The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Linking folding and binding
Open accessAbstract
Many cellular proteins are intrinsically disordered and undergo folding, in whole or in part, upon binding to their physiological targets. The past few years have seen an exponential increase in papers describing characterization of intrinsically disordered proteins, both free and bound to targets. Although NMR spectroscopy remains the favored tool, a number of new biophysical techniques are proving exceptionally useful in defining the limits of the conformational ensembles. Advances have been made in prediction of the recognition elements in disordered proteins, in elucidating the kinetics and mechanism of the coupled folding and binding process, and in understanding the role of post-translational modifications in tuning the biological response. Here we review these and other recent advances that are providing new insights into the conformational propensities and interactions of intrinsically disordered proteins and are beginning to reveal general principles underlying their biological functions.
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Cites
Intrinsically unstructured proteins and their functions
Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871
Self-citationRadhakrishnan, I., Pérez-Alvarado, G. C., Parker, D., Dyson, H. J., Montminy, M. R., & Wright, P. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80463-8 · Cited by 728
Self-citationIntrinsic disorder as a mechanism to optimize allosteric coupling in proteins
Hilser, V. J., & Thompson, E. B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700329104 · Cited by 406
Variable Control of Ets-1 DNA Binding by Multiple Phosphates in an Unstructured Region
Pufall, M. A., Lee, G. M., Nelson, M. L., Kang, H.-S., Velyvis, A., Kay, L. E., McIntosh, L. P., & Graves, B. J. (2005) · Science · doi:10.1126/science.1111915 · Cited by 246
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Cited by
AlphaFold 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
Extreme disorder in an ultrahigh-affinity protein complex
Borgia, A., Borgia, M. B., Bugge, K., Kissling, V. M., Heidarsson, P. O., Fernandes, C. B., Sottini, A., Soranno, A., Buholzer, K. J., Nettels, D., et al. (2018) · Nature · doi:10.1038/nature25762 · Cited by 653
Conformational selection or induced fit: A flux description of reaction mechanism
Hammes, G. G., Chang, Y.-C., & Oas, T. G. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907195106 · Cited by 577
Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2
Alderson, T. R., Pritišanac, I., Kolarić, Đ., Moses, A. M., & Forman-Kay, J. D. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2304302120 · Cited by 240
Fuzzy Complexes: A More Stochastic View of Protein Function
Fuxreiter, M., & Tompa, P. (2012) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4614-0659-4_1 · Cited by 240
Metadata
- Authors
- Wright, P. E., & Dyson, H. J.
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2009-02
- Volume
- 19
- Issue
- 1
- Pages
- 31-38
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2044730187
- Cited by
- 1,019
- References
- 5
- FWCI
- 4.80
- Type
- journal article
- Language
- en
- Open access
- green
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