메뉴 건너뛰기




Volumn 22, Issue 4, 2013, Pages 747-764

Targeting the p53 Pathway

Author keywords

Apoptosis; FAK; Mdm 2; P53; Survival

Indexed keywords

3 (4 CHLOROPHENYL) 3 (1 HYDROXYMETHYLCYCLOPROPYLMETHOXY) 2 (4 NITROBENZYL) 2,3 DIHYDROISOINDOL 1 ONE; 4 (3 DIMETHYLAMINOPROPYLAMINO) 2 (4 METHOXYSTYRYL)QUINAZOLINE; ANTINEOPLASTIC AGENT; CELECOXIB; CONTUSUGENE LADENOVEC; DOXORUBICIN; ELLIPTICINE; FOCAL ADHESION KINASE; FOCAL ADHESION KINASE INHIBITOR; GENDICINE; LONTUCIREV; MI 219; MI 319; MI 43; MI 63; MIRA 3; NSC 319726; NSC 66811; NUTLIN 3; P53 REACTIVATION AND INDUCTION OF MASSIVE APOPTOSIS; PF 562271; PROTEIN MDM2; PROTEIN P53; REACTIVATION OF P53 AND INDUCTION OF TUMOR APOPTOSIS; REACTIVATION OF TRANSCRIPTIONAL RECEPTOR ACTIVITY; SCH 529074; STIMA 1; SULFONAMIDE; TD 665759; TERPHENYL 14; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84883556393     PISSN: 10553207     EISSN: 15585042     Source Type: Journal    
DOI: 10.1016/j.soc.2013.06.003     Document Type: Review
Times cited : (32)

References (124)
  • 1
    • 0030941458 scopus 로고    scopus 로고
    • P53, the cellular gatekeeper for growth and division
    • Levine A.J. p53, the cellular gatekeeper for growth and division. Cell 1997, 88:323-331.
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 2
    • 0026770424 scopus 로고
    • Wild-type p53 activates transcription invitro
    • Farmer G., Bargonetti J., Zhu H., et al. Wild-type p53 activates transcription invitro. Nature 1992, 358:83-86.
    • (1992) Nature , vol.358 , pp. 83-86
    • Farmer, G.1    Bargonetti, J.2    Zhu, H.3
  • 3
    • 34548085454 scopus 로고    scopus 로고
    • Focal adhesion kinase and p53 signaling in cancer cells
    • Golubovskaya V.M., Cance W.G. Focal adhesion kinase and p53 signaling in cancer cells. Int Rev Cytol 2007, 263:103-153.
    • (2007) Int Rev Cytol , vol.263 , pp. 103-153
    • Golubovskaya, V.M.1    Cance, W.G.2
  • 7
    • 0013484134 scopus 로고
    • Structural basis for the binding of proline-rich peptides to SH3 domains
    • Yu H., Chen J.K., Feng S., et al. Structural basis for the binding of proline-rich peptides to SH3 domains. Cell 1994, 76:933-945.
    • (1994) Cell , vol.76 , pp. 933-945
    • Yu, H.1    Chen, J.K.2    Feng, S.3
  • 8
    • 0043170851 scopus 로고    scopus 로고
    • The proline-rich region of mouse p53 influences transactivation and apoptosis but is largely dispensable for these functions
    • Edwards S.J., Hananeia L., Eccles M.R., et al. The proline-rich region of mouse p53 influences transactivation and apoptosis but is largely dispensable for these functions. Oncogene 2003, 22:4517-4523.
    • (2003) Oncogene , vol.22 , pp. 4517-4523
    • Edwards, S.J.1    Hananeia, L.2    Eccles, M.R.3
  • 9
    • 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
  • 10
    • 23644436345 scopus 로고    scopus 로고
    • Prospects for p53-based cancer therapy
    • Stoklsa T., Golab J. Prospects for p53-based cancer therapy. Acta Biochim Pol 2005, 52:321-328.
    • (2005) Acta Biochim Pol , vol.52 , pp. 321-328
    • Stoklsa, T.1    Golab, J.2
  • 11
    • 70349442548 scopus 로고    scopus 로고
    • The first 30 years of p53: growing ever more complex
    • Levine A.J., Oren M. The first 30 years of p53: growing ever more complex. Nat Rev Cancer 2009, 9:749-758.
    • (2009) Nat Rev Cancer , vol.9 , pp. 749-758
    • Levine, A.J.1    Oren, M.2
  • 12
    • 0025634118 scopus 로고
    • P53 gene mutations occur in combination with 17p allelic deletions as late events in colorectal tumorigenesis
    • Baker S.J., Preisinger A.C., Jessup J.M., et al. p53 gene mutations occur in combination with 17p allelic deletions as late events in colorectal tumorigenesis. Cancer Res 1990, 50:7717-7722.
    • (1990) Cancer Res , vol.50 , pp. 7717-7722
    • Baker, S.J.1    Preisinger, A.C.2    Jessup, J.M.3
  • 13
    • 0025312728 scopus 로고
    • Agenetic model for colorectal tumorigenesis
    • Fearon E.R., Vogelstein B. Agenetic model for colorectal tumorigenesis. Cell 1990, 61:759-767.
    • (1990) Cell , vol.61 , pp. 759-767
    • Fearon, E.R.1    Vogelstein, B.2
  • 14
    • 0032192140 scopus 로고    scopus 로고
    • The complexity of p53 modulation: emerging patterns from divergent signals
    • Giaccia A.J., Kastan M.B. The complexity of p53 modulation: emerging patterns from divergent signals. Genes Dev 1998, 12:2973-2983.
    • (1998) Genes Dev , vol.12 , pp. 2973-2983
    • Giaccia, A.J.1    Kastan, M.B.2
  • 15
    • 0036479115 scopus 로고    scopus 로고
    • Transcriptional repression of the anti-apoptotic survivin gene by wild type p53
    • Hoffman W.H., Biade S., Zilfou J.T., et al. Transcriptional repression of the anti-apoptotic survivin gene by wild type p53. JBiol Chem 2002, 277:3247-3257.
    • (2002) JBiol Chem , vol.277 , pp. 3247-3257
    • Hoffman, W.H.1    Biade, S.2    Zilfou, J.T.3
  • 16
    • 0035843156 scopus 로고    scopus 로고
    • Negative regulation of bcl-2 expression by p53 in hematopoietic cells
    • Wu Y., Mehew J.W., Heckman C.A., et al. Negative regulation of bcl-2 expression by p53 in hematopoietic cells. Oncogene 2001, 20:240-251.
    • (2001) Oncogene , vol.20 , pp. 240-251
    • Wu, Y.1    Mehew, J.W.2    Heckman, C.A.3
  • 17
    • 0035810054 scopus 로고    scopus 로고
    • Regulation of the G2/M transition by p53
    • Taylor W.R., Stark G.R. Regulation of the G2/M transition by p53. Oncogene 2001, 20:1803-1815.
    • (2001) Oncogene , vol.20 , pp. 1803-1815
    • Taylor, W.R.1    Stark, G.R.2
  • 18
    • 0034669312 scopus 로고    scopus 로고
    • The tumour suppressor protein p53 can repress transcription of cyclin B
    • Krause K., Wasner M., Reinhard W., et al. The tumour suppressor protein p53 can repress transcription of cyclin B. Nucleic Acids Res 2000, 28:4410-4418.
    • (2000) Nucleic Acids Res , vol.28 , pp. 4410-4418
    • Krause, K.1    Wasner, M.2    Reinhard, W.3
  • 19
    • 0034569902 scopus 로고    scopus 로고
    • P53-mediated negative regulation of stathmin/Op18 expression is associated with G(2)/M cell-cycle arrest
    • Johnsen J.I., Aurelio O.N., Kwaja Z., et al. p53-mediated negative regulation of stathmin/Op18 expression is associated with G(2)/M cell-cycle arrest. Int J Cancer 2000, 88:685-691.
