메뉴 건너뛰기




Volumn 16, Issue 2, 2006, Pages 165-188

Patented small molecule inhibitors of p53-MDM2 interaction

Author keywords

Anticancer drug; MDM2; Mutant p53; p53 MDM2 interaction; Protein protein interaction; Ubiquitin ligase inhibitor

Indexed keywords

1 PHENYLPIPERAZINE DERIVATIVE; 2 (4 CHLOROPHENYL) 4,5 DIPHENYL 2 IMIDAZOLINE; 3,4 DIBENZYLOXYPIPERIDINE DERIVATIVE; 4 (3 DIMETHYLAMINOPROPYLAMINO) 2 (4 METHOXYSTYRYL)QUINAZOLINE; 5 DEAZAFLAVINE DERIVATIVE; 7 NITRO 5 DEAZAFLAVIN; ANTINEOPLASTIC AGENT; BENZODIAZEPINE DERIVATIVE; BENZODIAZEPINEDIONE DERIVATIVE; BENZOTHIADIAZINE DERIVATIVE; BORONIC ACID DERIVATIVE; CISPLATIN; CP 257042; DONEPEZIL DERIVATIVE; IMIDAZOLINE DERIVATIVE; INDOLE DERIVATIVE; LIGASE INHIBITOR; MALEIMIDE DERIVATIVE; MIRA 1; NUTLIN; NUTLIN DERIVATIVE; OXINDOLE DERIVATIVE; PIPERAZINE DERIVATIVE; PIPERIDINE DERIVATIVE; PRIMA 1; PROTEIN MDM2; PROTEIN P53; SMALL MOLECULE INHIBITOR; UBIQUITIN PROTEIN LIGASE INHIBITOR; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 33144462783     PISSN: 13543776     EISSN: None     Source Type: Journal    
DOI: 10.1517/13543776.16.2.165     Document Type: Review
Times cited : (20)

References (96)
  • 1
    • 0023339504 scopus 로고
    • Molecular analysis and chromosomal mapping of amplified genes isolated from a transformed mouse 3T3 cell line
    • CAHILLY-SNYDER L, YANG-FENG T, FRANCKE U, GEORGE DL: Molecular analysis and chromosomal mapping of amplified genes isolated from a transformed mouse 3T3 cell line. Somat. Cell Mol. Genet. (1987) 13:235.
    • (1987) Somat. Cell Mol. Genet. , vol.13 , pp. 235
    • Cahilly-Snyder, L.1    Yang-Feng, T.2    Francke, U.3    George, D.L.4
  • 2
    • 0026649648 scopus 로고
    • The MDM-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation
    • MOMAND J, ZAMBETTI GP, OLSON DC, GEORGE D, LEVINE AJ: The MDM-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation. Cell (1992) 69(7):1237-1245.
    • (1992) Cell , vol.69 , Issue.7 , pp. 1237-1245
    • Momand, J.1    Zambetti, G.P.2    Olson, D.C.3    George, D.4    Levine, A.J.5
  • 3
    • 0026740449 scopus 로고
    • Amplification of a gene encoding a p53-associated protein in human sarcomas
    • OLINER JD, KINZLER KW, MELTZER PS, GEORGE DL, VOGELSTEIN B: Amplification of a gene encoding a p53-associated protein in human sarcomas. Nature (1992) 358(6381):80-83.
    • (1992) Nature , vol.358 , Issue.6381 , pp. 80-83
    • Oliner, J.D.1    Kinzler, K.W.2    Meltzer, P.S.3    George, D.L.4    Vogelstein, B.5
  • 4
    • 0032407592 scopus 로고    scopus 로고
    • p53/MDM-2 immunohistochemical expression correlated with proliferative activity in different subtypes of human sarcomas: A ten-year follow-up study
    • STEFANOU DG, NONNI AV, AGNANTIS NJ et al.: p53/MDM-2 immunohistochemical expression correlated with proliferative activity in different subtypes of human sarcomas: a ten-year follow-up study. Anticancer Res. (1998) 18(6B):4673-4681.
    • (1998) Anticancer Res. , vol.18 , Issue.6 B , pp. 4673-4681
    • Stefanou, D.G.1    Nonni, A.V.2    Agnantis, N.J.3
  • 5
    • 0031737424 scopus 로고    scopus 로고
    • MDM-2 oncoprotein overexpression, p53 gene mutation, and VEGF up-regulation in angiosarcomas
    • ZIETZ C, ROSSLE M, HAAS C et al.: MDM-2 oncoprotein overexpression, p53 gene mutation, and VEGF up-regulation in angiosarcomas. Am. J. Pathol. (1998) 153(5):1425-1433.
    • (1998) Am. J. Pathol. , vol.153 , Issue.5 , pp. 1425-1433
    • Zietz, C.1    Rossle, M.2    Haas, C.3
  • 6
    • 0038699629 scopus 로고    scopus 로고
    • The p53-MDM2 pathway: Targets for the development of new anticancer therapeutics
    • ZHELEVA DI, LANE DP, FISCHER PM: The p53-MDM2 pathway: targets for the development of new anticancer therapeutics. Mini Rev. Med. Chem. (2003) 3(3):257-270.
    • (2003) Mini Rev. Med. Chem. , vol.3 , Issue.3 , pp. 257-270
    • Zheleva, D.I.1    Lane, D.P.2    Fischer, P.M.3
  • 7
    • 14644403700 scopus 로고    scopus 로고
    • MDM2 and human malignancies: Expression, clinical pathology, prognostic markers, and implications for chemotherapy
    • RAYBURN E, ZHANG R, HE J, WANG H: MDM2 and human malignancies: expression, clinical pathology, prognostic markers, and implications for chemotherapy. Curr. Cancer Drug Targets (2005) 5(1):27-41.
    • (2005) Curr. Cancer Drug Targets , vol.5 , Issue.1 , pp. 27-41
    • Rayburn, E.1    Zhang, R.2    He, J.3    Wang, H.4
  • 8
    • 0344995254 scopus 로고    scopus 로고
    • MDM2 and MDMX inhibit the transcriptional activity of ectopically expressed SMAD proteins
    • YAM CH, SIU WY, AROOZ T et al.: MDM2 and MDMX inhibit the transcriptional activity of ectopically expressed SMAD proteins. Cancer Res. (1999) 59(20):5075-5078.
