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p53-A natural cancer killer: Structural insights and therapeutic concepts
Abstract
Every single day, the DNA of each cell in the human body is mutated thousands of times, even in absence of oncogenes or extreme radiation. Many of these mutations could lead to cancer and, finally, death. To fight this, multicellular organisms have evolved an efficient control system with the tumor‐suppressor protein p53 as the central element. An intact p53 network ensures that DNA damage is detected early on. The importance of p53 for preventing cancer is highlighted by the fact that p53 is inactivated in more than 50 % of all human tumors. Thus, for good reason, p53 is one of the most intensively studied proteins. Despite the great effort that has been made to characterize this protein, the complex function and the structural properties of p53 are still only partially known. This review highlights basic concepts and recent progress in understanding the structure and regulation of p53, focusing on emerging new mechanistic and therapeutic concepts.
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“p53 is a homotetramer, with folded tetramerization and core domains that are linked together and flanked by intrinsically disordered (or natively unfolded) domains at the N and C termini (1, 2).”
From Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain (2008) · cites this paper as [2]
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Lane, D. P. (1992) · Nature · doi:10.1038/358015a0 · Cited by 5,138
In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661
Self-citationCrystal 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
HSP90 and the chaperoning of cancer
Whitesell, L., & Lindquist, S. L. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1716 · Cited by 2,502
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
DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
Shieh, S.-Y., Ikeda, M., Taya, Y., & Prives, C. (1997) · Cell · doi:10.1016/s0092-8674(00)80416-x · Cited by 2,100
The p53 pathway: positive and negative feedback loops
Harris, S. L., & Levine, A. J. (2005) · Oncogene · doi:10.1038/sj.onc.1208615 · Cited by 1,967
Small-molecule inhibitors of protein–protein interactions: progressing towards the dream
Arkin, M. R., & Wells, J. A. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1343 · Cited by 1,705
p53 mutant mice that display early ageing-associated phenotypes
Tyner, S. D., Venkatachalam, S., Choi, J., Jones, S., Ghebranious, N., Igelmann, H., Lu, X., Soron, G., Cooper, B., Brayton, C., et al. (2002) · Nature · doi:10.1038/415045a · Cited by 1,459
Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
de Oca Luna, R. M., Wagner, D. S., & Lozano, G. (1995) · Nature · doi:10.1038/378203a0 · Cited by 1,420
Research works printed but not linked: 293
- Chang C., 1979, J. Virol., 31, 463, 10.1128/jvi.31.2.463-471.1979 · DOI
- 10.1038/278261a0 · DOI · Paper page
