메뉴 건너뛰기




Volumn 1278, Issue , 2015, Pages 567-585

Case study: Discovery of inhibitors of the MDM2–p53 protein-protein interaction

Author keywords

Cancer therapy; High throughput screening; MDM2; p53; Protein protein interaction; Virtual screening

Indexed keywords

PROTEIN INHIBITOR; PROTEIN MDM2; PROTEIN P53;

EID: 84927926193     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4939-2425-7_38     Document Type: Article
Times cited : (2)

References (73)
  • 1
    • 28544446811 scopus 로고    scopus 로고
    • Targeting proteinprotein interactions for cancer therapy
    • Fry DC, Vassilev LT (2005) Targeting proteinprotein interactions for cancer therapy. J Mol Med 83: 955-963.
    • (2005) J Mol Med , vol.83 , pp. 955-963
    • Fry, D.C.1    Vassilev, L.T.2
  • 2
    • 35048895357 scopus 로고    scopus 로고
    • Targeting protein-protein interactions: Lessons from p53/MDM2
    • Murray JK, Gellman SH (2007) Targeting protein-protein interactions: lessons from p53/MDM2. Biopolymers 88: 657-686.
    • (2007) Biopolymers , vol.88 , pp. 657-686
    • Murray, J.K.1    Gellman, S.H.2
  • 3
    • 1542353401 scopus 로고    scopus 로고
    • Control of apoptosis by p53
    • Fridman JS, Lowe SW (2003) Control of apoptosis by p53. Oncogene 22: 9030-9040.
    • (2003) Oncogene , vol.22 , pp. 9030-9040
    • Fridman, J.S.1    Lowe, S.W.2
  • 4
    • 0033992478 scopus 로고    scopus 로고
    • p53 and human cancer: The first ten thousand mutations
    • Hainaut P, HollsteinM(2000) p53 and human cancer: the first ten thousand mutations. Adv Cancer Res 77: 81-137.
    • (2000) Adv Cancer Res , vol.77 , pp. 81-137
    • Hainaut, P.1    Hollstein, M.2
  • 6
    • 0036674617 scopus 로고    scopus 로고
    • Live or let die: The cell's response to p53
    • Vousden KH, Lu X (2002) Live or let die: the cell's response to p53. Nat Rev Cancer 2: 594-604.
    • (2002) Nat Rev Cancer , vol.2 , pp. 594-604
    • Vousden, K.H.1    Lu, X.2
  • 7
    • 7044224706 scopus 로고    scopus 로고
    • Mutational spectrum of p53 mutations in primary breast and ovarian tumors
    • Feki A, Irminger-Finger I (2004) Mutational spectrum of p53 mutations in primary breast and ovarian tumors. Crit Rev Oncol Hematol 52: 103-116.
    • (2004) Crit Rev Oncol Hematol , vol.52 , pp. 103-116
    • Feki, A.1    Irminger-Finger, I.2
  • 8
    • 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 et al (1992) The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation. Cell 69: 1237-1245.
    • (1992) Cell , vol.69 , pp. 1237-1245
    • Momand, J.1    Zambetti, G.P.2    Olson, D.C.3
  • 9
    • 0025853776 scopus 로고
    • Tumorigenic potential associated with enhanced expression of a gene that is amplified in a mouse tumor cell line
    • Fakharzadeh SS, Trusko SP, George DL (1991) Tumorigenic potential associated with enhanced expression of a gene that is amplified in a mouse tumor cell line. EMBO J 10: 1565-1569.
    • (1991) EMBO J , vol.10 , pp. 1565-1569
    • Fakharzadeh, S.S.1    Trusko, S.P.2    George, D.L.3
  • 10
    • 0027415741 scopus 로고
    • Structure and organization of amplified DNA on double minutes containing the mdm2 oncogene
    • Fakharzadeh SS, Rosenblum-Vos L, MurphyM et al (1993) Structure and organization of amplified DNA on double minutes containing the mdm2 oncogene. Genomics 15: 283-290.
