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Volumn 108, Issue 12, 2013, Pages 2495-2504

P28, A first in class peptide inhibitor of cop1 binding to p53

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN C JUN; PROTEIN MDM2; PROTEIN P28; PROTEIN P53; T 140; UBIQUITIN PROTEIN LIGASE COP1;

EID: 84879689690     PISSN: 00070920     EISSN: 15321827     Source Type: Journal    
DOI: 10.1038/bjc.2013.266     Document Type: Article
Times cited : (63)

References (51)
  • 1
    • 20444410796 scopus 로고    scopus 로고
    • Unique complex between bacterial azurin and tumor-suppressor protein p53
    • Apiyo D, Wittung-Stafshede P (2005) Unique complex between bacterial azurin and tumor-suppressor protein p53. Biochem Biophys Res Commun 332(4): 965-968.
    • (2005) Biochem Biophys Res Commun , vol.332 , Issue.4 , pp. 965-968
    • Apiyo, D.1    Wittung-Stafshede, P.2
  • 3
    • 0030048731 scopus 로고    scopus 로고
    • Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules
    • Belmont LD, Mitchison TJ (1996) Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules. Cell 84(4): 623-631.
    • (1996) Cell , vol.84 , Issue.4 , pp. 623-631
    • Belmont, L.D.1    Mitchison, T.J.2
  • 4
    • 0038165532 scopus 로고    scopus 로고
    • Characterization of human constitutive photomorphogenesis protein 1, a RING finger ubiquitin ligase that interacts with Jun transcription factors and modulates their transcriptional activity
    • Bianchi E, Denti S, Catena R, Rossetti G, Polo S, Gasparian S, Putignano S, Rogge L, Pardi R (2003) Characterization of human constitutive photomorphogenesis protein 1, a RING finger ubiquitin ligase that interacts with Jun transcription factors and modulates their transcriptional activity. J Biol Chem 278(22): 19682-19690.
    • (2003) J Biol Chem , vol.278 , Issue.22 , pp. 19682-19690
    • Bianchi, E.1    Denti, S.2    Catena, R.3    Rossetti, G.4    Polo, S.5    Gasparian, S.6    Putignano, S.7    Rogge, L.8    Pardi, R.9
  • 5
    • 73349110968 scopus 로고    scopus 로고
    • Atomic force spectroscopy in biological complex formation: Strategies and perspectives
    • Bizzarri AR, Cannistraro S (2009) Atomic force spectroscopy in biological complex formation: strategies and perspectives. J Phys Chem B 113(52): 16449-16464.
    • (2009) J Phys Chem B , vol.113 , Issue.52 , pp. 16449-16464
    • Bizzarri, A.R.1    Cannistraro, S.2
  • 6
    • 70349931469 scopus 로고    scopus 로고
    • A combined atomic force microscopy imaging and docking study to investigate the complex between p53 DNA binding domain and Azurin
    • Bizzarri AR, Di Agostino S, Andolfi L, Cannistraro S (2009) A combined atomic force microscopy imaging and docking study to investigate the complex between p53 DNA binding domain and Azurin. J Mol Recognit 22(6): 506-515.
    • (2009) J Mol Recognit , vol.22 , Issue.6 , pp. 506-515
    • Bizzarri, A.R.1    Di Agostino, S.2    Andolfi, L.3    Cannistraro, S.4
  • 10
    • 34948865835 scopus 로고    scopus 로고
    • Docking study and free energy simulation of the complex between p53 DNA-binding domain and azurin
    • De Grandis V, Bizzarri AR, Cannistraro S (2007) Docking study and free energy simulation of the complex between p53 DNA-binding domain and azurin. J Mol Recognit 20(4): 215-226.
    • (2007) J Mol Recognit , vol.20 , Issue.4 , pp. 215-226
    • De Grandis, V.1    Bizzarri, A.R.2    Cannistraro, S.3
  • 14
    • 33748604311 scopus 로고    scopus 로고
    • Differential response between the p53 ubiquitin-protein ligases Pirh2 and MdM2 following DNA damage in human cancer cells
    • Duan W, Gao L, Wu X, Zhang Y, Otterson GA, Villalona-Calero MA (2006) Differential response between the p53 ubiquitin-protein ligases Pirh2 and MdM2 following DNA damage in human cancer cells. Exp Cell Res 312(17): 3370-3378.