- 10.1016/0092-8674(79)90293-9 · DOI · Paper page
- 10.1002/ijc.2910570102 · DOI · Paper page
- 10.1038/35042675 · DOI · Paper page
- 10.1016/S0092-8674(00)81871-1 · DOI · Paper page
- 10.1093/emboj/17.7.1847 · DOI · Paper page
- 10.1002/(SICI)1098-1004(1999)14:1<1::AID-HUMU1>3.0.CO;2-H · doi:10.1002/(sici)1098-1004(1999)14:1<1::aid-humu1>3.0.co;2-h
- Jin S., 2001, J. Cell Sci., 114, 4139, 10.1242/jcs.114.23.4139 · DOI · Paper page
- 10.1038/35077213 · DOI · Paper page
- 10.1128/MCB.4.9.1689 · DOI · Paper page
- 10.1007/BF01534845 · doi:10.1007/bf01534845
- 10.1038/319783a0 · DOI · Paper page
- 10.1073/pnas.85.14.5146 · DOI
- Soussi T., 1990, Oncogene, 5, 945
- 10.1007/978-3-642-80481-6_1 · DOI
- 10.1038/sj.onc.1201263 · DOI · Paper page
- 10.1073/pnas.93.26.15335 · DOI · Paper page
- 10.1093/emboj/17.16.4668 · DOI · Paper page
- 10.1126/science.2144363 · DOI · Paper page
- 10.1073/pnas.92.11.5154 · DOI · Paper page
- 10.1126/science.7809597 · DOI · Paper page
- 10.1038/sj.onc.1203312 · DOI
- 10.1073/pnas.96.26.14801 · DOI
- 10.1128/jvi.69.3.1851-1859.1995 · DOI · Paper page
- 10.1126/science.281.5383.1674 · DOI · Paper page
- 10.1006/jmbi.2001.5082 · DOI
- 10.1016/S0022-2836(02)00848-3 · DOI · Paper page
- 10.1016/j.jmb.2003.08.008 · DOI · Paper page
- 10.1074/jbc.M003107200 · DOI · Paper page
- 10.1016/S1093-3263(00)00138-8 · DOI · Paper page
- 10.1002/1097-0134(20001115)41:3<415::AID-PROT130>3.0.CO;2-7 · DOI · Paper page
- 10.1016/S0959-440X(02)00289-0 · DOI · Paper page
- 10.1074/jbc.M508149200 · DOI
- 10.1101/gad.7.12b.2565 · DOI · Paper page
- 10.1101/gad.7.12b.2556 · DOI · Paper page
- 10.1016/0092-8674(92)90562-Q · DOI · Paper page
- 10.1128/MCB.14.8.5182 · DOI · Paper page
- Hainaut P., 1994, Oncogene, 9, 299
- 10.1021/bi00016a002 · DOI
- 10.1093/emboj/17.10.2748 · DOI
- 10.1038/5880 · DOI
- 10.1038/nsb0495-321 · DOI
- 10.1038/nsb1294-877 · DOI · Paper page
- 10.1126/science.7878469 · DOI · Paper page
- 10.1016/j.jmb.2004.06.071 · DOI · Paper page
- 10.1006/jmbi.2001.4450 · DOI
- 10.1038/nsb0901-730 · DOI
- 10.1074/jbc.M107516200 · DOI · Paper page
- 10.1101/SQB.1994.059.01.024 · DOI
- 10.1016/0092-8674(95)90165-5 · DOI · Paper page
- 10.1128/MCB.17.11.6255 · DOI
- 10.1016/j.jmb.2004.07.042 · DOI · Paper page
- 10.1038/sj.onc.1203285 · DOI · Paper page
- 10.1016/j.str.2005.01.020 · DOI · Paper page
- 10.1128/MCB.4.9.1689 · DOI · Paper page
- 10.1074/jbc.271.7.3917 · DOI
- 10.1006/jmbi.1997.1507 · DOI
- 10.1074/jbc.M407687200 · DOI
- 10.1074/jbc.M407601200 · DOI
- 10.1021/bi011736r · DOI
- 10.1021/bi970759w · DOI · Paper page
- 10.1016/j.febslet.2004.07.014 · DOI
- 10.1073/pnas.132393699 · DOI
- 10.1074/jbc.M102817200 · DOI · Paper page
- 10.1074/jbc.M206697200 · DOI
- 10.1016/S0092-8674(00)80540-1 · DOI · Paper page
- 10.1016/S1097-2765(00)80275-0 · DOI · Paper page
- Moll U. M., 2004, Mol. Cancer Res., 2, 371, 10.1158/1541-7786.371.2.7 · DOI · Paper page
- 10.1016/j.tibs.2003.10.004 · DOI · Paper page
- 10.1038/nm0798-747 · DOI · Paper page
