메뉴 건너뛰기




Volumn 20, Issue 1, 2008, Pages 90-96

Restoration of p53 to limit tumor growth

Author keywords

Acridine derivatives; Carboline derivatives; CP 31398; Nutlins; p53; p63; p73; PRIMA 1; Transcriptional activation

Indexed keywords

4 (3 DIMETHYLAMINOPROPYLAMINO) 2 (4 METHOXYSTYRYL)QUINAZOLINE; ADENOVIRUS VECTOR; ANTINEOPLASTIC AGENT; DOXORUBICIN; ELLIPTICINE; IMIDAZOLINE DERIVATIVE; NUTLIN; PRIMA 1; PROTEIN MDM2; PROTEIN P53; PROTEIN P63; PROTEIN P73; RETROVIRUS VECTOR; UNCLASSIFIED DRUG;

EID: 36549009637     PISSN: 10408746     EISSN: None     Source Type: Journal    
DOI: 10.1097/CCO.0b013e3282f31d6f     Document Type: Review
Times cited : (108)

References (68)
  • 1
    • 0031987277 scopus 로고    scopus 로고
    • Regulation of p53 downstream genes
    • El-Deiry WS. Regulation of p53 downstream genes. Semin Cancer Biol 1998; 8:345-357.
    • (1998) Semin Cancer Biol , vol.8 , pp. 345-357
    • El-Deiry, W.S.1
  • 3
    • 0348134742 scopus 로고    scopus 로고
    • Mono- versus polyubiquitination: Differential control of p53 fate by Mdm2
    • Li M, Brooks CL, Wu-Baer F, et al. Mono- versus polyubiquitination: differential control of p53 fate by Mdm2. Science 2003; 302:1972-1975.
    • (2003) Science , vol.302 , pp. 1972-1975
    • Li, M.1    Brooks, C.L.2    Wu-Baer, F.3
  • 4
    • 0028823020 scopus 로고    scopus 로고
    • Montes de Oca Luna R, Wagner DS, Lozano G. Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53. Nature 1995; 378:203-206.
    • Montes de Oca Luna R, Wagner DS, Lozano G. Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53. Nature 1995; 378:203-206.
  • 5
    • 0028834902 scopus 로고
    • Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
    • Jones SN, Roe AE, Donehower LA, Bradley A. Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53. Nature 1995; 378:206-208.
    • (1995) Nature , vol.378 , pp. 206-208
    • Jones, S.N.1    Roe, A.E.2    Donehower, L.A.3    Bradley, A.4
  • 6
    • 2342447397 scopus 로고    scopus 로고
    • The ubiquitin ligase COP1 is a critical negative regulator of p53
    • Dornan D, Wertz I, Shimizu H, et al. The ubiquitin ligase COP1 is a critical negative regulator of p53. Nature 2004; 429:86-92.
    • (2004) Nature , vol.429 , pp. 86-92
    • Dornan, D.1    Wertz, I.2    Shimizu, H.3
  • 7
    • 0037459377 scopus 로고    scopus 로고
    • Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation
    • Leng RP, Lin Y, Ma W, et al. Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation. Cell 2003; 112:779-791.
    • (2003) Cell , vol.112 , pp. 779-791
    • Leng, R.P.1    Lin, Y.2    Ma, W.3
  • 8
    • 33746648187 scopus 로고    scopus 로고
    • Tang J, Qu LK, Zhang J, et al. Critical role for Daxx in regulating Mdm2. Nat Cell Biol 2006; 8:855-862. Daxx, a death domain-associated protein, was shown to stabilize Mdm2. Downregulation of Daxx decreases Mdm2 levels, whereas overexpression of Daxx strongly stabilizes Mdm2. Daxx simultaneously binds to Mdm2 and the deubiquitinase Hausp, and it mediates the stabilizing effect of Hausp on Mdm2. In addition, Daxx enhances the intrinsic E3 activity of Mdm2 towards p53.
