The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Evolution and disorder
Open accessAbstract
The evolution of disordered proteins or regions of proteins differs from ordered proteins because of the differences in their sequence composition, intramolecular contacts and function. Recent assessments of disordered protein evolution at the sequence, structural and functional levels support this hypothesis. Disordered proteins have a different pattern of accepted point mutations, exhibit higher rates of insertions and deletions, and generally, but not always, evolve more rapidly than ordered proteins. Even with these high rates of sequence evolution, a few examples have shown that disordered proteins maintain their flexibility under physiological conditions, and it is hypothesized that they maintain specific structural ensembles.
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Cites
Intrinsic Disorder and Protein Function
Dunker, A. K., Brown, C. J., Lawson, J. D., Iakoucheva, L. M., & Obradović, Z. (2002) · Biochemistry · doi:10.1021/bi012159+ · Cited by 1,731
Self-citationCoupling of folding and binding for unstructured proteins
Dyson, H. J., & Wright, P. E. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00289-0 · Cited by 1,327
Intrinsic Disorder in Cell-signaling and Cancer-associated Proteins
Iakoucheva, L. M., Brown, C. J., Lawson, J. D., Obradović, Z., & Dunker, A. K. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00969-5 · Cited by 1,214
Self-citationStructure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain
Wells, M., Tidow, H., Rutherford, T. J., Markwick, P., Jensen, M. R., Mylonas, E., Svergun, D. I., Blackledge, M., & Fersht, A. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801353105 · Cited by 434
Cited by
Nott, T. J., Petsalaki, E., Farber, P., Jervis, D., Fussner, E., Plochowietz, A., Craggs, T. D., Bazett-Jones, D. P., Pawson, T., Forman-Kay, J. D., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.013 · Cited by 1,803
Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions
Oldfield, C. J., & Dunker, A. K. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072711-164947 · Cited by 1,057
Self-citationAlphaFold and Implications for Intrinsically Disordered Proteins
Ruff, K. M., & Pappu, R. V. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167208 · Cited by 635
Buljan, M., Chalancon, G., Eustermann, S., Wagner, G. P., Fuxreiter, M., Bateman, A., & Babu, M. M. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.039 · Cited by 396
“Given that tissue-specific protein segments are enriched in disordered regions, they are expected to evolve rapidly due to the absence of structural constraints (Bellay et al., 2011; Brown et al., 2011; Romero et al., 2006).”
The human gene damage index as a gene-level approach to prioritizing exome variants
Itan, Y., Shang, L., Boisson, B., Patin, E., Bolze, A., Moncada-Vélez, M., Scott, E., Ciancanelli, M. J., Lafaille, F. G., Markle, J. G., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1518646112 · Cited by 275
Metadata
- Authors
- Brown, C. J., Johnson, A. K., Dunker, A. K., & Daughdrill, G. W.
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2011-06
- Volume
- 21
- Issue
- 3
- Pages
- 441-446
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2038972833
- Cited by
- 298
- References
- 4
- FWCI
- 1.23
- Type
- journal article
- Language
- en
- Open access
- green
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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.