메뉴 건너뛰기




Volumn 1, Issue 6, 2009, Pages 1075-1094

Inhibitors of MDM2 and MDMX: A structural perspective

Author keywords

[No Author keywords available]

Indexed keywords

BENZODIAZEPINEDIONE; CHALCONE; CHLOROFUSIN; DIAZEPINE DERIVATIVE; HEXYLITACONIC ACID; MI 17; MI 219; MI 43; MI 63; NU 8231; NUTLIN 1; NUTLIN 2; NUTLIN 3; NXN 6; NXN 7; PEPTIDE 8; PROTEIN INHIBITOR; PROTEIN MDM2; PROTEIN MDMX; PROTEIN P53; SPIROOXINDOLE; SULFONAMIDE; SYC; UNCLASSIFIED DRUG;

EID: 77953424554     PISSN: 17568919     EISSN: None     Source Type: Journal    
DOI: 10.4155/fmc.09.75     Document Type: Review
Times cited : (29)

References (149)
  • 1
    • 0030941458 scopus 로고    scopus 로고
    • P53, the cellular gatekeeper for growth and division
    • Levine AJ. p53, the cellular gatekeeper for growth and division. Cell 88, 323-331 (1997).
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 2
  • 3
    • 0033992478 scopus 로고    scopus 로고
    • P53 and human cancer: The first ten thousand mutations
    • Hainaut P, Hollstein M. p53 and human cancer: the first ten thousand mutations. Adv. Cancer Res. 77, 81-137 (2000).
    • (2000) Adv. Cancer Res. , vol.77 , pp. 81-137
    • Hainaut, P.1    Hollstein, M.2
  • 4
    • 0037051095 scopus 로고    scopus 로고
    • P53: A ubiquitous target of anticancer drugs
    • Blagosklonny MV. p53: a ubiquitous target of anticancer drugs. Int. J. Cancer 98, 161-166 (2002).
    • (2002) Int. J. Cancer , vol.98 , pp. 161-166
    • Blagosklonny, M.V.1
  • 6
    • 33845270990 scopus 로고    scopus 로고
    • Regulating the p53 pathway: In vitro hypotheses, in vivo veritas
    • Toledo F, Wahl GM. Regulating the p53 pathway: in vitro hypotheses, in vivo veritas. Nat. Rev. Cancer 6, 909-923 (2006).
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 909-923
    • Toledo, F.1    Wahl, G.M.2
  • 7
    • 33845611951 scopus 로고    scopus 로고
    • Modeling the therapeutic efficacy of p53 restoration in tumors
    • Martins CP, Brown-Swigart L, Evan GI. Modeling the therapeutic efficacy of p53 restoration in tumors. Cell 127, 1323-1334 (2006).
    • (2006) Cell , vol.127 , pp. 1323-1334
    • Martins, C.P.1    Brown-Swigart, L.2    Evan, G.I.3
  • 8
    • 33846937033 scopus 로고    scopus 로고
    • Senescence and tumour clearance is triggered by p53 restoration in murine liver carcinomas
    • Xue W, Zender L, Miething C et al. Senescence and tumour clearance is triggered by p53 restoration in murine liver carcinomas. Nature 445, 656-660 (2007).
    • (2007) Nature , vol.445 , pp. 656-660
    • Xue, W.1    Zender, L.2    Miething, C.3
  • 9
    • 33846899456 scopus 로고    scopus 로고
    • Restoration of p53 function leads to tumour regression in vivo
    • Ventura A, Kirsch DG, McLaughlin ME et al. Restoration of p53 function leads to tumour regression in vivo. Nature 445, 661-665 (2007).
    • (2007) Nature , vol.445 , pp. 661-665
    • Ventura, A.1    Kirsch, D.G.2    McLaughlin, M.E.3
  • 10
    • 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 274, 948-953 (1996).
    • (1996) Science , vol.274 , pp. 948-953
    • Kussie, P.H.1    Gorina, S.2    Marechal, V.3
  • 11
    • 35948933091 scopus 로고    scopus 로고
    • Molecular basis for the inhibition of p53 by Mdmx
    • Popowicz GM, Czarna A, Rothweiler U et al. Molecular basis for the inhibition of p53 by Mdmx. Cell Cycle 6, 2386-2392 (2007).
    • (2007) Cell Cycle , vol.6 , pp. 2386-2392
    • Popowicz, G.M.1    Czarna, A.2    Rothweiler, U.3
  • 12
    • 0027109075 scopus 로고
    • Cancer. p53, guardian of the genome
    • Lane DP. Cancer. p53, guardian of the genome. Nature 358, 15-16 (1992).
    • (1992) Nature , vol.358 , pp. 15-16
    • Lane, D.P.1
  • 13
    • 0026560995 scopus 로고
    • Formation of stable p53 homotetramers and multiples of tetramers
    • Stenger JE, Mayr GA, Mann K, Tegtmeyer P. Formation of stable p53 homotetramers and multiples of tetramers. Mol. Carcinog. 5, 102-106 (1992).
    • (1992) Mol. Carcinog. , vol.5 , pp. 102-106
    • Stenger, J.E.1    Mayr, G.A.2    Mann, K.3    Tegtmeyer, P.4
  • 14
    • 0025024469 scopus 로고
    • Presence of a potent transcription activating sequence in the p53 protein
    • Fields S, Jang SK. Presence of a potent transcription activating sequence in the p53 protein. Science 249, 1046-1049 (1990).
    • (1990) Science , vol.249 , pp. 1046-1049
    • Fields, S.1    Jang, S.K.2
  • 15
    • 0025193635 scopus 로고
    • Transcriptional activation by wild-type but not transforming mutants of the p53 anti-oncogene
    • Raycroft L, Wu HY, Lozano G. Transcriptional activation by wild-type but not transforming mutants of the p53 anti-oncogene. Science 249, 1049-1051 (1990).
    • (1990) Science , vol.249 , pp. 1049-1051
    • Raycroft, L.1    Wu, H.Y.2    Lozano, G.3
  • 16
    • 0028812627 scopus 로고
    • Transactivation ability of p53 transcriptional activation domain is directly related to the binding affinity to TATAbinding protein
    • Chang J, Kim DH, Lee SW, Choi KY, Sung YC. Transactivation ability of p53 transcriptional activation domain is directly related to the binding affinity to TATAbinding protein. J. Biol. Chem. 270, 25014-25019 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 25014-25019
    • Chang, J.1    Kim, D.H.2    Lee, S.W.3    Choi, K.Y.4    Sung, Y.C.5
  • 17
    • 0030448650 scopus 로고    scopus 로고
    • Identification of a novel p53 functional domain that is necessary for efficient growth suppression
    • Walker KK, Levine AJ. Identification of a novel p53 functional domain that is necessary for efficient growth suppression. Proc. Natl Acad. Sci. USA 93, 15335-15340 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 15335-15340
    • Walker, K.K.1    Levine, A.J.2
  • 19
  • 23
    • 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 267, 1498-1502 (1995).