    • (1993) Genomics , vol.15 , pp. 283-290
    • Fakharzadeh, S.S.1    Rosenblum-Vos, L.2    Murphy, M.3
  • 11
    • 0018348655 scopus 로고
    • T antigen is bound to a host protein in SV40-transformed cells
    • Lane DP, Crawford LV (1979) T antigen is bound to a host protein in SV40-transformed cells. Nature 278: 261-263.
    • (1979) Nature , vol.278 , pp. 261-263
    • Lane, D.P.1    Crawford, L.V.2
  • 12
    • 0018760324 scopus 로고
    • Characterization of a 54 K dalton cellular SV40 tumor antigen present in SV40-transformed cells and uninfected embryonal carcinoma cells
    • Linzer DI, Levine AJ (1979)Characterization of a 54 K dalton cellular SV40 tumor antigen present in SV40-transformed cells and uninfected embryonal carcinoma cells. Cell 17: 43-52.
    • (1979) Cell , vol.17 , pp. 43-52
    • Linzer, D.I.1    Levine, A.J.2
  • 13
    • 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 et al (1979) Detection of a transformation-related antigen in chemically induced sarcomas and other transformed cells of the mouse. Proc Natl Acad Sci U S A 76: 2420-2424.
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 2420-2424
    • DeLeo, A.B.1    Jay, G.2    Appella, E.3
  • 14
    • 8844278362 scopus 로고    scopus 로고
    • A single nucleotide polymorphism in the MDM2 promoter attenuates the p53 tumor suppressor pathway and accelerates tumor formation in humans
    • Bond GL, Hu W, Bond EE et al (2004) A single nucleotide polymorphism in the MDM2 promoter attenuates the p53 tumor suppressor pathway and accelerates tumor formation in humans. Cell 119: 591-602.
    • (2004) Cell , vol.119 , pp. 591-602
    • Bond, G.L.1    Hu, W.2    Bond, E.E.3
  • 15
    • 0026740449 scopus 로고
    • Amplification of a gene encoding a p53-associated protein in human sarcomas
    • Oliner JD, Kinzler KW, Meltzer PS et al (1992) Amplification of a gene encoding a p53-associated protein in human sarcomas. Nature 358: 80-83.
    • (1992) Nature , vol.358 , pp. 80-83
    • Oliner, J.D.1    Kinzler, K.W.2    Meltzer, P.S.3
  • 16
    • 0033959324 scopus 로고    scopus 로고
    • Incidence and prognostic significance of MDM2 oncoprotein overexpression in relapsed childhood acute lymphoblastic leukemia
    • Zhou M, Gu L, Abshire TC et al (2000) Incidence and prognostic significance of MDM2 oncoprotein overexpression in relapsed childhood acute lymphoblastic leukemia. Leukemia 14: 61-67.
    • (2000) Leukemia , vol.14 , pp. 61-67
    • Zhou, M.1    Gu, L.2    Abshire, T.C.3
  • 17
    • 14644403700 scopus 로고    scopus 로고
    • MDM2 and human malignancies: Expression, clinical pathology, prognostic markers, and implications for chemotherapy
    • Rayburn E, Zhang R, He J et al (2005) MDM2 and human malignancies: expression, clinical pathology, prognostic markers, and implications for chemotherapy. Curr Cancer Drug Targets 5: 27-41.
    • (2005) Curr Cancer Drug Targets , vol.5 , pp. 27-41
    • Rayburn, E.1    Zhang, R.2    He, J.3
  • 18
  • 19
    • 0343193103 scopus 로고    scopus 로고
    • Mdm2 gene amplification in gastric cancer correlation with expression of Mdm2 protein and p53 alterations
    • Gunther T, Schneider-Stock R, Hackel C et al (2000) Mdm2 gene amplification in gastric cancer correlation with expression of Mdm2 protein and p53 alterations. Mod Pathol 13: 621-626.
    • (2000) Mod Pathol , vol.13 , pp. 621-626
    • Gunther, T.1    Schneider-Stock, R.2    Hackel, C.3
  • 20
    • 14644437751 scopus 로고    scopus 로고
    • MDM2 is a central node in the p53 pathway: 12 years and counting
    • Bond GL, HuW, Levine AJ (2005) MDM2 is a central node in the p53 pathway: 12 years and counting. Curr Cancer Drug Targets 5: 3-8.
