Mdm2 and MdmX inhibitors for the treatment of cancer: a patent review (2011 – present)

Bibliography

• Jemal A, Bray F, Center MM, Global cancer statistics. CA Cancer J Clin 2011;61:69-90
   PubMed Web of Science ®Google Scholar
• Hainaut P, Hollstein M. p53 and human cancer: the first ten thousand mutations. Adv Cancer Res 2000;77:81-137
   PubMed Web of Science ®Google Scholar
• Marchenko ND, Moll UM. The role of ubiquitination in the direct mitochondrial death program of p53. Cell Cycle 2007;6:1718-23
   PubMed Web of Science ®Google Scholar
• Vousden KH, Lane DP. p53 in health and disease. Nat Rev Mol Cell Biol 2007;8:275-83
   PubMed Web of Science ®Google Scholar
• Lane DP. Cancer. p53, guardian of the genome. Nature 1992;358:15-16
   PubMed Web of Science ®Google Scholar
• Toledo F, Wahl GM. MDM2 and MDM4: p53 regulators as targets in anticancer therapy. Int J Biochem Cell Biol 2007;39:1476-82
   PubMed Web of Science ®Google Scholar
• Clegg HV, Zhang Y. Regulation of the p53 tumor suppressor pathway: the problems and promises of studying Mdm2's E3 ligase function. Crit Rev Eukaryot Gene Expr 2010;20:77-86
   Google Scholar
• Tang Y, Zhao W, Chen Y, Acetylation is indispensable for p53 activation. Cell 2008;133:612-26
   PubMed Web of Science ®Google Scholar
• Brooks CL, Gu W. p53 ubiquitination: mdm2 and beyond. Mol Cell 2006;21:307-15
   PubMed Web of Science ®Google Scholar
• Wade M, Wahl GM. Targeting Mdm2 and Mdmx in cancer therapy: better living through medicinal chemistry? Mol Cancer Res 2009;7:1-11
   PubMed Web of Science ®Google Scholar
• Wagner J, Ma L, Rice JJ, p53-Mdm2 loop controlled by a balance of its feedback strength and effective dampening using ATM and delayed feedback. Syst Biol (Stevenage) 2005;152:109-18
   PubMedGoogle Scholar
• Brown CJ, Cheok CF, Verma CS, Lane DP. Reactivation of p53: from peptides to small molecules. Trends Pharmacol Sci 2011;32:53-62
   PubMed Web of Science ®Google Scholar
• Ding K, Lu Y, Nikolovska-Coleska Z, Structure-based design of spiro-oxindoles as potent, specific small-molecule inhibitors of the MDM2-p53 interaction. J Med Chem 2006;49:3432-5
   PubMed Web of Science ®Google Scholar
• Koblish HK, Zhao S, Franks CF, Benzodiazepinedione inhibitors of the Hdm2:p53 complex suppress human tumor cell proliferation in vitro and sensitize tumors to doxorubicin in vivo. Mol Cancer Ther 2006;5:160-9
   PubMed Web of Science ®Google Scholar
• Vassilev LT, Vu BT, Graves B, In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science 2004;303:844-8
   PubMed Web of Science ®Google Scholar
• Xue W, Zender L, Miething C, Senescence and tumour clearance is triggered by p53 restoration in murine liver carcinomas. Nature 2007;445:656-60
   PubMed Web of Science ®Google Scholar
• Yu X, Vazquez A, Levine AJ, Carpizo DR. Allele-specific p53 mutant reactivation. Cancer Cell 2012;21:614-25
   PubMed Web of Science ®Google Scholar
• Basse N, Kaar JL, Settanni G, Toward the rational design of p53-stabilizing drugs: probing the surface of the oncogenic Y220C mutant. Chem Biol 2010;17:46-56
   PubMedGoogle Scholar
• Klein C, Vassilev LT. Targeting the p53-MDM2 interaction to treat cancer. Br J Cancer 2004;91:1415-19
   PubMed Web of Science ®Google Scholar
• Toledo F, Wahl GM. Regulating the p53 pathway: in vitro hypotheses, in vivo veritas. Nat Rev Cancer 2006;6:909-23
   PubMed Web of Science ®Google Scholar
• Levine AJ, Hu W, Feng Z. The P53 pathway: what questions remain to be explored? Cell Death Differ 2006;13:1027-36
   PubMed Web of Science ®Google Scholar
• Laurie NA, Donovan SL, Shih CS, Inactivation of the p53 pathway in retinoblastoma. Nature 2006;444:61-6
   PubMed Web of Science ®Google Scholar
• Dawson R, Muller L, Dehner A, The N-terminal domain of p53 is natively unfolded. J Mol Biol 2003;332:1131-41
   Google Scholar
• Popowicz GM, Czarna A, Holak TA. Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain. Cell Cycle 2008;7:2441-3
   PubMed Web of Science ®Google Scholar