    • (1995) Science , vol.267 , pp. 1498-1502
    • Jeffrey, P.D.1    Gorina, S.2    Pavletich, N.P.3
  • 25
    • 0029013273 scopus 로고
    • P53 and its 14 kDa C-terminal domain recognize primary DNA damage in the form of insertion/ deletion mismatches
    • Lee S, Elenbaas B, Levine A, Griffith J. p53 and its 14 kDa C-terminal domain recognize primary DNA damage in the form of insertion/ deletion mismatches. Cell 81, 1013-1020 (1995).
    • (1995) Cell , vol.81 , pp. 1013-1020
    • Lee, S.1    Elenbaas, B.2    Levine, A.3    Griffith, J.4
  • 26
    • 34547634446 scopus 로고    scopus 로고
    • Quaternary structures of tumor suppressor p53 and a specific p53 DNA complex
    • Tidow H, Melero R, Mylonas E et al. Quaternary structures of tumor suppressor p53 and a specific p53 DNA complex. Proc. Natl Acad. Sci. USA 104, 12324-12329 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 12324-12329
    • Tidow, H.1    Melero, R.2    Mylonas, E.3
  • 27
    • 47649096991 scopus 로고    scopus 로고
    • Structural biology of the tumor suppressor p53
    • Joerger AC, Fersht AR. Structural biology of the tumor suppressor p53. Annu. Rev. Biochem. 77, 557-582 (2008).
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 557-582
    • Joerger, A.C.1    Fersht, A.R.2
  • 29
    • 33646757232 scopus 로고    scopus 로고
    • The complexity of p53 stabilization and activation
    • Lavin MF, Gueven N. The complexity of p53 stabilization and activation. Cell Death Differ. 13, 941-950 (2006).
    • (2006) Cell Death Differ , vol.13 , pp. 941-950
    • Lavin, M.F.1    Gueven, N.2
  • 30
    • 33846148980 scopus 로고    scopus 로고
    • Outcomes of p53 activation-spoilt for choice
    • Vousden KH. Outcomes of p53 activation-spoilt for choice. J. Cell Sci. 119, 5015-5020 (2006).
    • (2006) J. Cell Sci. , vol.119 , pp. 5015-5020
    • Vousden, K.H.1
  • 31
    • 3242890575 scopus 로고    scopus 로고
    • Mammalian cell cycle checkpoints: Signalling pathways and their organization in space and time
    • Lukas J, Lukas C, Bartek J. Mammalian cell cycle checkpoints: signalling pathways and their organization in space and time. DNA Repair (Amst.) 3, 997-1007 (2004).
    • (2004) DNA Repair (Amst.) , vol.3 , pp. 997-1007
    • Lukas, J.1    Lukas, C.2    Bartek, J.3
  • 32
    • 0036169417 scopus 로고    scopus 로고
    • Disruption of oncogene/tumor suppressor networks during human carcinogenesis
    • Munger K. Disruption of oncogene/tumor suppressor networks during human carcinogenesis. Cancer Invest. 20, 71-81 (2002).
    • (2002) Cancer Invest , vol.20 , pp. 71-81
    • Munger, K.1
  • 33
    • 24644438102 scopus 로고    scopus 로고
    • Apoptosis. p53 and PUMA: A deadly duo
    • Vousden KH. Apoptosis. p53 and PUMA: a deadly duo. Science 309, 1685-1686 (2005).
    • (2005) Science , vol.309 , pp. 1685-1686
    • Vousden, K.H.1
  • 34
    • 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. 13, 235-244 (1987).
    • (1987) Somat. Cell Mol. Genet. , vol.13 , pp. 235-244
    • Cahilly-Snyder, L.1    Yang-Feng, T.2    Francke, U.3    George, D.L.4
  • 35
    • 0025853776 scopus 로고
    • Tumorigenic portential associated with enhanced expression of a gene that is amplified in a mouse tumor cell line
    • Fakharzadeh SS, Trusko SP, George DL. Tumorigenic portential associated with enhanced expression of a gene that is amplified in a mouse tumor cell line. EMBO J. 10, 1565-1569 (1991).
    • (1991) EMBO J , vol.10 , pp. 1565-1569
    • Fakharzadeh, S.S.1    Trusko, S.P.2    George, D.L.3
  • 36
    • 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 358, 80-83 (1992).
    • (1992) Nature , vol.358 , pp. 80-83
    • Oliner, J.D.1    Kinzler, K.W.2    Meltzer, P.S.3    George, D.L.4    Vogelstein, B.5
  • 37
    • 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 69, 1237-1245 (1992).
    • (1992) Cell , vol.69 , pp. 1237-1245
    • Momand, J.1    Zambetti, G.P.2    Olson, D.C.3    George, D.4    Levine, A.J.5
  • 38
    • 0027508092 scopus 로고
    • The tumor suppressor p53 and the oncoprotein simian virus 40 T antigen bind to overlapping domains on the MDM2 protein
    • Brown DR, Deb S, Munoz RM, Subler MA, Deb SP. The tumor suppressor p53 and the oncoprotein simian virus 40 T antigen bind to overlapping domains on the MDM2 protein. Mol. Cell Biol. 13, 6849-6857 (1993).
    • (1993) Mol. Cell Biol. , vol.13 , pp. 6849-6857
    • Brown, D.R.1    Deb, S.2    Munoz, R.M.3    Subler, M.A.4    Deb, S.P.5
  • 39
    • 0032518917 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein
    • Roth J, Dobbelstein M, Freedman DA, Shenk T, Levine AJ. Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein. EMBO J. 17, 554-564 (1998).
    • (1998) EMBO J , vol.17 , pp. 554-564
    • Roth, J.1    Dobbelstein, M.2    Freedman, D.A.3    Shenk, T.4    Levine, A.J.5
  • 40
    • 0035868386 scopus 로고    scopus 로고
    • The contribution of the acidic domain of MDM2 to p53 and MDM2 stability
    • Argentini M, Barboule N, Wasylyk B. The contribution of the acidic domain of MDM2 to p53 and MDM2 stability. Oncogene 20, 1267-1275 (2001).
    • (2001) Oncogene , vol.20 , pp. 1267-1275
    • Argentini, M.1    Barboule, N.2    Wasylyk, B.3
  • 41
    • 48849114168 scopus 로고    scopus 로고
    • Acidic domain is indispensable for MDM2 to negatively regulate the acetylation of p53
    • Wang Q, Yang Y, Wang L, Zhang PZ, Yu L. Acidic domain is indispensable for MDM2 to negatively regulate the acetylation of p53. Biochem. Biophys. Res. Commun. 374, 437-441 (2008).