    • (2005) Curr Cancer Drug Targets , vol.5 , pp. 3-8
    • Bond, G.L.1    Hu, W.2    Levine, A.J.3
  • 21
    • 0028834902 scopus 로고
    • Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
    • Jones SN, Roe AE, Donehower LA et al (1995) Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53. Nature 378: 206-208.
    • (1995) Nature , vol.378 , pp. 206-208
    • Jones, S.N.1    Roe, A.E.2    Donehower, L.A.3
  • 22
    • 0028823020 scopus 로고
    • Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
    • de Oca M, Luna R, Wagner DS, Lozano G (1995) Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53. Nature 378: 203-206.
    • (1995) Nature , vol.378 , pp. 203-206
    • de Oca, M.1    Luna, R.2    Wagner, D.S.3    Lozano, G.4
  • 23
    • 33845901313 scopus 로고    scopus 로고
    • MDM2 inhibitors for cancer therapy
    • Vassilev LT (2007) MDM2 inhibitors for cancer therapy. Trends Mol Med 13: 23-31.
    • (2007) Trends Mol Med , vol.13 , pp. 23-31
    • Vassilev, L.T.1
  • 24
    • 0037317840 scopus 로고    scopus 로고
    • Inhibiting the p53-MDM2 interaction: An important target for cancer therapy
    • Chene P (2003) Inhibiting the p53-MDM2 interaction: an important target for cancer therapy. Nat Rev Cancer 3: 102-109.
    • (2003) Nat Rev Cancer , vol.3 , pp. 102-109
    • Chene, P.1
  • 25
    • 53049108040 scopus 로고    scopus 로고
    • Targeting the MDM2-p53 interaction for cancer therapy
    • Shangary S, Wang S (2008) Targeting the MDM2-p53 interaction for cancer therapy. Clin Cancer Res 14: 5318-5324.
    • (2008) Clin Cancer Res , vol.14 , pp. 5318-5324
    • Shangary, S.1    Wang, S.2
  • 27
    • 0032952004 scopus 로고    scopus 로고
    • Mdm2: The ups and downs
    • Juven-Gershon T, Oren M (1999) Mdm2: the ups and downs. Mol Med 5: 71-83.
    • (1999) Mol Med , vol.5 , pp. 71-83
    • Juven-Gershon, T.1    Oren, M.2
  • 28
    • 0027244853 scopus 로고
    • The p53-mdm-2 autoregulatory feedback loop
    • Wu X, Bayle JH, Olson D et al (1993) The p53-mdm-2 autoregulatory feedback loop. Genes Dev 7: 1126-1132.
    • (1993) Genes Dev , vol.7 , pp. 1126-1132
    • Wu, X.1    Bayle, J.H.2    Olson, D.3
  • 29
    • 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 (1996) Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science 274: 948-953.
    • (1996) Science , vol.274 , pp. 948-953
    • Kussie, P.H.1    Gorina, S.2    Marechal, V.3
  • 30
    • 79953666206 scopus 로고    scopus 로고
    • Small-molecule inhibitors of p53-MDM2 interaction: The 2006-2010 update
    • Millard M, Pathania D, Grande F et al (2011) Small-molecule inhibitors of p53-MDM2 interaction: the 2006-2010 update. Curr Pharm Des 17: 536-559.
    • (2011) Curr Pharm Des , vol.17 , pp. 536-559
    • Millard, M.1    Pathania, D.2    Grande, F.3
  • 31
    • 79953672054 scopus 로고    scopus 로고
    • Peptide activators of the p53 tumor suppressor
    • Zhan C, Lu W (2011) Peptide activators of the p53 tumor suppressor. Curr Pharm Des 17: 603-609.
    • (2011) Curr Pharm Des , vol.17 , pp. 603-609
    • Zhan, C.1    Lu, W.2
  • 32
    • 84875169018 scopus 로고    scopus 로고
    • Mdm2 and MdmX inhibitors for the treatment of cancer: A patent review (2011-present)
    • Zak K, Pecak A, Rys B et al (2013) Mdm2 and MdmX inhibitors for the treatment of cancer: a patent review (2011-present). Expert Opin Ther Pat 23: 425-448.