    • (1999) Cancer Res. , vol.59 , Issue.20 , pp. 5075-5078
    • Yam, C.H.1    Siu, W.Y.2    Arooz, T.3
  • 9
    • 14644437751 scopus 로고    scopus 로고
    • MDM2 is a central node in the p53 pathway: 12 years and counting
    • BOND GL, HU W, LEVINE AJ: MDM2 is a central node in the p53 pathway: 12 years and counting. Curr. Cancer Drug Targets (2005) 5(1):3-8.
    • (2005) Curr. Cancer Drug Targets , vol.5 , Issue.1 , pp. 3-8
    • Bond, G.L.1    Hu, W.2    Levine, A.J.3
  • 10
    • 0033946629 scopus 로고    scopus 로고
    • Overexpression of MDM2 protein in intrahepatic cholangiocarcinoma: Relationship with p53 overexpression, Ki-67 labeling, and clinicopathological features
    • HORIE S, ENDO K, KAWASAKI H, TERADA T: Overexpression of MDM2 protein in intrahepatic cholangiocarcinoma: relationship with p53 overexpression, Ki-67 labeling, and clinicopathological features. Virchows Arch. (2000) 437(1):25-30.
    • (2000) Virchows Arch. , vol.437 , Issue.1 , pp. 25-30
    • Horie, S.1    Endo, K.2    Kawasaki, H.3    Terada, T.4
  • 11
    • 0035977168 scopus 로고    scopus 로고
    • High levels of the MDM2 oncogene in paediatric rhabdomyosarcoma cell lines may confer multidrug resistance
    • COCKER HA, HOBBS SM, TIFFIN N et al.: High levels of the MDM2 oncogene in paediatric rhabdomyosarcoma cell lines may confer multidrug resistance. Br. J. Cancer (2001) 85(11):1746-1752.
    • (2001) Br. J. Cancer , vol.85 , Issue.11 , pp. 1746-1752
    • Cocker, H.A.1    Hobbs, S.M.2    Tiffin, N.3
  • 12
    • 0031890636 scopus 로고    scopus 로고
    • Role of MDM2 overexpression in doxorubicin resistance of breast carcinoma
    • SUZUKI A, TOI M, YAMAMOTO Y et al.: Role of MDM2 overexpression in doxorubicin resistance of breast carcinoma. Jpn. J. Cancer Res. (1998) 89(2):221-227.
    • (1998) Jpn. J. Cancer Res. , vol.89 , Issue.2 , pp. 221-227
    • Suzuki, A.1    Toi, M.2    Yamamoto, Y.3
  • 13
    • 0035162434 scopus 로고    scopus 로고
    • MDM2 mediated nuclear exclusion of p53 attenuates etoposide-induced apoptosis in neuroblastoma cells
    • RODRIGUEZ-LOPEZ AM, XENAKI D, EDEN TO, HICKMAN JA, CHRESTA CM: MDM2 mediated nuclear exclusion of p53 attenuates etoposide-induced apoptosis in neuroblastoma cells. Mol. Pharmacol. (2001) 59(1):135-143.
    • (2001) Mol. Pharmacol. , vol.59 , Issue.1 , pp. 135-143
    • Rodriguez-Lopez, A.M.1    Xenaki, D.2    Eden, T.O.3    Hickman, J.A.4    Chresta, C.M.5
  • 14
    • 0036205872 scopus 로고    scopus 로고
    • Alterations in p53 and pRb pathways and their prognostic significance in oesophageal cancer
    • MATHEW R, ARORA S, KHANNA R et al.: Alterations in p53 and pRb pathways and their prognostic significance in oesophageal cancer. Eur. J. Cancer (2002) 38(6):832-841.
    • (2002) Eur. J. Cancer , vol.38 , Issue.6 , pp. 832-841
    • Mathew, R.1    Arora, S.2    Khanna, R.3
  • 15
    • 3042616216 scopus 로고    scopus 로고
    • Hypoxia enhances metastatic efficiency by up-regulating MDM2 in KHT cells and increasing resistance to apoptosis
    • ZHANG L, HILL RP: Hypoxia enhances metastatic efficiency by up-regulating MDM2 in KHT cells and increasing resistance to apoptosis. Cancer Res. (2004) 64(12):4180-4189.
    • (2004) Cancer Res. , vol.64 , Issue.12 , pp. 4180-4189
    • Zhang, L.1    Hill, R.P.2
  • 16
    • 0347716455 scopus 로고    scopus 로고
    • MDM2, an introduction
    • IWAKUMA T, LOZANO G: MDM2, an introduction. Mol. Cancer Res. (2003) 1(14):993-1000.
    • (2003) Mol. Cancer Res. , vol.1 , Issue.14 , pp. 993-1000
    • Iwakuma, T.1    Lozano, G.2
  • 17
    • 14644417208 scopus 로고    scopus 로고
    • p53-Independent activities of MDM2 and their relevance to cancer therapy
    • ZHANG Z, ZHANG R: p53-Independent activities of MDM2 and their relevance to cancer therapy. Curr. Cancer Drug Targets (2005) 5(1):9-20.
    • (2005) Curr. Cancer Drug Targets , vol.5 , Issue.1 , pp. 9-20
    • Zhang, Z.1    Zhang, R.2
  • 18
    • 0024382760 scopus 로고
    • The p53 proto-oncogene can act as a suppressor of transformation
    • FINLAY CA, HINDS PW, LEVINE AJ: The p53 proto-oncogene can act as a suppressor of transformation. Cell (1989) 57(7):1083-1093.
    • (1989) Cell , vol.57 , Issue.7 , pp. 1083-1093
    • Finlay, C.A.1    Hinds, P.W.2    Levine, A.J.3
  • 19
    • 14744278462 scopus 로고    scopus 로고
    • Small molecule antagonists of the MDM2 oncoprotein as anticancer agents
    • BUOLAMWINI JK, ADDO J, KAMATH S et al.: Small molecule antagonists of the MDM2 oncoprotein as anticancer agents. Curr. Cancer Drug Targets (2005) 5(1):57-68.
    • (2005) Curr. Cancer Drug Targets , vol.5 , Issue.1 , pp. 57-68
    • Buolamwini, J.K.1    Addo, J.2    Kamath, S.3
  • 20
    • 0035835820 scopus 로고    scopus 로고
    • Regulation of p53 function
    • WOODS DB, VOUSDEN KH: Regulation of p53 function. Exp. Cell Res. (2001) 264(1):56-66.