    • (2008) Biochem. Biophys. Res. Commun. , vol.374 , pp. 437-441
    • Wang, Q.1    Yang, Y.2    Wang, L.3    Zhang, P.Z.4    Yu, L.5
  • 42
    • 66449094959 scopus 로고    scopus 로고
    • A function for the RING finger domain in the allosteric control of MDM2 conformation and activity
    • Wawrzynow B, Pettersson S, Zylicz A et al. A function for the RING finger domain in the allosteric control of MDM2 conformation and activity. J. Biol. Chem. 284, 11517-11530 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 11517-11530
    • Wawrzynow, B.1    Pettersson, S.2    Zylicz, A.3
  • 43
    • 0032080297 scopus 로고    scopus 로고
    • The human oncoprotein MDM2 arrests the cell cycle: Elimination of its cell-cycleinhibitory function induces tumorigenesis
    • Brown DR, Thomas CA, Deb SP. The human oncoprotein MDM2 arrests the cell cycle: elimination of its cell-cycleinhibitory function induces tumorigenesis. Embo. J. 17, 2513-2525 (1998).
    • (1998) Embo. J. , vol.17 , pp. 2513-2525
    • Brown, D.R.1    Thomas, C.A.2    Deb, S.P.3
  • 45
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • Honda R, Tanaka H, Yasuda H. Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett. 420, 25-27 (1997).
    • (1997) FEBS Lett , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 46
    • 0034282102 scopus 로고    scopus 로고
    • An intact HDM2 RING-finger domain is required for nuclear exclusion of p53
    • Boyd SD, Tsai KY, Jacks T. An intact HDM2 RING-finger domain is required for nuclear exclusion of p53. Nat. Cell Biol. 2, 563-568 (2000).
    • (2000) Nat. Cell Biol. , vol.2 , pp. 563-568
    • Boyd, S.D.1    Tsai, K.Y.2    Jacks, T.3
  • 47
    • 33748920505 scopus 로고    scopus 로고
    • Solution structure of the Hdm2 C2H2C4 RING, a domain critical for ubiquitination of p53
    • Kostic M, Matt T, Martinez-Yamout MA, Dyson HJ, Wright PE. Solution structure of the Hdm2 C2H2C4 RING, a domain critical for ubiquitination of p53. J. Mol. Biol. 363, 433-450 (2006).
    • (2006) J. Mol. Biol. , vol.363 , pp. 433-450
    • Kostic, M.1    Matt, T.2    Martinez-Yamout, M.A.3    Dyson, H.J.4    Wright, P.E.5
  • 48
    • 0028834902 scopus 로고
    • Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
    • Jones SN, Roe AE, Donehower LA, Bradley A. Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53. Nature 378, 206-208 (1995).
    • (1995) Nature , vol.378 , pp. 206-208
    • Jones, S.N.1    Roe, A.E.2    Donehower, L.A.3    Bradley, A.4
  • 49
    • 0028823020 scopus 로고
    • Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
    • Montes de Oca Luna R, Wagner DS, Lozano G. Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53. Nature 378, 203-206 (1995).
    • (1995) Nature , vol.378 , pp. 203-206
    • Montes De Oca Luna, R.1    Wagner, D.S.2    Lozano, G.3
  • 50
    • 0026561121 scopus 로고
    • Mice deficient for p53 are developmentally normal but susceptible to spontaneous tumours
    • Donehower LA, Harvey M, Slagle BL et al. Mice deficient for p53 are developmentally normal but susceptible to spontaneous tumours. Nature 356, 215-221 (1992).
    • (1992) Nature , vol.356 , pp. 215-221
    • Donehower, L.A.1    Harvey, M.2    Slagle, B.L.3
  • 51
    • 10344243572 scopus 로고    scopus 로고
    • Mdm2 deletion does not alter growth characteristics of p53-deficient embryo fibroblasts
    • McMasters KM, Montes de Oca Luna R, Pena JR, Lozano G. mdm2 deletion does not alter growth characteristics of p53-deficient embryo fibroblasts. Oncogene 13, 1731-1736 (1996).
    • (1996) Oncogene , vol.13 , pp. 1731-1736
    • McMasters, K.M.1    Montes De Oca Luna, R.2    Pena, J.R.3    Lozano, G.4
  • 52
    • 0037372014 scopus 로고    scopus 로고
    • Concomitant expression of p16INK4a and p14ARF in primary breast cancer and analysis of inactivation mechanisms
    • Silva J, Silva JM, Dominguez G et al. Concomitant expression of p16INK4a and p14ARF in primary breast cancer and analysis of inactivation mechanisms. J. Pathol. 199, 289-297 (2003).
    • (2003) J. Pathol. , vol.199 , pp. 289-297
    • Silva, J.1    Silva, J.M.2    Dominguez, G.3
  • 53
    • 0032549711 scopus 로고    scopus 로고
    • ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways
    • Zhang Y, Xiong Y, Yarbrough WG. ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways. Cell 92, 725-734 (1998).
    • (1998) Cell , vol.92 , pp. 725-734
    • Zhang, Y.1    Xiong, Y.2    Yarbrough, W.G.3
  • 54
    • 0029587551 scopus 로고
    • Alternative reading frames of the INK4a tumor suppressor gene encode two unrelated proteins capable of inducing cell cycle arrest
    • Quelle DE, Zindy F, Ashmun RA, Sherr CJ. Alternative reading frames of the INK4a tumor suppressor gene encode two unrelated proteins capable of inducing cell cycle arrest. Cell 83, 993-1000 (1995).
    • (1995) Cell , vol.83 , pp. 993-1000
    • Quelle, D.E.1    Zindy, F.2    Ashmun, R.A.3    Sherr, C.J.4
  • 56
    • 0027673764 scopus 로고
    • The p53-mdm2 autoregulatory feedback loop: A paradigm for the regulation of growth control by p53?
    • Picksley SM, Lane DP. The p53-mdm2 autoregulatory feedback loop: a paradigm for the regulation of growth control by p53? Bioessays 15, 689-690 (1993).
    • (1993) Bioessays , vol.15 , pp. 689-690
    • Picksley, S.M.1    Lane, D.P.2
  • 57
    • 0027244853 scopus 로고
    • The p53-mdm-2 autoregulatory feedback loop
    • Wu X, Bayle JH, Olson D, Levine AJ. The p53-mdm-2 autoregulatory feedback loop. Genes Dev. 7, 1126-1132 (1993).
    • (1993) Genes Dev , vol.7 , pp. 1126-1132
    • Wu, X.1    Bayle, J.H.2    Olson, D.3    Levine, A.J.4
  • 58
    • 0027459198 scopus 로고
    • Mdm2 expression is induced by wild type p53 activity
    • Barak Y, Juven T, Haffner R, Oren M. mdm2 expression is induced by wild type p53 activity. Embo. J. 12, 461-468 (1993).
