The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Protein Design, a Minimalist Approach
Abstract
The question of how the amino acid sequence of a protein specifies its three-dimensional structure remains to be answered. Proteins are so large and complex that it is difficult to discern the features in their sequences that contribute to their structural stability and function. One approach to this problem is de novo design of model proteins, much simpler than their natural counterparts, yet containing sufficient information in their sequences to specify a given function (for example, folding in aqueous solution, folding in membranes, or formation of ion channels). Designed proteins provide simple model systems for understanding protein structure and function.
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Cites
The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding Proteins
Landschulz, W. H., Johnson, P. F., & McKnight, S. L. (1988) · Science · doi:10.1126/science.3289117 · Cited by 3,443
The packing of α-helices: simple coiled-coils
Crick, F. H. C. (1953) · Acta Crystallographica · doi:10.1107/s0365110x53001964 · Cited by 1,578
Cited by
Protein Design: Toward Functional Metalloenzymes
Yu, F., Cangelosi, V. M., Zastrow, M. L., Tegoni, M., Plegaria, J. S., Tebo, A. G., Mocny, C. S., Ruckthong, L., Qayyum, H., & Pecoraro, V. L. (2014) · Chemical Reviews · doi:10.1021/cr400458x · Cited by 441
Protein Design: From the Aspect of Water Solubility and Stability
Qing, R., Hao, S., Smorodina, E., Jin, D., Zalevsky, A., & Zhang, S. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00757 · Cited by 312
De novo design of the hydrophobic cores of proteins
Desjarlais, J. R., & Handel, T. M. (1995) · Protein Science · doi:10.1002/pro.5560041006 · Cited by 306
Controlling Allosteric Networks in Proteins
Dokholyan, N. V. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00544 · Cited by 260
Simmerman, H. K. B., Kobayashi, Y. M., Autry, J. M., & Jones, L. R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.10.5941 · Cited by 256
Metadata
- Authors
- DeGrado, W. F., Wasserman, Z. R., & Lear, J. D.
- Venue
- Science
- Published
- 1989-02-03
- Volume
- 243
- Issue
- 4891
- Pages
- 622-628
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1987630197
- Cited by
- 474
- References
- 2
- FWCI
- 9.92
- Type
- journal article
- Language
- en
- Open access
- closed
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- DeGrado, W. F., Wasserman, Z. R., & Lear, J. D. (1989). Protein Design, a Minimalist Approach. Science. https://doi.org/10.1126/science.2464850
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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.
