The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Nanohedra: Using symmetry to design self assembling protein cages, layers, crystals, and filaments
Open accessAbstract
A general strategy is described for designing proteins that self assemble into large symmetrical nanomaterials, including molecular cages, filaments, layers, and porous materials. In this strategy, one molecule of protein A, which naturally forms a self-assembling oligomer, A n , is fused rigidly to one molecule of protein B, which forms another self-assembling oligomer, B m . The result is a fusion protein, A-B, which self assembles with other identical copies of itself into a designed nanohedral particle or material, (A-B) p . The strategy is demonstrated through the design, production, and characterization of two fusion proteins: a 49-kDa protein designed to assemble into a cage approximately 15 nm across, and a 44-kDa protein designed to assemble into long filaments approximately 4 nm wide. The strategy opens a way to create a wide variety of potentially useful protein-based materials, some of which share similar features with natural biological assemblies.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Helical microtubules of graphitic carbon
Iijima, S. (1991) · Nature · doi:10.1038/354056a0 · Cited by 43,098
Kroto, H. W., Heath, J. R., O’Brien, S. C., Curl, R. F., & Smalley, R. E. (1985) · Nature · doi:10.1038/318162a0 · Cited by 16,083
A Chemically Functionalizable Nanoporous Material [Cu 3 (TMA) 2 (H 2 O) 3 ] n
Chui, S. S.-Y., Lo, S. M.-F., Charmant, J. P. H., Orpen, A. G., & Williams, I. D. (1999) · Science · doi:10.1126/science.283.5405.1148 · Cited by 6,063
Molecular Self-Assembly and Nanochemistry: a Chemical Strategy for the Synthesis of Nanostructures
Whitesides, G. M., Mathias, J. P., & Seto, C. T. (1991) · Science · doi:10.1126/science.1962191 · Cited by 3,632
Design and self-assembly of two-dimensional DNA crystals
Winfree, E., Liu, F., Wenzler, L. A., & Seeman, N. C. (1998) · Nature · doi:10.1038/28998 · Cited by 2,857
Physical Principles in the Construction of Regular Viruses
Caspar, D. L. D., & Klug, A. (1962) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1962.027.001.005 · Cited by 2,522
Self-assembling organic nanotubes based on a cyclic peptide architecture
Ghadiri, M. R., Granja, J. R., Milligan, R. A., McRee, D. E., & Khazanovich, N. (1993) · Nature · doi:10.1038/366324a0 · Cited by 1,746
Host–guest encapsulation of materials by assembled virus protein cages
Douglas, T., & Young, M. (1998) · Nature · doi:10.1038/30211 · Cited by 906
Alternative conformations of amyloidogenic proteins govern their behavior
Kelly, J. W. (1996) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(96)80089-3 · Cited by 593
Construction of a DNA-Truncated Octahedron
Zhang, Y., & Seeman, N. C. (1994) · Journal of the American Chemical Society · doi:10.1021/ja00084a006 · Cited by 585
Cited by
Self-assembling protein nanoparticles in the design of vaccines
López-Sagaseta, J., Malito, E., Rappuoli, R., & Bottomley, M. J. (2016) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2015.11.001 · Cited by 353
Chemically Controlled Protein Assembly: Techniques and Applications
Fegan, A., White, B., Carlson, J. C. T., & Wagner, C. R. (2010) · Chemical Reviews · doi:10.1021/cr8002888 · Cited by 294
Structure of a 16-nm Cage Designed by Using Protein Oligomers
Lai, Y.-T., Cascio, D., & Yeates, T. O. (2012) · Science · doi:10.1126/science.1219351 · Cited by 278
Self-citationSelf-Assembly of Proteins into Designed Networks
Ringler, P., & Schulz, G. E. (2003) · Science · doi:10.1126/science.1088074 · Cited by 277
Proteins evolve on the edge of supramolecular self-assembly
Garcia-Seisdedos, H., Empereur-Mot, C., Elad, N., & Levy, E. D. (2017) · Nature · doi:10.1038/nature23320 · Cited by 253
Metadata
- Authors
- Padilla, J. E., Colovos, C., & Yeates, T. O.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2001-02-20
- Volume
- 98
- Issue
- 5
- Pages
- 2217-2221
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2113495611
- Cited by
- 441
- References
- 23
- FWCI
- 5.98
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Nanohedra: Using symmetry to design self assembling protein cages, layers, crystals, and filaments. https://app.cochat.ai/papers/10.1073/pnas.041614998
- The paper
- Padilla, J. E., Colovos, C., & Yeates, T. O. (2001). Nanohedra: Using symmetry to design self assembling protein cages, layers, crystals, and filaments. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.041614998
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.