    • (2001) Exp. Cell Res. , vol.264 , Issue.1 , pp. 56-66
    • Woods, D.B.1    Vousden, K.H.2
  • 21
    • 0035006916 scopus 로고    scopus 로고
    • The role of p53 in human cancer
    • MALKIN D: The role of p53 in human cancer. J. Neurooncol. (2001) 51(3):231-243.
    • (2001) J. Neurooncol. , vol.51 , Issue.3 , pp. 231-243
    • Malkin, D.1
  • 23
    • 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(17):3551-3555.
    • (1994) Nucleic Acids Res. , vol.22 , Issue.17 , pp. 3551-3555
    • Hollstein, M.1    Rice, K.2    Greenblatt, M.S.3
  • 24
    • 0029845760 scopus 로고    scopus 로고
    • Structure and function of the p53 tumor suppressor gene: Clues for rational cancer therapeutic strategies
    • HARRIS CC: Structure and function of the p53 tumor suppressor gene: clues for rational cancer therapeutic strategies. J. Natl. Cancer Inst. (1996) 88(20):1442-1455.
    • (1996) J. Natl. Cancer Inst. , vol.88 , Issue.20 , pp. 1442-1455
    • Harris, C.C.1
  • 25
    • 0033959744 scopus 로고    scopus 로고
    • MDM2-master regulator of the p53 tumor suppressor protein
    • MOMAND J, WU HH, DASGUPTA G: MDM2-master regulator of the p53 tumor suppressor protein. Gene (2000) 242(1-2):15-29.
    • (2000) Gene , vol.242 , Issue.1-2 , pp. 15-29
    • Momand, J.1    Wu, H.H.2    Dasgupta, G.3
  • 26
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • CHO Y, GORINA S, JEFFREY PD, PAVLETICH NP: Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science (1994) 265(5170):346-355.
    • (1994) Science , vol.265 , Issue.5170 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 27
    • 0030722137 scopus 로고    scopus 로고
    • Hydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domain
    • MCCOY M, STAVRIDI ES, WATERMAN JL et al.: Hydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domain. EMBO J. (1997) 16(20):6230-6236.
    • (1997) EMBO J. , vol.16 , Issue.20 , pp. 6230-6236
    • McCoy, M.1    Stavridi, E.S.2    Waterman, J.L.3
  • 28
    • 0028965832 scopus 로고
    • Refined solution structure of the oligomerization domain of the tumour suppressor p53
    • CLORE GM, ERNST J, CLUBB R et al.: Refined solution structure of the oligomerization domain of the tumour suppressor p53. Nat. Struct. Biol. (1995) 2(4):321-333.
    • (1995) Nat. Struct. Biol. , vol.2 , Issue.4 , pp. 321-333
    • Clore, G.M.1    Ernst, J.2    Clubb, R.3
  • 29
    • 84970061891 scopus 로고
    • Solution structure of the tetrameric minimum transforming domain of p53
    • LEE W, HARVEY TS, YIN Y et al.: Solution structure of the tetrameric minimum transforming domain of p53. Nat. Struct. Biol. (1994) 1(12):877-890.
    • (1994) Nat. Struct. Biol. , vol.1 , Issue.12 , pp. 877-890
    • Lee, W.1    Harvey, T.S.2    Yin, Y.3
  • 30
    • 0033936746 scopus 로고    scopus 로고
    • Solution structure of a dynein motor domain associated light chain
    • WU H, MACIEJEWSKI MW, MARINTCHEVA et al.: Solution structure of a dynein motor domain associated light chain. Nat. Struct. Biol. (2000) 7(7):575-579.
    • (2000) Nat. Struct. Biol. , vol.7 , Issue.7 , pp. 575-579
    • Wu, H.1    Maciejewski, M.W.2    Marintchev, A.3
  • 31
    • 0028952841 scopus 로고
    • Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms
    • JEFFREY PD, GORINA S, PAVLETICH NP: Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms. Science (1995) 267(5203):1498-1502.
    • (1995) Science , vol.267 , Issue.5203 , pp. 1498-1502
    • Jeffrey, P.D.1    Gorina, S.2    Pavletich, N.P.3
  • 32
    • 0031951844 scopus 로고    scopus 로고
    • Crystallization and structure solution of p53 (residues 326-356) by molecular replacement using an NMR model as template
    • MITTL PR, CHENE P, GRUTTER MG: Crystallization and structure solution of p53 (residues 326-356) by molecular replacement using an NMR model as template. Acta Crystallogr. D Biol. Crystallogr. (1998) 54(Pt. 1):86-89.
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , Issue.PART 1 , pp. 86-89
    • Mittl, P.R.1    Chene, P.2    Grutter, M.G.3
  • 33
    • 0347723910 scopus 로고    scopus 로고
    • Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations
    • JOERGER AC, ALLEN MD, FERSHT AR: Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations. J. Biol. Chem. (2004) 279(2):1291-1296.
    • (2004) J. Biol. Chem. , vol.279 , Issue.2 , pp. 1291-1296
    • Joerger, A.C.1    Allen, M.D.2    Fersht, A.R.3
  • 34
    • 18144387188 scopus 로고    scopus 로고
    • Structures of p53 cancer mutants and mechanism of rescue by second-site suppressor mutations
    • JOERGER AC, ANG HC, VEPRINTSEV DB, BLAIR CM, FERSHT AR: Structures of p53 cancer mutants and mechanism of rescue by second-site suppressor mutations. J. Biol. Chem. (2005) 280(16):16030-16037.
    • (2005) J. Biol. Chem. , vol.280 , Issue.16 , pp. 16030-16037
    • Joerger, A.C.1    Ang, H.C.2    Veprintsev, D.B.3    Blair, C.M.4    Fersht, A.R.5
  • 35
    • 0030575937 scopus 로고    scopus 로고
    • Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain
    • KUSSIE PH, GORINA S, MARECHAL V et al.: Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science (1996) 274(5289):948-953.
    • (1996) Science , vol.274 , Issue.5289 , pp. 948-953
    • Kussie, P.H.1    Gorina, S.2    Marechal, V.3
  • 37
    • 0035827308 scopus 로고    scopus 로고
    • Molecular biology. Getting p53 out of the nucleus
    • GOTTIFREDI V, PRIVES C: Molecular biology. Getting p53 out of the nucleus. Science (2001) 292(5523):1851-1852.