    • Tang J, Qu LK, Zhang J, et al. Critical role for Daxx in regulating Mdm2. Nat Cell Biol 2006; 8:855-862. Daxx, a death domain-associated protein, was shown to stabilize Mdm2. Downregulation of Daxx decreases Mdm2 levels, whereas overexpression of Daxx strongly stabilizes Mdm2. Daxx simultaneously binds to Mdm2 and the deubiquitinase Hausp, and it mediates the stabilizing effect of Hausp on Mdm2. In addition, Daxx enhances the intrinsic E3 activity of Mdm2 towards p53.
  • 9
    • 34249933682 scopus 로고    scopus 로고
    • Li L, Deng B, Xing G, et al. PACT is a negative regulator of p53 and essential for cell growth and embryonic development. Proc Natl Acad Sci USA 2007; 104:7951-7956. PACT can interact with Hdm2 and enhance Hdm2-mediated ubiquitination and degradation of p53 as a result of the increase of the p53-Hdm2 affinity. Consequently, PACT represses p53-dependent gene transcription. Knockdown of PACT significantly attenuates the p53-Hdm2 interaction, reduces p53 poly-ubiquitination, and enhances p53 accumulation, leading to both apoptosis and retardation of cell growth.
    • Li L, Deng B, Xing G, et al. PACT is a negative regulator of p53 and essential for cell growth and embryonic development. Proc Natl Acad Sci USA 2007; 104:7951-7956. PACT can interact with Hdm2 and enhance Hdm2-mediated ubiquitination and degradation of p53 as a result of the increase of the p53-Hdm2 affinity. Consequently, PACT represses p53-dependent gene transcription. Knockdown of PACT significantly attenuates the p53-Hdm2 interaction, reduces p53 poly-ubiquitination, and enhances p53 accumulation, leading to both apoptosis and retardation of cell growth.
  • 10
    • 34047261783 scopus 로고    scopus 로고
    • CARPs are ubiquitin ligases that promote MDM2-independent p53 and phospho-p53ser20 degradation
    • Yang W, Rozan LM, McDonald ER 3rd, et al. CARPs are ubiquitin ligases that promote MDM2-independent p53 and phospho-p53ser20 degradation. J Biol Chem 2007; 282:3273-3281.
    • (2007) J Biol Chem , vol.282 , pp. 3273-3281
    • Yang, W.1    Rozan, L.M.2    McDonald 3rd, E.R.3
  • 11
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Huibregtse JM, Scheffner M, Beaudenon S, Howley PM. A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc Natl Acad Sci USA 1995; 92:2563-2567.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2563-2567
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 12
    • 0032741446 scopus 로고    scopus 로고
    • Structure of an E6AP-UbcH7 complex: Insights into ubiquitination by the E2-E3 enzyme cascade
    • Huang L, Kinnucan E, Wang G, et al. Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Science 1999; 286:1321-1326.
    • (1999) Science , vol.286 , pp. 1321-1326
    • Huang, L.1    Kinnucan, E.2    Wang, G.3
  • 13
    • 10844280830 scopus 로고    scopus 로고
    • Adenoviral E1A targets Mdm4 to stabilize tumor suppressor p53
    • Li Z, Day CP, Yang JY, et al. Adenoviral E1A targets Mdm4 to stabilize tumor suppressor p53. Cancer Res 2004; 64:9080-9085.
    • (2004) Cancer Res , vol.64 , pp. 9080-9085
    • Li, Z.1    Day, C.P.2    Yang, J.Y.3
  • 14
    • 0028089283 scopus 로고
    • Adenovirus E1B oncoprotein tethers a transcriptional repression domain to p53
    • Yew PR, Liu X, Berk AJ. Adenovirus E1B oncoprotein tethers a transcriptional repression domain to p53. Genes Dev 1994; 8:190-202.
    • (1994) Genes Dev , vol.8 , pp. 190-202
    • Yew, P.R.1    Liu, X.2    Berk, A.J.3
  • 15
    • 0028108985 scopus 로고
    • Database of p53 gene somatic mutations in human tumors and cell lines
    • Hollstein M, Rice K, Greenblatt MS, et al. Database of p53 gene somatic mutations in human tumors and cell lines. Nucleic Acids Res 1994; 22:3551-3555.
    • (1994) Nucleic Acids Res , vol.22 , pp. 3551-3555
    • Hollstein, M.1    Rice, K.2    Greenblatt, M.S.3
  • 16
    • 0031869758 scopus 로고    scopus 로고
    • Predicting response to cancer chemotherapy: The role of p53
    • Weller M. Predicting response to cancer chemotherapy: the role of p53. Cell Tissue Res 1998; 292:435-445.
