메뉴 건너뛰기




Volumn 368, Issue 2, 2008, Pages 350-356

Activation of p53-dependent responses in tumor cells treated with a PARC-interacting peptide

Author keywords

Apoptosis; Etoposide; p53; PARC; TAT

Indexed keywords

CASPASE; DOXORUBICIN; ETOPOSIDE; PROTEIN P53; PROTEIN PARC; TRANSACTIVATOR PROTEIN;

EID: 39549119777     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.01.093     Document Type: Article
Times cited : (7)

References (21)
  • 1
    • 11344252796 scopus 로고    scopus 로고
    • Reassessment of the TP53 mutation database in human disease by data mining with a library of TP53 missense mutations
    • Soussi T., Kato S., Levy P.P., and Ishioka C. Reassessment of the TP53 mutation database in human disease by data mining with a library of TP53 missense mutations. Hum. Mutat. 25 (2005) 6-17
    • (2005) Hum. Mutat. , vol.25 , pp. 6-17
    • Soussi, T.1    Kato, S.2    Levy, P.P.3    Ishioka, C.4
  • 2
    • 0029049828 scopus 로고
    • Wild-type p53 protein undergoes cytoplasmic sequestration in undifferentiated neuroblastomas but not in differentiated tumors
    • Moll U.M., LaQuaglia M., Benard J., and Riou G. Wild-type p53 protein undergoes cytoplasmic sequestration in undifferentiated neuroblastomas but not in differentiated tumors. Proc. Natl. Acad. Sci. USA 92 (1995) 4407-4411
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4407-4411
    • Moll, U.M.1    LaQuaglia, M.2    Benard, J.3    Riou, G.4
  • 3
  • 6
    • 0028845158 scopus 로고
    • Small peptides activate the latent sequence-specific DNA binding function of p53
    • Hupp T.R., Sparks A., and Lane D.P. Small peptides activate the latent sequence-specific DNA binding function of p53. Cell 83 (1995) 237-245
    • (1995) Cell , vol.83 , pp. 237-245
    • Hupp, T.R.1    Sparks, A.2    Lane, D.P.3
  • 7
    • 19344365470 scopus 로고    scopus 로고
    • Treatment of terminal peritoneal carcinomatosis by a transducible p53-activating peptide
    • Snyder E.L., Meade B.R., Saenz C.C., and Dowdy S.F. Treatment of terminal peritoneal carcinomatosis by a transducible p53-activating peptide. PLoS Biol. 2 (2004) E36
    • (2004) PLoS Biol. , vol.2
    • Snyder, E.L.1    Meade, B.R.2    Saenz, C.C.3    Dowdy, S.F.4
  • 8
    • 0035863391 scopus 로고    scopus 로고
    • Synthetic protein transduction domains: enhanced transduction potential in vitro and in vivo
    • Ho A., Schwarze S.R., Mermelstein S.J., Waksman G., and Dowdy S.F. Synthetic protein transduction domains: enhanced transduction potential in vitro and in vivo. Cancer Res. 61 (2001) 474-477
    • (2001) Cancer Res. , vol.61 , pp. 474-477
    • Ho, A.1    Schwarze, S.R.2    Mermelstein, S.J.3    Waksman, G.4    Dowdy, S.F.5
  • 10
    • 33845313289 scopus 로고    scopus 로고
    • Down-regulation of insulin-like growth factor I receptor activity by NVP-AEW541 has an antitumor effect on neuroblastoma cells in vitro and in vivo
    • Tanno B., Mancini C., Vitali R., Mancuso M., McDowell H.P., Dominici C., and Raschella G. Down-regulation of insulin-like growth factor I receptor activity by NVP-AEW541 has an antitumor effect on neuroblastoma cells in vitro and in vivo. Clin. Cancer Res. 12 (2006) 6772-6780
    • (2006) Clin. Cancer Res. , vol.12 , pp. 6772-6780
    • Tanno, B.1    Mancini, C.2    Vitali, R.3    Mancuso, M.4    McDowell, H.P.5    Dominici, C.6    Raschella, G.7
  • 15
    • 23144459132 scopus 로고    scopus 로고