    • (2001) Science , vol.292 , Issue.5523 , pp. 1851-1852
    • Gottifredi, V.1    Prives, C.2
  • 38
    • 0037048646 scopus 로고    scopus 로고
    • Study of the cytotoxic effect of a peptidic inhibitor of the p53-HDM2 interaction in tumor cells
    • CHENE P, FUCHS J, CARENA I, FURET P, GARCIA-ECHEVERRIA C: Study of the cytotoxic effect of a peptidic inhibitor of the p53-HDM2 interaction in tumor cells. FEBS Lett. (2002) 529(2-3):293-297.
    • (2002) FEBS Lett. , vol.529 , Issue.2-3 , pp. 293-297
    • Chene, P.1    Fuchs, J.2    Carena, I.3    Furet, P.4    Garcia-Echeverria, C.5
  • 39
    • 0028303752 scopus 로고
    • Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to MDM2 and the adenovirus 5 E1B 55 kD protein
    • LIN J, CHEN J, ELENBAAS B, LEVINE AJ: Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to MDM2 and the adenovirus 5 E1B 55 kD protein. Genes Dev. (1994) 8(10):1235-1246.
    • (1994) Genes Dev. , vol.8 , Issue.10 , pp. 1235-1246
    • Lin, J.1    Chen, J.2    Elenbaas, B.3    Levine, A.J.4
  • 40
    • 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 SM, VOJTESEK B, SPARKS A, LANE DP: Immunochemical analysis of the interaction of p53 with MDM2; fine mapping of the MDM2 binding site on p53 using synthetic peptides. Oncogene (1994) 9(9):2523-2529.
    • (1994) Oncogene , vol.9 , Issue.9 , pp. 2523-2529
    • Picksley, S.M.1    Vojtesek, B.2    Sparks, A.3    Lane, D.P.4
  • 41
    • 0031588025 scopus 로고    scopus 로고
    • Molecular characterization of the hdm2-p53 interaction
    • BOTTGER A, BOTTGER V, GARCIA-ECHEVERRIA C et al.: Molecular characterization of the hdm2-p53 interaction. J. Mol. Biol. (1997) 269(5):744-756.
    • (1997) J. Mol. Biol. , vol.269 , Issue.5 , pp. 744-756
    • Bottger, A.1    Bottger, V.2    Garcia-Echeverria, C.3
  • 42
    • 0029818380 scopus 로고    scopus 로고
    • Identification of novel mdm2 binding peptides by phage display
    • BOTTGER V, BOTTGER A, HOWARD SF et al.: Identification of novel mdm2 binding peptides by phage display. Oncogene (1996) 13(10):2141-2147.
    • (1996) Oncogene , vol.13 , Issue.10 , pp. 2141-2147
    • Bottger, V.1    Bottger, A.2    Howard, S.F.3
  • 43
    • 0842325666 scopus 로고    scopus 로고
    • Inhibition of the p53-MDM2 interaction: Targeting a protein-protein interface
    • CHENE P: Inhibition of the p53-MDM2 interaction: targeting a protein-protein interface. Mol. Cancer Res. (2004) 2(1):20-28.
    • (2004) Mol. Cancer Res. , vol.2 , Issue.1 , pp. 20-28
    • Chene, P.1
  • 44
    • 0347761215 scopus 로고    scopus 로고
    • Binding of p53-derived ligands to MDM2 induces a variety of long range conformational changes
    • SCHON O, FRIEDLER A, FREUND S, FERSHT AR: Binding of p53-derived ligands to MDM2 induces a variety of long range conformational changes. J. Mol. Biol. (2004) 336(1):197-202.
    • (2004) J. Mol. Biol. , vol.336 , Issue.1 , pp. 197-202
    • Schon, O.1    Friedler, A.2    Freund, S.3    Fersht, A.R.4
  • 45
    • 21344461945 scopus 로고    scopus 로고
    • p53 α-Helix mimetics antagonize p53/MDM2 interaction and activate p53
    • CHEN L, YIN H, FAROOQI B et al.: p53 α-Helix mimetics antagonize p53/MDM2 interaction and activate p53. Mol. Cancer Ther. (2005) 4(6):1019-1025.
    • (2005) Mol. Cancer Ther. , vol.4 , Issue.6 , pp. 1019-1025
    • Chen, L.1    Yin, H.2    Farooqi, B.3
  • 46
    • 0035895350 scopus 로고    scopus 로고
    • Chalcone derivatives antagonize interactions between the human oncoprotein MDM2 and p53
    • STOLL R, RENNER C, HANSEN S et al.: Chalcone derivatives antagonize interactions between the human oncoprotein MDM2 and p53. Biochemistry (2001) 40(2):336-344.
    • (2001) Biochemistry , vol.40 , Issue.2 , pp. 336-344
    • Stoll, R.1    Renner, C.2    Hansen, S.3
  • 47
    • 0035977612 scopus 로고    scopus 로고
    • Isolation and structure elucidation of Chlorofusin, a novel p53-MDM2 antagonist from a Fusarium sp
    • DUNCAN SJ, GRUSCHOW S, WILLIAMS DH et al.: Isolation and structure elucidation of Chlorofusin, a novel p53-MDM2 antagonist from a Fusarium sp. J. Am. Chem. Soc. (2001) 123(4):554-560.
    • (2001) J. Am. Chem. Soc. , vol.123 , Issue.4 , pp. 554-560
    • Duncan, S.J.1    Gruschow, S.2    Williams, D.H.3
  • 48
    • 0037044103 scopus 로고    scopus 로고
    • The initial evaluation of non-peptidic small-molecule HDM2 inhibitors based on p53-HDM2 complex structure
    • ZHAO J, WANG M, CHEN J et al.: The initial evaluation of non-peptidic small-molecule HDM2 inhibitors based on p53-HDM2 complex structure. Cancer Lett. (2002) 183(1):69-77.
    • (2002) Cancer Lett. , vol.183 , Issue.1 , pp. 69-77
    • Zhao, J.1    Wang, M.2    Chen, J.3
  • 49
    • 0037784028 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of novel boronic-chalcone derivatives as antitumor agents
    • KUMAR SK, HAGER E, PETTIT C et al.: Design, synthesis, and evaluation of novel boronic-chalcone derivatives as antitumor agents. J. Med. Chem. (2003) 46(14):2813-2815.
