The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Regulation of DNA Binding of p53 by its C-terminal Domain
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In the citing paper
“The CTD is highly basic and binds non-specifically to DNA both as an isolated peptide and within the full-length p53 tetramer.23”
From Mapping Interactions of the Intrinsically Disordered C-Terminal Regions of Tetrameric p53 by Segmental Isotope Labeling and NMR (2022) · cites this paper as [23]
In the citing paper
“Two regions of the CTD, spanning residues 369-374 and 381-388 and with high lysine content, make dynamic and sequence-independent interactions with DNA in regions that flank the p53 recognition element.”
From Mapping Interactions of the Intrinsically Disordered C-Terminal Regions of Tetrameric p53 by Segmental Isotope Labeling and NMR (2022) · cites this paper as [23]
In the citing paper
“The CTD can undergo disorder-to-order transitions as a result of binding to protein interactors or nonspecific DNA (Rustandi et al. 2000;Weinberg et al. 2004).”
From Structural Evolution and Dynamics of the p53 Proteins (2017) · cites this paper as Weinberg et al. 2004
In the citing paper
“Interaction of the p53 CTD with no specific DNA sequences regulates binding of the core domain to specific recognition sequences in promoters (Weinberg et al. 2004).”
From Structural Evolution and Dynamics of the p53 Proteins (2017) · cites this paper as Weinberg et al. 2004
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Citations
Cites
Momand, J., Zambetti, G. P., Olson, D. C., George, D., & Levine, A. J. (1992) · Cell · doi:10.1016/0092-8674(92)90644-r · Cited by 3,113
Crystal 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
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
Research works printed but not linked: 40
- Levine, 1997, p53, the cellular gatekeeper for growth and division, Cell, 88, 323, 10.1016/S0092-8674(00)81871-1 · DOI · Paper page
- Zhao, 2000, Analysis of p53-regulated gene expression patterns using oligonucleotide arrays, Genes Dev., 14, 981, 10.1101/gad.14.8.981 · DOI · Paper page
- Vousden, 2002, Live or let die: the cell's response to p53, Nature Rev. Cancer, 2, 594, 10.1038/nrc864 · DOI · Paper page
- Fields, 1990, Presence of a potent transcription activating sequence in the p53 protein, Science, 249, 1046, 10.1126/science.2144363 · DOI · Paper page
- Walker, 1996, Identification of a novel p53 functinal domain that is necessary for efficient growth suppression, Proc. Natl Acad. Sci. USA, 93, 15335, 10.1073/pnas.93.26.15335 · DOI · Paper page
- Oliner, 1993, Oncoprotein MDM2 conceals the activation domain of tumour suppressor p53, Nature, 362, 857, 10.1038/362857a0 · DOI · Paper page
- Thut, 1995, p53 transcriptional activation mediated by coactivators TAFII40 and TAFII60, Science, 267, 100, 10.1126/science.7809597 · DOI · Paper page
- Lu, 1995, Human TAFII3 protein is a transcriptional co-activator of the p53 protein, Proc. Natl Acad. Sci. USA, 92, 5154, 10.1073/pnas.92.11.5154 · DOI · Paper page
- Bargonetti, 1993, A proteolytic fragment from the central region of p53 has marked sequence-specific DNA-binding activity when generated from wild-type but not from oncogenic mutant p53 protein, Genes Dev., 7, 2565, 10.1101/gad.7.12b.2565 · DOI · Paper page
- Jeffrey, 1995, Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7angstroms, Science, 267, 1498, 10.1126/science.7878469 · DOI · Paper page
- Clore, 1995, Refined solution structure of the oligomerization domain of the tumour suppressor p53, Nature Struct. Biol., 2, 321, 10.1038/nsb0495-321 · DOI
- Clore, 1994, High-resolution structure of the oligomerization domain of p53 by multidimensional NMR, Science, 265, 386, 10.1126/science.8023159 · DOI · Paper page
- Yakovleva, 2002, p53 latency—out of the blind alley, Trends Biochem. Sci., 27, 612, 10.1016/S0968-0004(02)02209-0 · DOI
- Ahn, 2001, The C-terminus of p53: the more you learn the less you know, Nature Struct. Biol., 8, 730, 10.1038/nsb0901-730 · DOI
- Hupp, 1995, Small peptides activate the latent sequence-specific DNA binding function of p53, Cell, 83, 237, 10.1016/0092-8674(95)90165-5 · DOI · Paper page
- Hupp, 1994, Allosteric activation of latent p53 tetramers, Curr. Biol., 4, 865, 10.1016/S0960-9822(00)00195-0 · DOI · Paper page
- Gu, 1997, Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain, Cell, 90, 595, 10.1016/S0092-8674(00)80521-8 · DOI · Paper page
- Ayed, 2001, Latent and active p53 are identical in conformation, Nature Struct. Biol., 8, 756, 10.1038/nsb0901-756 · DOI
- Yakovleva, 2001, p53 latency—C-terminal domain prevents binding of p53 core to target but not to nonspecific DNA sequences, J. Biol. Chem., 276, 15650, 10.1074/jbc.M100482200 · DOI
- Kim, 1999, Influence of promoter DNA topology on sequence-specific DNA binding and transactivation by tumor suppressor p53, Oncogene, 18, 7310, 10.1038/sj.onc.1203139 · DOI