    • (2000) Int J Cancer , vol.88 , pp. 685-691
    • Johnsen, J.I.1    Aurelio, O.N.2    Kwaja, Z.3
  • 20
    • 0029803281 scopus 로고    scopus 로고
    • Wild-type p53 negatively regulates the expression of a microtubule-associated protein
    • Murphy M., Hinman A., Levine A.J. Wild-type p53 negatively regulates the expression of a microtubule-associated protein. Genes Dev 1996, 10:2971-2980.
    • (1996) Genes Dev , vol.10 , pp. 2971-2980
    • Murphy, M.1    Hinman, A.2    Levine, A.J.3
  • 21
    • 0025784539 scopus 로고
    • Wild-type p53 induces apoptosis of myeloid leukaemic cells that is inhibited by interleukin-6
    • Yonish-Rouach E., Resnitzky D., Lotem J., et al. Wild-type p53 induces apoptosis of myeloid leukaemic cells that is inhibited by interleukin-6. Nature 1991, 352:345-347.
    • (1991) Nature , vol.352 , pp. 345-347
    • Yonish-Rouach, E.1    Resnitzky, D.2    Lotem, J.3
  • 22
    • 0038075338 scopus 로고    scopus 로고
    • Decision making by p53: life, death and cancer
    • Oren M. Decision making by p53: life, death and cancer. Cell Death Differ 2003, 10:431-442.
    • (2003) Cell Death Differ , vol.10 , pp. 431-442
    • Oren, M.1
  • 23
    • 0027451668 scopus 로고
    • P53-dependent apoptosis modulates the cytotoxicity of anticancer agents
    • Lowe S.W., Ruley H.E., Jacks T., et al. p53-dependent apoptosis modulates the cytotoxicity of anticancer agents. Cell 1993, 74:957-967.
    • (1993) Cell , vol.74 , pp. 957-967
    • Lowe, S.W.1    Ruley, H.E.2    Jacks, T.3
  • 24
    • 0028323294 scopus 로고
    • Abrogation of oncogene-associated apoptosis allows transformation of p53-deficient cells
    • Lowe S.W., Jacks T., Housman D.E., et al. Abrogation of oncogene-associated apoptosis allows transformation of p53-deficient cells. Proc Natl Acad Sci USA 1994, 91:2026-2030.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2026-2030
    • Lowe, S.W.1    Jacks, T.2    Housman, D.E.3
  • 25
    • 1542353401 scopus 로고    scopus 로고
    • Control of apoptosis by p53
    • Fridman J.S., Lowe S.W. Control of apoptosis by p53. Oncogene 2003, 22:9030-9040.
    • (2003) Oncogene , vol.22 , pp. 9030-9040
    • Fridman, J.S.1    Lowe, S.W.2
  • 26
    • 0029039421 scopus 로고
    • Overexpression of the focal adhesion kinase (p125FAK) in invasive human tumors
    • Owens L.V., Xu L., Craven R.J., et al. Overexpression of the focal adhesion kinase (p125FAK) in invasive human tumors. Cancer Res 1995, 55:2752-2755.
    • (1995) Cancer Res , vol.55 , pp. 2752-2755
    • Owens, L.V.1    Xu, L.2    Craven, R.J.3
  • 27
    • 48849112195 scopus 로고    scopus 로고
    • Focal adhesion kinase versus p53: apoptosis or survival?
    • Cance W.G., Golubovskaya V.M. Focal adhesion kinase versus p53: apoptosis or survival?. Sci Signal 2008, 1:pe22.
    • (2008) Sci Signal , vol.1
    • Cance, W.G.1    Golubovskaya, V.M.2
  • 28
    • 0034044795 scopus 로고    scopus 로고
    • Immunohistochemical analyses of focal adhesion kinase expression in benign and malignant human breast and colon tissues: correlation with preinvasive and invasive phenotypes
    • Cance W.G., Harris J.E., Iacocca M.V., et al. Immunohistochemical analyses of focal adhesion kinase expression in benign and malignant human breast and colon tissues: correlation with preinvasive and invasive phenotypes. Clin Cancer Res 2000, 6:2417-2423.
    • (2000) Clin Cancer Res , vol.6 , pp. 2417-2423
    • Cance, W.G.1    Harris, J.E.2    Iacocca, M.V.3
  • 29
    • 0029690892 scopus 로고    scopus 로고
    • Focal adhesion kinase as a marker of invasive potential in differentiated human thyroid cancer
    • Owens L.V., Xu L., Dent G.A., et al. Focal adhesion kinase as a marker of invasive potential in differentiated human thyroid cancer. Ann Surg Oncol 1996, 3:100-105.
    • (1996) Ann Surg Oncol , vol.3 , pp. 100-105
    • Owens, L.V.1    Xu, L.2    Dent, G.A.3
  • 30
    • 79955037380 scopus 로고    scopus 로고
    • Targeting focal adhesion kinase in cancer-part I
    • Golubovskaya V.M. Targeting focal adhesion kinase in cancer-part I. Anticancer Agents Med Chem 2010, 10:713.
    • (2010) Anticancer Agents Med Chem , vol.10 , pp. 713
    • Golubovskaya, V.M.1
  • 31
    • 0032547796 scopus 로고    scopus 로고
    • Extracellular matrix survival signals transduced by focal adhesion kinase suppress p53-mediated apoptosis
    • Ilic D., Almeida E.A., Schlaepfer D.D., et al. Extracellular matrix survival signals transduced by focal adhesion kinase suppress p53-mediated apoptosis. JCell Biol 1998, 143:547-560.
    • (1998) JCell Biol , vol.143 , pp. 547-560
    • Ilic, D.1    Almeida, E.A.2    Schlaepfer, D.D.3
  • 32
    • 9144256723 scopus 로고    scopus 로고
    • Squamous cell carcinoma cell aggregates escape suspension-induced, p53-mediated anoikis: Fibronectin and integrin {alpha} mediate survival signals through focal adhesion kinase
    • Zhang Y., Lu H., Dazin P., et al. Squamous cell carcinoma cell aggregates escape suspension-induced, p53-mediated anoikis: Fibronectin and integrin {alpha} mediate survival signals through focal adhesion kinase. JBiol Chem 2004, 279:48342-48349.
    • (2004) JBiol Chem , vol.279 , pp. 48342-48349
    • Zhang, Y.1    Lu, H.2    Dazin, P.3
  • 33
    • 10044290586 scopus 로고    scopus 로고
    • Focal adhesion kinase overexpression in endometrial neoplasia
    • Livasy C.A., Moore D., Cance W.G., et al. Focal adhesion kinase overexpression in endometrial neoplasia. Appl Immunohistochem Mol Morphol 2004, 12:342-345.
    • (2004) Appl Immunohistochem Mol Morphol , vol.12 , pp. 342-345
    • Livasy, C.A.1    Moore, D.2    Cance, W.G.3
  • 34
    • 2442583529 scopus 로고    scopus 로고
    • Cloning and characterization of the promoter region of human focal adhesion kinase gene: nuclear factor kappa B and p53 binding sites
    • Golubovskaya V., Kaur A., Cance W. Cloning and characterization of the promoter region of human focal adhesion kinase gene: nuclear factor kappa B and p53 binding sites. Biochim Biophys Acta 2004, 1678:111-125.