    • (2003) J. Med. Chem. , vol.46 , Issue.14 , pp. 2813-2815
    • Kumar, S.K.1    Hager, E.2    Pettit, C.3
  • 50
    • 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(5659):844-848.
    • (2004) Science , vol.303 , Issue.5659 , pp. 844-848
    • Vassilev, L.T.1    Vu, B.T.2    Graves, B.3
  • 51
    • 13944274061 scopus 로고    scopus 로고
    • Discovery and cocrystal structure of benzodiazepinedione HDM2 antagonists that activate p53 in cells
    • GRASBERGER BL, LU T, SCHUBERT C et al.: Discovery and cocrystal structure of benzodiazepinedione HDM2 antagonists that activate p53 in cells. J. Med. Chem. (2005) 48(4):909-912.
    • (2005) J. Med. Chem. , vol.48 , Issue.4 , pp. 909-912
    • Grasberger, B.L.1    Lu, T.2    Schubert, C.3
  • 52
    • 0346455771 scopus 로고    scopus 로고
    • The MDM2-p53 interaction
    • MOLL UM, PETRENKO O: The MDM2-p53 interaction. Mol. Cancer Res. (2003) 1(14):1001-1008.
    • (2003) Mol. Cancer Res. , vol.1 , Issue.14 , pp. 1001-1008
    • Moll, U.M.1    Petrenko, O.2
  • 53
    • 0037317840 scopus 로고    scopus 로고
    • Inhibiting the p53-MDM2 interaction: An important target for cancer therapy
    • CHENE P: Inhibiting the p53-MDM2 interaction: an important target for cancer therapy. Nat Rev Cancer (2003) 3(2):102-109.
    • (2003) Nat Rev Cancer , vol.3 , Issue.2 , pp. 102-109
    • Chene, P.1
  • 54
    • 0036247821 scopus 로고    scopus 로고
    • p53-MDM2 - The affair that never ends
    • ALARCON-VARGAS D, RONAI Z: p53-MDM2 - the affair that never ends. Carcinogenesis (2002) 23(4):541-547.
    • (2002) Carcinogenesis , vol.23 , Issue.4 , pp. 541-547
    • Alarcon-Vargas, D.1    Ronai, Z.2
  • 55
    • 0034716943 scopus 로고    scopus 로고
    • A small synthetic peptide, which inhibits the p53-HDM2 interaction, stimulates the p53 pathway in tumour cell lines
    • CHENE P, FUCHS J, BOHN J et al.: A small synthetic peptide, which inhibits the p53-HDM2 interaction, stimulates the p53 pathway in tumour cell lines. J. Mol. Biol. (2000) 299(1):245-253.
    • (2000) J. Mol. Biol. , vol.299 , Issue.1 , pp. 245-253
    • Chene, P.1    Fuchs, J.2    Bohn, J.3
  • 56
    • 0029085397 scopus 로고
    • Effect of a novel anti-rheumatic drug, TA-383, on type II collagen-induced arthritis
    • UENO M, IMAIZUMI K, SUGITA T, TAKATA I, TAKESHITA M: Effect of a novel anti-rheumatic drug, TA-383, on type II collagen-induced arthritis. Int. J. Immunopharmacol. (1995) 17(7):597-603.
    • (1995) Int. J. Immunopharmacol. , vol.17 , Issue.7 , pp. 597-603
    • Ueno, M.1    Imaizumi, K.2    Sugita, T.3    Takata, I.4    Takeshita, M.5
  • 57
    • 0030811201 scopus 로고    scopus 로고
    • The novel anti-rheumatic drug TA-383 has a macrophage migration enhancing activity
    • UENO M, SUGITA T, MURAKAMI T, TAKATA I: The novel anti-rheumatic drug TA-383 has a macrophage migration enhancing activity. Jpn. J. Pharmacol. (1997) 74(2):221-224.
    • (1997) Jpn. J. Pharmacol. , vol.74 , Issue.2 , pp. 221-224
    • Ueno, M.1    Sugita, T.2    Murakami, T.3    Takata, I.4
  • 58
    • 10644228446 scopus 로고    scopus 로고
    • Synthesis and SAR of novel 4,5-diarylimidazolines as potent P2X7 receptor antagonists
    • MERRIMAN GH, MA L, SHUM P et al.: Synthesis and SAR of novel 4,5-diarylimidazolines as potent P2X7 receptor antagonists. Bioorg. Med. Chem. Lett (2005) 15(2):435-438.
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , Issue.2 , pp. 435-438
    • Merriman, G.H.1    Ma, L.2    Shum, P.3
  • 59
    • 22244443786 scopus 로고    scopus 로고
    • p53 activation by small molecules: Application in oncology
    • VASSILEV LT: p53 activation by small molecules: application in oncology. J. Med. Chem. (2005) 48(14):4491-4499.
    • (2005) J. Med. Chem. , vol.48 , Issue.14 , pp. 4491-4499
    • Vassilev, L.T.1
  • 60
    • 7944239221 scopus 로고    scopus 로고
    • Targeting the p53-MDM2 interaction to treat cancer
    • KLEIN C, VASSILEV LT: Targeting the p53-MDM2 interaction to treat cancer. Br. J. Cancer (2004) 91(8):1415-1419.
    • (2004) Br. J. Cancer , vol.91 , Issue.8 , pp. 1415-1419
    • Klein, C.1    Vassilev, L.T.2
  • 61
    • 17944391288 scopus 로고    scopus 로고
    • Synthesis and anti-HIV activity of 1,3,4,5-tetrahydro-2H-1,4-benzodiazepin-2-one (TBO) derivatives Truncated. 4,5,6,7-tetrahydro-5-methylimidazo[4,5,1-jk][1,4]benzodiazepin-2(1H)-ones (TIBO) analogues
    • BRESLIN HJ, KUKLA MJ, KROMIS T et al.: Synthesis and anti-HIV activity of 1,3,4,5-tetrahydro-2H-1,4-benzodiazepin-2-one (TBO) derivatives. Truncated 4,5,6,7-tetrahydro-5-methylimidazo[4,5,1-jk][1,4]benzodiazepin-2(1H)-ones (TIBO) analogues. Bioorg. Med. Chem. (1999) 7(11):2427-2436.
