ATP-noncompetitive CDK inhibitors for cancer therapy: an overview

Bibliography

• Rubin GM, Yandell MD, Wortman JR, et al. Comparative Genomics of the Eukaryotes Science. 2000;287:2204
   Google Scholar
• Manning G, Whyte DB, Martinez R, et al. The Protein Kinase Complement of the Human Genome. Science 2002;298:1912-34
   PubMed Web of Science ®Google Scholar
• Satyanarayana A, Kaldis P. Mammalian cell-cycle regulation: several Cdks, numerous cyclins and diverse compensatory mechanisms. Oncogene 2009;28:2925-39
   PubMed Web of Science ®Google Scholar
• Senderowicz AM. Small-molecule cyclin-dependent kinase modulators. Oncogene 2003;22:6609
   PubMed Web of Science ®Google Scholar
• Nigg EA. Targets of cyclin-dependent protein kinases. Curr Opin Cell Biol 1993;5:187
   PubMed Web of Science ®Google Scholar
• Johnson DG, Walker CL. Cyclins and cell cycle checkpoints. Ann Rev Pharmacol Toxicol 1999;39:295-312
   PubMed Web of Science ®Google Scholar
• Norbury C, Nurse P. Animal cell cycles and their control. Annu Rev Biochem 1992;61:441-70
   PubMed Web of Science ®Google Scholar
• Weinberg RA. The retinoblastoma protein and cell cycle control. Cell 1995;81:323-30
   PubMed Web of Science ®Google Scholar
• Genovese C, Trani D, Caputi M, et al. Cell cycle control and beyond: emerging roles for the retinoblastoma gene family. Oncogene 2006;25:5201-9
   PubMed Web of Science ®Google Scholar
• Schaffer BE, Park KS, Yiu G, et al. Loss of p130 accelerates tumor development in a mouse model for human small-cell lung carcinoma. Cancer Res 2010;70:3877-83
   PubMed Web of Science ®Google Scholar
• Baldi A, De Luca A, Claudio PP, et al. The RB2/p130 gene product is a nuclear protein whose phosphorylation is cell cycle regulated. J Cell Biochem 1995;59:402-8
   PubMed Web of Science ®Google Scholar
• Haigis K, Sage J, Glickman J, et al. The related Retinoblastoma (pRb) and p130 proteins cooperate to regulate homeostasis in the intestinal epithelium. J Biol Chem 2006;281:638-47
   PubMed Web of Science ®Google Scholar
• Malumbres M, Harlow E, Hunt T, et al. Cyclin-dependent kinases: a family portrait. Nat Cell Biol 2009;11:1275-6
   PubMed Web of Science ®Google Scholar
• Pines J, Hunter T. Cyclin-dependent kinases: a new cell cycle motif? Trends Cell Biol 1991;1:117-21
   PubMedGoogle Scholar
• Malumbres M, Barbacid M. To cycle or not to cycle: a critical decision in cancer. Nat Rev Cancer 2001;1:222-31
   PubMed Web of Science ®Google Scholar
• Nobori T, Miura K, Wu DJ, et al. Deletions of the cyclin-dependent kinase-4 inhibitor gene in multiple human cancers. Nature 1994;368:753-6
   PubMed Web of Science ®Google Scholar
• Pines J. Cyclins, cdks and cancer. Semin Cancer Biol 1995;6:63-72
   PubMed Web of Science ®Google Scholar
• Hartwell LH, Kastan MB. Cell cycle control and cancer. Science 1994;266:1821-8
   PubMed Web of Science ®Google Scholar
• Catalogue of somatic mutations in cancer COSMIC, Trust Genome Campus, Hinxton, Cambridge. Available from: http://www.sanger.ac.uk/genetics/CGP/cosmic/ [Last accessed 5 November 2012]
   Google Scholar
• Pentimalli F, Giordano A. Promises and drawbacks of targeting cell cycle kinases in cancer. Discov Med 2009;43:177-80
   Google Scholar
• Wolfel T, Hauer M, Schneider J, et al. p16INK4a-insensitive CDK4 mutant targeted by cytolytic T lymphocytes in a human melanoma. Science 1995;269:1281-4
   PubMed Web of Science ®Google Scholar
