The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes
Abstract
Proteins are constantly involved in the multitude of various interactions creating sophisticated networks which define and control all (or almost all) the biological processes taking place in any living organism. Intrinsically disordered proteins or regions play a number of crucial roles in mediating protein interactions. The lack of fixed structure protruding to the high level of intrinsic dynamics and almost unrestricted flexibility at various structure levels, being the major characteristics of intrinsically disordered proteins, provides them with unprecedented advantages over the ordered proteins. The binding modes attainable by disordered proteins are highly diverse, creating a multitude of unusual complexes. Although the majority of studied to date intrinsic disorder-based complexes are ordered or static entities originating due to the global or local disorder-to-order transitions, a new development is the discovery of dynamic complexes in which intrinsically disordered proteins continue to sample an ensemble of rapidly interconverting conformations mostly devoid of structure even in their bound state. The goal of this critical review is to illustrate binding plasticity of intrinsically disordered proteins by representing a portrait gallery of the disorder-based complexes (119 references).
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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
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
Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2005) · Journal of Molecular Recognition · doi:10.1002/jmr.747 · Cited by 847
Self-citationThe interplay between structure and function in intrinsically unstructured proteins
Tompa, P. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.03.072 · Cited by 717
Folding funnels, binding funnels, and protein function
Tsai, C., Kumar, S., Ma, B., & Nussinov, R. (1999) · Protein Science · doi:10.1110/ps.8.6.1181 · Cited by 648
Folding funnels and binding mechanisms
Ma, B., Kumar, S., Tsai, C.-J., & Nussinov, R. (1999) · Protein Engineering, Design and Selection · doi:10.1093/protein/12.9.713 · Cited by 594
The protein trinity—linking function and disorder
Dunker, A. K., & Obradovic, Z. (2001) · Nature Biotechnology · doi:10.1038/nbt0901-805 · Cited by 581
Romero, P. R., Zaidi, S., Fang, Y. Y., Uversky, V. N., Radivojac, P., Oldfield, C. J., Cortese, M. S., Sickmeier, M., LeGall, T., Obradovic, Z., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507916103 · Cited by 480
Self-citationPontius, B. W. (1993) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(93)90111-y · Cited by 183
Permyakov, S. E., Millett, I. S., Doniach, S., Permyakov, E. A., & Uversky, V. N. (2003) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.10481 · Cited by 113
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Cited by
AlphaFold2: A Role for Disordered Protein/Region Prediction?
Wilson, C. J., Choy, W.-Y., & Karttunen, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094591 · Cited by 173
Fonin, A. V., Darling, A. L., Kuznetsova, I. M., Turoverov, K. K., & Uversky, V. N. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03276-1 · Cited by 91
Self-citationConformational Recognition of an Intrinsically Disordered Protein
Krieger, J. M., Fusco, G., Lewitzky, M., Simister, P. C., Marchant, J., Camilloni, C., Feller, S. M., & De Simone, A. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.03.004 · Cited by 56
Metadata
- Authors
- Uversky, V. N.
- Venue
- Chem. Soc. Rev.
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2011
- Volume
- 40
- Issue
- 3
- Pages
- 1623-1634
- ISSN
- 0306-0012 (ISSN-L)
- 1460-4744
- OpenAlex
- W1964213103
- Cited by
- 259
- References
- 10
- FWCI
- 1.29
- Type
- journal article
- Language
- en
- Open access
- closed
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