    • (1999) Bioorg. Med. Chem. , vol.7 , Issue.11 , pp. 2427-2436
    • Breslin, H.J.1    Kukla, M.J.2    Kromis, T.3
  • 62
    • 4544328629 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of mixed imine-amine pyrrolobenzodiazepine dimers with efficient DNA binding affinity and potent cytotoxicity
    • KAMAL A, RAMESH C, SRINIVAS O et al.: Design, synthesis, and evaluation of mixed imine-amine pyrrolobenzodiazepine dimers with efficient DNA binding affinity and potent cytotoxicity. Bioorg. Med. Chem. (2004) 12(20):5427-5436.
    • (2004) Bioorg. Med. Chem. , vol.12 , Issue.20 , pp. 5427-5436
    • Kamal, A.1    Ramesh, C.2    Srinivas, O.3
  • 63
    • 3242809006 scopus 로고    scopus 로고
    • Synthesis and DNA binding affinity of novel A-C8/C-C2-exo unsaturated alkoxyamido-linked pyrrolo[2,1-c][1,4]benzodiazepine dimers
    • KAMAL A, SRINIVAS O, RAMULU P et al.: Synthesis and DNA binding affinity of novel A-C8/C-C2-exo unsaturated alkoxyamido-linked pyrrolo[2,1-c][1,4]benzodiazepine dimers. Bioorg. Med. Chem. (2004) 12(16):4337-4350.
    • (2004) Bioorg. Med. Chem. , vol.12 , Issue.16 , pp. 4337-4350
    • Kamal, A.1    Srinivas, O.2    Ramulu, P.3
  • 64
    • 0035282633 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of a novel pyrrolobenzodiazepine DNA-interactive agent with highly efficient cross-linking ability and potent cytotoxicity
    • GREGSON SJ, HOWARD PW, HARTLEY JA et al.: Design, synthesis, and evaluation of a novel pyrrolobenzodiazepine DNA-interactive agent with highly efficient cross-linking ability and potent cytotoxicity. J. Med. Chem. (2001) 44(5):737-748.
    • (2001) J. Med. Chem. , vol.44 , Issue.5 , pp. 737-748
    • Gregson, S.J.1    Howard, P.W.2    Hartley, J.A.3
  • 65
    • 0037295132 scopus 로고    scopus 로고
    • Design, synthesis and biological activity of YM-60828 derivatives. Part 2: Potent and orally-bioavailable Factor Xa inhibitors based on benzothiadiazine-4-one template
    • HIRAYAMA F, KOSHIO H, KATAYAMA N et al.: Design, synthesis and biological activity of YM-60828 derivatives. Part 2: potent and orally-bioavailable Factor Xa inhibitors based on benzothiadiazine-4-one template. Bioorg. Med. Chem. (2003) 11(3):367-381.
    • (2003) Bioorg. Med. Chem. , vol.11 , Issue.3 , pp. 367-381
    • Hirayama, F.1    Koshio, H.2    Katayama, N.3
  • 66
    • 0037057577 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of new noncross-linking pyrrolobenzodiazepine dimers with efficient DNA binding ability and potent antitumor activity
    • KAMAL A, RAMESH G, LAXMAN N et al.: Design, synthesis, and evaluation of new noncross-linking pyrrolobenzodiazepine dimers with efficient DNA binding ability and potent antitumor activity. J. Med. Chem. (2002) 45(21):4679-4688.
    • (2002) J. Med. Chem. , vol.45 , Issue.21 , pp. 4679-4688
    • Kamal, A.1    Ramesh, G.2    Laxman, N.3
  • 67
    • 0031455043 scopus 로고    scopus 로고
    • Synthesis of new N-substituted benzodiazepine derivatives with potential anxiolytic activity
    • KOSSAKOWSKI J, ZAWADOWSKI T, TURIO J: Synthesis of new N-substituted benzodiazepine derivatives with potential anxiolytic activity. Acta Pol. Pharm. (1997) 54(6):483-485.
    • (1997) Acta Pol. Pharm. , vol.54 , Issue.6 , pp. 483-485
    • Kossakowski, J.1    Zawadowski, T.2    Turio, J.3
  • 68
    • 0000228887 scopus 로고    scopus 로고
    • Synthesis and herbicidal activity of 1H-1,4-benzodiazepine-2,5-diones
    • KARP G, MANFREDI MC, GUACIARO MA et al.: Synthesis and herbicidal activity of 1H-1,4-benzodiazepine-2,5-diones. J. Agric. Food Chem. (1997) 45(2):493-500.
    • (1997) J. Agric. Food Chem. , vol.45 , Issue.2 , pp. 493-500
    • Karp, G.1    Manfredi, M.C.2    Guaciaro, M.A.3
  • 69
    • 20144382874 scopus 로고    scopus 로고
    • Structure-based design, synthesis, and biological evaluation of novel 1,4-diazepines as HDM2 antagonists
    • RABOISSON P, MARUGAN JJ, SCHUBERT C et al.: Structure-based design, synthesis, and biological evaluation of novel 1,4-diazepines as HDM2 antagonists. Bioorg. Med. Chem. Lett. (2005) 15(7):1857-1861.
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , Issue.7 , pp. 1857-1861
    • Raboisson, P.1    Marugan, J.J.2    Schubert, C.3
  • 70
    • 21144436251 scopus 로고    scopus 로고
    • N-Arylpiperazine-1-carboxamide derivatives: A novel series of orally active nonsteroidal androgen receptor antagonists
    • KINOYAMA I, TANIGUCHI N, KAWAMINAMI E et al.: N-Arylpiperazine-1-carboxamide derivatives: a novel series of orally active nonsteroidal androgen receptor antagonists. Chem. Pharm. Bull. (2005) 53(4):402-409.
    • (2005) Chem. Pharm. Bull. , vol.53 , Issue.4 , pp. 402-409
    • Kinoyama, I.1    Taniguchi, N.2    Kawaminami, E.3
  • 71
    • 21144448834 scopus 로고    scopus 로고
    • Synthesis and pharmacological evaluation of novel arylpiperazine derivatives as nonsteroidal androgen receptor antagonists
    • KINOYAMA I, TANIGUCHI N, YODEN T et al.: Synthesis and pharmacological evaluation of novel arylpiperazine derivatives as nonsteroidal androgen receptor antagonists. Chem. Pharm. Bull. (2004) 52(11):1330-1333.