• Domling A. Small molecular weight protein-protein interaction antagonists: an insurmountable challenge? Curr Opin Chem Biol 2008;12:281-91
   PubMed Web of Science ®Google Scholar
• Popowicz GM, Domling A, Holak TA. The structure-based design of Mdm2/Mdmx-p53 inhibitors gets serious. Angew Chem Int Ed Engl 2011;50:2680-8
   PubMed Web of Science ®Google Scholar
• Khoury K, Popowicz GM, Holak TA, Domling A. The p53-MDM2/MDMX axis – a chemotype perspective. Med Chem Commun 2011;2:246-60
   Google Scholar
• Ray-Coquard I, Blay JY, Italiano A, Effect of the MDM2 antagonist RG7112 on the P53 pathway in patients with MDM2-amplified, well-differentiated or dedifferentiated liposarcoma: an exploratory proof-of-mechanism study. Lancet Oncol 2012;13:1133-40
   PubMed Web of Science ®Google Scholar
• Results of the Phase 1 Trial of RG7112, Basel, 11 December 2012, F. Hoffmann-La Roche Ltd
   Google Scholar
• Hu B, Gilkes DM, Farooqi B, MDMX overexpression prevents p53 activation by the MDM2 inhibitor Nutlin. J Biol Chem 2006;281:33030-5
   PubMed Web of Science ®Google Scholar
• Bernal F, Wade M, Godes M, A stapled p53 helix overcomes HDMX-mediated suppression of p53. Cancer Cell 2010;18:411-22
   PubMed Web of Science ®Google Scholar
• Graves B, Thompson T, Xia M, Activation of the p53 pathway by small-molecule-induced MDM2 and MDMX dimerization. Proc Natl Acad Sci USA 2012;109:11788-93
   PubMed Web of Science ®Google Scholar
• Mullard A. Protein-protein interaction inhibitors get into the groove. Nat Rev Drug Discov 2012;11:173-5
   PubMed Web of Science ®Google Scholar
• Q2 2012 Report, Sanofi-Aventis Indonesia
   Google Scholar
• University of Michigan. Spiro-oxindole Mdm2 antagonists. WO2012065022; 2012
   Google Scholar
• Kamal A, Mohammed AA, Shaik TB. p53-Mdm2 inhibitors: patent review (2009 – 2010). Expert Opin Ther Patents 2012;22:95-105
   PubMed Web of Science ®Google Scholar
• Weber L. Patented inhibitors of p53-Mdm2 interaction (2006 – 2008). Expert Opin Ther Patents 2010;20:179-91
   PubMed Web of Science ®Google Scholar
• Deng J, Dayam R, Neamati N. Patented small molecule inhibitors of p53-MDM2 interaction. Expert Opin Ther Patents 2006;16:165-88
   PubMed Web of Science ®Google Scholar
• Hoffman-La Roche AG. CIS-imidazolines. US7893278; 2011
   Google Scholar
• Hoffman-La Roche AG. Provisional application No. 60580441; 2004
   Google Scholar
• Hoffman-La Roche AG. Provisional application No. 60674196; 2005
   Google Scholar
• Bottger A, Bottger V, Sparks A, Design of a synthetic Mdm2-binding mini protein that activates the p53 response in vivo. Curr Biol 1997;7:860-9
   PubMed Web of Science ®Google Scholar
• Hoffmann-La Roche AG. Chiral cis-imidazolines. US7964724; 2011
   Google Scholar
• Hoffman-La Roche AG. Provisional application No. 60572275; 2004
   Google Scholar
• Hoffman-La Roche AG. Provisional application No. 60615534; 2004
   Google Scholar
• Hoffman-La Roche AG. Provisional application No. 60668772; 2005
   Google Scholar
• St. Jude Children's Research Hospital. Aryl-substituted imidazoles. WO2012045018; 2012
   Google Scholar
• Hoffmann-La Roche AG. N-substituted-pyrrolidines as inhibitors of MDM2-P-53 interactions. US8017607; 2011
   Google Scholar
• Hoffman-La Roche AG. Provisional application No. 61251413; 2009
   Google Scholar
• Hoffman-La Roche AG. Provisional application No. 61345626; 2010
   Google Scholar
• Hoffmann-La Roche AG. 3-cyano-1-hydroxymethyl-2-phenylpyrrolidine derivatives as inhibitors of Mdm2-p53 interactions useful for the treatment of cancer. WO2012076513; 2012
   Google Scholar
• Hoffmann-La Roche AG. Substituted pyrrolidine-2-carboxamides. WO2011061139; 2011
   Google Scholar
• Hoffmann-La Roche AG. Substituted hexahydropyrrolo [1,2-C] imidazoles useful as Mdm2 inhibitors. WO2012034954; 2012
   Google Scholar
• Novartis AG. Tetra-substituted heteroaryl compounds and their use as Mdm2 and/or Mdm4 modulators. WO2011023677; 2011
   Google Scholar
• University of Pittsburgh. Novel p53-Mdm2/p53-Mdm4 antagonists to treat proliferative disease. WO2011106650; 2011
