ArticleNature2015
Rational design of α-helical tandem repeat proteins with closed architectures.
Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 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
65 citing papers in PubMed, 128 citations in OpenAlex.
- HURDLER: a cloning method to overcome length limits in designed repeat proteins.Nucleic acids research · 2026Article
- Tandem repeat variation within and between species reveals signatures of selection in humans and chimpanzees.bioRxiv : the preprint server for biology · 2026Article
- Inhibition of ice recrystallization with designed twistless helical repeat proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Modular protein frameworks via supramolecular synthons.Biophysical reviews · 2025Review
- GeomeTRe: accurate calculation of geometrical descriptors of tandem repeat proteins.Bioinformatics (Oxford, England) · 2025Article
- De novo design and evolution of an artificial metathase for cytoplasmic olefin metathesis.Nature catalysis · 2025Article
- De novo design of alpha-beta repeat proteins.bioRxiv : the preprint server for biology · 2024Article
- Diversifying de novo TIM barrels by hallucination.Protein science : a publication of the Protein Society · 2024Article
- Stepwise introduction of stabilizing mutations reveals nonlinear additive effects in de novo TIM barrels.Protein science : a publication of the Protein Society · 2024Article
- Design of complicated all-α protein structures.Nature structural & molecular biology · 2024Article
- Hallucination of closed repeat proteins containing central pockets.Nature structural & molecular biology · 2023Article
- De novo design of knotted tandem repeat proteins.Nature communications · 2023Article
- Design of Heme Enzymes with a Tunable Substrate Binding Pocket Adjacent to an Open Metal Coordination Site.Journal of the American Chemical Society · 2023Article
- Long-Time Dynamics of Selected Molecular-Motor Components Using a Physics-Based Coarse-Grained Approach.Biomolecules · 2023Article
- Leveraging deep learning to improve vaccine design.Trends in immunology · 2023Review
- Article
- Hallucinating symmetric protein assemblies.Science (New York, N.Y.) · 2022Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- De novo design of protein homodimers containing tunable symmetric protein pockets.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Structural Rule Distinguishing a Superfold: A Case Study of Ferredoxin Fold and the Reverse Ferredoxin Fold.Molecules (Basel, Switzerland) · 2022Article
5 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Tandem repeat proteins, which are formed by repetition of modular units of protein sequence and structure, play important biological roles as macromolecular binding and scaffolding domains, enzymes, and building blocks for the assembly of fibrous materials. The modular nature of repeat proteins enables the rapid construction and diversification of extended binding surfaces by duplication and recombination of simple building blocks. The overall architecture of tandem repeat protein structures--which is dictated by the internal geometry and local packing of the repeat building blocks--is highly diverse, ranging from extended, super-helical folds that bind peptide, DNA, and RNA partners, to closed and compact conformations with internal cavities suitable for small molecule binding and catalysis. Here we report the development and validation of computational methods for de novo design of tandem repeat protein architectures driven purely by geometric criteria defining the inter-repeat geometry, without reference to the sequences and structures of existing repeat protein families. We have applied these methods to design a series of closed α-solenoid repeat structures (α-toroids) in which the inter-repeat packing geometry is constrained so as to juxtapose the amino (N) and carboxy (C) termini; several of these designed structures have been validated by X-ray crystallography. Unlike previous approaches to tandem repeat protein engineering, our design procedure does not rely on template sequence or structural information taken from natural repeat proteins and hence can produce structures unlike those seen in nature. As an example, we have successfully designed and validated closed α-solenoid repeats with a left-handed helical architecture that--to our knowledge--is not yet present in the protein structure database.
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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.