• Lapointe J, Lachance Y, Labrie Y, et al. A p18 mutant defective in CDK6 binding in human breast cancer cells. Cancer Res 1996;56:4586-9
   Google Scholar
• Shennan MG, Badin A, Walsh S, et al. Lack of germline CDK6 mutations in familial melanoma. Oncogene 2000;19:1849-52
   PubMed Web of Science ®Google Scholar
• Indovina P, Marcelli E, Casina N, et al. Emerging roles of RB family: new defense mechanisms against tumor progression. J Cell Physiol 2013;228:525-35
   PubMed Web of Science ®Google Scholar
• Siddik ZH. Checkpoint controls and targets in cancer therapy. Humana press; Springer New York; 2009
   Google Scholar
• Giordano A, McCall C, Whyte P, et al. Human cyclin A and the retinoblastoma protein interact with similar but distinguishable sequences in the adenovirus E1A gene product. Oncogene 1991;6:481-5
   PubMed Web of Science ®Google Scholar
• Giordano A, Lee JH, Scheppler JA, et al. Cell cycle regulation of histone H1 kinase activity associated with the adenoviral protein E1A. Science 1991;253:1271-5
   PubMed Web of Science ®Google Scholar
• Giordano A, Whyte P, Harlow E, et al. A 60 kd cdc2-associated polypeptide complexes with the E1A proteins in adenovirus-infected cells. Cell 1989;58:981-90
   PubMed Web of Science ®Google Scholar
• Lapenna S, Giordano A. Cell cycle kinases as therapeutic targets for cancer. Nat Rev Drug Discov 2009;8:547-66
   PubMed Web of Science ®Google Scholar
• Galons H, Oumata N, Meijer L. Cyclin-dependent kinase inhibitors: a survey of recent patent literature. Expert Opin Ther Patent 2010;20:377-404
   PubMed Web of Science ®Google Scholar
• Malumbres M, Pevarello P, Barbacid M, et al. CDK inhibitors in cancer therapy: what is next? Trends Pharmacol Sci 2008;29:16-21
   PubMed Web of Science ®Google Scholar
• Thoms HC, Dunlop MG, Stark LA. CDK4 Inhibitors and apoptosis a novel mechanism requiring nucleolar targeting of RelA. Cell Cycle 2007;6:1293-7
   PubMed Web of Science ®Google Scholar
• Ferrer J, Dupuy J, Borel F. Structural basis for the modulation of cdk dependent/independent activity of cyclin D1. Cell Cycle 2006;5:2760-8
   PubMed Web of Science ®Google Scholar
• Davies TG, Pratt DJ, Endicott JA, et al. Structure-based design of cyclin-dependent kinase inhibitors. Pharmacol Ther 2002;93:125-33
   PubMed Web of Science ®Google Scholar
• Liu Y, Gray NS. Rational design of inhibitors that bind to inactive kinase conformations. Nat Chem Biol 2006;2:358-64
   PubMed Web of Science ®Google Scholar
• Johnson LN. Protein kinase inhibitors: contributions from structure to clinical compounds. Q Rev Biophys 2009;42:1-40
   PubMed Web of Science ®Google Scholar
• Hanks SK, Hunter T. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J 1995;9:576
   PubMed Web of Science ®Google Scholar
• Fischer PM, Gianella-Borradori A. CDK inhibitors in clinical development for the treatment of cancer. Expert Opin Investig Drugs 2003;12:955-70
   PubMed Web of Science ®Google Scholar
• Christian BA, Grever MR, Byrd JC, et al. Flavopiridol in the treatment of chronic lymphocytic leukemia. Curr Opin Oncol 2007;19:573-8
   PubMed Web of Science ®Google Scholar
• Takahashi I, Saitoh Y, Yoshida M, et al. UCN-01 and UCN-02, new selective inhibitors of protein kinase C. II. Purification, physico-chemical properties, structural determination and biological activities. J Antibiot 1989;42:571-6
   PubMed Web of Science ®Google Scholar
