ArticleScience (New York, N.Y.)2016
Design of structurally distinct proteins using strategies inspired by evolution.
Article in Science (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 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.
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Who cites it
70 citing papers in PubMed.
- Evaluating zero-shot prediction of monomeric protein design success by AlphaFold, ESMFold, and ProteinMPNN.Protein science : a publication of the Protein Society · 2026Article
- AI-driven antimicrobial peptide characterization unveils novel motifs for drug design.Scientific reports · 2025Article
- Use of High Pressure NMR Spectroscopy to Rapidly Identify Proteins with Internal Ligand-Binding Voids.bioRxiv : the preprint server for biology · 2025Article
- Computational design of highly signalling-active membrane receptors through solvent-mediated allosteric networks.Nature chemistry · 2025Article
- Reused Protein Segments Linked to Functional Dynamics.Molecular biology and evolution · 2024Article
- Addressing epistasis in the design of protein function.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Context-dependent design of induced-fit enzymes using deep learning generates well-expressed, thermally stable and active enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Review
- Design of complicated all-α protein structures.Nature structural & molecular biology · 2024Article
- De novo design of stable proteins that efficaciously inhibit oncogenic G proteins.Protein science : a publication of the Protein Society · 2023Article
- Protein salvage and repurposing in evolution: Phospholipase D toxins are stabilized by a remodeled scrap of a membrane association domain.Protein science : a publication of the Protein Society · 2023Article
- Article
- Inside-Out Design of Zinc-Binding Proteins with Non-Native Backbones.Biochemistry · 2023Article
- De novo protein fold design through sequence-independent fragment assembly simulations.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Review
- Deep learning of protein sequence design of protein-protein interactions.Bioinformatics (Oxford, England) · 2023Article
- Sampling of structure and sequence space of small protein folds.Nature communications · 2022Article
- A generic framework for hierarchical de novo protein design.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Assessing and enhancing foldability in designed proteins.Protein science : a publication of the Protein Society · 2022Article
- Design and Engineering of Miniproteins.ACS bio & med chem Au · 2022Review
10 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Natural recombination combines pieces of preexisting proteins to create new tertiary structures and functions. We describe a computational protocol, called SEWING, which is inspired by this process and builds new proteins from connected or disconnected pieces of existing structures. Helical proteins designed with SEWING contain structural features absent from other de novo designed proteins and, in some cases, remain folded at more than 100°C. High-resolution structures of the designed proteins CA01 and DA05R1 were solved by x-ray crystallography (2.2 angstrom resolution) and nuclear magnetic resonance, respectively, and there was excellent agreement with the design models. This method provides a new strategy to rapidly create large numbers of diverse and designable protein scaffolds.
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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.