    • (2006) Exp Cell Res , vol.312 , Issue.17 , pp. 3370-3378
    • Duan, W.1    Gao, L.2    Wu, X.3    Zhang, Y.4    Otterson, G.A.5    Villalona-Calero, M.A.6
  • 15
    • 0030905284 scopus 로고    scopus 로고
    • MDM2 promotes the rapid degradation of p53
    • Haupt Y, Maya R, Kazaz A, Oren M (1997) MDM2 promotes the rapid degradation of p53. Nature 387(6630): 296-299.
    • (1997) Nature , vol.387 , Issue.6630 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 16
    • 27844494185 scopus 로고    scopus 로고
    • Interaction between secretogranin III and carboxypeptidase e facilitates prohormone sorting within secretory granules
    • Hosaka M, Watanabe T, Sakai Y, Kato T, Takeuchi T (2005) Interaction between secretogranin III and carboxypeptidase E facilitates prohormone sorting within secretory granules. J Cell Sci 118(Part 20): 4785-4795.
    • (2005) J Cell Sci , vol.118 , Issue.PART 20 , pp. 4785-4795
    • Hosaka, M.1    Watanabe, T.2    Sakai, Y.3    Kato, T.4    Takeuchi, T.5
  • 18
    • 0042066359 scopus 로고    scopus 로고
    • Melanoma cells can tolerate high levels of transcriptionally active endogenous p53 but are sensitive to retrovirus-transduced p53
    • Kichina JV, Rauth S, Das Gupta TK, Gudkov AV (2003) Melanoma cells can tolerate high levels of transcriptionally active endogenous p53 but are sensitive to retrovirus-transduced p53. Oncogene 22(31): 4911-4917.
    • (2003) Oncogene , vol.22 , Issue.31 , pp. 4911-4917
    • Kichina, J.V.1    Rauth, S.2    Das Gupta, T.K.3    Gudkov, A.V.4
  • 19
    • 77956563054 scopus 로고    scopus 로고
    • The novel tryptamine derivative JNJ-26854165 induces wild-type p53-and E2F1-mediated apoptosis in acute myeloid and lymphoid leukemias
    • Kojima K, Burks JK, Arts J, Andreeff M (2010) The novel tryptamine derivative JNJ-26854165 induces wild-type p53-and E2F1-mediated apoptosis in acute myeloid and lymphoid leukemias. Mol Cancer Ther 9(9): 2545-2557.
    • (2010) Mol Cancer Ther , vol.9 , Issue.9 , pp. 2545-2557
    • Kojima, K.1    Burks, J.K.2    Arts, J.3    Andreeff, M.4
  • 20
    • 77957963055 scopus 로고    scopus 로고
    • Achieving reliability and high accuracy in automated protein docking: ClusPro, PIPER, SDU, and stability analysis in CAPRI rounds 13-19
    • Kozakov D, Hall DR, Beglov D, Brenke R, Comeau SR, Shen Y, Li K, Zheng J, Vakili P, Paschalidis I, Vajda S (2010) Achieving reliability and high accuracy in automated protein docking: ClusPro, PIPER, SDU, and stability analysis in CAPRI rounds 13-19. Proteins 78(15): 3124-3130.
    • (2010) Proteins , vol.78 , Issue.15 , pp. 3124-3130
    • Kozakov, D.1    Hall, D.R.2    Beglov, D.3    Brenke, R.4    Comeau, S.R.5    Shen, Y.6    Li, K.7    Zheng, J.8    Vakili, P.9    Paschalidis, I.10    Vajda, S.11
  • 21
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutat MH, Jones SN, Vousden KH (1997) Regulation of p53 stability by Mdm2. Nature 387(6630): 299-303.