• Akiyama T, Yoshida T, Tsujita T, et al. G1 phase accumulation induced by UCN-01 is associated with dephosphorylation of Rb and CDK2 proteins as well as induction of CDK inhibitor p21/Cip1/WAF1/Sdi1 inp53-mutated human epidermoid carcinoma A431 cells. Cancer Res 1997;57:1495-501
   PubMed Web of Science ®Google Scholar
• Akiyama T, Sugiyama K, Shimizu M, et al. G1-checkpoint function including a cyclin-dependent kinase 2 regulatory pathway as potential determinant of 7-hydroxystaurosporine (UCN-01)-induced apoptosis and G1-phase accumulation. Jpn J Cancer Res 1999;90:1364-72
   PubMedGoogle Scholar
• Bhonde MR, Hanski ML, Magrini R, et al. The broad-range cyclin-dependent kinase inhibitor UCN-01 induces apoptosis in colon carcinoma cells through transcriptional suppression of the Bcl-x(L) protein. Oncogene 2005;24:148-56
   PubMed Web of Science ®Google Scholar
• Malumbres M, Barbacid M. Cell cycle. CDKs, and cancer: a changing paradigm46. Nat Rev Cancer 2009;9:153-66
   PubMed Web of Science ®Google Scholar
• Santamaria D, Barriere C, Cerqueira A, et al. Cdk1 is sufficient to drive the mammalian cell cycle. Nature 2007;448:811-15
   PubMed Web of Science ®Google Scholar
• Malumbres M, Barbacid M. Is cyclin D1–CDK4 kinase a bona fide cancer target? Cancer Cell 2006;9:2-4
   PubMed Web of Science ®Google Scholar
• Karp JE, Smith BD, Levis MJ, et al. Sequential flavopiridol, cytosine arabinoside, and mitoxantrone: a phase II trial in adults with poor-risk acute myelogenous leukemia. Clin Cancer Res 2007;13:4467-73
   PubMed Web of Science ®Google Scholar
• Huang J, Sheard MA, Ji L, et al. Combination of vorinostat and flavopiridol is selectively cytotoxic to multidrug-resistant neuroblastoma cell lines with mutant TP53. Mol Cancer Ther 2010;9:3289-301
   PubMed Web of Science ®Google Scholar
• De Azevedo WF, Lecrerc S, Meijer L, et al. Inhibition of cyclin-dependent kinases by purine analogues. Crystal structure of human cdk2 complexed with roscovitine. Eur J Biochem 1997;243:518-26
   PubMedGoogle Scholar
• Meijer L, Borgne A, Mulner O, et al. Biochemical and cellular effects of roscovitine, a potent and selective inhibitor of the cyclin-dependent kinases cdc2, cdk2 and cdk5. Eur J Biochem 1997;243:527-36
   PubMedGoogle Scholar
• Meijer L, Bettayeb K, Galons H. Roscovitine (CYC202, seliciclib). inhibitors of cyclin-dependent kinases as anti-tumor agents. CRC Press, Taylor & Francis group, Boca Raton, FL 33487-2742; 2007
   Google Scholar
• Genzyme. Purine derivatives for the treatment of cystic diseases. WO08051502; 2008
   Google Scholar
• Benson C, Raynoud F, O'Donnel A, et al. Pharmacokinetics (PK) and oral cyclic dependent kinase inhibitor CYC202 (R-roscovitine) in patients with cancer. Proc Am Assoc Cancer Res 2002;43:1354
   Google Scholar
• Stearns ME, Jenkins DP, Tew KD. Dansylated estramustine, a fluorescent probe for studies of estramustine uptake and identification of intracellular targets. Proc Natl Acad Sci USA 1985;82:8483-7
   PubMed Web of Science ®Google Scholar
• Summerer D, Chen S, Wu N, et al. A genetically encoded fluorescent amino acid. Proc Natl Acad Sci USA 2006;103:9785-9
   PubMed Web of Science ®Google Scholar
• Damianovich M, Ziv I, Heyman SN, et al. ApoSense: a novel technology for functional molecular imaging of cell death in models of acute renal tubular necrosis. Eur J Nucl Med Mol Imaging 2006;33:281-91
   PubMed Web of Science ®Google Scholar