    • (2013) Expert Opin Ther Pat , vol.23 , pp. 425-448
    • Zak, K.1    Pecak, A.2    Rys, B.3
  • 33
    • 4344610526 scopus 로고    scopus 로고
    • Small-molecule antagonists of p53-MDM2 binding: Research tools and potential therapeutics
    • Vassilev LT (2004) Small-molecule antagonists of p53-MDM2 binding: research tools and potential therapeutics. Cell Cycle 3: 419-421.
    • (2004) Cell Cycle , vol.3 , pp. 419-421
    • Vassilev, L.T.1
  • 34
    • 33745154819 scopus 로고    scopus 로고
    • Structure-based design of spirooxindoles as potent, specific small-molecule inhibitors of the MDM2-p53 interaction
    • Ding K, Lu Y, Nikolovska-Coleska Z et al (2006) Structure-based design of spirooxindoles as potent, specific small-molecule inhibitors of the MDM2-p53 interaction. J Med Chem 49: 3432-3435.
    • (2006) J Med Chem , vol.49 , pp. 3432-3435
    • Ding, K.1    Lu, Y.2    Nikolovska-Coleska, Z.3
  • 35
    • 22944473048 scopus 로고    scopus 로고
    • Structure-based design of potent nonpeptide MDM2 inhibitors
    • Ding K, Lu Y, Nikolovska-Coleska Z et al (2005) Structure-based design of potent nonpeptide MDM2 inhibitors. J Am Chem Soc 127: 10130-10131.
    • (2005) J Am Chem Soc , vol.127 , pp. 10130-10131
    • Ding, K.1    Lu, Y.2    Nikolovska-Coleska, Z.3
  • 36
    • 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 (2005) Discovery and cocrystal structure of benzodiazepinedione HDM2 antagonists that activate p53 in cells. J Med Chem 48: 909-912.
    • (2005) J Med Chem , vol.48 , pp. 909-912
    • Grasberger, B.L.1    Lu, T.2    Schubert, C.3
  • 37
    • 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 (2005) 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) Bioorg Med Chem Lett , vol.15 , pp. 765-770
    • Parks, D.J.1    Lafrance, L.V.2    Calvo, R.R.3
  • 38
    • 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 (2006) 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) Mol Cancer Ther , vol.5 , pp. 160-169
    • Koblish, H.K.1    Zhao, S.2    Franks, C.F.3
  • 39
    • 70949084205 scopus 로고    scopus 로고
    • Discovery and optimization of chromenotriazolopyrimidines as potent inhibitors of the mouse double minute 2-tumor protein 53 protein-protein interaction
    • Allen JG, Bourbeau MP, Wohlhieter GE et al (2009) Discovery and optimization of chromenotriazolopyrimidines as potent inhibitors of the mouse double minute 2-tumor protein 53 protein-protein interaction. J Med Chem 52: 7044-7053.
    • (2009) J Med Chem , vol.52 , pp. 7044-7053
    • Allen, J.G.1    Bourbeau, M.P.2    Wohlhieter, G.E.3
  • 40
    • 84862296171 scopus 로고    scopus 로고
    • Structure-based design of novel inhibitors of the MDM2-p53 interaction
    • Rew Y, Sun D, Gonzalez-Lopez De Turiso F et al (2012) Structure-based design of novel inhibitors of the MDM2-p53 interaction. J Med Chem 55: 4936-4954.
    • (2012) J Med Chem , vol.55 , pp. 4936-4954
    • Rew, Y.1    Sun, D.2    Gonzalez-Lopez De Turiso, F.3
  • 41
    • 84863966819 scopus 로고    scopus 로고
    • Activation of the p53 pathway by small-molecule-induced MDM2 and MDMX dimerization
    • Graves B, Thompson T, Xia M et al (2012) Activation of the p53 pathway by small-molecule-induced MDM2 and MDMX dimerization. Proc Natl Acad Sci U S A 109: 11788-11793.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 11788-11793
    • Graves, B.1    Thompson, T.2    Xia, M.3
  • 42
    • 84866739593 scopus 로고    scopus 로고
    • Discovery of novel dihydroimidazothiazole derivatives as p53-MDM2 protein-protein interaction inhibitors: Synthesis, biological evaluation and structure-activity relationships
    • Miyazaki M, Kawato H, Naito H et al (2012) Discovery of novel dihydroimidazothiazole derivatives as p53-MDM2 protein-protein interaction inhibitors: synthesis, biological evaluation and structure-activity relationships. Bioorg Med Chem Lett 22: 6338-6342.