    • (1993) Embo. J. , vol.12 , pp. 461-468
    • Barak, Y.1    Juven, T.2    Haffner, R.3    Oren, M.4
  • 59
    • 0027222956 scopus 로고
    • Mapping of the p53 and mdm-2 interaction domains
    • Chen J, Marechal V, Levine AJ. Mapping of the p53 and mdm-2 interaction domains. Mol. Cell Biol. 13, 4107-4114 (1993).
    • (1993) Mol. Cell Biol. , vol.13 , pp. 4107-4114
    • Chen, J.1    Marechal, V.2    Levine, A.J.3
  • 61
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y, Maya R, Kazaz A, Oren M. Mdm2 promotes the rapid degradation of p53. Nature 387, 296-299 (1997).
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 63
    • 58749094954 scopus 로고    scopus 로고
    • Targeting Mdm2 and Mdmx in cancer therapy: Better living through medicinal chemistry?
    • Wade M, Wahl GM. Targeting Mdm2 and Mdmx in cancer therapy: better living through medicinal chemistry? Mol. Cancer Res. 7, 1-11 (2009).
    • (2009) Mol. Cancer Res. , vol.7 , pp. 1-11
    • Wade, M.1    Wahl, G.M.2
  • 64
    • 0031194666 scopus 로고    scopus 로고
    • Isolation and identification of the human homolog of a new p53-binding protein, Mdmx
    • Shvarts A, Bazuine M, Dekker P et al. Isolation and identification of the human homolog of a new p53-binding protein, Mdmx. Genomics 43, 34-42 (1997).
    • (1997) Genomics , vol.43 , pp. 34-42
    • Shvarts, A.1    Bazuine, M.2    Dekker, P.3
  • 65
    • 0033531252 scopus 로고    scopus 로고
    • Comparative study of the p53-mdm2 and p53-MDMX interfaces
    • Bottger V, Bottger A, Garcia-Echeverria C et al. Comparative study of the p53-mdm2 and p53-MDMX interfaces. Oncogene 18, 189-199 (1999).
    • (1999) Oncogene , vol.18 , pp. 189-199
    • Bottger, V.1    Bottger, A.2    Garcia-Echeverria, C.3
  • 67
    • 0034623074 scopus 로고    scopus 로고
    • Hdmx stabilizes mdm2 and p53
    • Stad R, Ramos YF, Little N et al. Hdmx stabilizes mdm2 and p53. J. Biol. Chem. 275, 28039-28044 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 28039-28044
    • Stad, R.1    Ramos, Y.F.2    Little, N.3
  • 68
    • 0036510399 scopus 로고    scopus 로고
    • Hdmx recruitment into the nucleus by Hdm2 is essential for its ability to regulate p53 stability and transactivation
    • Migliorini D, Danovi D, Colombo E, Carbone R, Pelicci PG, Marine JC. Hdmx recruitment into the nucleus by Hdm2 is essential for its ability to regulate p53 stability and transactivation. J. Biol. Chem. 277, 7318-7323 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 7318-7323
    • Migliorini, D.1    Danovi, D.2    Colombo, E.3    Carbone, R.4    Pelicci, P.G.5    Marine, J.C.6
  • 69
    • 0033621415 scopus 로고    scopus 로고
    • Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein
    • Sharp DA, Kratowicz SA, Sank MJ, George DL. Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein. J. Biol. Chem. 274, 38189-38196 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 38189-38196
    • Sharp, D.A.1    Kratowicz, S.A.2    Sank, M.J.3    George, D.L.4
  • 72
    • 0035884407 scopus 로고    scopus 로고
    • Subcellular distribution of p53 and p73 are differentially regulated by MDM2
    • Gu J, Nie L, Kawai H, Yuan ZM. Subcellular distribution of p53 and p73 are differentially regulated by MDM2. Cancer Res. 61, 6703-6707 (2001).
    • (2001) Cancer Res , vol.61 , pp. 6703-6707
    • Gu, J.1    Nie, L.2    Kawai, H.3    Yuan, Z.M.4
  • 73
    • 0033963335 scopus 로고    scopus 로고
    • MdmX protects p53 from Mdm2-mediated degradation
    • Jackson MW, Berberich SJ. MdmX protects p53 from Mdm2-mediated degradation. Mol. Cell Biol. 20, 1001-1007 (2000).
    • (2000) Mol. Cell Biol. , vol.20 , pp. 1001-1007
    • Jackson, M.W.1    Berberich, S.J.2
  • 74
    • 0030665146 scopus 로고    scopus 로고
    • Mdm-2 phosphorylation by DNA-dependent protein kinase prevents interaction with p53
    • Mayo LD, Turchi JJ, Berberich SJ. Mdm-2 phosphorylation by DNA-dependent protein kinase prevents interaction with p53. Cancer Res. 57, 5013-5016 (1997).
    • (1997) Cancer Res , vol.57 , pp. 5013-5016
    • Mayo, L.D.1    Turchi, J.J.2    Berberich, S.J.3
  • 75
    • 63649142709 scopus 로고    scopus 로고
    • C-Abl phosphorylates Hdmx and regulates its interaction with p53
    • Zuckerman V, Lenos K, Popowicz GM et al. c-Abl phosphorylates Hdmx and regulates its interaction with p53. J. Biol. Chem. 284, 4031-4039 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 4031-4039
    • Zuckerman, V.1    Lenos, K.2    Popowicz, G.M.3
  • 78
    • 0037047345 scopus 로고    scopus 로고
    • The conformationally flexible S9-S10 linker region in the core domain of p53 contains a novel MDM2 binding site whose mutation increases ubiquitination of p53 in vivo
    • Shimizu H, Burch LR, Smith AJ et al. The conformationally flexible S9-S10 linker region in the core domain of p53 contains a novel MDM2 binding site whose mutation increases ubiquitination of p53 in vivo. J. Biol. Chem. 277, 28446-28458 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 28446-28458
    • Shimizu, H.1    Burch, L.R.2    Smith, A.J.3
  • 80
    • 20444463203 scopus 로고    scopus 로고
    • Structure of free MDM2 N-terminal domain reveals conformational adjustments that accompany p53-binding
    • Uhrinova S, Uhrin D, Powers H et al. Structure of free MDM2 N-terminal domain reveals conformational adjustments that accompany p53-binding. J. Mol. Biol. 350, 587-598 (2005).
