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Cited by 110

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The structure of p53 tumour suppressor protein reveals the basis for its functional plasticity

Okorokov, Andrei L, Sherman, Michael B, Plisson, Celia, Grinkevich, Vera, Sigmundsson, Kristmundur, Selivanova, Galina, Milner, Jo, Orlova, Elena V·2006·The EMBO Journal

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Research works printed but not linked: 56

  1. 25 Years of P53 research (2005) Hainaut P, Wiman K (eds) Springer
  2. Ahn J, Prives C (2001) The C‐terminus of p53: the more you learn the less you know. Nat Struct Biol 8: 730–732 · DOI
  3. Anderson ME, Woelker B, Reed M, Wang P, Tegtmeyer P (1997) Reciprocal interference between the sequence‐specific core and nonspecific C‐terminal DNA‐binding domains of p53: implications for regulation. Mol Cell Biol 17: 6255–6264 · DOI
  4. Avalos JL, Celic I, Muhammad S, Cosgrove MS, Boeke JD, Wolberger C (2002) Structure of a Sir2 enzyme bound to an acetylated p53 peptide. Mol Cell 10: 523–535 · DOI
  5. Ayed A, Mulder FA, Yi GS, Lu Y, Kay LE, Arrowsmith CH (2001) bLatent and active p53 are identical in conformation. Nat Struct Biol 8: 756–760 · DOI
  6. Bakalkin G, Yakovleva T, Selivanova G, Magnusson KP, Szekely L, Kiseleva E, Klein G, Terenius L, Wiman KG (1995) p53 binds single‐stranded DNA ends through the C‐terminal domain and internal DNA segments via the middle domain. Nucleic Acids Res 23: 362–369 · DOI · Paper page
  7. Bayle JH, Elenbaas B, Levine AJ (1995) The carboxyl‐terminal domain of the p53 protein regulates sequence‐specific DNA binding through its nonspecific nucleic acid‐binding activity. Proc Natl Acad Sci USA 92: 5729–5733 · DOI
  8. Bochkareva E, Kaustov L, Ayed A, Yi GS, Lu Y, Pineda‐Lucena A, Liao JC, Okorokov AL, Milner J, Arrowsmith CH, Bochkarev A (2005) Single‐stranded DNA mimicry in the p53 transactivation domain interaction with replication protein A. Proc Natl Acad Sci USA 102: 15412–15417 · DOI · Paper page
  9. Cain C, Miller S, Ahn J, Prives C (2000) The N terminus of p53 regulates its dissociation from DNA. J Biol Chem 275: 39944–39953 · DOI
  10. Clore GM, Ernst J, Clubb R, Omichinski JG, Kennedy WM, Sakaguchi K, Appella E, Gronenborn AM (1995) Refined solution structure of the oligomerization domain of the tumour suppressor p53. Nat Struct Biol 2: 321–333 · DOI
  11. Deibert M, Grazulis S, Sasnauskas G, Siksnys V, Huber R (2000) Structure of the tetrameric restriction endonuclease NgoMIV in complex with cleaved DNA. Nat Struct Biol 7: 792–799 · doi:10.1038/79032
  12. Derbyshire DJ, Basu BP, Serpell LC, Joo WS, Date T, Iwabuchi K, Doherty AJ (2002) Crystal structure of human 53BP1 BRCT domains bound to p53 tumour suppressor. EMBO J 21: 3863–3872 · DOI · Paper page
  13. Espinosa JM, Emerson BM (2001) Transcriptional regulation by p53 through intrinsic DNA/chromatin binding and site‐directed cofactor recruitment. Mol Cell 8: 57–69 · DOI · Paper page
  14. Friedman PN, Chen X, Bargonetti J, Prives C (1993) The p53 protein is an unusually shaped tetramer that binds directly to DNA. Proc Natl Acad Sci USA 90: 3319–3323 · DOI · Paper page
  15. Gorina S, Pavletich NP (1996) Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2. Science 274: 1001–1005 · DOI · Paper page
  16. Goodsell DS (2003) p53 tumour suppressor—molecule of the month http://www‐iphicles.rcsb.org/pdb/molecules/pdb31_1.html · doi:10.2210/rcsb_pdb/mom_2002_7
  17. Hansen S, Lane DP, Midgley CA (1998) The N terminus of the murine p53 tumour suppressor is an independent regulatory domain affecting activation and thermostability. J Mol Biol 275: 575–588 · DOI
