The DOI matches its Crossref record; 563 of the 563 references it cites were found in a registry or an index.
Protein Assembly by Design
Open accessAbstract
Proteins are nature's primary building blocks for the construction of sophisticated molecular machines and dynamic materials, ranging from protein complexes such as photosystem II and nitrogenase that drive biogeochemical cycles to cytoskeletal assemblies and muscle fibers for motion. Such natural systems have inspired extensive efforts in the rational design of artificial protein assemblies in the last two decades. As molecular building blocks, proteins are highly complex, in terms of both their three-dimensional structures and chemical compositions. To enable control over the self-assembly of such complex molecules, scientists have devised many creative strategies by combining tools and principles of experimental and computational biophysics, supramolecular chemistry, inorganic chemistry, materials science, and polymer chemistry, among others. Owing to these innovative strategies, what started as a purely structure-building exercise two decades ago has, in short order, led to artificial protein assemblies with unprecedented structures and functions and protein-based materials with unusual properties. Our goal in this review is to give an overview of this exciting and highly interdisciplinary area of research, first outlining the design strategies and tools that have been devised for controlling protein self-assembly, then describing the diverse structures of artificial protein assemblies, and finally highlighting the emergent properties and functions of these 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
A Programmable Dual-RNA–Guided DNA Endonuclease in Adaptive Bacterial Immunity
Jinek, M., Chylinski, K., Fonfara, I., Hauer, M., Doudna, J. A., & Charpentier, E. (2012) · Science · doi:10.1126/science.1225829 · Cited by 17,116
CHARMM: A program for macromolecular energy, minimization, and dynamics calculations
Brooks, B. R., Bruccoleri, R. E., Olafson, B. D., States, D. J., Swaminathan, S., & Karplus, M. (1983) · Journal of Computational Chemistry · doi:10.1002/jcc.540040211 · Cited by 14,944
Comparative Protein Modelling by Satisfaction of Spatial Restraints
Šali, A., & Blundell, T. L. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1626 · Cited by 12,977
Pearson, R. G. (1963) · Journal of the American Chemical Society · doi:10.1021/ja00905a001 · Cited by 10,475
Reticular synthesis and the design of new materials
Yaghi, O. M., O'Keeffe, M., Ockwig, N. W., Chae, H. K., Eddaoudi, M., & Kim, J. (2003) · Nature · doi:10.1038/nature01650 · Cited by 9,101
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
A DNA-based method for rationally assembling nanoparticles into macroscopic materials
Mirkin, C. A., Letsinger, R. L., Mucic, R. C., & Storhoff, J. J. (1996) · Nature · doi:10.1038/382607a0 · Cited by 6,683
DREIDING: a generic force field for molecular simulations
Mayo, S. L., Olafson, B. D., & Goddard, W. A. (1990) · The Journal of Physical Chemistry · doi:10.1021/j100389a010 · Cited by 6,585
Jones, D. T. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3091 · Cited by 5,449
Insulin signalling and the regulation of glucose and lipid metabolism
Saltiel, A. R., & Kahn, C. R. (2001) · Nature · doi:10.1038/414799a · Cited by 5,326
Cited by
East, N. J., Clifton, B. E., Jackson, C. J., & Kaczmarski, J. A. (2022) · Protein Science · doi:10.1002/pro.4510 · Cited by 13
Protein design of two-component tubular assemblies similar to cytoskeletons
Noji, M., Sugita, Y., Yamazaki, Y., Miyazaki, M., & Suzuki, Y. (2025) · Nature Communications · doi:10.1038/s41467-025-62076-3 · Cited by 3
Metadata
- Authors
- Zhu, J., Avakyan, N., Kakkis, A., Hoffnagle, A. M., Han, K., Li, Y., Zhang, Z., Choi, T. S., Na, Y., Yu, C.-J., & Tezcan, F. A.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2021-08-18
- Volume
- 121
- Issue
- 22
- Pages
- 13701-13796
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W3196231042
- Cited by
- 285
- References
- 563
- FWCI
- 3.03
- 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: Protein Assembly by Design. https://app.cochat.ai/papers/10.1021/acs.chemrev.1c00308
- The paper
- Zhu, J., Avakyan, N., Kakkis, A., Hoffnagle, A. M., Han, K., Li, Y., Zhang, Z., Choi, T. S., Na, Y., Yu, C.-J., & Tezcan, F. A. (2021). Protein Assembly by Design. Chemical Reviews. https://doi.org/10.1021/acs.chemrev.1c00308
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.