    • (2012) Bioorg Med Chem Lett , vol.22 , pp. 6338-6342
    • Miyazaki, M.1    Kawato, H.2    Naito, H.3
  • 43
    • 18844423053 scopus 로고    scopus 로고
    • Terphenyl-based helical mimetics that disrupt the p53/HDM2 interaction
    • Yin H, Lee GI, Park HS et al (2005) Terphenyl-based helical mimetics that disrupt the p53/HDM2 interaction. Angew Chem Int Ed Engl 44: 2704-2707.
    • (2005) Angew Chem Int Ed Engl , vol.44 , pp. 2704-2707
    • Yin, H.1    Lee, G.I.2    Park, H.S.3
  • 44
    • 21344461945 scopus 로고    scopus 로고
    • p53 alpha-helix mimetics antagonize p53/MDM2 interaction and activate p53
    • Chen L, Yin H, Farooqi B et al (2005) p53 alpha-helix mimetics antagonize p53/MDM2 interaction and activate p53. Mol Cancer Ther 4: 1019-1025.
    • (2005) Mol Cancer Ther , vol.4 , pp. 1019-1025
    • Chen, L.1    Yin, H.2    Farooqi, B.3
  • 45
    • 33745645832 scopus 로고    scopus 로고
    • Discovery of a nanomolar inhibitor of the human murine double minute 2 (MDM2)-p53 interaction through an integrated, virtual database screening strategy
    • Lu Y, Nikolovska-Coleska Z, Fang X et al (2006) Discovery of a nanomolar inhibitor of the human murine double minute 2 (MDM2)-p53 interaction through an integrated, virtual database screening strategy. J Med Chem 49: 3759-3762.
    • (2006) J Med Chem , vol.49 , pp. 3759-3762
    • Lu, Y.1    Nikolovska-Coleska, Z.2    Fang, X.3
  • 46
    • 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 (2004) A nonpeptidic sulfonamide inhibits the p53-mdm2 interaction and activates p53-dependent transcription in mdm2-overexpressing cells. J Med Chem 47: 4163-4165.
    • (2004) J Med Chem , vol.47 , pp. 4163-4165
    • Galatin, P.S.1    Abraham, D.J.2
  • 47
    • 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 (2004) In vivo activation of the p53 pathway by smallmolecule antagonists of MDM2. Science 303: 844-848.
    • (2004) Science , vol.303 , pp. 844-848
    • Vassilev, L.T.1    Vu, B.T.2    Graves, B.3
  • 49
    • 28844484583 scopus 로고    scopus 로고
    • Development of E3-substrate (MDM2-p53)-binding inhibitors: Structural aspects
    • Fry DC, Graves B, Vassilev LT (2005) Development of E3-substrate (MDM2-p53)-binding inhibitors: structural aspects. Methods Enzymol 399: 622-633.
    • (2005) Methods Enzymol , vol.399 , pp. 622-633
    • Fry, D.C.1    Graves, B.2    Vassilev, L.T.3
  • 50
    • 84877690432 scopus 로고    scopus 로고
    • Discovery of RG7112: A small-molecule MDM2 inhibitor in clinical development
    • Vu B, Wovkulich P, Pizzolato G et al (2013) Discovery of RG7112: A small-molecule MDM2 inhibitor in clinical development. ACS Med Chem Lett 4: 466-469.
    • (2013) ACS Med Chem Lett , vol.4 , pp. 466-469
    • Vu, B.1    Wovkulich, P.2    Pizzolato, G.3
  • 51
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • Ericsson UB, Hallberg BM, Detitta GT et al (2006) Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal Biochem 357: 289-298.