- Kim, 1997, DNA-conformation is an important determinant of sequence-specific DNA binding by tumor suppressor p53, Oncogene, 15, 857, 10.1038/sj.onc.1201412 · DOI
- Kaeser, 2002, Chromatin immunoprecipitation analysis fails to support the latency model for regulation of p53 DNA binding activity in vivo, Proc. Natl Acad. Sci. USA, 99, 95, 10.1073/pnas.012283399 · DOI · Paper page
- Espinosa, 2001, Transcriptional regulation by p53 through intrinsic DNA/chromatin binding and site-directed cofactor recruitment, Mol. Cell, 8, 57, 10.1016/S1097-2765(01)00283-0 · DOI · Paper page
- Bayle, 1995, The carboxy-terminal domain of the p53 protein regulates sequence-specific DNA binding through its non-specific nucleic acid-binding activity, Proc. Natl Acad. Sci. USA, 92, 5729, 10.1073/pnas.92.12.5729 · DOI
- Anderson, 1997, Reciprocal interference between the sequence-specific core and non-specific C-terminal DNA binding domains of p53: implications for regulation, Mol. Cell. Biol., 17, 6255, 10.1128/MCB.17.11.6255 · DOI
- LeTilly, 1993, Fluorescence anisotropy assays implicate protein–protein interactions in regulating trp repressor DNA binding, Biochemistry, 32, 7753, 10.1021/bi00081a021 · DOI
- Funk, 1992, A transcriptionally active DNA-binding site for human p53 protein complexes, Mol. Cell. Biol., 12, 2866, 10.1128/MCB.12.6.2866 · DOI · Paper page
- Mujtaba, 2004, Structural mechanism of the bromodomain of the coactivator CP in p53 transcriptional activation, Mol. Cell, 13, 251, 10.1016/S1097-2765(03)00528-8 · DOI · Paper page
- Rustandi, 2000, Structure of the negative regulatory domain of p53 bound to S100B, Nature Struct. Biol., 7, 570, 10.1038/76797 · DOI
- Record, 1991, Analysis of equilibrium and kinetic measurements to determine thermodynamic origins of stability and specificity and mechanism of formation of site-specific complexes between proteins and helical DNA, Methods Enzymol., 208, 291, 10.1016/0076-6879(91)08018-D · DOI · Paper page
- Prives, 2001, Why is p53 acetylated?, Cell, 107, 815, 10.1016/S0092-8674(01)00619-5 · DOI
- Barlev, 2001, Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases, Mol. Cell, 8, 1243, 10.1016/S1097-2765(01)00414-2 · DOI · Paper page
- Jiao, 2001, Dynamic interactions of p53 with DNA in solution by time-lapse atomic force microscopy, J. Mol. Biol., 314, 233, 10.1006/jmbi.2001.5129 · DOI
- Midgley, 1992, Analysis of p53 expression in human tumors—an antibody raised against human P53 expressed in Escherichia coli, J. Cell Sci., 101, 183, 10.1242/jcs.101.1.183 · DOI · Paper page
- Miroux, 1996, Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels, J. Mol. Biol., 260, 289, 10.1006/jmbi.1996.0399 · DOI · Paper page
- Neidhardt, 1974, Culture medium for enterobacteria, J. Bacteriol., 119, 736, 10.1128/JB.119.3.736-747.1974 · DOI · Paper page
- Gill, 1989, Calculation of protein extinction coefficients from amino acid sequence data, Anal. Biochem., 182, 319, 10.1016/0003-2697(89)90602-7 · DOI · Paper page
- Johnson, 1994, NMR View - computer program for the visualization and analysis of NMR data, J. Biomol. NMR, 4, 603, 10.1007/BF00404272 · DOI · Paper page
- Hajduk, 1997, NMR-based discovery of lead inhibitors that block DNA binding of the human papilomavirus E2 proein, J. Med. Chem., 40, 3144, 10.1021/jm9703404 · DOI · Paper page
- Weinberg, 2004, Cooperative binding of tetrameric p53 to DNA, J. Mol. Biol., 341, 1145, 10.1016/j.jmb.2004.06.071 · DOI · Paper page
Cited by
Regulating the p53 pathway: in vitro hypotheses, in vivo veritas
Toledo, F., & Wahl, G. M. (2006) · Nature reviews. Cancer · doi:10.1038/nrc2012 · Cited by 1,286
Pathological Unfoldomics of Uncontrolled Chaos: Intrinsically Disordered Proteins and Human Diseases
Uversky, V. N., Davé, V., Iakoucheva, L. M., Malaney, P., Metallo, S. J., Pathak, R. R., & Joerger, A. C. (2014) · Chemical Reviews · doi:10.1021/cr400713r · Cited by 288
Core 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
Self-citationStructural Evolution and Dynamics of the p53 Proteins
Chillemi, G., Kehrloesser, S., Bernassola, F., Desideri, A., Dötsch, V., Levine, A. J., & Melino, G. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a028308 · Cited by 65
Wang, Y. V., Leblanc, M., Fox, N., Mao, J.-H., Tinkum, K. L., Krummel, K., Engle, D., Piwnica-Worms, D., Piwnica-Worms, H., Balmain, A., et al. (2011) · Genes & Development · doi:10.1101/gad.2024411 · Cited by 53
Metadata
- Authors
- Weinberg, R. L., Freund, S. M. V., Veprintsev, D. B., Bycroft, M., & Fersht, A. R.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2004-09
- Volume
- 342
- Issue
- 3
- Pages
- 801-811
- ISSN
- 0022-2836
- Cited by
- 97
- References
- 3
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
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