ArticleACS combinatorial science2019
Biophysical Characterization Platform Informs Protein Scaffold Evolvability.
Article in ACS combinatorial science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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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.
- Artificial intelligence-driven framework for discovering synthetic binding protein-like scaffolds from the entire protein universe.Briefings in bioinformatics · 2025Article
- PROSCA: an online platform for humanized scaffold mining facilitating rational protein engineering.Nucleic acids research · 2024Article
- Determinants of Developability and Evolvability of Synthetic Miniproteins as Ligand Scaffolds.Journal of molecular biology · 2023Article
- Predicting and Interpreting Protein Developability Via Transfer of Convolutional Sequence Representation.ACS synthetic biology · 2023Article
- Design of an artificial phage-display library based on a new scaffold improved for average stability of the randomized proteins.Scientific reports · 2023Article
- Deep Antimicrobial Activity and Stability Analysis Inform Lysin Sequence-Function Mapping.ACS synthetic biology · 2023Article
- Probing ion channel functional architecture and domain recombination compatibility by massively parallel domain insertion profiling.Nature communications · 2021Article
- High-throughput developability assays enable library-scale identification of producible protein scaffold variants.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Chemical Diversification of Simple Synthetic Antibodies.ACS chemical biology · 2021Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Evolving specific molecular recognition function of proteins requires strategic navigation of a complex mutational landscape. Protein scaffolds aid evolution via a conserved platform on which a modular paratope can be evolved to alter binding specificity. Although numerous protein scaffolds have been discovered, the underlying properties that permit binding evolution remain unknown. We present an algorithm to predict a protein scaffold's ability to evolve novel binding function based upon computationally calculated biophysical parameters. The ability of 17 small proteins to evolve binding functionality across seven discovery campaigns was determined via magnetic activated cell sorting of 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.