The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Identifying long-range structure in the intrinsically unstructured transactivation domain of p53
Abstract
Paramagnetic relaxation enhancement (PRE) was used to identify a compact dynamic structure for the intrinsically unstructured transactivation domain of the tumor suppressor protein, p53. Our results show that p53 residues essential for binding to the ubiquitin ligase, MDM2, and the 70 kDa subunit of replication protein A, RPA70, are separated by an average distance of 10–15 Å. This result suggests that a more extended member of the ensemble must be populated prior to binding either MDM2 or RPA70. We also show that PRE can be used to detect intermolecular distances between p53 and RPA70. Proteins 2007. © 2007 Wiley‐Liss, Inc.
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“The SAXS profile was not consistent with a collapsed structure of the transactivation domain, reported from paramagnetic relaxation enhancement experiments (Fig. S7) (28).”
From Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain (2008) · cites this paper as [28]
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Cites
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
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Cited by
Clore, G. M., & Iwahara, J. (2009) · Chemical Reviews · doi:10.1021/cr900033p · Cited by 782
Unusual biophysics of intrinsically disordered proteins
Uversky, V. N. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.12.008 · Cited by 566
Structure 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
Finding Our Way in the Dark Proteome
Bhowmick, A., Brookes, D. H., Yost, S. R., Dyson, H. J., Forman-Kay, J. D., Gunter, D., Head-Gordon, M., Hura, G. L., Pande, V. S., Wemmer, D. E., et al. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b06543 · Cited by 128
Metadata
- Authors
- Vise, P., Baral, B., Stancik, A., Lowry, D. F., & Daughdrill, G. W.
- Venue
- Proteins: Structure, Function, and Bioinformatics
- Publisher
- Wiley
- Published
- 2007-03-02
- Volume
- 67
- Issue
- 3
- Pages
- 526-530
- ISSN
- 0887-3585
- 1097-0134
- Cited by
- 47
- References
- 4
- Language
- en
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- Vise, P., Baral, B., Stancik, A., Lowry, D. F., & Daughdrill, G. W. (2007). Identifying long-range structure in the intrinsically unstructured transactivation domain of p53. Proteins: Structure, Function, and Bioinformatics. https://doi.org/10.1002/prot.21364
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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.