    • (2004) Biochim Biophys Acta , vol.1678 , pp. 111-125
    • Golubovskaya, V.1    Kaur, A.2    Cance, W.3
  • 35
    • 30344478870 scopus 로고    scopus 로고
    • Aglobal map of p53 transcription-factor binding sites in the human genome
    • Wei C.L., Wu Q., Vega V.B., et al. Aglobal map of p53 transcription-factor binding sites in the human genome. Cell 2006, 124:207-219.
    • (2006) Cell , vol.124 , pp. 207-219
    • Wei, C.L.1    Wu, Q.2    Vega, V.B.3
  • 36
    • 68549133222 scopus 로고    scopus 로고
    • FAK overexpression and p53 mutations are highly correlated in human breast cancer
    • Golubovskaya V.M., Conway-Dorsey K., Edmiston S.N., et al. FAK overexpression and p53 mutations are highly correlated in human breast cancer. Int J Cancer 2009, 125:1735-1738.
    • (2009) Int J Cancer , vol.125 , pp. 1735-1738
    • Golubovskaya, V.M.1    Conway-Dorsey, K.2    Edmiston, S.N.3
  • 37
    • 84867401795 scopus 로고    scopus 로고
    • In oral squamous cell carcinoma, high FAK expression is correlated with low P53 expression
    • Rosado P., Lequerica-Fernandez P., Pena I., et al. In oral squamous cell carcinoma, high FAK expression is correlated with low P53 expression. Virchows Arch 2012, 461:163-168.
    • (2012) Virchows Arch , vol.461 , pp. 163-168
    • Rosado, P.1    Lequerica-Fernandez, P.2    Pena, I.3
  • 38
    • 21644466387 scopus 로고    scopus 로고
    • Direct Interaction of the N-terminal domain of focal adhesion kinase with the N-terminal transactivation domain of p53
    • Golubovskaya V.M., Finch R., Cance W.G. Direct Interaction of the N-terminal domain of focal adhesion kinase with the N-terminal transactivation domain of p53. JBiol Chem 2005, 280:25008-25021.
    • (2005) JBiol Chem , vol.280 , pp. 25008-25021
    • Golubovskaya, V.M.1    Finch, R.2    Cance, W.G.3
  • 39
    • 0036433351 scopus 로고    scopus 로고
    • The focal adhesion kinase amino-terminal domain localises to nuclei and intercellular junctions in HEK 293 and MDCK cells independently of tyrosine 397 and the carboxy-terminal domain
    • Stewart A., Ham C., Zachary I. The focal adhesion kinase amino-terminal domain localises to nuclei and intercellular junctions in HEK 293 and MDCK cells independently of tyrosine 397 and the carboxy-terminal domain. Biochem Biophys Res Commun 2002, 299:62-73.
    • (2002) Biochem Biophys Res Commun , vol.299 , pp. 62-73
    • Stewart, A.1    Ham, C.2    Zachary, I.3
  • 40
    • 0038005805 scopus 로고    scopus 로고
    • Focal adhesion kinase N-terminus in breast carcinoma cells induces rounding, detachment and apoptosis
    • Beviglia L., Golubovskaya V., Xu L., et al. Focal adhesion kinase N-terminus in breast carcinoma cells induces rounding, detachment and apoptosis. Biochem J 2003, 373:201-210.
    • (2003) Biochem J , vol.373 , pp. 201-210
    • Beviglia, L.1    Golubovskaya, V.2    Xu, L.3
  • 41
    • 0347356250 scopus 로고    scopus 로고
    • Nuclear import of N-terminal FAK by activation of the FcepsilonRI receptor in RBL-2H3 cells
    • Jones G., Stewart G. Nuclear import of N-terminal FAK by activation of the FcepsilonRI receptor in RBL-2H3 cells. Biochem Biophys Res Commun 2004, 314:39-45.
    • (2004) Biochem Biophys Res Commun , vol.314 , pp. 39-45
    • Jones, G.1    Stewart, G.2
  • 42
    • 0034610067 scopus 로고    scopus 로고
    • Nuclear localization and apoptotic regulation of an amino-terminal domain focal adhesion kinase fragment in endothelial cells
    • Lobo M., Zachary I. Nuclear localization and apoptotic regulation of an amino-terminal domain focal adhesion kinase fragment in endothelial cells. Biochem Biophys Res Commun 2000, 276:1068-1074.
    • (2000) Biochem Biophys Res Commun , vol.276 , pp. 1068-1074
    • Lobo, M.1    Zachary, I.2
  • 43
    • 4644250606 scopus 로고    scopus 로고
    • Cytoplasmic p53: bax and forward
    • Chipuk J.E., Green D.R. Cytoplasmic p53: bax and forward. Cell Cycle 2004, 3:429-431.
    • (2004) Cell Cycle , vol.3 , pp. 429-431
    • Chipuk, J.E.1    Green, D.R.2
  • 44
    • 41649107660 scopus 로고    scopus 로고
    • The 7-amino-acid site in the proline-rich region of the N-terminal domain of p53 is involved in the interaction with FAK and is critical for p53 functioning
    • Golubovskaya V.M., Finch R., Zheng M., et al. The 7-amino-acid site in the proline-rich region of the N-terminal domain of p53 is involved in the interaction with FAK and is critical for p53 functioning. Biochem J 2008, 411:151-160.
    • (2008) Biochem J , vol.411 , pp. 151-160
    • Golubovskaya, V.M.1    Finch, R.2    Zheng, M.3
  • 45
    • 77956626576 scopus 로고    scopus 로고
    • Focal adhesion kinase and p53 signal transduction pathways in cancer
    • Golubovskaya V.M., Cance W. Focal adhesion kinase and p53 signal transduction pathways in cancer. Front Biosci 2010, 15:901-912.
    • (2010) Front Biosci , vol.15 , pp. 901-912
    • Golubovskaya, V.M.1    Cance, W.2
  • 46
    • 38149070791 scopus 로고    scopus 로고
    • Nuclear FAK promotes cell proliferation and survival through FERM-enhanced p53 degradation
    • Lim S.T., Chen X.L., Lim Y., et al. Nuclear FAK promotes cell proliferation and survival through FERM-enhanced p53 degradation. Mol Cell 2008, 29:9-22.
    • (2008) Mol Cell , vol.29 , pp. 9-22
    • Lim, S.T.1    Chen, X.L.2    Lim, Y.3
  • 47
    • 23044453057 scopus 로고    scopus 로고
    • Mechanism of cell cycle regulation by FIP200 in human breast cancer cells
    • Melkoumian Z.K., Peng X., Gan B., et al. Mechanism of cell cycle regulation by FIP200 in human breast cancer cells. Cancer Res 2005, 65:6676-6684.
    • (2005) Cancer Res , vol.65 , pp. 6676-6684
    • Melkoumian, Z.K.1    Peng, X.2    Gan, B.3
  • 48
    • 33748286819 scopus 로고    scopus 로고
    • Integrin-regulated FAK-Src signaling in normal and cancer cells
    • Mitra S.K., Schlaepfer D.D. Integrin-regulated FAK-Src signaling in normal and cancer cells. Curr Opin Cell Biol 2006, 18:516-523.
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 516-523
    • Mitra, S.K.1    Schlaepfer, D.D.2
  • 49
    • 84861535841 scopus 로고    scopus 로고
    • Nanog increases Focal Adhesion Kinase (FAK) promoter activity and expression and directly binds to FAK protein to be phosphorylated
    • Ho B., Olson G., Figel S., et al. Nanog increases Focal Adhesion Kinase (FAK) promoter activity and expression and directly binds to FAK protein to be phosphorylated. JBiol Chem 2012, 287:18656-18673.