    • (2006) Anal Biochem , vol.357 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    Detitta, G.T.3
  • 52
    • 4143121255 scopus 로고    scopus 로고
    • Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery
    • Lo MC, Aulabaugh A, Jin G et al (2004) Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery. Anal Biochem 332: 153-159.
    • (2004) Anal Biochem , vol.332 , pp. 153-159
    • Lo, M.C.1    Aulabaugh, A.2    Jin, G.3
  • 53
    • 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 (2008) Temporal activation of p53 by a specific MDM2 inhibitor is selectively toxic to tumors and leads to complete tumor growth inhibition. Proc Natl Acad SciUS A 105: 3933-3938.
    • (2008) Proc Natl Acad SciUS A , vol.105 , pp. 3933-3938
    • Shangary, S.1    Qin, D.2    McEachern, D.3
  • 54
    • 73249140963 scopus 로고    scopus 로고
    • Potent and orally active small-molecule inhibitors of the MDM2-p53 interaction
    • Yu S, Qin D, Shangary S et al (2009) Potent and orally active small-molecule inhibitors of the MDM2-p53 interaction. J Med Chem 52: 7970-7973.
    • (2009) J Med Chem , vol.52 , pp. 7970-7973
    • Yu, S.1    Qin, D.2    Shangary, S.3
  • 55
    • 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 et al (2000) Discovery of potent antagonists of the interaction between human double minute 2 and tumor suppressor p53. J Med Chem 43: 3205-3208.
    • (2000) J Med Chem , vol.43 , pp. 3205-3208
    • Garcia-Echeverria, C.1    Chene, P.2    Blommers, M.J.3
  • 56
    • 7444262377 scopus 로고    scopus 로고
    • Development and optimization of a binding assay for the XIAP BIR3 domain using fluorescence polarization
    • Nikolovska-Coleska Z, Wang R, Fang X et al (2004) Development and optimization of a binding assay for the XIAP BIR3 domain using fluorescence polarization. Anal Biochem 332: 261-273.
    • (2004) Anal Biochem , vol.332 , pp. 261-273
    • Nikolovska-Coleska, Z.1    Wang, R.2    Fang, X.3
  • 57
    • 0042468972 scopus 로고    scopus 로고
    • Fluorescence polarization competition assay: The range of resolvable inhibitor potency is limited by the affinity of the fluorescent ligand
    • Huang X (2003) Fluorescence polarization competition assay: the range of resolvable inhibitor potency is limited by the affinity of the fluorescent ligand. J Biomol Screen 8: 34-38.
    • (2003) J Biomol Screen , vol.8 , pp. 34-38
    • Huang, X.1
  • 59
    • 0023918636 scopus 로고
    • An exact correction to the "Cheng-Prusoff" correction
    • Munson PJ, Rodbard D (1988) An exact correction to the "Cheng-Prusoff" correction. J Recept Res 8: 533-546.
    • (1988) J Recept Res , vol.8 , pp. 533-546
    • Munson, P.J.1    Rodbard, D.2
  • 60
    • 3042712875 scopus 로고    scopus 로고
    • Fluorescence polarization assay and inhibitor design for MDM2/p53 interaction
    • Zhang R, Mayhood T, Lipari P et al (2004) Fluorescence polarization assay and inhibitor design for MDM2/p53 interaction. Anal Biochem 331: 138-146.
    • (2004) Anal Biochem , vol.331 , pp. 138-146
    • Zhang, R.1    Mayhood, T.2    Lipari, P.3
  • 61
    • 0037048711 scopus 로고    scopus 로고
    • Development of a potent Bcl-x(L) antagonist based on alpha-helix mimicry
    • Kutzki O, Park HS, Ernst JT et al (2002) Development of a potent Bcl-x(L) antagonist based on alpha-helix mimicry. J Am Chem Soc 124: 11838-11839.
    • (2002) J Am Chem Soc , vol.124 , pp. 11838-11839
    • Kutzki, O.1    Park, H.S.2    Ernst, J.T.3
  • 63
    • 20144367578 scopus 로고    scopus 로고
    • Chalcones: An update on cytotoxic and chemoprotective properties
    • Go ML, Wu X, Liu XL (2005) Chalcones: an update on cytotoxic and chemoprotective properties. Curr Med Chem 12: 481-499.
