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Items: 1 to 20 of 78

1.

The interaction of p53 with replication protein A mediates suppression of homologous recombination.

Romanova LY, Willers H, Blagosklonny MV, Powell SN.

Oncogene. 2004 Dec 2;23(56):9025-33.

PMID:
15489903
2.

Dissociation of p53-mediated suppression of homologous recombination from G1/S cell cycle checkpoint control.

Willers H, McCarthy EE, Wu B, Wunsch H, Tang W, Taghian DG, Xia F, Powell SN.

Oncogene. 2000 Feb 3;19(5):632-9.

3.

p53's double life: transactivation-independent repression of homologous recombination.

Bertrand P, Saintigny Y, Lopez BS.

Trends Genet. 2004 Jun;20(6):235-43. Review. Erratum in: Trends Genet. 2005 Jan;21(1):36.

PMID:
15145576
4.

Interaction of p53 with the human Rad51 protein.

Buchhop S, Gibson MK, Wang XW, Wagner P, Stürzbecher HW, Harris CC.

Nucleic Acids Res. 1997 Oct 1;25(19):3868-74.

5.

The recombination-deficient mutant RPA (rfa1-t11) is displaced slowly from single-stranded DNA by Rad51 protein.

Kantake N, Sugiyama T, Kolodner RD, Kowalczykowski SC.

J Biol Chem. 2003 Jun 27;278(26):23410-7.

6.
7.

ATR-p53 restricts homologous recombination in response to replicative stress but does not limit DNA interstrand crosslink repair in lung cancer cells.

Sirbu BM, Lachmayer SJ, Wülfing V, Marten LM, Clarkson KE, Lee LW, Gheorghiu L, Zou L, Powell SN, Dahm-Daphi J, Willers H.

PLoS One. 2011;6(8):e23053. doi: 10.1371/journal.pone.0023053.

8.

Dynamic regulatory interactions of rad51, rad52, and replication protein-a in recombination intermediates.

Sugiyama T, Kantake N.

J Mol Biol. 2009 Jul 3;390(1):45-55. doi: 10.1016/j.jmb.2009.05.009.

PMID:
19445949
9.

Structural basis of restoring sequence-specific DNA binding and transactivation to mutant p53 by suppressor mutations.

Suad O, Rozenberg H, Brosh R, Diskin-Posner Y, Kessler N, Shimon LJ, Frolow F, Liran A, Rotter V, Shakked Z.

J Mol Biol. 2009 Jan 9;385(1):249-65. doi: 10.1016/j.jmb.2008.10.063.

PMID:
18996393
10.

P53 inhibits strand exchange and replication fork regression promoted by human Rad51.

Yoon D, Wang Y, Stapleford K, Wiesmüller L, Chen J.

J Mol Biol. 2004 Feb 20;336(3):639-54.

PMID:
15095978
11.

Mutant p53 proteins behave in a dominant, negative fashion in vivo.

Hachiya M, Chumakov A, Miller CW, Akashi M, Said J, Koeffler HP.

Anticancer Res. 1994 Sep-Oct;14(5A):1853-9.

PMID:
7847818
12.

Differences in the association of p53 phosphorylated on serine 15 and key enzymes of homologous recombination.

Restle A, Janz C, Wiesmüller L.

Oncogene. 2005 Jun 23;24(27):4380-7.

PMID:
15806145
13.

Discriminatory suppression of homologous recombination by p53.

Yun S, Lie-A-Cheong C, Porter AC.

Nucleic Acids Res. 2004 Dec 15;32(22):6479-89.

14.

Physical interaction between human RAD52 and RPA is required for homologous recombination in mammalian cells.

Park MS, Ludwig DL, Stigger E, Lee SH.

J Biol Chem. 1996 Aug 2;271(31):18996-9000.

15.

Knockin mice expressing a chimeric p53 protein reveal mechanistic differences in how p53 triggers apoptosis and senescence.

Johnson TM, Meade K, Pathak N, Marques MR, Attardi LD.

Proc Natl Acad Sci U S A. 2008 Jan 29;105(4):1215-20. doi: 10.1073/pnas.0706764105.

16.

Restoring wild-type conformation and DNA-binding activity of mutant p53 is insufficient for restoration of transcriptional activity.

Brazda V, Muller P, Brozkova K, Vojtesek B.

Biochem Biophys Res Commun. 2006 Dec 15;351(2):499-506.

PMID:
17070499
17.

[Direct role of p53 on homologous recombination].

Saintigny Y, Bertrand P, Lopez BS.

Med Sci (Paris). 2005 Jan;21(1):43-8. Review. French.

18.
19.

Role of heteroduplex joints in the functional interactions between human Rad51 and wild-type p53.

Süsse S, Janz C, Janus F, Deppert W, Wiesmüller L.

Oncogene. 2000 Sep 14;19(39):4500-12.

20.

p53 modulates homologous recombination at I-SceI-induced double-strand breaks through cell-cycle regulation.

Rieckmann T, Kriegs M, Nitsch L, Hoffer K, Rohaly G, Kocher S, Petersen C, Dikomey E, Dornreiter I, Dahm-Daphi J.

Oncogene. 2013 Feb 21;32(8):968-75. doi: 10.1038/onc.2012.123.

PMID:
22484423

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