• Cohen A, Ziv I, Aloya T, et al. Monitoring of chemotherapy-induced cell death in melanoma tumors by N,N'-Didansyl-L-cystine. Technol Cancer Res Treat 2007;6:221-34
   PubMed Web of Science ®Google Scholar
• Kong Y, Jung M, Wang K, et al. Histone deacetylase cytoplasmic trapping by a novel fluorescent HDAC inhibitor. Mol Cancer Ther 2011;10:1591-9
   PubMed Web of Science ®Google Scholar
• Bhardwaj A, Kaur J, Sharma SK, et al. Hybrid fluorescent conjugates of COX-2 inhibitors: search for a COX-2 isozyme imaging cancer biomarker. Bioorgan Med Chem Lett 2013;23:163-8
   PubMed Web of Science ®Google Scholar
• Joubert J, van Dyk S, Green IR, et al. Synthesis, evaluation and application of polycyclic fluorescent analogues as N-methyl-D-aspartate receptor and voltage gated calcium channel ligands. Eur J Med Chem 2011;46:5010-20
   PubMed Web of Science ®Google Scholar
• Sheikh KD, Banerjee PP, Jagadeesh S, et al. Fluorescent epigenetic small molecule induces expression of the tumor suppressor ras-association domain family 1a and inhibits human prostate xenograft. J Med Chem 2010;53:2376-82
   PubMed Web of Science ®Google Scholar
• Yenugonda VM, Deb TB, Grindrod SC, et al. Fluorescent cyclin-dependent kinase inhibitors block the proliferation of human breast cancer cells. Bioorg Med Chem 2011;19:2714-25
   Google Scholar
• Albert Einstein College of Medicine of Yeshiva University. Fluorescent assays for screening for protein kinase inhibitors applicable in cancer treatment and diagnosis. WO2004062475
   Google Scholar
• Stearns ME, Jenkins DP, Tew KD. Dansylated estramustine, a fluorescent probe for studies of estramustine uptake and identification of intracellular targets. Proc Natl Acad Sci USA 1985;82:8483-7
   PubMed Web of Science ®Google Scholar
• Atkinson GE, Cowan A, McInnes C, et al. Peptide inhibitors of CDK2-cyclin A that target the cyclin recruitment-site: structural variants of the C-terminal Phe. Bioorg Med Chem Lett 2002;12:2501-5
   PubMed Web of Science ®Google Scholar
• Rizzolio F, Tuccinardi T, Caligiuri I, et al. CDK Inhibitors: from the bench to clinical trials. Curr Drug Targets 2010;11:279-90
   PubMed Web of Science ®Google Scholar
• Cirillo D, Pentimalli F, Giordano A. Peptides or small molecules? Different approaches to develop more effective CDK inhibitors. Curr Med Chem 2011;18:1-13
   PubMedGoogle Scholar
• Adams PD, Sellers WR, Sharma SK, et al. Identification of a cyclin-cdk2 recognition motif present in substrates and p21-Like cyclin-dependent kinase inhibitors. Mol Cell Biol 1996;16:6623-33
   PubMed Web of Science ®Google Scholar
• Canela N, Orzaez M, Fucho R, et al. Identification of an hexapeptide that binds to a surface pocket in cyclin a and inhibits the catalytic activity of the complex cyclin-dependent kinase 2-cyclin A. J Biol Chem 2006;281:35942-53
   PubMed Web of Science ®Google Scholar
• Vadivelan S, Sinha BN, Irudayam SJ, et al. Virtual Screening Studies to Design Potent CDK2-Cyclin A Inhibitors. J Chem Inf Model 2007;47:1526-35
   PubMed Web of Science ®Google Scholar
• Knockaert M, Greengard P, Meijer L. Pharmacological inhibitors of cyclin-dependent kinases. Trends Pharmacol Sci 2002;23:417-25
   PubMed Web of Science ®Google Scholar
• Russo AA, Jeffrey PD, Pavletich NP. Structural basis of cyclin-dependent kinase activation by phosphorylation. Nat Struct Biol 1996;3:696-700
   PubMedGoogle Scholar