    • (2004) Chem. Pharm. Bull. , vol.52 , Issue.11 , pp. 1330-1333
    • Kinoyama, I.1    Taniguchi, N.2    Yoden, T.3
  • 72
    • 3242755097 scopus 로고    scopus 로고
    • Synthesis and antibacterial activity of 2-(4-substituted phenyl)-3(2H)-isothiazolones
    • KHALAJ A, ADIBPOUR N, SHAHVERDI AR, DANESHTALAB M: Synthesis and antibacterial activity of 2-(4-substituted phenyl)-3(2H)-isothiazolones. Eur J. Med. Chem. (2004) 39(8):699-705.
    • (2004) Eur J. Med. Chem. , vol.39 , Issue.8 , pp. 699-705
    • Khalaj, A.1    Adibpour, N.2    Shahverdi, A.R.3    Daneshtalab, M.4
  • 73
    • 16644402498 scopus 로고    scopus 로고
    • Antiangiogenic and anti-tumor apoptotic activities of SJ-8002, a new piperazine derivative
    • YI EY, JEONG EJ, SONG HS et al.: Antiangiogenic and anti-tumor apoptotic activities of SJ-8002, a new piperazine derivative. Int. J. Oncol. (2004) 25(2):365-372.
    • (2004) Int. J. Oncol. , vol.25 , Issue.2 , pp. 365-372
    • Yi, E.Y.1    Jeong, E.J.2    Song, H.S.3
  • 74
    • 1642452634 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of piperazine-based derivatives as inhibitors of plasminogen activator inhibitor-1 (PAI-1)
    • YE B, CHOU YL, KARANJAWALA R et al.: Synthesis and biological evaluation of piperazine-based derivatives as inhibitors of plasminogen activator inhibitor-1 (PAI-1). Bioorg. Med. Chem. Lett. (2004) 14(3):761-765.
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , Issue.3 , pp. 761-765
    • Ye, B.1    Chou, Y.L.2    Karanjawala, R.3
  • 75
    • 0035214342 scopus 로고    scopus 로고
    • Current advances in the inhibition of the auto-regulatory interaction between the p53 tumour suppressor protein and MDM2 protein
    • PICKSLEY SM, DART DA, MANSOOR MS, LOADMAN PM: Current advances in the inhibition of the auto-regulatory interaction between the p53 tumour suppressor protein and MDM2 protein. Expert Opin. Ther. Patents (2001) 11(12):1825-1835.
    • (2001) Expert Opin. Ther. Patents , vol.11 , Issue.12 , pp. 1825-1835
    • Picksley, S.M.1    Dart, D.A.2    Mansoor, M.S.3    Loadman, P.M.4
  • 76
    • 0034975161 scopus 로고    scopus 로고
    • p53 as drug target in cancer therapy
    • CHENE P: p53 as drug target in cancer therapy. Expert Opin. Ther. Patents (2001) 11(6):923-935.
    • (2001) Expert Opin. Ther. Patents , vol.11 , Issue.6 , pp. 923-935
    • Chene, P.1
  • 77
    • 13844314649 scopus 로고    scopus 로고
    • Structure-activity relationship for aryl and heteroaryl boronic acid inhibitors of hormone-sensitive lipase
    • EBDRUP S, JACOBSEN P, FARRINGTON AD, VEDSO P: Structure-activity relationship for aryl and heteroaryl boronic acid inhibitors of hormone-sensitive lipase. Bioorg. Med. Chem. (2005) 13(6):2305-2312.
    • (2005) Bioorg. Med. Chem. , vol.13 , Issue.6 , pp. 2305-2312
    • Ebdrup, S.1    Jacobsen, P.2    Farrington, A.D.3    Vedso, P.4
  • 78
    • 2942555566 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of aminoboronic acids as growth-factor receptor inhibitors of EGFR and VEGFR-1 tyrosine kinases
    • ASANO T, NAKAMURA H, UEHARA Y, YAMAMOTO Y: Design, synthesis, and biological evaluation of aminoboronic acids as growth-factor receptor inhibitors of EGFR and VEGFR-1 tyrosine kinases. Chembiochem (2004) 5(4):483-490.
    • (2004) Chembiochem , vol.5 , Issue.4 , pp. 483-490
    • Asano, T.1    Nakamura, H.2    Uehara, Y.3    Yamamoto, Y.4
  • 79
    • 22944473048 scopus 로고    scopus 로고
    • Structure-based design of potent non-peptide MDM2 inhibitors
    • DING K, LU Y, NIKOLOVSKA-COLESKA Z et al.: Structure-based design of potent non-peptide MDM2 inhibitors. J. Am. Chem. Soc. (2005) 127(29):10130-10131.
    • (2005) J. Am. Chem. Soc. , vol.127 , Issue.29 , pp. 10130-10131
    • Ding, K.1    Lu, Y.2    Nikolovska-Coleska, Z.3
  • 80
    • 0037061646 scopus 로고    scopus 로고
    • Inhibition of protein-protein association by small molecules: Approaches and progress
    • TOOGOOD PL: Inhibition of protein-protein association by small molecules: approaches and progress. J. Med. Chem. (2002) 45(8):1543-1558.
    • (2002) J. Med. Chem. , vol.45 , Issue.8 , pp. 1543-1558
    • Toogood, P.L.1
  • 81
    • 0032705432 scopus 로고    scopus 로고
    • Designed molecules that fold to mimic protein secondary structures
    • STIGERS KD, SOTH MJ, NOWICK JS: Designed molecules that fold to mimic protein secondary structures. Curr. Opin. Chem. Biol. (1999) 3(6):714-723.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , Issue.6 , pp. 714-723
    • Stigers, K.D.1    Soth, M.J.2    Nowick, J.S.3
  • 82
    • 22244448954 scopus 로고    scopus 로고
    • Synthesis of pipecolic acid-based spiro bicyclic lactam scaffolds as beta-turn mimics
    • SOMU RV, JOHNSON RL: Synthesis of pipecolic acid-based spiro bicyclic lactam scaffolds as beta-turn mimics. J. Org. Chem. (2005) 70(15):5954-5963.
    • (2005) J. Org. Chem. , vol.70 , Issue.15 , pp. 5954-5963
    • Somu, R.V.1    Johnson, R.L.2
  • 83
    • 3242792576 scopus 로고    scopus 로고
    • Design, synthesis, and conformational analysis of eight-membered cydic peptidomimetics prepared using ring closing metathesis
    • CREIGHTON CJ, LEO GC, DU Y, REITZ AB: Design, synthesis, and conformational analysis of eight-membered cydic peptidomimetics prepared using ring closing metathesis. Bioorg. Med. Chem. (2004) 12(16):4375-4385.
