The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Coiled Coil Domains: Stability, Specificity, and Biological Implications
Abstract
Twist and shout: Coiled-coil forming α-helices are of great significance in understanding tertiary structural formation (the figure shows GCN4; an example of a parallel dimeric coiled coil), the design of new proteins, and the control of the oligomeric state. The apparent simplicity of coiled coils is misleading, and rules governing such features are far from fully established. Requirements for the specific pairings of helices during coiled-coil formation are discussed, as are the peculiarities within such domains that give proteins their unique function. By taking advantage of our increasing understanding of this structural class, a growing number of biological and therapeutic applications are being sought.
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Citations
Cites
Predicting coiled coils from protein sequences.
Lupas, A., Van Dyke, M., & Stock, J. (1991) · Science · doi:10.1126/science.252.5009.1162 · Cited by 3,953
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
A Switch Between Two-, Three-, and Four-stranded Coiled Coils in GCN4 Leucine Zipper Mutants
Harbury, P. B., Zhang, T., Kim, P. S., & Alber, T. (1993) · Science · doi:10.1126/science.8248779 · Cited by 1,490
Peppas, N. A. (1997) · Current Opinion in Colloid & Interface Science · doi:10.1016/s1359-0294(97)80103-3 · Cited by 454
Walshaw, J., & Woolfson, D. N. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4545 · Cited by 357
Controlled formation of model homo- and heterodimer coiled coil polypeptides
Graddis, T. J., Myszka, D. G., & Chaiken, I. M. (1993) · Biochemistry · doi:10.1021/bi00210a015 · Cited by 153
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Oligomerization properties of GCN4 leucine zipper e and g position mutants
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Cited by
Smart polymeric gels: Redefining the limits of biomedical devices
Chaterji, S., Kwon, I. K., & Park, K. (2007) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2007.05.018 · Cited by 615
Hydrogels as smart biomaterials
Kopeček, J., & Yang, J. (2007) · Polymer International · doi:10.1002/pi.2253 · Cited by 425
Multicomponent peptide assemblies
Raymond, D. M., & Nilsson, B. L. (2018) · Chemical Society Reviews · doi:10.1039/c8cs00115d · Cited by 346
Structure and interactions of biological helices
Kornyshev, A. A., Lee, D. J., Leikin, S., & Wynveen, A. (2007) · Reviews of Modern Physics · doi:10.1103/revmodphys.79.943 · Cited by 320
Uversky, V. N. (2011) · Chem. Soc. Rev. · doi:10.1039/c0cs00057d · Cited by 259
Metadata
- Authors
- Mason, J. M., & Arndt, K. M.
- Venue
- ChemBioChem
- Publisher
- Wiley
- Published
- 2004-01-29
- Volume
- 5
- Issue
- 2
- Pages
- 170-176
- ISSN
- 1439-4227 (ISSN-L)
- 1439-7633
- OpenAlex
- W2172219847
- Cited by
- 700
- References
- 9
- FWCI
- 7.87
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