• Lo Conte L, Chothia C, Janin J. The atomic structure of protein–protein recognition sites. J Mol Biol 1999;285:2177-98
   PubMed Web of Science ®Google Scholar
• Bogan AA, Thorn KS. Anatomy of hot spots in protein interfaces. J Mol Biol 1998;280:1-9
   PubMed Web of Science ®Google Scholar
• Tsai CJ, Lin SL, Wolfson HJ, et al. Protein–protein interfaces: architectures and interactions in protein–protein interfaces and in protein cores. Their similarities and differences. Crit Rev Biochem Mol Biol 1996;1:127-52
   Google Scholar
• Stites WE. Protein–protein interactions: interface structure, binding thermodynamics, and mutational analysis. Chem Rev 1997;97:1233-50
   PubMed Web of Science ®Google Scholar
• Arkin MR, Wells JA. Small-molecule inhibitors of protein-protein interactions: processing towards the dream. Nat Rev Drug Discov 2004;3:301-17
   PubMed Web of Science ®Google Scholar
• Kubo A, Nakagawa K, Varma RK, et al. The p16 status of tumor cell lines identifies small molecule inhibitors specific for cyclin-dependent kinase 4. Clin Cancer Res 1999;5:4279-86
   PubMed Web of Science ®Google Scholar
• Diccianni MB, Yu J, Meppelink G, et al. 3-amino thioacridone inhibits DNA synthesis and induce DNA damage in T-cell acute lymphoblastic leukemia (T-ALL) in a p16-dependent manner. J Exp Ther Oncol 2004;4:223-37
   PubMedGoogle Scholar
• Diccianni MB, Batova A, Yu J, et al. Shortened survival after relapse in T-cell acute lymphoblastic leukemia patients with p16/p15 deletions. Leuk Res 1997;21:549-58
   PubMed Web of Science ®Google Scholar
• ` Verdaguer E, JordaEG, et al. 3-Amino thioacridone, a selective cyclin-dependent kinase 4 inhibitor, attenuates kainic acid-induced apoptosis in neurons. Neuroscience 2003;120:599-603
   PubMed Web of Science ®Google Scholar
• Moshinsky DJ, Bellamacina CR, Boisvert DC, et al. SU9516: biochemical analysis of cdk inhibition and crystal structure in complex with cdk2. Biochem Biophys Res Commun 2003;310:1026-31
   PubMed Web of Science ®Google Scholar
• Uchiyama H, Sowa Y, Wakada M, et al. Cyclin-dependent kinase inhibitor SU9516 enhances sensitivity to methotrexate in human T-cell leukemia Jurkat cells. Cancer Sci 2010;101:728-34
   PubMed Web of Science ®Google Scholar
• D'Assoro AB, Busby R, Acu ID, et al. Impaired p53 function leads to centrosome amplification, acquired ERα phenotypic heterogeneity and distant metastases in breast cancer MCF-7 xenografts. Oncogene 2008;27:3901-11
   PubMed Web of Science ®Google Scholar
• Takagi K, Sowa Y, Cevik OM, et al. CDK inhibitor enhances the sensitivity to 5-fluorouracil in colorectal cancer cells. Int J Oncol 2008;32:1105-10
   PubMed Web of Science ®Google Scholar
• Gao N, Kramer L, Rahmani M, et al. The three-substituted indolinone cyclin-dependent kinase 2 inhibitor 3-[1-(3H-imidazol-4-yl)-meth-(Z)-ylidene]-5-methoxy-1,3-dihydro-indol-2-one (SU9516) kills human leukemia cells via down-regulation of Mcl-1 through a transcriptional mechanism. Mol Pharmacol 2006;70:645-55
   PubMed Web of Science ®Google Scholar
• Lane ME, Yu B, Rice A, et al. A novel cdk2-selective inhibitor, SU9516, induces apoptosis in colon carcinoma cells. Cancer Res 2001;61:6170-7
   PubMed Web of Science ®Google Scholar
• Lo M, Ngo R, Dai K, et al. Development of a time-resolved fluorescence resonance energy transfer assay for cyclin-dependent kinase 4 and identification of its ATP-noncompetitive inhibitors. Anal Biochem 2012;421:368-77