   Google Scholar
• Bista M, Kowalska K, Janczyk W, Robust NMR screening for lead compounds using tryptophan-containing proteins. J Am Chem Soc 2009;131:7500-1
   PubMed Web of Science ®Google Scholar
• Dudgeon DD, Shinde SN, Shun TY, Characterization and optimization of a novel protein-protein interaction biosensor high-content screening assay to identify disruptors of the interactions between p53 and hDM2. Assay Drug Dev Technol 2010;8:437-58
   Google Scholar
• Popowicz GM, Czarna A, Wolf S, Structures of low molecular weight inhibitors bound to MDMX and MDM2 reveal new approaches for p53-MDMX/MDM2 antagonist drug discovery. Cell Cycle 2010;9:1104-11
   PubMed Web of Science ®Google Scholar
• Khoury K, Domling A. P53 mdm2 inhibitors. Curr Pharm Des 2012;18:4668-78
   PubMed Web of Science ®Google Scholar
• University of Pittsburgh. p53-Mdm2 antagonists. WO2012033525; 2012
   Google Scholar
• Huang Y, Wolf S, Koes D, Exhaustive fluorine scanning toward potent p53-Mdm2 antagonists. ChemMedChem 2012;7:49-52
   Google Scholar
• Hoffman-La Roche AG. Oxindole derivatives. US8058269; 2011
   Google Scholar
• Hoffman-La Roche AG. Provisional application No. 60846201; 2006
   Google Scholar
• Sanofi-Aventis Indonesia
   Google Scholar
• U.S. National Institutes of Health
   Google Scholar
• Wang Z, Jonca M, Lambros T, Exploration of liquid and supercritical fluid chromatographic chiral separation and purification of Nutlin-3–a small molecule antagonist of MDM2. J Pharm Biomed Anal 2007;45:720-9
   Google Scholar
• University of Michigan. Small molecule inhibitors of MDM2 and the uses thereof. US7759383; 2010
   Google Scholar
• University of Michigan. Small molecule inhibitors of MDM2 and the uses thereof. US8088931; 2012
   Google Scholar
• University of Michigan. Provisional application No. 60655135; 2005
   Google Scholar
• University of Michigan. Indole inhibitors of MDM2 and the uses thereof. US7737174; 2010
   Google Scholar
• University of Michigan. Small molecule inhibitors of MDM2 and the uses thereof. US8222288; 2012
   Google Scholar
• University of Michigan. Provisional application No. 60841150; 2006
   Google Scholar
• University of Michigan. Provisional application No. 60878795; 2007
   Google Scholar
• University of Michigan. Spiro-oxindole Mdm2 antagonists. WO2011060049; 2011
   Google Scholar
• Hoffman-La Roche AG. Spiroindolinone pyrrolidines. US8088815; 2012
   Google Scholar
• Hoffman-La Roche AG. Provisional application No. 61265972; 2009
   Google Scholar
• Hoffman-La Roche AG. Provisional application No. 61388054; 2010
   Google Scholar
• Hoffmann-La Roche AG. 3,3′-spiroindolinone derivatives. US8076482; 2011
   Google Scholar
• Hoffman-La Roche AG. Provisional application No. 61171970; 2009
   Google Scholar
• Hoffmann-La Roche AG. Spiroindolinone derivatives. US8217051; 2012
   Google Scholar
• Hoffman-La Roche AG. Provisional application No. 61153089; 2010
   Google Scholar
• Hoffmann-La Roche AG. Spiro substituted pyrrolo [1,2-C] imidazole derivatives useful as Mdm2 inhibitors. WO2012038307; 2012
   Google Scholar
• Daiichi Sankyo LTD. Dispiropyrrolidine derivatives. US20120264738; 2012
   Google Scholar
• Merck AG. Substituted piperidines that increase P53 activity and the uses thereof. US7884107; 2011
   Google Scholar
• Novartis AG. Substituted isoquinolinones and quinazolinones. WO2011076786; 2011
   Google Scholar
• Novartis AG. Crystalline form of an inhibitor of Mdm2/4 and p53 interaction. WO2012066095; 2012
   Google Scholar
• 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 2000;43:3205-8
   PubMed Web of Science ®Google Scholar
• Agency for Science, Technology and Research Singapore. WO201105219; 2011
   Google Scholar
• Aileron Therapeutics, Inc
   Google Scholar
• Serrata, LLC. Mdm2 inhibitors for treatment of ocular conditions. WO2012047587; 2012
   Google Scholar
• Roche Glycart AG. Combination therapy of an afucosylated CD20 antibody with a Mdm2 inhibitor. WO2012080389; 2012
   Google Scholar