    • (2012) JBiol Chem , vol.287 , pp. 18656-18673
    • Ho, B.1    Olson, G.2    Figel, S.3
  • 50
    • 13944273471 scopus 로고    scopus 로고
    • P53 induces differentiation of mouse embryonic stem cells by suppressing Nanog expression
    • Lin T., Chao C., Saito S., et al. p53 induces differentiation of mouse embryonic stem cells by suppressing Nanog expression. Nat Cell Biol 2005, 7:165-171.
    • (2005) Nat Cell Biol , vol.7 , pp. 165-171
    • Lin, T.1    Chao, C.2    Saito, S.3
  • 51
    • 83755220071 scopus 로고    scopus 로고
    • Translational approaches targeting the p53 pathway for anti-cancer therapy
    • Essmann F., Schulze-Osthoff K. Translational approaches targeting the p53 pathway for anti-cancer therapy. Br J Pharmacol 2012, 165:328-344.
    • (2012) Br J Pharmacol , vol.165 , pp. 328-344
    • Essmann, F.1    Schulze-Osthoff, K.2
  • 52
    • 70350028481 scopus 로고    scopus 로고
    • An update on gene therapy in China
    • Shi J., Zheng D. An update on gene therapy in China. Curr Opin Mol Ther 2009, 11:547-553.
    • (2009) Curr Opin Mol Ther , vol.11 , pp. 547-553
    • Shi, J.1    Zheng, D.2
  • 53
    • 77949270204 scopus 로고    scopus 로고
    • Clinical study of recombinant adenovirus-p53 combined with fractionated stereotactic radiotherapy for hepatocellular carcinoma
    • Yang Z.X., Wang D., Wang G., et al. Clinical study of recombinant adenovirus-p53 combined with fractionated stereotactic radiotherapy for hepatocellular carcinoma. JCancer Res Clin Oncol 2010, 136:625-630.
    • (2010) JCancer Res Clin Oncol , vol.136 , pp. 625-630
    • Yang, Z.X.1    Wang, D.2    Wang, G.3
  • 54
    • 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 L.M., Myers T.G., 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
  • 55
    • 0033452649 scopus 로고    scopus 로고
    • Mutant p53 mediated induction of cell cycle arrest and apoptosis at G1 phase by 9-hydroxyellipticine
    • Sugikawa E., Hosoi T., Yazaki N., et al. Mutant p53 mediated induction of cell cycle arrest and apoptosis at G1 phase by 9-hydroxyellipticine. Anticancer Res 1999, 19:3099-3108.
    • (1999) Anticancer Res , vol.19 , pp. 3099-3108
    • Sugikawa, E.1    Hosoi, T.2    Yazaki, N.3
  • 56
    • 0033601370 scopus 로고    scopus 로고
    • Pharmacological rescue of mutant p53 conformation and function
    • Foster B.A., Coffey H.A., Morin M.J., et al. 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
  • 57
    • 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., et al. 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
  • 58
    • 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 D.T., 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
  • 59
    • 0037192628 scopus 로고    scopus 로고
    • Characterization of the p53-rescue drug CP-31398 invitro and in living cells
    • Rippin T.M., Bykov V.J., Freund S.M., et al. Characterization of the p53-rescue drug CP-31398 invitro 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
  • 60
    • 0036301402 scopus 로고    scopus 로고
    • Recognition of DNA by p53 core domain and location of intermolecular contacts of cooperative binding
    • Rippin T.M., Freund S.M., Veprintsev D.B., et al. Recognition of DNA by p53 core domain and location of intermolecular contacts of cooperative binding. JMol Biol 2002, 319:351-358.
    • (2002) JMol Biol , vol.319 , pp. 351-358
    • Rippin, T.M.1    Freund, S.M.2    Veprintsev, D.B.3
  • 61
    • 8544257375 scopus 로고    scopus 로고
    • CP-31398 restores DNA-binding activity to mutant p53 invitro but does not affect p53 homologs p63 and p73
    • Demma M.J., Wong S., Maxwell E., et al. CP-31398 restores DNA-binding activity to mutant p53 invitro but does not affect p53 homologs p63 and p73. JBiol Chem 2004, 279:45887-45896.
    • (2004) JBiol Chem , vol.279 , pp. 45887-45896
    • Demma, M.J.1    Wong, S.2    Maxwell, E.3
  • 62
    • 36849084779 scopus 로고    scopus 로고
    • CP-31398 restores mutant p53 tumor suppressor function and inhibits UVB-induced skin carcinogenesis in mice
    • Tang X., Zhu Y., Han L., et al. CP-31398 restores mutant p53 tumor suppressor function and inhibits UVB-induced skin carcinogenesis in mice. JClin Invest 2007, 117:3753-3764.
    • (2007) JClin Invest , vol.117 , pp. 3753-3764
    • Tang, X.1    Zhu, Y.2    Han, L.3
  • 63
    • 36849006530 scopus 로고    scopus 로고
    • Targeting mutant p53 shows promise for sunscreens and skin cancer
    • El-Deiry W.S. Targeting mutant p53 shows promise for sunscreens and skin cancer. JClin Invest 2007, 117:3658-3660.
    • (2007) JClin Invest , vol.117 , pp. 3658-3660
    • El-Deiry, W.S.1
  • 64
    • 54749111456 scopus 로고    scopus 로고
    • Suppression of familial adenomatous polyposis by CP-31398, a TP53 modulator, in APCmin/+ mice
    • Rao C.V., Swamy M.V., Patlolla J.M., et al. Suppression of familial adenomatous polyposis by CP-31398, a TP53 modulator, in APCmin/+ mice. Cancer Res 2008, 68:7670-7675.
    • (2008) Cancer Res , vol.68 , pp. 7670-7675
    • Rao, C.V.1    Swamy, M.V.2    Patlolla, J.M.3
  • 65
    • 70350234715 scopus 로고    scopus 로고
    • Inhibition of azoxymethane-induced colorectal cancer by CP-31398, a TP53 modulator, alone or in combination with low doses of celecoxib in male F344 rats
    • Rao C.V., Steele V.E., Swamy M.V., et al. Inhibition of azoxymethane-induced colorectal cancer by CP-31398, a TP53 modulator, alone or in combination with low doses of celecoxib in male F344 rats. Cancer Res 2009, 69:8175-8182.
    • (2009) Cancer Res , vol.69 , pp. 8175-8182
    • Rao, C.V.1    Steele, V.E.2    Swamy, M.V.3
  • 66
    • 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 V.J., Issaeva N., Selivanova G., et al. 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
  • 67
    • 19444387176 scopus 로고    scopus 로고
    • PRIMA-1(MET) synergizes with cisplatin to induce tumor cell apoptosis
    • Bykov V.J., Zache N., Stridh H., et al. PRIMA-1(MET) synergizes with cisplatin to induce tumor cell apoptosis. Oncogene 2005, 24:3484-3491.
    • (2005) Oncogene , vol.24 , pp. 3484-3491
    • Bykov, V.J.1    Zache, N.2    Stridh, H.3
  • 68
    • 52449087539 scopus 로고    scopus 로고
    • PRIMA-1MET inhibits growth of mouse tumors carrying mutant p53
    • Zache N., Lambert J.M., Wiman K.G., et al. PRIMA-1MET inhibits growth of mouse tumors carrying mutant p53. Cell Oncol 2008, 30:411-418.
    • (2008) Cell Oncol , vol.30 , pp. 411-418
    • Zache, N.1    Lambert, J.M.2    Wiman, K.G.3
  • 69
    • 77951238151 scopus 로고    scopus 로고
    • SCH529074, a small molecule activator of mutant p53, which binds p53 DNA binding domain (DBD), restores growth-suppressive function to mutant p53 and interrupts HDM2-mediated ubiquitination of wild type p53
    • Demma M., Maxwell E., Ramos R., et al. SCH529074, a small molecule activator of mutant p53, which binds p53 DNA binding domain (DBD), restores growth-suppressive function to mutant p53 and interrupts HDM2-mediated ubiquitination of wild type p53. JBiol Chem 2010, 285:10198-10212.