    • (1998) Cell Tissue Res , vol.292 , pp. 435-445
    • Weller, M.1
  • 17
    • 0035156737 scopus 로고    scopus 로고
    • Insights into cancer therapeutic design based on p53 and TRAIL receptor signaling
    • El-Deiry WS. Insights into cancer therapeutic design based on p53 and TRAIL receptor signaling. Cell Death Differ 2001; 8:1066-1075.
    • (2001) Cell Death Differ , vol.8 , pp. 1066-1075
    • El-Deiry, W.S.1
  • 18
    • 0034183775 scopus 로고    scopus 로고
    • Cell cycle control as a basis for cancer drug development
    • McDonald ER 3rd, El-Deiry WS. Cell cycle control as a basis for cancer drug development. Int J Oncol 2000; 16:871-886.
    • (2000) Int J Oncol , vol.16 , pp. 871-886
    • McDonald 3rd, E.R.1    El-Deiry, W.S.2
  • 19
    • 33746809119 scopus 로고    scopus 로고
    • 201 (Advexin): Adenoviral p53 gene therapy for cancer
    • Gabrilovich DI. INGN 201 (Advexin): adenoviral p53 gene therapy for cancer. Expert Opin Biol Ther 2006; 6:823-832.
    • (2006) Expert Opin Biol Ther , vol.6 , pp. 823-832
    • Gabrilovich, D.I.1
  • 20
    • 10744221485 scopus 로고    scopus 로고
    • In vivo activation of the p53 pathway by small-molecule antagonists of MDM2
    • Vassilev LT, Vu BT, Graves B, et al. In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science 2004; 303:844-848.
    • (2004) Science , vol.303 , pp. 844-848
    • Vassilev, L.T.1    Vu, B.T.2    Graves, B.3
  • 21
    • 33845901313 scopus 로고    scopus 로고
    • MDM2 inhibitors for cancer therapy
    • Vassilev LT. MDM2 inhibitors for cancer therapy. Trends Mol Med 2007; 13:23-31.
    • (2007) Trends Mol Med , vol.13 , pp. 23-31
    • Vassilev, L.T.1
  • 22
    • 0030961889 scopus 로고    scopus 로고
    • Restoration of the growth suppression function of mutant p53 by a synthetic peptide derived from the p53 C-terminal domain
    • Selivanova G, Iotsova V, Okan I, et al. Restoration of the growth suppression function of mutant p53 by a synthetic peptide derived from the p53 C-terminal domain. Nat Med 1997; 3:632-638.
    • (1997) Nat Med , vol.3 , pp. 632-638
    • Selivanova, G.1    Iotsova, V.2    Okan, I.3
  • 23
    • 0032911047 scopus 로고    scopus 로고
    • Reactivation of mutant p53 through interaction of a C-terminal peptide with the core domain
    • Selivanova G, Ryabchenko L, Jansson E, et al. Reactivation of mutant p53 through interaction of a C-terminal peptide with the core domain. Mol Cell Biol 1999; 19:3395-3402.
    • (1999) Mol Cell Biol , vol.19 , pp. 3395-3402
    • Selivanova, G.1    Ryabchenko, L.2    Jansson, E.3
  • 24
    • 0035940401 scopus 로고    scopus 로고
    • Peptides from the amino terminal mdm-2-binding domain of p53, designed from conformational analysis, are selectively cytotoxic to transformed cells
    • Kanovsky M, Raffo A, Drew L, et al. Peptides from the amino terminal mdm-2-binding domain of p53, designed from conformational analysis, are selectively cytotoxic to transformed cells. Proc Natl Acad Sci USA 2001; 98:12438-12443.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12438-12443
    • Kanovsky, M.1    Raffo, A.2    Drew, L.3
  • 25
    • 0037435045 scopus 로고    scopus 로고
    • Preferential induction of necrosis in human breast cancer cells by a p53 peptide derived from the MDM2 binding site
    • Do TN, Rosal RV, Drew L, et al. Preferential induction of necrosis in human breast cancer cells by a p53 peptide derived from the MDM2 binding site. Oncogene 2003; 22:1431-1444.