    • (1997) Nature , vol.387 , Issue.6630 , pp. 299-303
    • Kubbutat, M.H.1    Jones, S.N.2    Vousden, K.H.3
  • 23
    • 84870828710 scopus 로고    scopus 로고
    • Cell-type, dose, and mutation-type specificity dictate mutant p53 functions in vivo
    • Lee MK, Teoh WW, Phang BH, Tong WM, Wang ZQ, Sabapathy K (2012) Cell-type, dose, and mutation-type specificity dictate mutant p53 functions in vivo. Cancer Cell 22(6): 751-764.
    • (2012) Cancer Cell , vol.22 , Issue.6 , pp. 751-764
    • Lee, M.K.1    Teoh, W.W.2    Phang, B.H.3    Tong, W.M.4    Wang, Z.Q.5    Sabapathy, K.6
  • 28
    • 0029742781 scopus 로고    scopus 로고
    • Differential activation of target cellular promoters by p53 mutants with impaired apoptotic function
    • Ludwig RL, Bates S, Vousden KH (1996) Differential activation of target cellular promoters by p53 mutants with impaired apoptotic function. Mol Cell Biol 16(9): 4952-4960.
    • (1996) Mol Cell Biol , vol.16 , Issue.9 , pp. 4952-4960
    • Ludwig, R.L.1    Bates, S.2    Vousden, K.H.3
  • 31
    • 0037329056 scopus 로고    scopus 로고
    • The p53-Mdm2 module and the ubiquitin system
    • Michael D, Oren M (2003) The p53-Mdm2 module and the ubiquitin system. Semin Cancer Biol 13(1): 49-58.
    • (2003) Semin Cancer Biol , vol.13 , Issue.1 , pp. 49-58
    • Michael, D.1    Oren, M.2
  • 33
    • 0036258111 scopus 로고    scopus 로고
    • The IARC TP53 database: New online mutation analysis and recommendations to users
    • Olivier M, Eeles R, Hollstein M, Khan MA, Harris CC, Hainaut P (2002) The IARC TP53 database: new online mutation analysis and recommendations to users. Hum Mutat 19(6): 607-614.
    • (2002) Hum Mutat , vol.19 , Issue.6 , pp. 607-614
    • Olivier, M.1    Eeles, R.2    Hollstein, M.3    Khan, M.A.4    Harris, C.C.5    Hainaut, P.6
  • 36
    • 59549088662 scopus 로고    scopus 로고
    • ProtorP: A protein-protein interaction analysis server
    • Reynolds C, Damerell D, Jones S (2009) ProtorP: a protein-protein interaction analysis server. Bioinformatics 25(3): 413-414.
    • (2009) Bioinformatics , vol.25 , Issue.3 , pp. 413-414
    • Reynolds, C.1    Damerell, D.2    Jones, S.3
  • 37
    • 3142754273 scopus 로고    scopus 로고
    • The topoisomerase I-and p53-binding protein topors is differentially expressed in normal and malignant human tissues and may function as a tumor suppressor
    • Saleem A, Dutta J, Malegaonkar D, Rasheed F, Rasheed Z, Rajendra R, Marshall H, Luo M, Li H, Rubin EH (2004) The topoisomerase I-and p53-binding protein topors is differentially expressed in normal and malignant human tissues and may function as a tumor suppressor. Oncogene 23(31): 5293-5300.
    • (2004) Oncogene , vol.23 , Issue.31 , pp. 5293-5300
    • Saleem, A.1    Dutta, J.2    Malegaonkar, D.3    Rasheed, F.4    Rasheed, Z.5    Rajendra, R.6    Marshall, H.7    Luo, M.8    Li, H.9    Rubin, E.H.10
  • 38
    • 0026446686 scopus 로고
    • Identification of a minimal transforming domain of p53: Negative dominance through abrogation of sequence-specific DNA binding
    • Shaulian E, Zauberman A, Ginsberg D, Oren M (1992) Identification of a minimal transforming domain of p53: negative dominance through abrogation of sequence-specific DNA binding. Mol Cell Biol 12(12): 5581-5592.
    • (1992) Mol Cell Biol , vol.12 , Issue.12 , pp. 5581-5592
    • Shaulian, E.1    Zauberman, A.2    Ginsberg, D.3    Oren, M.4
  • 40
    • 39749143144 scopus 로고    scopus 로고
    • Probing the interaction between p53 and the bacterial protein azurin by single molecule force spectroscopy
    • Taranta M, Bizzarri AR, Cannistraro S (2008) Probing the interaction between p53 and the bacterial protein azurin by single molecule force spectroscopy. J Mol Recognit 21(1): 63-70.