    • (2010) JBiol Chem , vol.285 , pp. 10198-10212
    • Demma, M.1    Maxwell, E.2    Ramos, R.3
  • 70
    • 24044466754 scopus 로고    scopus 로고
    • Reactivation of mutant p53 and induction of apoptosis in human tumor cells by maleimide analogs
    • Bykov V.J., Issaeva N., Zache N., et al. Reactivation of mutant p53 and induction of apoptosis in human tumor cells by maleimide analogs. JBiol Chem 2005, 280:30384-30391.
    • (2005) JBiol Chem , vol.280 , pp. 30384-30391
    • Bykov, V.J.1    Issaeva, N.2    Zache, N.3
  • 71
    • 43649096147 scopus 로고    scopus 로고
    • Mutant p53 targeting by the low molecular weight compound STIMA-1
    • Zache N., Lambert J.M., Rokaeus N., et al. Mutant p53 targeting by the low molecular weight compound STIMA-1. Mol Oncol 2008, 2:70-80.
    • (2008) Mol Oncol , vol.2 , pp. 70-80
    • Zache, N.1    Lambert, J.M.2    Rokaeus, N.3
  • 72
    • 44049091429 scopus 로고    scopus 로고
    • Small-molecule RETRA suppresses mutant p53-bearing cancer cells through a p73-dependent salvage pathway
    • Kravchenko J.E., Ilyinskaya G.V., Komarov P.G., et al. Small-molecule RETRA suppresses mutant p53-bearing cancer cells through a p73-dependent salvage pathway. Proc Natl Acad Sci USA 2008, 105:6302-6307.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 6302-6307
    • Kravchenko, J.E.1    Ilyinskaya, G.V.2    Komarov, P.G.3
  • 73
    • 84861368058 scopus 로고    scopus 로고
    • Allele-specific p53 mutant reactivation
    • Yu X., Vazquez A., Levine A.J., et al. Allele-specific p53 mutant reactivation. Cancer Cell 2012, 21:614-625.
    • (2012) Cancer Cell , vol.21 , pp. 614-625
    • Yu, X.1    Vazquez, A.2    Levine, A.J.3
  • 74
    • 0027964904 scopus 로고
    • Immunochemical analysis of the interaction of p53 with MDM2; fine mapping of the MDM2 binding site on p53 using synthetic peptides
    • Picksley S.M., Vojtesek B., Sparks A., et al. Immunochemical analysis of the interaction of p53 with MDM2; fine mapping of the MDM2 binding site on p53 using synthetic peptides. Oncogene 1994, 9:2523-2529.
    • (1994) Oncogene , vol.9 , pp. 2523-2529
    • Picksley, S.M.1    Vojtesek, B.2    Sparks, A.3
  • 75
    • 0030575937 scopus 로고    scopus 로고
    • Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain
    • Kussie P.H., Gorina S., Marechal V., et al. Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science 1996, 274:948-953.
    • (1996) Science , vol.274 , pp. 948-953
    • Kussie, P.H.1    Gorina, S.2    Marechal, V.3
  • 76
    • 0030981049 scopus 로고    scopus 로고
    • Agenetic approach to mapping the p53 binding site in the MDM2 protein
    • Freedman D.A., Epstein C.B., Roth J.C., et al. Agenetic approach to mapping the p53 binding site in the MDM2 protein. Mol Med 1997, 3:248-259.
    • (1997) Mol Med , vol.3 , pp. 248-259
    • Freedman, D.A.1    Epstein, C.B.2    Roth, J.C.3
  • 77
    • 33644673642 scopus 로고    scopus 로고
    • Structural details on mdm2-p53 interaction
    • Chi S.W., Lee S.H., Kim D.H., et al. Structural details on mdm2-p53 interaction. JBiol Chem 2005, 280:38795-38802.
    • (2005) JBiol Chem , vol.280 , pp. 38795-38802
    • Chi, S.W.1    Lee, S.H.2    Kim, D.H.3
  • 78
    • 3843055877 scopus 로고    scopus 로고
    • Anonpeptidic sulfonamide inhibits the p53-mdm2 interaction and activates p53-dependent transcription in mdm2-overexpressing cells
    • Galatin P.S., Abraham D.J. Anonpeptidic sulfonamide inhibits the p53-mdm2 interaction and activates p53-dependent transcription in mdm2-overexpressing cells. JMed Chem 2004, 47:4163-4165.
    • (2004) JMed Chem , vol.47 , pp. 4163-4165
    • Galatin, P.S.1    Abraham, D.J.2
  • 79
    • 10744221485 scopus 로고    scopus 로고
    • Invivo activation of the p53 pathway by small-molecule antagonists of MDM2
    • Vassilev L.T., Vu B.T., Graves B., et al. Invivo 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
  • 80
    • 4344610526 scopus 로고    scopus 로고
    • Small-molecule antagonists of p53-MDM2 binding: research tools and potential therapeutics
    • Vassilev L.T. Small-molecule antagonists of p53-MDM2 binding: research tools and potential therapeutics. Cell Cycle 2004, 3:419-421.
    • (2004) Cell Cycle , vol.3 , pp. 419-421
    • Vassilev, L.T.1
  • 81
    • 32444449180 scopus 로고    scopus 로고
    • Small-molecule MDM2 antagonists reveal aberrant p53 signaling in cancer: implications for therapy
    • Tovar C., Rosinski J., Filipovic Z., et al. Small-molecule MDM2 antagonists reveal aberrant p53 signaling in cancer: implications for therapy. Proc Natl Acad Sci USA 2006, 103:1888-1893.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 1888-1893
    • Tovar, C.1    Rosinski, J.2    Filipovic, Z.3
  • 82
    • 79955518716 scopus 로고    scopus 로고
    • MDM2 antagonists boost antitumor effect of androgen withdrawal: implications for therapy of prostate cancer
    • Tovar C., Higgins B., Kolinsky K., et al. MDM2 antagonists boost antitumor effect of androgen withdrawal: implications for therapy of prostate cancer. Mol Cancer 2011, 10:49.
    • (2011) Mol Cancer , vol.10 , pp. 49
    • Tovar, C.1    Higgins, B.2    Kolinsky, K.3
  • 83
    • 43449131243 scopus 로고    scopus 로고
    • Differential effects of chemotherapeutic drugs versus the MDM-2 antagonist nutlin-3 on cell cycle progression and induction of apoptosis in SKW6.4 lymphoblastoid B-cells
    • Barbarotto E., Corallini F., Rimondi E., et al. Differential effects of chemotherapeutic drugs versus the MDM-2 antagonist nutlin-3 on cell cycle progression and induction of apoptosis in SKW6.4 lymphoblastoid B-cells. JCell Biochem 2008, 104:595-605.
    • (2008) JCell Biochem , vol.104 , pp. 595-605
    • Barbarotto, E.1    Corallini, F.2    Rimondi, E.3
  • 84
    • 35448932303 scopus 로고    scopus 로고
    • The MDM-2 antagonist nutlin-3 promotes the maturation of acute myeloid leukemic blasts
    • Secchiero P., Zerbinati C., Melloni E., et al. The MDM-2 antagonist nutlin-3 promotes the maturation of acute myeloid leukemic blasts. Neoplasia 2007, 9:853-861.