    • (2003) Oncogene , vol.22 , pp. 1431-1444
    • Do, T.N.1    Rosal, R.V.2    Drew, L.3
  • 26
    • 0037154149 scopus 로고    scopus 로고
    • A peptide that binds and stabilizes p53 core domain: Chaperone strategy for rescue of oncogenic mutants
    • Friedler A, Hansson LO, Veprintsev DB, et al. A peptide that binds and stabilizes p53 core domain: chaperone strategy for rescue of oncogenic mutants. Proc Natl Acad Sci USA 2002; 99:937-942.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 937-942
    • Friedler, A.1    Hansson, L.O.2    Veprintsev, D.B.3
  • 27
    • 0034603897 scopus 로고    scopus 로고
    • An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo
    • Midgley CA, Desterro JM, Saville MK, et al. An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo. Oncogene 2000; 19:2312-2323.
    • (2000) Oncogene , vol.19 , pp. 2312-2323
    • Midgley, C.A.1    Desterro, J.M.2    Saville, M.K.3
  • 28
    • 4344662352 scopus 로고    scopus 로고
    • Targeting p53 by PTD-mediated transduction
    • Wang W, El-Deiry WS. Targeting p53 by PTD-mediated transduction. Trends Biotechnol 2004; 22:431-434.
    • (2004) Trends Biotechnol , vol.22 , pp. 431-434
    • Wang, W.1    El-Deiry, W.S.2
  • 29
    • 19344365470 scopus 로고    scopus 로고
    • Treatment of terminal peritoneal carcinomatosis by a transducible p53-activating peptide
    • Snyder EL, Meade BR, Saenz CC, Dowdy SF. Treatment of terminal peritoneal carcinomatosis by a transducible p53-activating peptide. PLoS Biol 2004; 2:E36.
    • (2004) PLoS Biol , vol.2
    • Snyder, E.L.1    Meade, B.R.2    Saenz, C.C.3    Dowdy, S.F.4
  • 30
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • Wadia JS, Stan RV, Dowdy SF. Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nat Med 2004; 10:310-315.
    • (2004) Nat Med , vol.10 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 31
    • 0030896451 scopus 로고    scopus 로고
    • Correcting temperature-sensitive protein folding defects
    • Brown CR, Hong-Brown LQ, Welch WJ. Correcting temperature-sensitive protein folding defects. J Clin Invest 1997; 99:1432-1444.
    • (1997) J Clin Invest , vol.99 , pp. 1432-1444
    • Brown, C.R.1    Hong-Brown, L.Q.2    Welch, W.J.3
  • 32
    • 0031416652 scopus 로고    scopus 로고
    • The DNA binding regulatory domain of p53: See the C
    • Wolkowicz R, Rotter V. The DNA binding regulatory domain of p53: see the C. Pathol Biol (Paris) 1997; 45:785-796.
    • (1997) Pathol Biol (Paris) , vol.45 , pp. 785-796
    • Wolkowicz, R.1    Rotter, V.2
  • 34
    • 0033601370 scopus 로고    scopus 로고
    • Pharmacological rescue of mutant p53 conformation and function
    • Foster BA, Coffey HA, Morin MJ, Rastinejad F. Pharmacological rescue of mutant p53 conformation and function. Science 1999; 286:2507-2510.
    • (1999) Science , vol.286 , pp. 2507-2510
    • Foster, B.A.1    Coffey, H.A.2    Morin, M.J.3    Rastinejad, F.4
  • 35
    • 85047687410 scopus 로고    scopus 로고
    • The mutant p53-conformation modifying drug, CP-31398, can induce apoptosis of human cancer cells and can stabilize wild-type p53 protein
    • Takimoto R, Wang W, Dicker DT, et al. The mutant p53-conformation modifying drug, CP-31398, can induce apoptosis of human cancer cells and can stabilize wild-type p53 protein. Cancer Biol Ther 2002; 1:47-55.
