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The structure of p53 tumour suppressor protein reveals the basis for its functional plasticity
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In the citing paper
“The observation that NTAD41, NLS, and CTD resonances are narrow in spectra of full-length p53 and are shifted only slightly from their chemical shifts in isolated peptides is inconsistent with an oligomerization model proposed on the basis of low-resolution (13.7 Å) cryo-electron microscopy data, in which the TET adopts a radically different structure compared to its isolated state and forms st”
From Mapping Interactions of the Intrinsically Disordered C-Terminal Regions of Tetrameric p53 by Segmental Isotope Labeling and NMR (2022) · cites this paper as [37]
In the citing paper
“The aggregates participate in initiating processes in which molecules of p53 widely unfold and then aggregate, resulting in the emergence of amyloid-containing structures.150,151”
From p53: from understanding its structure to advances in therapeutic targeting (2026) · cites this paper as [151]
In the citing paper
“On DNA binding, the structure of p53 rigidifies, becoming more compacted.”
From Structural Evolution and Dynamics of the p53 Proteins (2017) · cites this paper as Okorokov et al. 2006
In the citing paper
“In the absence of DNA, p53 forms an open cross-shaped structure with loosely coupled dimers interacting via the core domain.”
From Structural Evolution and Dynamics of the p53 Proteins (2017) · cites this paper as Okorokov et al. 2006
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Citations
Cites
Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607 · cited 4×
“Its post-translational modifications and interactions with other proteins were reported to modulate the stability of p53-specific DNA complexes (Ko and Prives, 1996; Vogelstein et al, 2000).”
BackgroundInfluentialCrystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic Mutations
Cho, Y., Gorina, S., Jeffrey, P. D., & Pavletich, N. P. (1994) · Science · doi:10.1126/science.8023157 · Cited by 2,551 · cited 8×
“Docking of the core domain atomic structure into p53 EM map We used the atomic structures of the core domain determined for both human and murine p53 (1tup, Cho et al, 1994; 1hu8, Zhao et al, 2001) to identify the location of this domain within the EM structure.”
BackgroundMethodInfluentialStructure 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
Definition of a consensus binding site for p53
El-Deiry, W. S., Kern, S. E., Pietenpol, J. A., Kinzler, K. W., & Vogelstein, B. (1992) · Nature Genetics · doi:10.1038/ng0492-45 · Cited by 1,985
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 · cited 1×
“In addition, a number of reports link p53 to DNA repair processes (Sengupta and Harris, 2005).”
BackgroundCore domain interactions in full-length p53 in solution
Veprintsev, D. B., Freund, S. M. V., Andreeva, A., Rutledge, S. E., Tidow, H., Cañadillas, J. M. P., Blair, C. M., & Fersht, A. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511130103 · Cited by 95
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Cited by
Reactivation of mutant p53: molecular mechanisms and therapeutic potential
Selivanova, G., & Wiman, K. G. (2007) · Oncogene · doi:10.1038/sj.onc.1210295 · Cited by 186
Self-citationWu, S., & Chiang, C. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.83 · Cited by 125
DNA Binding Cooperativity of p53 Modulates the Decision between Cell-Cycle Arrest and Apoptosis
Schlereth, K., Beinoraviciute-Kellner, R., Zeitlinger, M. K., Bretz, A. C., Sauer, M., Charles, J. P., Vogiatzi, F., Leich, E., Samans, B., Eilers, M., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.037 · Cited by 113
Noncanonical DNA Motifs as Transactivation Targets by Wild Type and Mutant p53
Jordan, J. J., Menendez, D., Inga, A., Nourredine, M., Bell, D., & Resnick, M. A. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000104 · Cited by 103
Rescue of the apoptotic-inducing function of mutant p53 by small molecule RITA
Zhao, C. Y., Grinkevich, V., Nikulenkov, F., Bao, W., & Selivanova, G. (2010) · Cell Cycle · doi:10.4161/cc.9.9.11545 · Cited by 79
Self-citation
Metadata
- Authors
- Okorokov, A. L., Sherman, M. B., Plisson, C., Grinkevich, V., Sigmundsson, K., Selivanova, G., Milner, J., & Orlova, E. V.
- Venue
- The EMBO Journal
- Published
- 2006-10-19
- Volume
- 25
- Issue
- 21
- Pages
- 5191-5200
- ISSN
- 0261-4189
- 1460-2075
- Cited by
- 110
- References
- 6
- Language
- en
- Licence
- www.springernature.com/gp/researchers/text-and-data-mining (tdm)
- www.springernature.com/gp/researchers/text-and-data-mining (vor)
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- Okorokov, A. L., Sherman, M. B., Plisson, C., Grinkevich, V., Sigmundsson, K., Selivanova, G., Milner, J., & Orlova, E. V. (2006). The structure of p53 tumour suppressor protein reveals the basis for its functional plasticity. The EMBO Journal. https://doi.org/10.1038/sj.emboj.7601382
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