    • (2008) J Mol Recognit , vol.21 , Issue.1 , pp. 63-70
    • Taranta, M.1    Bizzarri, A.R.2    Cannistraro, S.3
  • 42
    • 43249084473 scopus 로고    scopus 로고
    • Impact of low-frequency hotspot mutation R282Q on the structure of p53 DNA-binding domain as revealed by crystallography at 1.54 angstroms resolution
    • Tu C, Tan YH, Shaw G, Zhou Z, Bai Y, Luo R, Ji X (2008) Impact of low-frequency hotspot mutation R282Q on the structure of p53 DNA-binding domain as revealed by crystallography at 1.54 angstroms resolution. Acta Crystallogr D Biol Crystallogr 64(Pt 5): 471-477.
    • (2008) Acta Crystallogr D Biol Crystallogr , vol.64 , Issue.PART 5 , pp. 471-477
    • Tu, C.1    Tan, Y.H.2    Shaw, G.3    Zhou, Z.4    Bai, Y.5    Luo, R.6    Ji, X.7
  • 44
    • 78651089988 scopus 로고    scopus 로고
    • Interplay between MDM2, MDMX, Pirh2 and COP1: The negative regulators of p53
    • Wang L, He G, Zhang P, Wang X, Jiang M, Yu L (2011) Interplay between MDM2, MDMX, Pirh2 and COP1: the negative regulators of p53. Mol Biol Rep 38(1): 229-236.
    • (2011) Mol Biol Rep , vol.38 , Issue.1 , pp. 229-236
    • Wang, L.1    He, G.2    Zhang, P.3    Wang, X.4    Jiang, M.5    Yu, L.6
  • 46
    • 0031912860 scopus 로고    scopus 로고
    • Assessment of sequence-based p53 gene analysis in human breast cancer: Messenger RNA in comparison with genomic DNA targets
    • Williams C, Norberg T, Ahmadian A, Ponten F, Bergh J, Inganas M, Lundeberg J, Uhlen M (1998) Assessment of sequence-based p53 gene analysis in human breast cancer: messenger RNA in comparison with genomic DNA targets. Clin Chem 44(3): 455-462.
    • (1998) Clin Chem , vol.44 , Issue.3 , pp. 455-462
    • Williams, C.1    Norberg, T.2    Ahmadian, A.3    Ponten, F.4    Bergh, J.5    Inganas, M.6    Lundeberg, J.7    Uhlen, M.8
  • 47
    • 33646799132 scopus 로고    scopus 로고
    • Strategies for therapeutic targeting of the p53 pathway in cancer
    • Wiman KG (2006) Strategies for therapeutic targeting of the p53 pathway in cancer. Cell Death Differ 13(6): 921-926.
    • (2006) Cell Death Differ , vol.13 , Issue.6 , pp. 921-926
    • Wiman, K.G.1
  • 48
    • 25144449123 scopus 로고    scopus 로고
    • Internalization of bacterial redox protein azurin in mammalian cells: Entry domain and specificity
    • Yamada T, Fialho AM, Punj V, Bratescu L, Gupta TK, Chakrabarty AM (2005) Internalization of bacterial redox protein azurin in mammalian cells: entry domain and specificity. Cell Microbiol 7(10): 1418-1431.
    • (2005) Cell Microbiol , vol.7 , Issue.10 , pp. 1418-1431
    • Yamada, T.1    Fialho, A.M.2    Punj, V.3    Bratescu, L.4    Gupta, T.K.5    Chakrabarty, A.M.6
  • 51
    • 33746012703 scopus 로고    scopus 로고
    • Mutational analysis of the p53 core domain L1 loop
    • Zupnick A, Prives C (2006) Mutational analysis of the p53 core domain L1 loop. J Biol Chem 281(29): 20464-20473.
    • (2006) J Biol Chem , vol.281 , Issue.29 , pp. 20464-20473
    • Zupnick, A.1    Prives, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.