    • (2005) Curr Med Chem , vol.12 , pp. 481-499
    • Go, M.L.1    Wu, X.2    Liu, X.L.3
  • 64
    • 0035895350 scopus 로고    scopus 로고
    • Chalcone derivatives antagonize interactions between the human oncoprotein MDM2 and p53
    • Stoll R, Renner C, Hansen S et al (2001) Chalcone derivatives antagonize interactions between the human oncoprotein MDM2 and p53. Biochemistry 40: 336-344.
    • (2001) Biochemistry , vol.40 , pp. 336-344
    • Stoll, R.1    Renner, C.2    Hansen, S.3
  • 66
    • 84867488138 scopus 로고    scopus 로고
    • Ordering of the N-terminus of human MDM2 by small molecule inhibitors
    • Michelsen K, Jordan JB, Lewis J et al (2012) Ordering of the N-terminus of human MDM2 by small molecule inhibitors. J Am Chem Soc 134: 17059-17067.
    • (2012) J Am Chem Soc , vol.134 , pp. 17059-17067
    • Michelsen, K.1    Jordan, J.B.2    Lewis, J.3
  • 67
    • 0028303752 scopus 로고
    • Several hydrophobic amino acids in the p53 aminoterminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein
    • Lin J, Chen J, Elenbaas B et al (1994) Several hydrophobic amino acids in the p53 aminoterminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein. Genes Dev 8: 1235-1246.
    • (1994) Genes Dev , vol.8 , pp. 1235-1246
    • Lin, J.1    Chen, J.2    Elenbaas, B.3
  • 68
    • 0029818380 scopus 로고    scopus 로고
    • Identification of novel mdm2 binding peptides by phage display
    • Bottger V, Bottger A, Howard SF et al (1996) Identification of novel mdm2 binding peptides by phage display. Oncogene 13: 2141-2147.
    • (1996) Oncogene , vol.13 , pp. 2141-2147
    • Bottger, V.1    Bottger, A.2    Howard, S.F.3
  • 69
    • 35548942306 scopus 로고    scopus 로고
    • Small molecule inhibitors of the MDM2-p53 interaction discovered by ensemble-based receptor models
    • Bowman AL, Nikolovska-Coleska Z, Zhong H et al (2007) Small molecule inhibitors of the MDM2-p53 interaction discovered by ensemble-based receptor models. J Am Chem Soc 129: 12809-12814.
    • (2007) J Am Chem Soc , vol.129 , pp. 12809-12814
    • Bowman, A.L.1    Nikolovska-Coleska, Z.2    Zhong, H.3
  • 70
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones G, Willett P, Glen RC et al (1997) Development and validation of a genetic algorithm for flexible docking. J Mol Biol 267: 727-748.
    • (1997) J Mol Biol , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3
  • 71
    • 0041919542 scopus 로고    scopus 로고
    • Improved protein-ligand docking using GOLD
    • Verdonk ML, Cole JC, Hartshorn MJ et al (2003) Improved protein-ligand docking using GOLD. Proteins 52: 609-623.
    • (2003) Proteins , vol.52 , pp. 609-623
    • Verdonk, M.L.1    Cole, J.C.2    Hartshorn, M.J.3
  • 72
    • 0031226772 scopus 로고    scopus 로고
    • Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes
    • Eldridge MD, Murray CW, Auton TR et al (1997) Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes. J Comput Aided Mol Des 11: 425-445.
    • (1997) J Comput Aided Mol Des , vol.11 , pp. 425-445
    • Eldridge, M.D.1    Murray, C.W.2    Auton, T.R.3
  • 73
    • 0036022960 scopus 로고    scopus 로고
    • Further development and validation of empirical scoring functions for structure-based binding affinity prediction
    • Wang R, Lai L, Wang W (2002) Further development and validation of empirical scoring functions for structure-based binding affinity prediction. J Comput Aided Mol Des 16: 11-26.
    • (2002) J Comput Aided Mol Des , vol.16 , pp. 11-26
    • Wang, R.1    Lai, L.2    Wang, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.