   PubMed Web of Science ®Google Scholar
• Ohren JF, Chen H, Pavlovsky A, et al. Structures of human MAP kinase kinase 1 (MEK1) and MEK2 describe novel noncompetitive kinase inhibition. Nat Struct Mol Biol 2004;12:1192-7
   Google Scholar
• Amgen. Preparation of pyrimidinecarboxamides, pyrimidinylcarbamates and related compounds as inhibitors of T cell activation for the treatment of inflammatory diseases. US7504396; 2009
   Google Scholar
• Amgen. Preparation of pyrimidinecarboxamides, pyrimidinylcarbamates and related compounds as inhibitors of T cell activation for the treatment of inflammatory diseases. WO2005009443; 2005
   Google Scholar
• Amgen. Preparation of 2-aminopyrimidines and 2-aminopyridine-4-carbamates for use in the treatment of autoimmune diseases. WO2005009978; 2005
   Google Scholar
• Amgen. Preparation of 2-aminopyrimidine-4-carbamates as inhibitors of Lck kinase enzyme. US7442698; 2008
   Google Scholar
• Lipinski CA, Lombardo F, Dominy BW, et al. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv Drug Deliv Rev 1997;23:3-25
   Web of Science ®Google Scholar
• Orzaez M, Guevara T, Sancho M, et al. Intrinsic caspase-8 activation mediates sensitization of erlotinib-resistant tumor cells to erlotinib/cell-cycle inhibitors combination treatment. Cell Death Discov 2012;3:e415
   PubMedGoogle Scholar
• Giordano A, Bellacchio E, Bagella L, et al. Interaction between the Cdk2/cyclin a complex and a small molecule derived from the pRb2/p130 spacer domain. Cell Cycle 2007;6:2591-3
   PubMed Web of Science ®Google Scholar
• Bagella L, Sun A, Tonini T, et al. A small molecule based on the pRb2/p130 spacer domain leads to inhibition of cdk2 activity, cell cycle arrest and tumor growth reduction in vivo. Oncogene 2007;26:1829-39
   Google Scholar
• Gondeau C, Gerbal-Chaloin S, Bello P, et al. Design of a novel class of peptide inhibitors of cyclin-dependent kinase/cyclin activation. J Biol Chem 2005;14:13793-800
   Google Scholar
• Morris CM, Gondeau C, Tainer JA, Divita G. Kinetic mechanism of activation of the Cdk2/Cyclin A complex. J Biol Chem 2002;277:23847-53
   PubMed Web of Science ®Google Scholar
• Liu S, Bolger JK, Kirkland LO, et al. Structural and functional analysis of cyclin D1 reveals p27 and substrate inhibitor binding requirements. ACS Chem Biol 2010;12:1169-82
   Google Scholar
• Zheleva DI, McInnes C, Gavine AL, et al. Highly potent p21WAF1 derived peptide inhibitors of CDK-mediated pRb phosphorylation: delineation and structural insight into their interactions with cyclin A. J Peptide Res 2002;60:257-70
   PubMedGoogle Scholar
• Ball KL, Lain S, Fahraeus R, et al. Cell-cycle arrest and inhibition of Cdk4 activity by small peptides based on the carboxy-terminal domain of p21WAF. Curr Biol 1996;7:71-80
   Web of Science ®Google Scholar
• Pazos E, Perez M, Gutierrez-de-Teran H, et al. Rational design of a cyclin A fluorescent peptide sensor. Org Biomol Chem 2011;9:7629-32
   PubMed Web of Science ®Google Scholar
• Andrews MJI, McInnes C, Kontopidis G. Design, synthesis, biological activity and structural analysis of cyclic peptide inhibitors targeting the substrate recruitment site of cyclin-dependent kinase complexes. Org Biomol Chem 2004;2:2735-41
   PubMed Web of Science ®Google Scholar
• Takeda DY, Wohlschlegel JA, Dutta A. A bipartite substrate recognition motif for cyclin-dependent kinases. J Biol Chem 2001;276:1993-7
   PubMedGoogle Scholar