    • (2007) Neoplasia , vol.9 , pp. 853-861
    • Secchiero, P.1    Zerbinati, C.2    Melloni, E.3
  • 85
    • 70449727603 scopus 로고    scopus 로고
    • Antitumor activity of the selective MDM2 antagonist nutlin-3 against chemoresistant neuroblastoma with wild-type p53
    • Van Maerken T., Ferdinande L., Taildeman J., et al. Antitumor activity of the selective MDM2 antagonist nutlin-3 against chemoresistant neuroblastoma with wild-type p53. JNatl Cancer Inst 2009, 101:1562-1574.
    • (2009) JNatl Cancer Inst , vol.101 , pp. 1562-1574
    • Van Maerken, T.1    Ferdinande, L.2    Taildeman, J.3
  • 86
    • 11144315535 scopus 로고    scopus 로고
    • Small molecule RITA binds to p53, blocks p53-HDM-2 interaction and activates p53 function in tumors
    • Issaeva N., Bozko P., Enge M., et al. Small molecule RITA binds to p53, blocks p53-HDM-2 interaction and activates p53 function in tumors. Nat Med 2004, 10:1321-1328.
    • (2004) Nat Med , vol.10 , pp. 1321-1328
    • Issaeva, N.1    Bozko, P.2    Enge, M.3
  • 87
    • 78649645749 scopus 로고    scopus 로고
    • RITA inhibits multiple myeloma cell growth through induction of p53-mediated caspase-dependent apoptosis and synergistically enhances nutlin-induced cytotoxic responses
    • Saha M.N., Jiang H., Mukai A., et al. RITA inhibits multiple myeloma cell growth through induction of p53-mediated caspase-dependent apoptosis and synergistically enhances nutlin-induced cytotoxic responses. Mol Cancer Ther 2010, 9:3041-3051.
    • (2010) Mol Cancer Ther , vol.9 , pp. 3041-3051
    • Saha, M.N.1    Jiang, H.2    Mukai, A.3
  • 88
    • 79960130289 scopus 로고    scopus 로고
    • RITA enhances chemosensivity of pre-B ALL cells to doxorubicin by inducing p53-dependent apoptosis
    • Kazemi A., Safa M., Shahbazi A. RITA enhances chemosensivity of pre-B ALL cells to doxorubicin by inducing p53-dependent apoptosis. Hematology 2011, 16:225-231.
    • (2011) Hematology , vol.16 , pp. 225-231
    • Kazemi, A.1    Safa, M.2    Shahbazi, A.3
  • 89
    • 84857791061 scopus 로고    scopus 로고
    • Synergistic growth inhibition based on small-molecule p53 activation as treatment for intraocular melanoma
    • de Lange J., Ly L.V., Lodder K., et al. Synergistic growth inhibition based on small-molecule p53 activation as treatment for intraocular melanoma. Oncogene 2012, 31:1105-1116.
    • (2012) Oncogene , vol.31 , pp. 1105-1116
    • de Lange, J.1    Ly, L.V.2    Lodder, K.3
  • 90
    • 84856041539 scopus 로고    scopus 로고
    • Targeting p53 via JNK pathway: a novel role of RITA for apoptotic signaling in multiple myeloma
    • Saha M.N., Jiang H., Yang Y., et al. Targeting p53 via JNK pathway: a novel role of RITA for apoptotic signaling in multiple myeloma. PLoS One 2012, 7:e30215.
    • (2012) PLoS One , vol.7
    • Saha, M.N.1    Jiang, H.2    Yang, Y.3
  • 91
    • 77951067833 scopus 로고    scopus 로고
    • Rescue of p53 function by small-molecule RITA in cervical carcinoma by blocking E6-mediated degradation
    • Zhao C.Y., Szekely L., Bao W., et al. Rescue of p53 function by small-molecule RITA in cervical carcinoma by blocking E6-mediated degradation. Cancer Res 2010, 70:3372-3381.
    • (2010) Cancer Res , vol.70 , pp. 3372-3381
    • Zhao, C.Y.1    Szekely, L.2    Bao, W.3
  • 92
    • 18844423053 scopus 로고    scopus 로고
    • Terphenyl-based helical mimetics that disrupt the p53/HDM2 interaction
    • Yin H., Lee G.I., Park H.S., et al. Terphenyl-based helical mimetics that disrupt the p53/HDM2 interaction. Angew Chem Int Ed Engl 2005, 44:2704-2707.
    • (2005) Angew Chem Int Ed Engl , vol.44 , pp. 2704-2707
    • Yin, H.1    Lee, G.I.2    Park, H.S.3
  • 93
    • 13944274061 scopus 로고    scopus 로고
    • Discovery and cocrystal structure of benzodiazepinedione HDM2 antagonists that activate p53 in cells
    • Grasberger B.L., Lu T., Schubert C., et al. Discovery and cocrystal structure of benzodiazepinedione HDM2 antagonists that activate p53 in cells. JMed Chem 2005, 48:909-912.
    • (2005) JMed Chem , vol.48 , pp. 909-912
    • Grasberger, B.L.1    Lu, T.2    Schubert, C.3
  • 94
    • 33644873086 scopus 로고    scopus 로고
    • Benzodiazepinedione inhibitors of the Hdm2:p53 complex suppress human tumor cell proliferation invitro and sensitize tumors to doxorubicin invivo
    • Koblish H.K., Zhao S., Franks C.F., et al. Benzodiazepinedione inhibitors of the Hdm2:p53 complex suppress human tumor cell proliferation invitro and sensitize tumors to doxorubicin invivo. Mol Cancer Ther 2006, 5:160-169.
    • (2006) Mol Cancer Ther , vol.5 , pp. 160-169
    • Koblish, H.K.1    Zhao, S.2    Franks, C.F.3
  • 95
    • 33745645832 scopus 로고    scopus 로고
    • Discovery of a nanomolar inhibitor of the human murine double minute 2 (MDM2)-p53 interaction through an integrated, virtual database screening strategy
    • Lu Y., Nikolovska-Coleska Z., Fang X., et al. Discovery of a nanomolar inhibitor of the human murine double minute 2 (MDM2)-p53 interaction through an integrated, virtual database screening strategy. JMed Chem 2006, 49:3759-3762.
    • (2006) JMed Chem , vol.49 , pp. 3759-3762
    • Lu, Y.1    Nikolovska-Coleska, Z.2    Fang, X.3
  • 96
    • 33745154819 scopus 로고    scopus 로고
    • Structure-based design of spiro-oxindoles as potent, specific small-molecule inhibitors of the MDM2-p53 interaction
    • Ding K., Lu Y., Nikolovska-Coleska Z., et al. Structure-based design of spiro-oxindoles as potent, specific small-molecule inhibitors of the MDM2-p53 interaction. JMed Chem 2006, 49:3432-3435.
    • (2006) JMed Chem , vol.49 , pp. 3432-3435
    • Ding, K.1    Lu, Y.2    Nikolovska-Coleska, Z.3
  • 97
    • 49849104827 scopus 로고    scopus 로고
    • Reactivation of p53 by a specific MDM2 antagonist (MI-43) leads to p21-mediated cell cycle arrest and selective cell death in colon cancer
    • Shangary S., Ding K., Qiu S., et al. Reactivation of p53 by a specific MDM2 antagonist (MI-43) leads to p21-mediated cell cycle arrest and selective cell death in colon cancer. Mol Cancer Ther 2008, 7:1533-1542.
    • (2008) Mol Cancer Ther , vol.7 , pp. 1533-1542
    • Shangary, S.1    Ding, K.2    Qiu, S.3
  • 98
    • 72549094296 scopus 로고    scopus 로고
    • An MDM2 antagonist (MI-319) restores p53 functions and increases the life span of orally treated follicular lymphoma bearing animals
    • Mohammad R.M., Wu J., Azmi A.S., et al. An MDM2 antagonist (MI-319) restores p53 functions and increases the life span of orally treated follicular lymphoma bearing animals. Mol Cancer 2009, 8:115.