    • (2005) J. Mol. Biol. , vol.350 , pp. 587-598
    • Uhrinova, S.1    Uhrin, D.2    Powers, H.3
  • 81
    • 0037452725 scopus 로고    scopus 로고
    • Flexible lid to the p53-binding domain of human Mdm2: Implications for p53 regulation
    • McCoy MA, Gesell JJ, Senior MM, Wyss DF. Flexible lid to the p53-binding domain of human Mdm2: implications for p53 regulation. Proc. Natl Acad. Sci. USA 100, 1645-1648 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 1645-1648
    • McCoy, M.A.1    Gesell, J.J.2    Senior, M.M.3    Wyss, D.F.4
  • 82
    • 11444264322 scopus 로고    scopus 로고
    • Use of a retroinverso p53 peptide as an inhibitor of MDM2
    • Sakurai K, Chung HS, Kahne D. Use of a retroinverso p53 peptide as an inhibitor of MDM2. J. Am. Chem. Soc. 126, 16288-16289 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 16288-16289
    • Sakurai, K.1    Chung, H.S.2    Kahne, D.3
  • 83
    • 48849117864 scopus 로고    scopus 로고
    • Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain
    • Popowicz GM, Czarna A, Holak TA. Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain. Cell Cycle 7, 2441-2443 (2008).
    • (2008) Cell Cycle , vol.7 , pp. 2441-2443
    • Popowicz, G.M.1    Czarna, A.2    Holak, T.A.3
  • 84
    • 0034710708 scopus 로고    scopus 로고
    • Discovery of potent antagonists of the interaction between human double minute 2 and tumor suppressor p53
    • Garcia-Echeverria C, Chene P, Blommers MJ, Furet P. Discovery of potent antagonists of the interaction between human double minute 2 and tumor suppressor p53. J. Med. Chem. 43, 3205-3208 (2000).
    • (2000) J. Med. Chem. , vol.43 , pp. 3205-3208
    • Garcia-Echeverria, C.1    Chene, P.2    Blommers, M.J.3    Furet, P.4
  • 85
    • 66149092109 scopus 로고    scopus 로고
    • Crystal structures of human MdmX (HdmX) in complex with p53 Peptide analogues reveal surprising conformational changes
    • Kallen J, Goepfert A, Blechschmidt A et al. Crystal structures of human MdmX (HdmX) in complex with p53 Peptide analogues reveal surprising conformational changes. J. Biol. Chem. 284, 8812-8821 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 8812-8821
    • Kallen, J.1    Goepfert, A.2    Blechschmidt, A.3
  • 86
    • 0035630691 scopus 로고    scopus 로고
    • Protein-protein interfaces: Mimics and inhibitors
    • Cochran AG. Protein-protein interfaces: mimics and inhibitors. Curr. Opin. Chem. Biol. 5, 654-659 (2001).
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 654-659
    • Cochran, A.G.1
  • 87
    • 0000372879 scopus 로고    scopus 로고
    • Protein-protein interactions: Interface structure, binding thermodynamics, and mutational analysis
    • Stites WE. Protein-protein interactions: interface structure, binding thermodynamics, and mutational analysis. Chem. Rev. 97, 1233-1250 (1997).
    • (1997) Chem. Rev. , vol.97 , pp. 1233-1250
    • Stites, W.E.1
  • 88
    • 27744586067 scopus 로고    scopus 로고
    • Small-molecule inhibition of TNF-α
    • He MM, Smith AS, Oslob JD et al. Small-molecule inhibition of TNF-α. Science 310, 1022-1025 (2005).
    • (2005) Science , vol.310 , pp. 1022-1025
    • He, M.M.1    Smith, A.S.2    Oslob, J.D.3
  • 89
    • 0037452709 scopus 로고    scopus 로고
    • Binding of small molecules to an adaptive protein-protein interface
    • Arkin MR, Randal M, DeLano WL et al. Binding of small molecules to an adaptive protein-protein interface. Proc. Natl Acad. Sci. USA 100, 1603-1608 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 1603-1608
    • Arkin, M.R.1    Randal, M.2    Delano, W.L.3
  • 90
    • 0037414274 scopus 로고    scopus 로고
    • Discovery of a potent small molecule IL-2 inhibitor through fragment assembly
    • Braisted AC, Oslob JD, Delano WL et al. Discovery of a potent small molecule IL-2 inhibitor through fragment assembly. J. Am. Chem. Soc. 125, 3714-3715 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 3714-3715
    • Braisted, A.C.1    Oslob, J.D.2    Delano, W.L.3
  • 91
    • 0032504007 scopus 로고    scopus 로고
    • A small nonpeptidyl mimic of granulocyte-colonystimulating factor
    • Tian SS, Lamb P, King AG et al. A small nonpeptidyl mimic of granulocyte-colonystimulating factor. Science 281, 257-259 (1998).
    • (1998) Science , vol.281 , pp. 257-259
    • Tian, S.S.1    Lamb, P.2    King, A.G.3
  • 92
    • 31544467109 scopus 로고    scopus 로고
    • Discovery of a potent inhibitor of the antiapoptotic protein Bcl-xL from NMR and parallel synthesis
    • Petros AM, Dinges J, Augeri DJ et al. Discovery of a potent inhibitor of the antiapoptotic protein Bcl-xL from NMR and parallel synthesis. J. Med. Chem. 49, 656-663 (2006).
    • (2006) J. Med. Chem. , vol.49 , pp. 656-663
    • Petros, A.M.1    Dinges, J.2    Augeri, D.J.3
  • 93
    • 20444486559 scopus 로고    scopus 로고
    • An inhibitor of Bcl-2 family proteins induces regression of solid tumours
    • Oltersdorf T, Elmore SW, Shoemaker AR et al. An inhibitor of Bcl-2 family proteins induces regression of solid tumours. Nature 435, 677-681 (2005).
    • (2005) Nature , vol.435 , pp. 677-681
    • Oltersdorf, T.1    Elmore, S.W.2    Shoemaker, A.R.3
  • 94
    • 0038648223 scopus 로고    scopus 로고
    • Discovery of the first series of inhibitors of human papillomavirus type 11: Inhibition of the assembly of the E1-E2-Origin DNA complex
    • Yoakim C, Ogilvie WW, Goudreau N et al. Discovery of the first series of inhibitors of human papillomavirus type 11: inhibition of the assembly of the E1-E2-Origin DNA complex. Bioorg. Med. Chem. Lett. 13, 2539-2541 (2003).
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 2539-2541
    • Yoakim, C.1    Ogilvie, W.W.2    Goudreau, N.3
  • 95
    • 33847619355 scopus 로고    scopus 로고
    • Optimization and determination of the absolute configuration of a series of potent inhibitors of human papillomavirus type-11 E1-E2 protein-protein interaction: A combined medicinal chemistry, NMR and computational chemistry approach
    • Goudreau N, Cameron DR, Deziel R et al. Optimization and determination of the absolute configuration of a series of potent inhibitors of human papillomavirus type-11 E1-E2 protein-protein interaction: a combined medicinal chemistry, NMR and computational chemistry approach. Bioorg. Med. Chem. 15, 2690-2700 (2007).
