ArticleJournal of the American Chemical Society2013
Structure and flexibility of nanoscale protein cages designed by symmetric self-assembly.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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Who cites it
28 citing papers in PubMed.
- Coupling of Spectrin Repeat Modules for the Assembly of Nanorods and Presentation of Protein Domains.ACS nano · 2024Article
- Advancing Tumor Therapy: Development and Utilization of Protein-Based Nanoparticles.Pharmaceutics · 2024Review
- Design, synthesis, and characterization of protein origami based on self-assembly of a brick and staple artificial protein pair.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Dissecting the general mechanisms of protein cage self-assembly by coarse-grained simulations.Protein science : a publication of the Protein Society · 2023Article
- Visualizing and accessing correlated SAXS data sets with Similarity Maps and Simple Scattering web resources.Methods in enzymology · 2023Article
- Crystals of TELSAM-target protein fusions that exhibit minimal crystal contacts and lack direct inter-TELSAM contacts.Open biology · 2022Article
- Protein Nanoparticles: Uniting the Power of Proteins with Engineering Design Approaches.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Review
- Protein Assembly by Design.Chemical reviews · 2021Review
- Artificial Protein Cage Delivers Active Protein Cargos to the Cell Interior.Biomacromolecules · 2021Article
- Generation of ordered protein assemblies using rigid three-body fusion.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Facile Fabrication of Protein-Macrocycle Frameworks.Journal of the American Chemical Society · 2021Article
- Design and structure of two new protein cages illustrate successes and ongoing challenges in protein engineering.Protein science : a publication of the Protein Society · 2020Article
- Review
- Protein cage assembly across multiple length scales.Chemical Society reviews · 2018Review
- Viral Capsid Assembly: A Quantified Uncertainty Approach.Journal of computational biology : a journal of computational molecular cell biology · 2018Article
- Engineering protein nanocages as carriers for biomedical applications.NPG Asia materials · 2017Review
- Uncertainty Quantified Computational Analysis of the Energetics of Virus Capsid Assembly.Proceedings. IEEE International Conference on Bioinformatics and Biomedicine · 2016Article
- Designing and defining dynamic protein cage nanoassemblies in solution.Science advances · 2016Article
- Fusion to a homo-oligomeric scaffold allows cryo-EM analysis of a small protein.Scientific reports · 2016Article
- Flexible, symmetry-directed approach to assembling protein cages.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Designing protein molecules that self-assemble into complex architectures is an outstanding goal in the area of nanobiotechnology. One design strategy for doing this involves genetically fusing together two natural proteins, each of which is known to form a simple oligomer on its own (e.g., a dimer or trimer). If two such components can be fused in a geometrically predefined configuration, that designed subunit can, in principle, assemble into highly symmetric architectures. Initial experiments showed that a 12-subunit tetrahedral cage, 16 nm in diameter, could be constructed following such a procedure [Padilla, J. E.; et al. Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 2217; Lai, Y. T.; et al. Science 2012, 336, 1129]. Here we characterize multiple crystal structures of protein cages constructed in this way, including cages assembled from two mutant forms of the same basic protein subunit. The flexibilities of the designed assemblies and their deviations from the target model are described, along with implications for further design developments.
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