    • (2009) Mol Cancer , vol.8 , pp. 115
    • Mohammad, R.M.1    Wu, J.2    Azmi, A.S.3
  • 99
    • 77949659052 scopus 로고    scopus 로고
    • MDM2 inhibitor MI-319 in combination with cisplatin is an effective treatment for pancreatic cancer independent of p53 function
    • Azmi A.S., Aboukameel A., Banerjee S., et al. MDM2 inhibitor MI-319 in combination with cisplatin is an effective treatment for pancreatic cancer independent of p53 function. Eur J Cancer 2010, 46:1122-1131.
    • (2010) Eur J Cancer , vol.46 , pp. 1122-1131
    • Azmi, A.S.1    Aboukameel, A.2    Banerjee, S.3
  • 100
    • 33750133440 scopus 로고    scopus 로고
    • Small-molecule inhibitors of the MDM2-p53 protein-protein interaction based on an isoindolinone scaffold
    • Hardcastle I.R., Ahmed S.U., Atkins H., et al. Small-molecule inhibitors of the MDM2-p53 protein-protein interaction based on an isoindolinone scaffold. JMed Chem 2006, 49:6209-6221.
    • (2006) JMed Chem , vol.49 , pp. 6209-6221
    • Hardcastle, I.R.1    Ahmed, S.U.2    Atkins, H.3
  • 101
    • 79952260443 scopus 로고    scopus 로고
    • Isoindolinone inhibitors of the murine double minute 2 (MDM2)-p53 protein-protein interaction: structure-activity studies leading to improved potency
    • Hardcastle I.R., Liu J., Valeur E., et al. Isoindolinone inhibitors of the murine double minute 2 (MDM2)-p53 protein-protein interaction: structure-activity studies leading to improved potency. JMed Chem 2011, 54:1233-1243.
    • (2011) JMed Chem , vol.54 , pp. 1233-1243
    • Hardcastle, I.R.1    Liu, J.2    Valeur, E.3
  • 102
    • 21744435478 scopus 로고    scopus 로고
    • The role of focal-adhesion kinase in cancer-a new therapeutic opportunity
    • McLean G.W., Carragher N.O., Avizienyte E., et al. The role of focal-adhesion kinase in cancer-a new therapeutic opportunity. Nat Rev Cancer 2005, 5:505-515.
    • (2005) Nat Rev Cancer , vol.5 , pp. 505-515
    • McLean, G.W.1    Carragher, N.O.2    Avizienyte, E.3
  • 103
    • 0032443850 scopus 로고    scopus 로고
    • The COOH-terminal domain of the focal adhesion kinase induces loss of adhesion and cell death in human tumor cells
    • Xu L.H., Yang X., Craven R.J., et al. The COOH-terminal domain of the focal adhesion kinase induces loss of adhesion and cell death in human tumor cells. Cell Growth Differ 1998, 9:999-1005.
    • (1998) Cell Growth Differ , vol.9 , pp. 999-1005
    • Xu, L.H.1    Yang, X.2    Craven, R.J.3
  • 104
    • 27644545721 scopus 로고    scopus 로고
    • Effect of focal adhesion kinase (FAK) downregulation with FAK antisense oligonucleotides and 5-fluorouracil on the viability of melanoma cell lines
    • Smith C.S., Golubovskaya V.M., Peck E., et al. Effect of focal adhesion kinase (FAK) downregulation with FAK antisense oligonucleotides and 5-fluorouracil on the viability of melanoma cell lines. Melanoma Res 2005, 15:357-362.
    • (2005) Melanoma Res , vol.15 , pp. 357-362
    • Smith, C.S.1    Golubovskaya, V.M.2    Peck, E.3
  • 105
    • 69349085098 scopus 로고    scopus 로고
    • The direct effect of focal adhesion kinase (FAK), dominant-negative FAK, FAK-CD and FAK siRNA on gene expression and human MCF-7 breast cancer cell tumorigenesis
    • Golubovskaya V.M., Zheng M., Zhang L., et al. The direct effect of focal adhesion kinase (FAK), dominant-negative FAK, FAK-CD and FAK siRNA on gene expression and human MCF-7 breast cancer cell tumorigenesis. BMC Cancer 2009, 9:280.
    • (2009) BMC Cancer , vol.9 , pp. 280
    • Golubovskaya, V.M.1    Zheng, M.2    Zhang, L.3
  • 106
    • 0029848157 scopus 로고    scopus 로고
    • Attenuation of the expression of the focal adhesion kinase induces apoptosis in tumor cells
    • Xu L.H., Owens L.V., Sturge G.C., et al. Attenuation of the expression of the focal adhesion kinase induces apoptosis in tumor cells. Cell Growth Differ 1996, 7:413-418.
    • (1996) Cell Growth Differ , vol.7 , pp. 413-418
    • Xu, L.H.1    Owens, L.V.2    Sturge, G.C.3
  • 107
    • 34447538483 scopus 로고    scopus 로고
    • Cellular characterization of a novel focal adhesion kinase inhibitor
    • Slack-Davis J.K., Martin K.H., Tilghman R.W., et al. Cellular characterization of a novel focal adhesion kinase inhibitor. JBiol Chem 2007, 282:14845-14852.
    • (2007) JBiol Chem , vol.282 , pp. 14845-14852
    • Slack-Davis, J.K.1    Martin, K.H.2    Tilghman, R.W.3
  • 108
    • 40949152523 scopus 로고    scopus 로고
    • Antitumor activity and pharmacology of a selective focal adhesion kinase inhibitor, PF-562,271
    • Roberts W.G., Ung E., Whalen P., et al. Antitumor activity and pharmacology of a selective focal adhesion kinase inhibitor, PF-562,271. Cancer Res 2008, 68:1935-1944.
    • (2008) Cancer Res , vol.68 , pp. 1935-1944
    • Roberts, W.G.1    Ung, E.2    Whalen, P.3
  • 109
    • 77953709612 scopus 로고    scopus 로고
    • PND-1186 FAK inhibitor selectively promotes tumor cell apoptosis in three-dimensional environments
    • Tanjoni I., Walsh C., Uryu S., et al. PND-1186 FAK inhibitor selectively promotes tumor cell apoptosis in three-dimensional environments. Cancer Biol Ther 2010, 9:764-777.
    • (2010) Cancer Biol Ther , vol.9 , pp. 764-777
    • Tanjoni, I.1    Walsh, C.2    Uryu, S.3
  • 110
    • 57349153946 scopus 로고    scopus 로고
    • Asmall molecule inhibitor, 1,2,4,5-benzenetetraamine tetrahydrochloride, targeting the y397 site of focal adhesion kinase decreases tumor growth
    • Golubovskaya V.M., Nyberg C., Zheng M., et al. Asmall molecule inhibitor, 1,2,4,5-benzenetetraamine tetrahydrochloride, targeting the y397 site of focal adhesion kinase decreases tumor growth. JMed Chem 2008, 51:7405-7416.
    • (2008) JMed Chem , vol.51 , pp. 7405-7416
    • Golubovskaya, V.M.1    Nyberg, C.2    Zheng, M.3
  • 111
    • 68449092818 scopus 로고    scopus 로고
    • Anovel small molecule inhibitor of FAK decreases growth of human pancreatic cancer
    • Hochwald S.N., Nyberg C., Zheng M., et al. Anovel small molecule inhibitor of FAK decreases growth of human pancreatic cancer. Cell Cycle 2009, 8:2435-2443.