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 2690-2700
    • Goudreau, N.1    Cameron, D.R.2    Deziel, R.3
  • 96
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • Wells JA, McClendon CL. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 450, 1001-1009 (2007).
    • (2007) Nature , vol.450 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 97
    • 33748076161 scopus 로고    scopus 로고
    • Crystallographic analysis of an 8-mer p53 peptide analogue complexed with MDM2
    • Sakurai K, Schubert C, Kahne D. Crystallographic analysis of an 8-mer p53 peptide analogue complexed with MDM2. J. Am. Chem. Soc. 128, 11000-11001 (2006).
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 11000-11001
    • Sakurai, K.1    Schubert, C.2    Kahne, D.3
  • 98
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • DeLano WL, Ultsch MH, de Vos AM, Wells JA. Convergent solutions to binding at a protein-protein interface. Science 287, 1279-1283 (2000).
    • (2000) Science , vol.287 , pp. 1279-1283
    • Delano, W.L.1    Ultsch, M.H.2    De Vos, A.M.3    Wells, J.A.4
  • 99
    • 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 91, 1415-1419 (2004).
    • (2004) Br. J. Cancer , vol.91 , pp. 1415-1419
    • Klein, C.1    Vassilev, L.T.2
  • 100
    • 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 13, 2141-2147 (1996).
    • (1996) Oncogene , vol.13 , pp. 2141-2147
    • Bottger, V.1    Bottger, A.2    Howard, S.F.3
  • 101
    • 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 9, 2523-2529 (1994).
    • (1994) Oncogene , vol.9 , pp. 2523-2529
    • Picksley, S.M.1    Vojtesek, B.2    Sparks, A.3    Lane, D.P.4
  • 102
    • 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. 269, 744-756 (1997).
    • (1997) J. Mol. Biol. , vol.269 , pp. 744-756
    • Bottger, A.1    Bottger, V.2    Garcia-Echeverria, C.3
  • 103
    • 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 40, 336-344 (2001).
    • (2001) Biochemistry , vol.40 , pp. 336-344
    • Stoll, R.1    Renner, C.2    Hansen, S.3
  • 104
    • 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. 183, 69-77 (2002).
    • (2002) Cancer Lett , vol.183 , pp. 69-77
    • Zhao, J.1    Wang, M.2    Chen, J.3
  • 105
    • 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. 123, 554-560 (2001).
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 554-560
    • Duncan, S.J.1    Gruschow, S.2    Williams, D.H.3
  • 106
    • 0016260143 scopus 로고
    • Antitumor chemotherapy. IX. Cytotoxic activity in cultured tumor cells of chalcone substituants and related compounds
    • Dore JC, Viel C. Antitumor chemotherapy. IX. Cytotoxic activity in cultured tumor cells of chalcone substituants and related compounds. J. Pharm. Belg. 29, 341-351 (1974).
    • (1974) J. Pharm. Belg. , vol.29 , pp. 341-351
    • Dore, J.C.1    Viel, C.2
  • 107
    • 27744466131 scopus 로고    scopus 로고
    • Hexylitaconic acid: A new inhibitor of p53-HDM2 interaction isolated from a marine-derived fungus, Arthrinium sp
    • Tsukamoto S, Yoshida T, Hosono H, Ohta T, Yokosawa H. Hexylitaconic acid: a new inhibitor of p53-HDM2 interaction isolated from a marine-derived fungus, Arthrinium sp. Bioorg. Med. Chem. Lett. 16, 69-71 (2006).
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 69-71
    • Tsukamoto, S.1    Yoshida, T.2    Hosono, H.3    Ohta, T.4    Yokosawa, H.5
  • 108
    • 3843055877 scopus 로고    scopus 로고
    • A nonpeptidic sulfonamide inhibits the p53-mdm2 interaction and activates p53-dependent transcription in mdm2-overexpressing cells
    • Galatin PS, Abraham DJ. A nonpeptidic sulfonamide inhibits the p53-mdm2 interaction and activates p53-dependent transcription in mdm2-overexpressing cells. J. Med. Chem. 47, 4163-4165 (2004).
    • (2004) J. Med. Chem. , vol.47 , pp. 4163-4165
    • Galatin, P.S.1    Abraham, D.J.2
  • 109
    • 13944282529 scopus 로고    scopus 로고
    • Isoindolinone-based inhibitors of the MDM2-p53 protein-protein interaction
    • Hardcastle IR, Ahmed SU, Atkins H et al. Isoindolinone-based inhibitors of the MDM2-p53 protein-protein interaction. Bioorg. Med. Chem. Lett. 15, 1515-1520 (2005).
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 1515-1520
    • Hardcastle, I.R.1    Ahmed, S.U.2    Atkins, H.3
  • 110
    • 33750133440 scopus 로고    scopus 로고
    • Small-molecule inhibitors of the MDM2-p53 protein-protein interaction based on an isoindolinone scaffold
    • Hardcastle IR, Ahmed SU, Atkins H et al. Small-molecule inhibitors of the MDM2-p53 protein-protein interaction based on an isoindolinone scaffold. J. Med. Chem. 49, 6209-6221 (2006).
    • (2006) J. Med. Chem. , vol.49 , pp. 6209-6221
    • Hardcastle, I.R.1    Ahmed, S.U.2    Atkins, H.3
  • 111
    • 56749152399 scopus 로고    scopus 로고
    • Analysis of chemical shift changes reveals the binding modes of isoindolinone inhibitors of the MDM2-p53 interaction
    • Riedinger C, Endicott JA, Kemp SJ et al. Analysis of chemical shift changes reveals the binding modes of isoindolinone inhibitors of the MDM2-p53 interaction. J. Am. Chem. Soc. 130, 16038-16044 (2008).
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 16038-16044
    • Riedinger, C.1    Endicott, J.A.2    Kemp, S.J.3
  • 112
    • 50249108644 scopus 로고    scopus 로고
    • Isoquinolin-1-one inhibitors of the MDM2-p53 interaction
    • Rothweiler U, Czarna A, Krajewski M et al. Isoquinolin-1-one inhibitors of the MDM2-p53 interaction. ChemMedChem 3, 1118-1128 (2008).
    • (2008) ChemMedChem , vol.3 , pp. 1118-1128
    • Rothweiler, U.1    Czarna, A.2    Krajewski, M.3
  • 113
    • 44949154279 scopus 로고    scopus 로고
    • Small molecular weight protein-protein interaction antagonists: An insurmountable challenge?
    • Domling A. Small molecular weight protein-protein interaction antagonists: an insurmountable challenge? Curr. Opin. Chem. Biol. 12, 281-291 (2008).
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 281-291
    • Domling, A.1
  • 114
    • 10744221485 scopus 로고    scopus 로고
    • In vivo activation of the p53 pathway by smallmolecule antagonists of MDM2
    • Vassilev LT, Vu BT, Graves B et al. In vivo activation of the p53 pathway by smallmolecule antagonists of MDM2. Science 303, 844-848 (2004).