    • (2002) Cancer Biol Ther , vol.1 , pp. 47-55
    • Takimoto, R.1    Wang, W.2    Dicker, D.T.3
  • 36
    • 0037370357 scopus 로고    scopus 로고
    • Stabilization of p53 by CP-31398 inhibits ubiquitination without altering phosphorylation at serine 15 or 20 or MDM2 binding
    • Wang W, Takimoto R, Rastinejad F, El-Deiry WS. Stabilization of p53 by CP-31398 inhibits ubiquitination without altering phosphorylation at serine 15 or 20 or MDM2 binding. Mol Cell Biol 2003; 23:2171-2181.
    • (2003) Mol Cell Biol , vol.23 , pp. 2171-2181
    • Wang, W.1    Takimoto, R.2    Rastinejad, F.3    El-Deiry, W.S.4
  • 37
    • 0037192628 scopus 로고    scopus 로고
    • Characterization of the p53-rescue drug CP-31398 in vitro and in living cells
    • Rippin TM, Bykov VJ, Freund SM, et al. Characterization of the p53-rescue drug CP-31398 in vitro and in living cells. Oncogene 2002; 21:2119-2129.
    • (2002) Oncogene , vol.21 , pp. 2119-2129
    • Rippin, T.M.1    Bykov, V.J.2    Freund, S.M.3
  • 38
    • 0027407260 scopus 로고
    • Wild-type p53 adopts a 'mutant'-like conformation when bound to DNA
    • Halazonetis TD, Davis LJ, Kandil AN. Wild-type p53 adopts a 'mutant'-like conformation when bound to DNA. EMBO J 1993; 12:1021-1028.
    • (1993) EMBO J , vol.12 , pp. 1021-1028
    • Halazonetis, T.D.1    Davis, L.J.2    Kandil, A.N.3
  • 39
    • 0037447175 scopus 로고    scopus 로고
    • A peroxisome proliferator-activated receptor-gamma agonist and the p53 rescue drug CP-31398 inhibit the spontaneous immortalization of breast epithelial cells
    • Herbert BS, Pearce VP, Hynan LS, et al. A peroxisome proliferator-activated receptor-gamma agonist and the p53 rescue drug CP-31398 inhibit the spontaneous immortalization of breast epithelial cells. Cancer Res 2003; 63:1914-1919.
    • (2003) Cancer Res , vol.63 , pp. 1914-1919
    • Herbert, B.S.1    Pearce, V.P.2    Hynan, L.S.3
  • 40
    • 0036352592 scopus 로고    scopus 로고
    • The p53 stabilizing compound CP-31398 induces apoptosis by activating the intrinsic Bax/mitochondrial/caspase-9 pathway
    • Luu Y, Bush J, Cheung KJ Jr, Li G. The p53 stabilizing compound CP-31398 induces apoptosis by activating the intrinsic Bax/mitochondrial/caspase-9 pathway. Exp Cell Res 2002; 276:214-222.
    • (2002) Exp Cell Res , vol.276 , pp. 214-222
    • Luu, Y.1    Bush, J.2    Cheung Jr, K.J.3    Li, G.4
  • 41
    • 0036128899 scopus 로고    scopus 로고
    • Restoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound
    • Bykov VJ, Issaeva N, Shilov A, et al. Restoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound. Nat Med 2002; 8:282-288.
    • (2002) Nat Med , vol.8 , pp. 282-288
    • Bykov, V.J.1    Issaeva, N.2    Shilov, A.3
  • 42
    • 0036949663 scopus 로고    scopus 로고
    • Mutant p53-dependent growth suppression distinguishes PRIMA-1 from known anticancer drugs: A statistical analysis of information in the National Cancer Institute database
    • Bykov VJ, Issaeva N, Selivanova G, Wiman KG. Mutant p53-dependent growth suppression distinguishes PRIMA-1 from known anticancer drugs: a statistical analysis of information in the National Cancer Institute database. Carcinogenesis 2002; 23:2011-2018.
    • (2002) Carcinogenesis , vol.23 , pp. 2011-2018
    • Bykov, V.J.1    Issaeva, N.2    Selivanova, G.3    Wiman, K.G.4
  • 43
    • 1642565147 scopus 로고    scopus 로고
    • Extending nature's leads: The anticancer agent ellipticine
    • Garbett NC, Graves DE. Extending nature's leads: the anticancer agent ellipticine. Curr Med Chem Anticancer Agents 2004; 4:149-172.