- 10.1016/S0168-9525(02)02595-7 · DOI · Paper page
- 10.1093/emboj/18.16.4438 · DOI · Paper page
- 10.1107/S0907444901002529 · DOI
- 10.1002/pro.5560060128 · DOI · Paper page
- 10.1074/jbc.M307846200 · DOI
- Lu H., 1999, FASEB J., 13, 1538
- 10.1038/sj.onc.1204427 · DOI · Paper page
- 10.1023/A:1024044805720 · DOI
- 10.1016/S0006-2952(03)00511-2 · DOI
- 10.4161/cbt.4.4.1619 · DOI
- 10.1016/j.ccr.2005.02.019 · DOI · Paper page
- 10.1038/416560a · DOI · Paper page
- 10.1016/S0092-8674(00)80627-3 · DOI · Paper page
- 10.1126/science.1065486 · DOI · Paper page
- 10.1073/pnas.97.13.7301 · DOI · Paper page
- 10.1016/S0092-8674(00)80626-1 · DOI · Paper page
- 10.1016/S0960-9822(01)00534-6 · DOI · Paper page
- 10.1038/35094077 · DOI · Paper page
- 10.1073/pnas.96.5.1875 · DOI
- 10.1073/pnas.92.19.8591 · DOI
- 10.1016/j.jmb.2005.03.014 · DOI · Paper page
- 10.1093/emboj/18.3.763 · DOI
- 10.1074/jbc.M103801200 · DOI
- 10.1016/S0022-2836(02)00326-1 · DOI · Paper page
- 10.1074/jbc.M011644200 · DOI
- 10.1002/ange.200501887 · DOI
- 10.1002/anie.200501887 · DOI
- 10.1101/SQB.1994.059.01.025 · DOI
- Arrowsmith C. H., 1996, Oncogene, 12, 1379
- 10.1093/protein/14.4.233 · DOI
- 10.1073/pnas.0500215102 · DOI
- 10.1073/pnas.90.8.3319 · DOI · Paper page
- 10.1074/jbc.M603634200 · DOI · Paper page
- Wang X., 1995, Cancer Epidemiol. Biomarkers Prev., 4, 543
- 10.1002/humu.10185 · DOI · Paper page
- 10.1038/sj.onc.1204468 · DOI
- 10.1074/jbc.M507611200 · DOI
- 10.1126/science.1905840 · DOI · Paper page
- Hollstein M., 1994, Nucleic Acids Res., 22, 3551
- 10.1093/nar/25.1.151 · DOI · Paper page
- 10.1128/MCB.12.6.2866 · DOI · Paper page
- Sigal A., 2000, Cancer Res., 60, 6788
- 10.1016/j.cell.2004.11.006 · DOI · Paper page
- 10.1093/nar/gki252 · DOI
- 10.1007/s000180050271 · DOI
- 10.1073/pnas.92.12.5729 · DOI
- 10.1016/S0968-0004(00)88954-9 · DOI
- 10.1038/sj.onc.1203434 · DOI · Paper page
- 10.1038/sj.onc.1202041 · DOI · Paper page
- 10.1016/S0955-0674(03)00003-6 · DOI · Paper page
- 10.1046/j.1432-1327.2001.02225.x · DOI · Paper page
- 10.1006/jmbi.1996.0560 · DOI
- 10.4161/cc.4.4.1598 · DOI · Paper page
- 10.1016/S0960-9822(00)00439-5 · DOI · Paper page
- 10.1038/sj.onc.1202480 · DOI · Paper page
- 10.1074/jbc.M410233200 · DOI · Paper page
- 10.1038/42972 · DOI · Paper page
- 10.1016/S0092-8674(00)80521-8 · DOI · Paper page
- 10.1046/j.1432-1327.2001.02226.x · DOI · Paper page
- 10.1016/S1097-2765(01)00414-2 · DOI · Paper page
- 10.1016/S0092-8674(01)00619-5 · DOI
- 10.1016/S0092-8674(01)00524-4 · DOI · Paper page
- 10.1016/S0092-8674(01)00527-X · DOI · Paper page
- 10.1002/0470862637.ch14 · DOI
- 10.1038/nrm731 · DOI · Paper page
- 10.1074/jbc.275.12.8945 · DOI · Paper page
- 10.1038/35096061 · DOI · Paper page
- 10.1016/S1357-4310(98)01260-X · DOI
- 10.1038/nature737 · DOI · Paper page
- 10.1016/S1097-2765(04)00157-1 · DOI · Paper page
- 10.1016/j.cell.2005.03.037 · DOI · Paper page
- 10.1038/nature02514 · DOI · Paper page