    • Multidrug-resistant neuroblastoma cells are responsive to arsenic trioxide at both normoxia and hypoxia
    • Karlsson J., Edsjo A., Pahlman S., and Pettersson H.M. Multidrug-resistant neuroblastoma cells are responsive to arsenic trioxide at both normoxia and hypoxia. Mol. Cancer Ther. 4 (2005) 1128-1135
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 1128-1135
    • Karlsson, J.1    Edsjo, A.2    Pahlman, S.3    Pettersson, H.M.4
  • 16
    • 33846849373 scopus 로고    scopus 로고
    • Functional characterization of a new p53 mutant generated by homozygous deletion in a neuroblastoma cell line
    • Nakamura Y., Ozaki T., Niizuma H., Ohira M., Kamijo T., and Nakagawara A. Functional characterization of a new p53 mutant generated by homozygous deletion in a neuroblastoma cell line. Biochem. Biophys. Res. Commun. 354 (2007) 892-898
    • (2007) Biochem. Biophys. Res. Commun. , vol.354 , pp. 892-898
    • Nakamura, Y.1    Ozaki, T.2    Niizuma, H.3    Ohira, M.4    Kamijo, T.5    Nakagawara, A.6
  • 17
    • 34249674388 scopus 로고    scopus 로고
    • The conserved CPH domains of Cul7 and PARC are protein-protein interaction modules that bind the tetramerization domain of p53
    • Kaustov L., Lukin J., Lemak A., Duan S., Ho M., Doherty R., Penn L.Z., and Arrowsmith C.H. The conserved CPH domains of Cul7 and PARC are protein-protein interaction modules that bind the tetramerization domain of p53. J. Biol. Chem. 282 (2007) 11300-11307
    • (2007) J. Biol. Chem. , vol.282 , pp. 11300-11307
    • Kaustov, L.1    Lukin, J.2    Lemak, A.3    Duan, S.4    Ho, M.5    Doherty, R.6    Penn, L.Z.7    Arrowsmith, C.H.8
  • 18
    • 0033559256 scopus 로고    scopus 로고
    • A leucine-rich nuclear export signal in the p53 tetramerization domain: regulation of subcellular localization and p53 activity by NES masking
    • Stommel J.M., Marchenko N.D., Jimenez G.S., Moll U.M., Hope T.J., and Wahl G.M. A leucine-rich nuclear export signal in the p53 tetramerization domain: regulation of subcellular localization and p53 activity by NES masking. EMBO J. 18 (1999) 1660-1672
    • (1999) EMBO J. , vol.18 , pp. 1660-1672
    • Stommel, J.M.1    Marchenko, N.D.2    Jimenez, G.S.3    Moll, U.M.4    Hope, T.J.5    Wahl, G.M.6
  • 19
    • 0030448760 scopus 로고    scopus 로고
    • Cytoplasmically sequestered wild-type p53 protein in neuroblastoma is relocated to the nucleus by a C-terminal peptide
    • Ostermeyer A.G., Runko E., Winkfield B., Ahn B., and Moll U.M. Cytoplasmically sequestered wild-type p53 protein in neuroblastoma is relocated to the nucleus by a C-terminal peptide. Proc. Natl. Acad. Sci. USA 93 (1996) 15190-15194
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15190-15194
    • Ostermeyer, A.G.1    Runko, E.2    Winkfield, B.3    Ahn, B.4    Moll, U.M.5
  • 21
    • 0031435461 scopus 로고    scopus 로고
    • Use of a membrane-localized green fluorescent protein allows simultaneous identification of transfected cells and cell cycle analysis by flow cytometry
    • Kalejta R.F., Shenk T., and Beavis A.J. Use of a membrane-localized green fluorescent protein allows simultaneous identification of transfected cells and cell cycle analysis by flow cytometry. Cytometry 29 (1997) 286-291
    • (1997) Cytometry , vol.29 , pp. 286-291
    • Kalejta, R.F.1    Shenk, T.2    Beavis, A.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.