    • (2004) Curr Med Chem Anticancer Agents , vol.4 , pp. 149-172
    • Garbett, N.C.1    Graves, D.E.2
  • 44
    • 0031911557 scopus 로고    scopus 로고
    • Mining the National Cancer Institute Anticancer Drug Discovery Database: Cluster analysis of ellipticine analogs with p53-inverse and central nervous system-selective patterns of activity
    • Shi LM, Myers TG, Fan Y, et al. Mining the National Cancer Institute Anticancer Drug Discovery Database: cluster analysis of ellipticine analogs with p53-inverse and central nervous system-selective patterns of activity. Mol Pharmacol 1998; 53:241-251.
    • (1998) Mol Pharmacol , vol.53 , pp. 241-251
    • Shi, L.M.1    Myers, T.G.2    Fan, Y.3
  • 45
    • 0043170883 scopus 로고    scopus 로고
    • Rescue of mutant p53 transcription function by ellipticine
    • Peng Y, Li C, Chen L, et al. Rescue of mutant p53 transcription function by ellipticine. Oncogene 2003; 22:4478-4487.
    • (2003) Oncogene , vol.22 , pp. 4478-4487
    • Peng, Y.1    Li, C.2    Chen, L.3
  • 46
    • 0030812331 scopus 로고    scopus 로고
    • Monoallelically expressed gene related to p53 at 1p36, a region frequently deleted in neuroblastoma and other human cancers
    • Kaghad M, Bonnet H, Yang A, et al. Monoallelically expressed gene related to p53 at 1p36, a region frequently deleted in neuroblastoma and other human cancers. Cell 1997; 90:809-819.
    • (1997) Cell , vol.90 , pp. 809-819
    • Kaghad, M.1    Bonnet, H.2    Yang, A.3
  • 47
    • 0033387525 scopus 로고    scopus 로고
    • Structure and function in the p53 family
    • Arrowsmith CH. Structure and function in the p53 family. Cell Death Differ 1999; 6:1169-1173.
    • (1999) Cell Death Differ , vol.6 , pp. 1169-1173
    • Arrowsmith, C.H.1
  • 48
    • 0034063604 scopus 로고    scopus 로고
    • A common polymorphism acts as an intragenic modifier of mutant p53 behaviour
    • Marin MC, Jost CA, Brooks LA, et al. A common polymorphism acts as an intragenic modifier of mutant p53 behaviour. Nat Genet 2000; 25:47-54.
    • (2000) Nat Genet , vol.25 , pp. 47-54
    • Marin, M.C.1    Jost, C.A.2    Brooks, L.A.3
  • 49
    • 0036468523 scopus 로고    scopus 로고
    • On the shoulders of giants: P63, p73 and the rise of p53
    • Yang A, Kaghad M, Caput D, McKeon F. On the shoulders of giants: p63, p73 and the rise of p53. Trends Genet 2002; 18:90-95.
    • (2002) Trends Genet , vol.18 , pp. 90-95
    • Yang, A.1    Kaghad, M.2    Caput, D.3    McKeon, F.4
  • 50
    • 0032161624 scopus 로고    scopus 로고
    • p63, a p53 homolog at 3q27-29, encodes multiple products with transactivating, death-inducing, and dominant-negative activities
    • Yang A, Kaghad M, Wang Y, et al. p63, a p53 homolog at 3q27-29, encodes multiple products with transactivating, death-inducing, and dominant-negative activities. Mol Cell 1998; 2:305-316.
    • (1998) Mol Cell , vol.2 , pp. 305-316
    • Yang, A.1    Kaghad, M.2    Wang, Y.3
  • 51
    • 0034192628 scopus 로고    scopus 로고
    • Regulation and function of the p53-related proteins: Same family, different rules
    • Lohrum MA, Vousden KH. Regulation and function of the p53-related proteins: same family, different rules. Trends Cell Biol 2000; 10:197-202.
    • (2000) Trends Cell Biol , vol.10 , pp. 197-202
    • Lohrum, M.A.1    Vousden, K.H.2
  • 52
    • 0034927749 scopus 로고    scopus 로고
    • p53 family update: P73 and p63 develop their own identities
    • Irwin MS, Kaelin WG. p53 family update: p73 and p63 develop their own identities. Cell Growth Differ 2001; 12:337-349.
