ArticleNature communications2021
Self-assembly and regulation of protein cages from pre-organised coiled-coil modules.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 23 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.
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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
23 citing papers in PubMed.
- Peptide cages: bioinspired supramolecular architectures for next-generation applications.Chemical science · 2026Review
- InsiliCoil: An Integrated Software Suite for Coiled Coil Design, Prediction, and Therapeutic Engineering.ACS synthetic biology · 2026Article
- Self-assembling protein cages: from coiled-coil module to machine learning-drivenMaterials advances · 2026Review
- Sequence Prediction, Structural Modelling and the Challenges of Plasticity in Coiled Coils.Sub-cellular biochemistry · 2026Review
- Programmable Protein-DNA Composite Nanostructures: from Nanostructure Construction to Protein-Induced Micro-Scale Material Self-Assembly and Functionalization.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Beyond Dimerization: Harnessing Tetrameric Coiled-Coils for Nanostructure Assembly.Angewandte Chemie (International ed. in English) · 2025Article
- Coiled Coil Peptide Tiles (CCPTs): Expanding the Peptide Building Block Design with Multivalent Peptide Macrocycles.Journal of the American Chemical Society · 2024Article
- Coupling of Spectrin Repeat Modules for the Assembly of Nanorods and Presentation of Protein Domains.ACS nano · 2024Article
- The art of designed coiled-coils for the regulation of mammalian cells.Cell chemical biology · 2024Review
- Subunits of an E3 Ligase Complex as Degrons for Efficient Degradation of Cytosolic, Nuclear, and Membrane Proteins.ACS synthetic biology · 2024Article
- Preorganized cyclic modules facilitate the self-assembly of protein nanostructures.Chemical science · 2024Article
- Article
- Crystal Structure ofJournal of the American Chemical Society · 2023Article
- Segmentation strategy of de novo designed four-helical bundles expands protein oligomerization modalities for cell regulation.Nature communications · 2023Article
- An abiotic, tetrameric, eight-helix bundle.Chemical science · 2023Article
- Measuring the Radius of Gyration and Intrinsic Flexibility of Viral Proteins in Buffer Solution Using Small-Angle X-ray Scattering.ACS measurement science au · 2022Article
- Intrinsically disordered ectodomain modulates ion permeation through a metal transporter.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Metal ion-regulated assembly of designed modular protein cages.Science advances · 2022Article
- De novo design and directed folding of disulfide-bridged peptide heterodimers.Nature communications · 2022Article
- Computational Design of Single-Peptide Nanocages with Nanoparticle Templating.Molecules (Basel, Switzerland) · 2022Article
Corrections and comments
- Erratum issued
Authors and funding
9 authors.
Funding
Abstract
Coiled-coil protein origami (CCPO) is a modular strategy for the de novo design of polypeptide nanostructures. CCPO folds are defined by the sequential order of concatenated orthogonal coiled-coil (CC) dimer-forming peptides, where a single-chain protein is programmed to fold into a polyhedral cage. Self-assembly of CC-based nanostructures from several chains, similarly as in DNA nanotechnology, could facilitate the design of more complex assemblies and the introduction of functionalities. Here, we show the design of a de novo triangular bipyramid fold comprising 18 CC-forming segments and define the strategy for the two-chain self-assembly of the bipyramidal cage from asymmetric and pseudo-symmetric pre-organised structural modules. In addition, by introducing a protease cleavage site and masking the interfacial CC-forming segments in the two-chain bipyramidal cage, we devise a proteolysis-mediated conformational switch. This strategy could be extended to other modular protein folds, facilitating the construction of dynamic multi-chain CC-based complexes.
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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.