Briefings in bioinformatics · 2025Article
- PANCS-Binders: a rapid, high-throughput binder discovery platform.Nature methods · 2025Article
- Microproteins in cancer: identification, biological functions, and clinical implications.Trends in genetics : TIG · 2025Review
- High-throughput protein binder discovery by rapid in vivo selection.bioRxiv : the preprint server for biology · 2025Article
- Sequence-developability mapping of affibody and fibronectin paratopes via library-scale variant characterization.Protein engineering, design & selection : PEDS · 2024Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Binding ligands empower molecular therapeutics and diagnostics. Despite an array of protein scaffolds engineered for binding, the biophysical elements that drive developability and evolvability are not fully understood. In particular, engineering novel function while maintaining biophysical integrity within the context of small, single-domain proteins is challenged by integration of the structural framework and the evolved binding site. Miniproteins present a challenge to our limits of protein engineering capability and provide advantages in physiological targeting, modularity for multi-functional constructs, and unique binding modes. Herein, we evaluate the ability of hyperstable synthetic miniproteins, originally designed for foldedness, to function as binding scaffolds. We synthesized 45 combinatorial libraries, with 10
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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.