- 10.1016/S0092-8674(03)00193-4 · DOI · Paper page
- 10.1016/j.cell.2005.06.018 · DOI
- 10.1093/emboj/18.22.6455 · DOI · Paper page
- 10.1093/emboj/18.22.6462 · DOI · Paper page
- 10.4161/cc.1.4.131 · DOI
- 10.1016/j.cell.2004.06.015 · DOI
- 10.1016/j.cell.2004.06.016 · DOI · Paper page
- Shaw P., 1996, Oncogene, 12, 921
- 10.1002/(SICI)1097-4644(199607)62:1<90::AID-JCB10>3.0.CO;2-J · doi:10.1002/(sici)1097-4644(199607)62:1<90::aid-jcb10>3.0.co;2-j
- 10.1073/pnas.0308762101 · DOI · Paper page
- 10.1038/nrc864 · DOI · Paper page
- 10.1093/nar/26.15.3453 · DOI · Paper page
- 10.1007/BF03402141 · DOI
- 10.1007/BF03401678 · DOI
- Picksley S. M., 1994, Oncogene, 9, 2523
- 10.1128/MCB.13.7.4107 · DOI · Paper page
- 10.1073/pnas.96.26.14801 · DOI
- 10.1016/S0022-2836(02)00852-5 · DOI · Paper page
- 10.1016/j.jmb.2003.11.051 · DOI
- 10.1073/pnas.0334477100 · DOI
- 10.1093/embo-reports/kve227 · DOI · Paper page
- 10.1016/j.bbrc.2005.03.151 · DOI · Paper page
- 10.1016/j.jmb.2005.05.010 · DOI
- 10.1023/B:JNMR.0000048856.84603.9b · DOI
- 10.1007/PL00012484 · doi:10.1007/pl00012484
- 10.1002/1521-3757(20020402)114:7<1142::AID-ANGE1142>3.0.CO;2-T · doi:10.1002/1521-3757(20020402)114:7<1142::aid-ange1142>3.0.co;2-t
- 10.1002/1521-3773(20020402)41:7<1098::AID-ANIE1098>3.0.CO;2-9 · DOI · Paper page
- 10.1146/annurev.cb.09.110193.003125 · DOI · Paper page
- 10.1016/S0092-8674(00)80928-9 · DOI · Paper page
- 10.1016/j.molcel.2005.09.028 · DOI · Paper page
- 10.1126/science.2188360 · DOI · Paper page
- 10.1038/370111a0 · DOI · Paper page
- 10.1146/annurev.bi.62.070193.002025 · DOI · Paper page
- 10.1093/emboj/18.24.6934 · DOI · Paper page
- 10.1007/s10254-003-0021-1 · DOI · Paper page
- Hupp T. R., 2000, Biochem. J., 1, 10.1042/bj3520001 · DOI
- 10.1093/emboj/20.22.6297 · DOI · Paper page
- 10.1016/0014-5793(94)01417-Y · DOI
- 10.1093/emboj/20.17.4634 · DOI · Paper page
- 10.1074/jbc.M100200200 · DOI
- 10.1046/j.1365-2184.2000.00189.x · DOI · Paper page
- 10.1074/jbc.274.39.27474 · DOI
- 10.1128/MCB.16.3.1126 · DOI · Paper page
- 10.1128/MCB.4.12.2802 · DOI · Paper page
- 10.1016/S0021-9258(18)33376-3 · DOI · Paper page
- 10.1074/jbc.272.30.18608 · DOI
- 10.1073/pnas.93.16.8379 · DOI · Paper page
- 10.1074/jbc.271.25.15084 · DOI
- 10.1128/MCB.18.3.1517 · DOI · Paper page
- 10.1038/sj.onc.1202978 · DOI
- 10.1016/S0014-5793(99)00505-0 · DOI
- 10.1093/emboj/20.4.914 · DOI · Paper page
- 10.1074/jbc.275.21.16202 · DOI · Paper page
- 10.1002/path.1704 · DOI
- 10.1016/j.mrfmmm.2004.08.022 · DOI
- 10.1016/j.ceb.2005.09.007 · DOI · Paper page
- 10.1378/chest.125.5_suppl.83S-a · DOI
200 of 293 shown
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Self-citation
Metadata
- Authors
- Römer, L., Klein, C., Dehner, A., Kessler, H., & Buchner, J.
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2006-09-29
- Volume
- 45
- Issue
- 39
- Pages
- 6440-6460
- ISSN
- 1433-7851
- 1521-3773
- Cited by
- 93
- References
- 38
- Language
- en
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