    • (2004) Science , vol.303 , pp. 844-848
    • Vassilev, L.T.1    Vu, B.T.2    Graves, B.3
  • 116
    • 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 103, 1888-1893 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 1888-1893
    • Tovar, C.1    Rosinski, J.2    Filipovic, Z.3
  • 117
    • 18244380348 scopus 로고    scopus 로고
    • High-density miniaturized thermal shift assays as a general strategy for drug discovery
    • Pantoliano MW, Petrella EC, Kwasnoski JD et al. High-density miniaturized thermal shift assays as a general strategy for drug discovery. J. Biomol. Screen 6, 429-440 (2001).
    • (2001) J. Biomol. Screen , vol.6 , pp. 429-440
    • Pantoliano, M.W.1    Petrella, E.C.2    Kwasnoski, J.D.3
  • 118
    • 19944431512 scopus 로고    scopus 로고
    • 1,4-benzodiazepine-2,5-diones as small molecule antagonists of the HDM2-p53 interaction: Discovery and SAR
    • Parks DJ, Lafrance LV, Calvo RR et al. 1,4-benzodiazepine-2,5-diones as small molecule antagonists of the HDM2-p53 interaction: discovery and SAR. Bioorg. Med. Chem. Lett. 15, 765-770 (2005).
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 765-770
    • Parks, D.J.1    Lafrance, L.V.2    Calvo, R.R.3
  • 119
    • 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. 48, 909-912 (2005).
    • (2005) J. Med. Chem. , vol.48 , pp. 909-912
    • Grasberger, B.L.1    Lu, T.2    Schubert, C.3
  • 120
    • 0035254951 scopus 로고    scopus 로고
    • Efficient electrostatic solvation model for proteinfragment docking
    • Majeux N, Scarsi M, Caflisch A. Efficient electrostatic solvation model for proteinfragment docking. Proteins 42, 256-268 (2001).
    • (2001) Proteins , vol.42 , pp. 256-268
    • Majeux, N.1    Scarsi, M.2    Caflisch, A.3
  • 121
    • 33645357208 scopus 로고    scopus 로고
    • Substituted 1,4-benzodiazepine-2,5-diones as α-helix mimetic antagonists of the HDM2-p53 protein-protein interaction
    • Cummings MD, Schubert C, Parks DJ et al. Substituted 1,4-benzodiazepine- 2,5-diones as α-helix mimetic antagonists of the HDM2-p53 protein-protein interaction. Chem. Biol. Drug Des. 67, 201-205 (2006).
    • (2006) Chem. Biol. Drug Des. , vol.67 , pp. 201-205
    • Cummings, M.D.1    Schubert, C.2    Parks, D.J.3
  • 122
    • 33644873086 scopus 로고    scopus 로고
    • Benzodiazepinedione inhibitors of the Hdm2:p53 complex suppress human tumor cell proliferation in vitro and sensitize tumors to doxorubicin in vivo
    • Koblish HK, Zhao S, Franks CF et al. Benzodiazepinedione inhibitors of the Hdm2:p53 complex suppress human tumor cell proliferation in vitro and sensitize tumors to doxorubicin in vivo. Mol. Cancer Ther. 5, 160-169 (2006).
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 160-169
    • Koblish, H.K.1    Zhao, S.2    Franks, C.F.3
  • 123
    • 33747126523 scopus 로고    scopus 로고
    • Enhanced pharmacokinetic properties of 1,4-benzodiazepine-2,5-dione antagonists of the HDM2-p53 protein-protein interaction through structure-based drug design
    • Parks DJ, LaFrance LV, Calvo RR et al. Enhanced pharmacokinetic properties of 1,4-benzodiazepine-2,5-dione antagonists of the HDM2-p53 protein-protein interaction through structure-based drug design. Bioorg. Med. Chem. Lett. 16, 3310-3314 (2006).
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 3310-3314
    • Parks, D.J.1    Lafrance, L.V.2    Calvo, R.R.3
  • 124
    • 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. 127, 10130-10131 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 10130-10131
    • Ding, K.1    Lu, Y.2    Nikolovska-Coleska, Z.3
  • 125
    • 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. J. Med. Chem. 49, 3432-3435 (2006).
    • (2006) J. Med. Chem. , vol.49 , pp. 3432-3435
    • Ding, K.1    Lu, Y.2    Nikolovska-Coleska, Z.3
  • 126
    • 41649102468 scopus 로고    scopus 로고
    • Temporal activation of p53 by a specific MDM2 inhibitor is selectively toxic to tumors and leads to complete tumor growth inhibition
    • Shangary S, Qin D, McEachern D et al. Temporal activation of p53 by a specific MDM2 inhibitor is selectively toxic to tumors and leads to complete tumor growth inhibition. Proc. Natl Acad. Sci. USA 105, 3933-3938 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 3933-3938
    • Shangary, S.1    Qin, D.2    McEachern, D.3
  • 127
    • 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. 7, 1533-1542 (2008).
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 1533-1542
    • Shangary, S.1    Ding, K.2    Qiu, S.3
  • 128
    • 33845256980 scopus 로고    scopus 로고
    • MDMX overexpression prevents p53 activation by the MDM2 inhibitor Nutlin
    • Hu B, Gilkes DM, Farooqi B, Sebti SM, Chen J. MDMX overexpression prevents p53 activation by the MDM2 inhibitor Nutlin. J. Biol. Chem. 281, 33030-33035 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 33030-33035
    • Hu, B.1    Gilkes, D.M.2    Farooqi, B.3    Sebti, S.M.4    Chen, J.5
  • 129
    • 33845251005 scopus 로고    scopus 로고
    • Hdmx modulates the outcome of p53 activation in human tumor cells
    • Wade M, Wong ET, Tang M, Stommel JM, Wahl GM. Hdmx modulates the outcome of p53 activation in human tumor cells. J. Biol. Chem. 281, 33036-33044 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 33036-33044
    • Wade, M.1    Wong, E.T.2    Tang, M.3    Stommel, J.M.4    Wahl, G.M.5
  • 130
    • 33750590095 scopus 로고    scopus 로고
    • Inactivation of the p53 pathway in retinoblastoma
    • Laurie NA, Donovan SL, Shih CS et al. Inactivation of the p53 pathway in retinoblastoma. Nature 444, 61-66 (2006).
    • (2006) Nature , vol.444 , pp. 61-66
    • Laurie, N.A.1    Donovan, S.L.2    Shih, C.S.3
  • 131
    • 34548780897 scopus 로고    scopus 로고
    • Efficient p53 activation and apoptosis by simultaneous disruption of binding to MDM2 and MDMX
    • Hu B, Gilkes DM, Chen J. Efficient p53 activation and apoptosis by simultaneous disruption of binding to MDM2 and MDMX. Cancer Res. 67, 8810-8817 (2007).