  18. Harauz G, van Heel M (1986) Exact filters for general geometry three dimensional reconstruction. Optik 73: 146–516
  19. Ho WC, Fitzgerald MX, Marmorstein R (2006) Structure of the p53 core domain dimer bound to DNA. J Biol Chem 281: 20494–20502 · DOI · Paper page
  20. Horikoshi N, Usheva A, Chen J, Levine AJ, Weinmann R, Shenk T (1995) Two domains of p53 interact with the TATA‐binding protein, and the adenovirus 13S E1A protein disrupts the association, relieving p53‐mediated transcriptional repression. Mol Cell Biol 15: 227–234 · DOI · Paper page
  21. Hupp TR, Lane DP (1994) Allosteric activation of latent p53 tetramers. Curr Biol 4: 865–875 · DOI · Paper page
  22. Hupp TR, Meek DW, Midgley CA, Lane DP (1992) Regulation of the specific DNA binding function of p53. Cell 71: 875–886 · DOI · Paper page
  23. Huyen Y, Jeffrey PD, Derry WB, Rothman JH, Pavletich NP, Stavridi ES, Halazonetis TD (2004) Structural differences in the DNA binding domains of human p53 and its C. elegans ortholog Cep‐1. Structure 12: 1237–1243 · DOI
  24. Iwabuchi K, Li B, Bartel P, Fields S (1993) Use of the two‐hybrid system to identify the domain of p53 involved in oligomerization. Oncogene 8: 1693–1696
  25. Jackson P, Mastrangelo I, Reed M, Tegtmeyer P, Yardley G, Barrett J (1998) Synergistic transcriptional activation of the MCK promoter by p53: tetramers link separated DNA response elements by DNA looping. Oncogene 16: 283–292 · DOI
  26. Jeffrey PD, Gorina S, Pavletich NP (1995) Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms. Science 267: 1498–1502 · DOI · Paper page
  27. Jiao Y, Cherny DI, Heim G, Jovin TM, Schaffer TE (2001) Dynamic interactions of p53 with DNA in solution by time‐lapse atomic force microscopy. J Mol Biol 314: 233–243 · DOI
  28. Kern SE, Kinzler KW, Bruskin A, Jarosz D, Friedman P, Prives C, Vogelstein B (1991) Identification of p53 as a sequence‐specific DNA‐binding protein. Science 252: 1708–1711 · DOI · Paper page
  29. Kim E, Deppert W (2005) The complex interaction of p53 with target DNA: we learn as we go. Biochem Cell Biol 81: 141–150 · DOI
  30. Kitayner M, Rozenberg H, Kessler N, Rabinovich D, Shaulov L, Haran TE, Shakked Z (2006) Structural basis of DNA recognition by p53 tetramers. Mol Cell 22: 741–753 · DOI · Paper page
  31. Ko LJ, Prives C (1996) p53: puzzle and paradigm. Genes Dev 10: 1054–1072 · DOI · Paper page
  32. Lee S, Elenbaas B, Levine A, Griffith J (1995) p53 and its 14 kDa C‐terminal domain recognize primary DNA damage in the form of insertion/deletion mismatches. Cell 81: 1013–1020 · DOI · Paper page
  33. Lin YL, Chen C, Keshav KF, Winchester E, Dutta A (1996) Dissection of functional domains of the human DNA replication protein complex replication protein A. J Biol Chem 271: 17190–17198 · DOI
  34. McKinney K, Mattia M, Gottifredi V, Prives C (2004) p53 linear diffusion along DNA requires its C terminus. Mol Cell 16: 413–424 · DOI · Paper page
  35. McKinney K, Prives C (2002) Efficient specific DNA binding by p53 requires both its central and C‐terminal domains as revealed by studies with high‐mobility group 1 protein. Mol Cell Biol 22: 6797–6808 · DOI
  36. Milner J, Medcalf EA (1991) Co‐translation of mutant p53 with wild type drives the wild‐type p53 into the mutant conformation. Cell 65: 765–774 · DOI · Paper page
  37. Muller‐Tiemann BF, Halazonetis TD, Elting JJ (1998) Identification of an additional negative regulatory region for p53 sequence‐specific DNA binding. Proc Natl Acad Sci USA 95: 6079–6084 · DOI
  38. Navaza J, Lepault J, Ray FA, Alvarez‐Rua C, Borge J (2002) On the fitting of model electron densities into EM reconstructions: a reciprocal‐space formulation. Acta Crystallogr D 58: 1820–1825 · DOI