    • (2001) Cell Growth Differ , vol.12 , pp. 337-349
    • Irwin, M.S.1    Kaelin, W.G.2
  • 53
    • 17444390129 scopus 로고    scopus 로고
    • Tumor predisposition in mice mutant for p63 and p73: Evidence for broader tumor suppressor functions for the p53 family
    • Flores ER, Sengupta S, Miller JB, et al. Tumor predisposition in mice mutant for p63 and p73: evidence for broader tumor suppressor functions for the p53 family. Cancer Cell 2005; 7:363-373.
    • (2005) Cancer Cell , vol.7 , pp. 363-373
    • Flores, E.R.1    Sengupta, S.2    Miller, J.B.3
  • 54
    • 0033594491 scopus 로고    scopus 로고
    • p63 is a p53 homologue required for limb and epidermal morphogenesis
    • Mills AA, Zheng B, Wang XJ, et al. p63 is a p53 homologue required for limb and epidermal morphogenesis. Nature 1999; 398:708-713.
    • (1999) Nature , vol.398 , pp. 708-713
    • Mills, A.A.1    Zheng, B.2    Wang, X.J.3
  • 55
    • 0033594485 scopus 로고    scopus 로고
    • p63 is essential for regenerative proliferation in limb, craniofacial and epithelial development
    • Yang A, Schweitzer R, Sun D, et al. p63 is essential for regenerative proliferation in limb, craniofacial and epithelial development. Nature 1999; 398:714-718.
    • (1999) Nature , vol.398 , pp. 714-718
    • Yang, A.1    Schweitzer, R.2    Sun, D.3
  • 56
    • 17544363909 scopus 로고    scopus 로고
    • p73-deficient mice have neurological, pheromonal and inflammatory defects but lack spontaneous tumours
    • Yang A, Walker N, Bronson R, et al. p73-deficient mice have neurological, pheromonal and inflammatory defects but lack spontaneous tumours. Nature 2000; 404:99-103.
    • (2000) Nature , vol.404 , pp. 99-103
    • Yang, A.1    Walker, N.2    Bronson, R.3
  • 57
    • 0033600267 scopus 로고    scopus 로고
    • DNA damage enables p73
    • White E, Prives C. DNA damage enables p73. Nature 1999; 399:734-735.
    • (1999) Nature , vol.399 , pp. 734-735
    • White, E.1    Prives, C.2
  • 58
    • 0041997348 scopus 로고    scopus 로고
    • Chemosensitivity linked to p73 function
    • Irwin MS, Kondo K, Marin MC, et al. Chemosensitivity linked to p73 function. Cancer Cell 2003; 3:403-410.
    • (2003) Cancer Cell , vol.3 , pp. 403-410
    • Irwin, M.S.1    Kondo, K.2    Marin, M.C.3
  • 59
    • 10744230945 scopus 로고    scopus 로고
    • p53 polymorphism influences response in cancer chemotherapy via modulation of p73-dependent apoptosis
    • Bergamaschi D, Gasco M, Hiller L, et al. p53 polymorphism influences response in cancer chemotherapy via modulation of p73-dependent apoptosis. Cancer Cell 2003; 3:387-402.
    • (2003) Cancer Cell , vol.3 , pp. 387-402
    • Bergamaschi, D.1    Gasco, M.2    Hiller, L.3
  • 60
    • 0042634489 scopus 로고    scopus 로고
    • p53 mutations and resistance to chemotherapy: A stab in the back for p73
    • Soussi T. p53 mutations and resistance to chemotherapy: a stab in the back for p73. Cancer Cell 2003; 3:303-305.
    • (2003) Cancer Cell , vol.3 , pp. 303-305
    • Soussi, T.1
  • 61
    • 0033881433 scopus 로고    scopus 로고
    • Down-regulation of p63 is required for epidermal UV-B-induced apoptosis
    • Liefer KM, Koster MI, Wang XJ, et al. Down-regulation of p63 is required for epidermal UV-B-induced apoptosis. Cancer Res 2000; 60:4016-4020.
