The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
The roles of intrinsic disorder in protein interaction networks
Abstract
Proteins participate in complex sets of interactions that represent the mechanistic foundation for much of the physiology and function of the cell. These protein–protein interactions are organized into exquisitely complex networks. The architecture of protein–protein interaction networks was recently proposed to be scale-free, with most of the proteins having only one or two connections but with relatively fewer ‘hubs’ possessing tens, hundreds or more links. The high level of hub connectivity must somehow be reflected in protein structure. What structural quality of hub proteins enables them to interact with large numbers of diverse targets? One possibility would be to employ binding regions that have the ability to bind multiple, structurally diverse partners. This trait can be imparted by the incorporation of intrinsic disorder in one or both partners. To illustrate the value of such contributions, this review examines the roles of intrinsic disorder in protein network architecture. We show that there are three general ways that intrinsic disorder can contribute: First, intrinsic disorder can serve as the structural basis for hub protein promiscuity; secondly, intrinsically disordered proteins can bind to structured hub proteins; and thirdly, intrinsic disorder can provide flexible linkers between functional domains with the linkers enabling mechanisms that facilitate binding diversity. An important research direction will be to determine what fraction of protein– protein interaction in regulatory networks relies on intrinsic disorder.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
Cross, D. A. E., Alessi, D. R., Cohen, P., Andjelkovich, M., & Hemmings, B. A. (1995) · Nature · doi:10.1038/378785a0 · Cited by 5,244
A comprehensive analysis of protein–protein interactions in Saccharomyces cerevisiae
Uetz, P., Giot, L., Cagney, G., Mansfield, T. A., Judson, R. S., Knight, J. R., Lockshon, D., Narayan, V., Srinivasan, M., Pochart, P., et al. (2000) · Nature · doi:10.1038/35001009 · Cited by 4,706
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
From molecular to modular cell biology.
Hartwell, L. H., Hopfield, J. J., Leibler, S., & Murray, A. W. (1999) · Nature · doi:10.1038/35011540 · Cited by 3,632
A comprehensive two-hybrid analysis to explore the yeast protein interactome
Ito, T., Chiba, T., Ozawa, R., Yoshida, M., Hattori, M., & Sakaki, Y. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.061034498 · Cited by 3,566
Polakis, P. (2000) · Genes & Development · doi:10.1101/gad.14.15.1837 · Cited by 3,183
Barabási, A.-L., & Bonabeau, E. (2003) · Scientific American · doi:10.1038/scientificamerican0503-60 · Cited by 2,494
Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206
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
Coupling 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
Discovering regulatory and signalling circuits in molecular interaction networks
Ideker, T., Ozier, O., Schwikowski, B., & Siegel, A. F. (2002) · Bioinformatics · doi:10.1093/bioinformatics/18.suppl_1.s233 · Cited by 1,197
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-citationYoshida, K., & Miki, Y. (2004) · Cancer Science · doi:10.1111/j.1349-7006.2004.tb02195.x · Cited by 753
The protein trinity—linking function and disorder
Dunker, A. K., & Obradovic, Z. (2001) · Nature Biotechnology · doi:10.1038/nbt0901-805 · Cited by 581
p53: traffic cop at the crossroads of DNA repair and recombination
Sengupta, S., & Harris, C. C. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1546 · Cited by 544
Latrunculin alters the actin-monomer subunit interface to prevent polymerization
Morton, W. M., Ayscough, K. R., & McLaughlin, P. J. (2000) · Nature Cell Biology · doi:10.1038/35014075 · Cited by 523
Ravichandran, V., Chawla, A., & Roche, P. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.23.13300 · Cited by 354
Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA
Jones, C. J., & Wood, R. D. (1993) · Biochemistry · doi:10.1021/bi00096a021 · Cited by 291
Solution structure of the DNA- and RPA-binding domain of the human repair factor XPA
Ikegami, T., Kuraoka, I., Saijo, M., Kodo, N., Kyogoku, Y., Morikawa, K., Tanaka, K., & Shirakawa, M. (1998) · Nature Structural & Molecular Biology · doi:10.1038/1400 · Cited by 139
Miyamoto, I., Miura, N., Niwa, H., Miyazaki, J., & Tanaka, K. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49821-9 · Cited by 122
A novel cytoplasmic GTPase XAB1 interacts with DNA repair protein XPA
Nitta, M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.21.4212 · Cited by 58
Cited by
Xue, B., Dunker, A. K., & Uversky, V. N. (2012) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2012.675145 · Cited by 561
Self-citationXie, H., Vucetic, S., Iakoucheva, L. M., Oldfield, C. J., Dunker, A. K., Uversky, V. N., & Obradovic, Z. (2007) · Journal of Proteome Research · doi:10.1021/pr060392u · Cited by 560
Self-citationStructure–function–rescue: the diverse nature of common p53 cancer mutants
Joerger, A. C., & Fersht, A. R. (2007) · Oncogene · doi:10.1038/sj.onc.1210291 · Cited by 434
Xie, H., Vucetic, S., Iakoucheva, L. M., Oldfield, C. J., Dunker, A. K., Obradovic, Z., & Uversky, V. N. (2007) · Journal of Proteome Research · doi:10.1021/pr060394e · Cited by 382
Self-citationUnderstanding eukaryotic linear motifs and their role in cell signaling and regulation
Diella, F. (2008) · Frontiers in Bioscience · doi:10.2741/3175 · Cited by 340
Metadata
- Authors
- Uversky, V. N.
- Venue
- The Biomedical & Life Sciences Collection
- Publisher
- Henry Stewart Talks
- Published
- 2013-08-20
- Volume
- 2013
- Issue
- 8
- Pages
- e1003303
- ISSN
- 2056-452X (ISSN-L)
- OpenAlex
- W196004681
- Cited by
- 174
- References
- 22
- FWCI
- 5.65
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
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.