    • (2009) Cell Cycle , vol.8 , pp. 2435-2443
    • Hochwald, S.N.1    Nyberg, C.2    Zheng, M.3
  • 112
    • 77953526787 scopus 로고    scopus 로고
    • Inhibition of focal adhesion kinase decreases tumor growth in human neuroblastoma
    • Beierle E.A., Ma X., Stewart J., et al. Inhibition of focal adhesion kinase decreases tumor growth in human neuroblastoma. Cell Cycle 2010, 9:1005-1015.
    • (2010) Cell Cycle , vol.9 , pp. 1005-1015
    • Beierle, E.A.1    Ma, X.2    Stewart, J.3
  • 113
    • 84874031013 scopus 로고    scopus 로고
    • Pharmacologic blockade of FAK autophosphorylation decreases human glioblastoma tumor growth and synergizes with temozolomide
    • Golubovskaya V.M., Huang G., Ho B., et al. Pharmacologic blockade of FAK autophosphorylation decreases human glioblastoma tumor growth and synergizes with temozolomide. Mol Cancer Ther 2013, 12:162-172.
    • (2013) Mol Cancer Ther , vol.12 , pp. 162-172
    • Golubovskaya, V.M.1    Huang, G.2    Ho, B.3
  • 114
    • 84881431783 scopus 로고    scopus 로고
    • Focal Adhesion kinase autophosphorylation inhibition decreases colon cancer cell growth and enhances the efficacy of chemotherapy
    • [Epub ahead of print]
    • Heffler M., Golubovskaya V.M., Dunn K.M., et al. Focal Adhesion kinase autophosphorylation inhibition decreases colon cancer cell growth and enhances the efficacy of chemotherapy. Cancer Biol Ther 2013, [Epub ahead of print].
    • (2013) Cancer Biol Ther
    • Heffler, M.1    Golubovskaya, V.M.2    Dunn, K.M.3
  • 115
    • 84860478933 scopus 로고    scopus 로고
    • Asmall molecule focal adhesion kinase (FAK) inhibitor, targeting Y397 site: 1-(2-hydroxyethyl)-3, 5, 7-triaza-1-azoniatricyclo [3.3.1.1(3,7)]decane; bromide effectively inhibits FAK autophosphorylation activity and decreases cancer cell viability, clonogenicity and tumor growth invivo
    • Golubovskaya V.M., Figel S., Ho B.T., et al. Asmall molecule focal adhesion kinase (FAK) inhibitor, targeting Y397 site: 1-(2-hydroxyethyl)-3, 5, 7-triaza-1-azoniatricyclo [3.3.1.1(3,7)]decane; bromide effectively inhibits FAK autophosphorylation activity and decreases cancer cell viability, clonogenicity and tumor growth invivo. Carcinogenesis 2012, 33:1004-1013.
    • (2012) Carcinogenesis , vol.33 , pp. 1004-1013
    • Golubovskaya, V.M.1    Figel, S.2    Ho, B.T.3
  • 116
    • 68549120961 scopus 로고    scopus 로고
    • Small molecule chloropyramine hydrochloride (C4) targets the binding site of focal adhesion kinase and vascular endothelial growth factor receptor 3 and suppresses breast cancer growth invivo
    • Kurenova E.V., Hunt D.L., He D., et al. Small molecule chloropyramine hydrochloride (C4) targets the binding site of focal adhesion kinase and vascular endothelial growth factor receptor 3 and suppresses breast cancer growth invivo. JMed Chem 2009, 52:4716-4724.
    • (2009) JMed Chem , vol.52 , pp. 4716-4724
    • Kurenova, E.V.1    Hunt, D.L.2    He, D.3
  • 117
    • 22244443786 scopus 로고    scopus 로고
    • P53 Activation by small molecules: application in oncology
    • Vassilev L.T. p53 Activation by small molecules: application in oncology. JMed Chem 2005, 48:4491-4499.
    • (2005) JMed Chem , vol.48 , pp. 4491-4499
    • Vassilev, L.T.1
  • 118
    • 84876705245 scopus 로고    scopus 로고
    • Asmall-molecule inhibitor, 5'-o-tritylthymidine, targets FAK And Mdm-2 interaction, and blocks breast and colon tumorigenesis invivo
    • Golubovskaya V., Palma N.L., Zheng M., et al. Asmall-molecule inhibitor, 5'-o-tritylthymidine, targets FAK And Mdm-2 interaction, and blocks breast and colon tumorigenesis invivo. Anticancer Agents Med Chem 2013, 13:532-545.
    • (2013) Anticancer Agents Med Chem , vol.13 , pp. 532-545
    • Golubovskaya, V.1    Palma, N.L.2    Zheng, M.3
  • 119
    • 84880013271 scopus 로고    scopus 로고
    • Disruption of focal adhesion kinase and p53 interaction with small molecule compound R2 reactivated p53 and blocked tumor growth
    • Golubovskaya V.M., Ho B., Zheng M., et al. Disruption of focal adhesion kinase and p53 interaction with small molecule compound R2 reactivated p53 and blocked tumor growth. BMC Cancer 2013, 13(1):342.
    • (2013) BMC Cancer , vol.13 , Issue.1 , pp. 342
    • Golubovskaya, V.M.1    Ho, B.2    Zheng, M.3
  • 120
    • 0032562289 scopus 로고    scopus 로고
    • Targeting the receptor-Gq interface to inhibit invivo pressure overload myocardial hypertrophy
    • Akhter S.A., Luttrell L.M., Rockman H.A., et al. Targeting the receptor-Gq interface to inhibit invivo pressure overload myocardial hypertrophy. Science 1998, 280:574-577.
    • (1998) Science , vol.280 , pp. 574-577
    • Akhter, S.A.1    Luttrell, L.M.2    Rockman, H.A.3
  • 121
    • 0032849010 scopus 로고    scopus 로고
    • Affinity-driven peptide selection of an NFAT inhibitor more selective than cyclosporin A
    • Aramburu J., Yaffe M.B., Lopez-Rodriguez C., et al. Affinity-driven peptide selection of an NFAT inhibitor more selective than cyclosporin A. Science 1999, 285:2129-2133.
    • (1999) Science , vol.285 , pp. 2129-2133
    • Aramburu, J.1    Yaffe, M.B.2    Lopez-Rodriguez, C.3
  • 122
    • 0034284715 scopus 로고    scopus 로고
    • Selective inhibition of NF-kappaB activation by a peptide that blocks the interaction of NEMO with the IkappaB kinase complex
    • May M.J., D'Acquisto F., Madge L.A., et al. Selective inhibition of NF-kappaB activation by a peptide that blocks the interaction of NEMO with the IkappaB kinase complex. Science 2000, 289:1550-1554.
    • (2000) Science , vol.289 , pp. 1550-1554
    • May, M.J.1    D'Acquisto, F.2    Madge, L.A.3
  • 123
    • 0037073786 scopus 로고    scopus 로고
    • Requirement of nuclear factor of activated T-cells in calcineurin-mediated cardiomyocyte hypertrophy
    • van Rooij E., Doevendans P.A., de Theije C.C., et al. Requirement of nuclear factor of activated T-cells in calcineurin-mediated cardiomyocyte hypertrophy. JBiol Chem 2002, 277:48617-48626.
    • (2002) JBiol Chem , vol.277 , pp. 48617-48626
    • van Rooij, E.1    Doevendans, P.A.2    de Theije, C.C.3
  • 124
    • 84875755348 scopus 로고    scopus 로고
    • Disrupting the scaffold to improve focal adhesion kinase-targeting therapeutics
    • Cance W.G., Kurenova E., Marlowe T., et al. Disrupting the scaffold to improve focal adhesion kinase-targeting therapeutics. Sci Signaling 2013, 6:pe10.
    • (2013) Sci Signaling , vol.6
    • Cance, W.G.1    Kurenova, E.2    Marlowe, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.