    • (2004) Bioorg. Med. Chem. , vol.12 , Issue.16 , pp. 4375-4385
    • Creighton, C.J.1    Leo, G.C.2    Du, Y.3    Reitz, A.B.4
  • 84
    • 18744403986 scopus 로고    scopus 로고
    • Systematic study of the synthesis of macrocyclic dipeptide β-turn mimics possessing 8-, 9- and 10-membered rings by ring-closing metathesis
    • KAUL R, SURPRENANT S, LUBELL WD: Systematic study of the synthesis of macrocyclic dipeptide β-turn mimics possessing 8-, 9- and 10-membered rings by ring-closing metathesis. J. Org. Chem. (2005) 70(10):3838-3844.
    • (2005) J. Org. Chem. , vol.70 , Issue.10 , pp. 3838-3844
    • Kaul, R.1    Surprenant, S.2    Lubell, W.D.3
  • 85
    • 0037139577 scopus 로고    scopus 로고
    • Effect of sequence on peptide geometry in 5-tert-butylprolyl type VI β-turn mimics
    • HALAB L, LUBELL WD: Effect of sequence on peptide geometry in 5-tert-butylprolyl type VI β-turn mimics. J. Am. Chem. Soc. (2002) 124(11):2474-2484.
    • (2002) J. Am. Chem. Soc. , vol.124 , Issue.11 , pp. 2474-2484
    • Halab, L.1    Lubell, W.D.2
  • 86
    • 0034801374 scopus 로고    scopus 로고
    • Toward proteomimetics: Terphenyl derivatives as structural and functional mimics of extended regions of an α-helix
    • ORNER BP, ERNST JT, HAMILTON AD: Toward proteomimetics: terphenyl derivatives as structural and functional mimics of extended regions of an α-helix. J. Am. Chem. Soc. (2001) 123(22):5382-5383.
    • (2001) J. Am. Chem. Soc. , vol.123 , Issue.22 , pp. 5382-5383
    • Orner, B.P.1    Ernst, J.T.2    Hamilton, A.D.3
  • 87
    • 0028898424 scopus 로고
    • Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade
    • SCHEFFNER M, NUBER U, HUIBREGTSE JM: Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade. Nature (1995) 373(6509):81-83.
    • (1995) Nature , vol.373 , Issue.6509 , pp. 81-83
    • Scheffner, M.1    Nuber, U.2    Huibregtse, J.M.3
  • 88
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • WEISSMAN AM: Themes and variations on ubiquitylation. Nat. Rev. Mol. Cell. Biol. (2001) 2(3):169-178.
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , Issue.3 , pp. 169-178
    • Weissman, A.M.1
  • 89
    • 0345086463 scopus 로고    scopus 로고
    • One ring to rule a superfamily of E3 ubiquitin ligases
    • 601
    • TYERS M, WILLEMS AR: One ring to rule a superfamily of E3 ubiquitin ligases. Science (1999) 284(5414):601, 603-604.
    • (1999) Science , vol.284 , Issue.5414 , pp. 603-604
    • Tyers, M.1    Willems, A.R.2
  • 90
    • 18744406282 scopus 로고    scopus 로고
    • Differentiation of HDM2-mediated p53 ubiquitination and HDM2 autoubiquitination activity by small molecular weight inhibitors
    • LAI Z, YANG T, KIM YB et al.: Differentiation of HDM2-mediated p53 ubiquitination and HDM2 autoubiquitination activity by small molecular weight inhibitors. Proc. Natl. Acad. Sci. USA (2002) 99(23):14734-14739.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.23 , pp. 14734-14739
    • Lai, Z.1    Yang, T.2    Kim, Y.B.3
  • 91
    • 20444369867 scopus 로고    scopus 로고
    • Small molecule inhibitors of HDM2 ubiquitin ligase activity stabilize and activate p53 in cells
    • YANG Y, LUDWIG RL, JENSEN JP et al.: Small molecule inhibitors of HDM2 ubiquitin ligase activity stabilize and activate p53 in cells. Cancer Cell (2005) 7(6):547-559.
    • (2005) Cancer Cell , vol.7 , Issue.6 , pp. 547-559
    • Yang, Y.1    Ludwig, R.L.2    Jensen, J.P.3
  • 92
    • 24044466754 scopus 로고    scopus 로고
    • Reactivation of mutant p53 and induction of apoptosis in human tumor cells by maleimide analogs
    • BYKOV VJ, ISSAEVA N, ZACHE N et al.: Reactivation of mutant p53 and induction of apoptosis in human tumor cells by maleimide analogs. J. Biol. Chem. (2005) 280(34):30384-30391.
    • (2005) J. Biol. Chem. , vol.280 , Issue.34 , pp. 30384-30391
    • Bykov, V.J.1    Issaeva, N.2    Zache, N.3
  • 93
    • 0142058248 scopus 로고    scopus 로고
    • Small molecules that reactivate mutant p53
    • BYKOV VJ, SELIVANOVA G, WIMAN KG: Small molecules that reactivate mutant p53. Eur. J. Cancer (2003) 39(13):1828-1834.
    • (2003) Eur. J. Cancer , vol.39 , Issue.13 , pp. 1828-1834
    • Bykov, V.J.1    Selivanova, G.2    Wiman, K.G.3
  • 94
    • 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(5449):2507-2510.
    • (1999) Science , vol.286 , Issue.5449 , pp. 2507-2510
    • Foster, B.A.1    Coffey, H.A.2    Morin, M.J.3    Rastinejad, F.4
  • 95
    • 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(3):282-288.
    • (2002) Nat. Med. , vol.8 , Issue.3 , pp. 282-288
    • Bykov, V.J.1    Issaeva, N.2    Shilov, A.3
  • 96
    • 19444387176 scopus 로고    scopus 로고
    • PRIMA-1(MET) synergizes with cisplatin to induce tumor cell apoptosis
    • BYKOV VJ, ZACHEN, STRIDH H et al.: PRIMA-1(MET) synergizes with cisplatin to induce tumor cell apoptosis. Oncogene (2005) 24(21):3484-3491.
    • (2005) Oncogene , vol.24 , Issue.21 , pp. 3484-3491
    • Bykov, V.J.1    Zachen Stridh, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.