    • (2000) Cancer Res , vol.60 , pp. 4016-4020
    • Liefer, K.M.1    Koster, M.I.2    Wang, X.J.3
  • 62
    • 0033168066 scopus 로고    scopus 로고
    • Overexpression of the wild type p73 gene in breast cancer tissues and cell lines
    • Zaika AI, Kovalev S, Marchenko ND, Moll UM. Overexpression of the wild type p73 gene in breast cancer tissues and cell lines. Cancer Res 1999; 59:3257-3263.
    • (1999) Cancer Res , vol.59 , pp. 3257-3263
    • Zaika, A.I.1    Kovalev, S.2    Marchenko, N.D.3    Moll, U.M.4
  • 63
    • 0035751937 scopus 로고    scopus 로고
    • Assessing TP53 status in human tumours to evaluate clinical outcome
    • Soussi T, Beroud C. Assessing TP53 status in human tumours to evaluate clinical outcome. Nat Rev Cancer 2001; 1:233-240.
    • (2001) Nat Rev Cancer , vol.1 , pp. 233-240
    • Soussi, T.1    Beroud, C.2
  • 64
    • 0037855838 scopus 로고    scopus 로고
    • Change of conformation of the DNA-binding domain of p53 is the only key element for binding of and interference with p73
    • Bensaad K, Le Bras M, Unsal K, et al. Change of conformation of the DNA-binding domain of p53 is the only key element for binding of and interference with p73. J Biol Chem 2003; 278:10546-10555.
    • (2003) J Biol Chem , vol.278 , pp. 10546-10555
    • Bensaad, K.1    Le Bras, M.2    Unsal, K.3
  • 65
    • 25144506616 scopus 로고    scopus 로고
    • Acridine derivatives activate p53 and induce tumor cell death through Bax
    • Wang W, Ho WC, Dicker DT, et al. Acridine derivatives activate p53 and induce tumor cell death through Bax. Cancer Biol Ther 2005; 4:893-898.
    • (2005) Cancer Biol Ther , vol.4 , pp. 893-898
    • Wang, W.1    Ho, W.C.2    Dicker, D.T.3
  • 66
    • 33746615125 scopus 로고    scopus 로고
    • Wang W, Kim SH, El-Deiry WS. Small-molecule modulators of p53 family signaling and antitumor effects in p53-deficient human colon tumor xenografts. Proc Natl Acad Sci USA 2006; 103:11003-11008. A number of small molecules were isolated that activate p53 reporter activity, increase expression of p53 target genes, such as p21(WAF1) or death receptor 5 (KILLER/DR5) of TRAIL, and induce apoptosis in p53 wild-type as well as p53-deficient tumor cells. Some of the compounds activate a p53 response by increasing p73 expression.
    • Wang W, Kim SH, El-Deiry WS. Small-molecule modulators of p53 family signaling and antitumor effects in p53-deficient human colon tumor xenografts. Proc Natl Acad Sci USA 2006; 103:11003-11008. A number of small molecules were isolated that activate p53 reporter activity, increase expression of p53 target genes, such as p21(WAF1) or death receptor 5 (KILLER/DR5) of TRAIL, and induce apoptosis in p53 wild-type as well as p53-deficient tumor cells. Some of the compounds activate a p53 response by increasing p73 expression.
  • 67
    • 34047165842 scopus 로고    scopus 로고
    • Restoration of wild-type p53 function in human tumors: Strategies for efficient cancer therapy
    • Wiman KG. Restoration of wild-type p53 function in human tumors: strategies for efficient cancer therapy. Adv Cancer Res 2007; 97:321-338.
    • (2007) Adv Cancer Res , vol.97 , pp. 321-338
    • Wiman, K.G.1
  • 68
    • 34147190124 scopus 로고    scopus 로고
    • A p53-derived apoptotic peptide derepresses p73 to cause tumor regression in vivo
    • Bell HS, Dufes C, O'Prey J, et al. A p53-derived apoptotic peptide derepresses p73 to cause tumor regression in vivo. J Clin Invest 2007; 117:1008-1018.
    • (2007) J Clin Invest , vol.117 , pp. 1008-1018
    • Bell, H.S.1    Dufes, C.2    O'Prey, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.