    • (2007) Cancer Res , vol.67 , pp. 8810-8817
    • Hu, B.1    Gilkes, D.M.2    Chen, J.3
  • 132
    • 65949087007 scopus 로고    scopus 로고
    • High affinity interaction of the p53 peptide-analogue with human Mdm2 and Mdmx
    • Czarna A, Popowicz GM, Pecak A, Wolf S, Dubin G, Holak TA. High affinity interaction of the p53 peptide-analogue with human Mdm2 and Mdmx. Cell Cycle 8, 1176-1184 (2009).
    • (2009) Cell Cycle , vol.8 , pp. 1176-1184
    • Czarna, A.1    Popowicz, G.M.2    Pecak, A.3    Wolf, S.4    Dubin, G.5    Holak, T.A.6
  • 133
    • 63849271797 scopus 로고    scopus 로고
    • Structural basis for high-affinity peptide inhibition of p53 interactions with MDM2 and MDMX
    • DOI: 10.1073/ pnas.0900947106, Epub ahead of print
    • Pazgier M, Liu M, Zou G et al. Structural basis for high-affinity peptide inhibition of p53 interactions with MDM2 and MDMX. Proc. Natl Acad. Sci. USA DOI: 10.1073/ pnas.0900947106 (2009) (Epub ahead of print).
    • (2009) Proc. Natl Acad. Sci. USA
    • Pazgier, M.1    Liu, M.2    Zou, G.3
  • 134
    • 33244473080 scopus 로고    scopus 로고
    • Probing the structural requirements of peptoids that inhibit HDM2-p53 interactions
    • Hara T, Durell SR, Myers MC, Appella DH. Probing the structural requirements of peptoids that inhibit HDM2-p53 interactions. J. Am. Chem. Soc. 128, 1995-2004 (2006).
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 1995-2004
    • Hara, T.1    Durell, S.R.2    Myers, M.C.3    Appella, D.H.4
  • 136
    • 66149113939 scopus 로고    scopus 로고
    • Study of MDM2 binding to p53-analogues: Affinity, helicity, and applicability to drug design
    • Kalid O, Ben-Tal N. Study of MDM2 binding to p53-analogues: affinity, helicity, and applicability to drug design. J. Chem. Inf. Model 49, 865-876 (2009).
    • (2009) J. Chem. Inf. Model , vol.49 , pp. 865-876
    • Kalid, O.1    Ben-Tal, N.2
  • 139
    • 16244416846 scopus 로고    scopus 로고
    • Solution structure of a β-peptide ligand for hDM2
    • Kritzer JA, Hodsdon ME, Schepartz A. Solution structure of a β-peptide ligand for hDM2. J. Am. Chem. Soc. 127, 4118-4119 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 4118-4119
    • Kritzer, J.A.1    Hodsdon, M.E.2    Schepartz, A.3
  • 140
    • 0018348655 scopus 로고
    • T antigen is bound to a host protein in SV40-transformed cells
    • Lane DP, Crawford LV. T antigen is bound to a host protein in SV40-transformed cells. Nature 278, 261-263 (1979).
    • (1979) Nature , vol.278 , pp. 261-263
    • Lane, D.P.1    Crawford, L.V.2
  • 141
    • 0018760324 scopus 로고
    • Characterization of a 54 kDa cellular SV40 tumor antigen present in SV40-transformed cells and uninfected embryonal carcinoma cells
    • Linzer DI, Levine AJ. Characterization of a 54 kDa cellular SV40 tumor antigen present in SV40-transformed cells and uninfected embryonal carcinoma cells. Cell 17, 43-52 (1979).
    • (1979) Cell , vol.17 , pp. 43-52
    • Linzer, D.I.1    Levine, A.J.2
  • 142
    • 0018743916 scopus 로고
    • Detection of a transformation-related antigen in chemically induced sarcomas and other transformed cells of the mouse
    • DeLeo AB, Jay G, Appella E, Dubois GC, Law LW, Old LJ. Detection of a transformation-related antigen in chemically induced sarcomas and other transformed cells of the mouse. Proc. Natl Acad. Sci. USA 76, 2420-2424 (1979).
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 2420-2424
    • Deleo, A.B.1    Jay, G.2    Appella, E.3    Dubois, G.C.4    Law, L.W.5    Old, L.J.6
  • 143
    • 0021675797 scopus 로고
    • Participation of p53 cellular tumour antigen in transformation of normal embryonic cells
    • Eliyahu D, Raz A, Gruss P, Givol D, Oren M. Participation of p53 cellular tumour antigen in transformation of normal embryonic cells. Nature 312, 646-649 (1984).
    • (1984) Nature , vol.312 , pp. 646-649
    • Eliyahu, D.1    Raz, A.2    Gruss, P.3    Givol, D.4    Oren, M.5
  • 144
    • 0021673319 scopus 로고
    • Cooperation between gene encoding p53 tumour antigen and Ras in cellular transformation
    • Parada LF, Land H, Weinberg RA, Wolf D, Rotter V. Cooperation between gene encoding p53 tumour antigen and Ras in cellular transformation. Nature 312, 649-651 (1984).
    • (1984) Nature , vol.312 , pp. 649-651
    • Parada, L.F.1    Land, H.2    Weinberg, R.A.3    Wolf, D.4    Rotter, V.5
  • 145
    • 0021676404 scopus 로고
    • Cellular immortalization by a cDNA clone encoding the transformation-associated phosphoprotein p53
    • Jenkins JR, Rudge K, Currie GA. Cellular immortalization by a cDNA clone encoding the transformation-associated phosphoprotein p53. Nature 312, 651-654 (1984).
    • (1984) Nature , vol.312 , pp. 651-654
    • Jenkins, J.R.1    Rudge, K.2    Currie, G.A.3
  • 146
    • 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 30, 1083-1093 (1989).
    • (1989) Cell , vol.30 , pp. 1083-1093
    • Finlay, C.A.1    Hinds, P.W.2    Levine, A.J.3
  • 147
    • 0025815451 scopus 로고
    • Identification of p53 as a sequence-specific DNA-binding protein
    • Kern SE, Kinzler KW, Bruskin A et al. Identification of p53 as a sequence-specific DNA-binding protein. Science 252, 1708-1711 (1991).
    • (1991) Science , vol.252 , pp. 1708-1711
    • Kern, S.E.1    Kinzler, K.W.2    Bruskin, A.3
  • 149
    • 0036674617 scopus 로고    scopus 로고
    • Live or let die: The cell's response to p53
    • Vousden KH, Lu X. Live or let die: the cell's response to p53. Nat. Rev. Cancer 2, 594-604 (2002).
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 594-604
    • Vousden, K.H.1    Lu, X.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.