  39. Okorokov AL, Milner J (1999) An ATP/ADP‐dependent molecular switch regulates the stability of p53–DNA complexes. Mol Cell Biol 19: 7501–7510 · DOI
  40. Okorokov AL, Ponchel F, Milner J (1997) Induced N‐ and C‐terminal cleavage of p53: a core fragment of p53, generated by interaction with damaged DNA, promotes cleavage of the N‐terminus of full‐length p53, whereas ssDNA induces C‐terminal cleavage of p53. EMBO J 16: 6008–6017 · DOI
  41. Radermacher M (1988) Three‐dimensional reconstruction of single particles from random and non‐random tilt series. J Electron Microsc Tech 9: 359–394 · DOI · Paper page
  42. Saxton WO, Baumeister W (1986) Principles of organization in S layers. J Mol Biol 187: 251–253 · DOI
  43. Selivanova G, Ryabchenko L, Jansson E, Iotsova V, Wiman KG (1999) Reactivation of mutant p53 through interaction of a C‐terminal peptide with the core domain. Mol Cell Biol 19: 3395–3402 · DOI · Paper page
  44. Siksnys V, Skirgaila R, Sasnauskas G, Urbanke C, Cherny D, Grazulis S, Huber R (1999) The Cfr10I restriction enzyme is functional as a tetramer. J Mol Biol 291: 1105–1118 · DOI
  45. Stenger JE, Tegtmeyer P, Mayr GA, Reed M, Wang Y, Wang P, Hough PV, Mastrangelo IA (1994) p53 oligomerization and DNA looping are linked with transcriptional activation. EMBO J 13: 6011–6020 · DOI · Paper page
  46. Sturzbecher HW, Brain R, Addison C, Rudge K, Remm M, Grimaldi M, Keenan E, Jenkins JR (1992) A C‐terminal alpha‐helix plus basic region motif is the major structural determinant of p53 tetramerization. Oncogene 7: 1513–1523
  47. Tarunina M, Jenkins JR (1993) Human p53 binds DNA as a protein homodimer but monomeric variants retain full transcription transactivation activity. Oncogene 8: 3165–3173
  48. Tokino T, Thiagalingam S, el‐Deiry WS, Waldman T, Kinzler KW, Vogelstein B (1994) p53 tagged sites from human genomic DNA. Hum Mol Genet 3: 1537–1542 · DOI · Paper page
  49. van Heel M (1987) Angular reconstitution: aposteriori assignment of projection directions for 3D reconstruction. Ultramicroscopy 21: 111–112 · DOI · Paper page
  50. van Heel M, Gowen B, Matadeen R, Orlova EV, Finn R, Pape T, Cohen D, Stark H, Schmidt R, Schatz M, Patwardhan A (2000) Single‐particle electron cryo‐microscopy: towards atomic resolution. Q Rev Biophys 33: 307–369 · DOI · Paper page
  51. van Heel M, Harauz G, Orlova EV, Schmidt R, Schatz M (1996) A new generation of the IMAGIC image processing system. J Struct Biol 116: 17–24 · DOI · Paper page
  52. Wang P, Reed M, Wang Y, Mayr G, Stenger JE, Anderson ME, Schwedes JF, Tegtmeyer P (1994) p53 domains: structure, oligomerization, and transformation. Mol Cell Biol 14: 5182–5191
  53. Wang Y, Schwedes JF, Parks D, Mann K, Tegtmeyer P (1995) Interaction of p53 with its consensus DNA‐binding site. Mol Cell Biol 15: 2157–2165 · DOI
  54. Wentzell LM, Halford SE (1998) DNA looping by the Sfi I restriction endonuclease. J Mol Biol 281: 433–444 · doi:10.1006/jmbi.1998.1967
  55. Yakovleva T, Pramanik A, Terenius L, Ekstrom TJ, Bakalkin G (2002) p53 latency—out of the blind alley. Trends Biochem Sci 27: 612–618 · DOI
  56. Zhao K, Chai X, Johnston K, Clements A, Marmorstein R (2001) Crystal structure of the mouse p53 core DNA‐binding domain at 2.7 Å resolution. J Biol Chem 276: 12120–12127 · DOI

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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
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CoChat. (2026). Citation check: The structure of p53 tumour suppressor protein reveals the basis for its functional plasticity. https://app.cochat.ai/papers/10.1038/sj.emboj.7601382
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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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