Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Having -c- – wherein x is chalcogen – bonded directly to...
Reexamination Certificate
2011-06-07
2011-06-07
Saeed, Kamal A (Department: 1626)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Having -c-, wherein x is chalcogen, bonded directly to...
C514S398000, C548S195000, C548S332500
Reexamination Certificate
active
07956076
ABSTRACT:
Provided herein are novel compounds that inhibit ribonucleotide reductase (RR) by binding to RRM2 and interfering with the activity of the RRM1/RRM2 holoenzyme. These inhibitors may be used to inhibit RR activity and to treat various conditions associated with RRM2 expression, such as for example certain cancer types, mitochondrial diseases, or degenerative diseases.
REFERENCES:
Vippagunta et al., Crystalline solids, 2001, Advanced Drug Delivery Reviews, 48, pp. 3 and 18.
Wolff et al., Burger's Medicinal Chemistry and Drug Discovery, 1994, Wiley-Interscience, Fifth Edition, vol. I: Principles and Practice, pp. 975-977.
Angus, S. P., et al., “Retinoblastoma Tumor Suppressor Targets dNTP Metabolism to Regulate DNA Replication,” J. Biol. Chem. 277:44376-44384 (2002).
Berge, S. M., et al., “Pharmaceutical Salts,” J. Pharm. Sci. 66:1-19 (1977).
Chabes, A.L., et al., “S Phase-specific Transcription of the Mouse Ribonucleotide Reductase R2 Gene Requires Both a Proximal Repressive E2F-binding Site and an Upstream Promoter Activating Region,” J. Biol. Chem. 279:10796-10807 (2004).
Chang, C. H., et al., “Substrate Specificity of Human Ribonucleotide Reductase from Molt-4F Cells,” Cancer Res. 39:5081-5086 (1979).
Chen, S., et al., “Inhibition of Human Cancer Cell Growth by Inducible Expression of Human Ribonucleotide Reductase Antisense cDNA,” Antisense Nucleic Acid Drug Dev. 10:111-116 (2000).
Cooperman, B. S., et al., “A Comprehensive Model for the Allosteric Regulation of Class la Ribonucleotide Reductases,” Adv. Enzyme Regul. 43:167-182 (2003).
Cory, J. G., et al., “Regulation of Ribonucleotide Reductase Activity in Mammalian Cells,” Mol. Cell. Biochem. 53-54:257-266 (1983).
Currie, R.A., et al., “NF-Y Is Associated with the Histone Acetyltransferases GCN5 and P/CAF,” J. Biol. Chem. 273:1430-1434 (1998).
Elledge, S.J., et al., “Two Genes Differentially Regulated in the Cell Cycle and by DNA—Damaging Agents Encode Alternative Regulatory Subunits of Ribonucleotide Reductase,” Genes Dev. 4:740-751 (1990).
Fan, H., et al., “The R1 Component of Mammalian Ribonucleotide Reductase Has Malignancy—Suppressing Activity as Demonstrated By Gene Transfer Experiments,” Proc. Nat. Acad. Sci. USA 94:13181-13186 (1997).
Fan, H., et al., “The Mammalian Ribonucleotide Reductase R2 Component Cooperates with a Variety of Oncogenes in Mechanisms of Cellular Transformation,” Cancer Res. 58:1650-1653 (1998).
Filatov, D., et al., “Role of a Proximal NF-Y Binding Promoter Element in S Phase—Specific Expression of Mouse Ribonucleotide Reductase R2 Gene,” J. Biol. Chem. 270:25239-25243 (1995).
Goan, Y.G., et al., “Overexpression of Ribonucleotide Reductase as a Mechanism of Resistance to 2,2-Difluorodeoxycytidine in the Human KB Cancer Cell Line,” Cancer Res. 59:4204-4207 (1999).
Guittet, O., et al., “Mammalian p53R2 Protein Forms an Active Ribonucleotide Reductase in Vitro with the R1 Protein, Which Is Expressed Both in Resting Cells in Response to DNA Damage and in Proliferating Cells,” J. Biol. Chem. 276:40647-40651 (2001).
Huang, A., et al., “Ribonucleotide Reductase R2 Gene Expression and Changes in Drug Sensitivity and Genome Stability,” Cancer Res. 57:4876-4881 (1997).
Jordan, A., et al., “Ribonucleotide Reductases,” Annu. Rev. Biochem. 67:71-98 (1998).
Kimura, T., et al., “Impaired Function of p53R2 in Rrm2b-null Mice Causes Severe Renal Failure Through Attenuation of dNTP Pools,” Nat. Genet. 34:440-445 (2003).
Kuschak, T. I., et al., “The Ribonucleotide Reductase R2 Gene is a Non-Transcribed Target of c-Myc-Induced Genomic Instability,” Gene 238:351-365 (1999).
Lassmann, G., et al., “EPR Stopped-Flow Studies of the Reaction of the Tyrosyl Radical of Protein R2 from Ribonucleotide Reductase with Hydroxyurea,” Biochem. Biophys. Res. Commun. 188:879-887 (1992).
Le, N.T., et al., “The Role of Iron in Cell Cycle Progression and the Proliferation of Neoplastic Cells,” Biochim. Biophys. Acta 1603:31-46 (2002).
Liu, X., et al, “Nuclear Factor Y Regulation and Promoter Transactivation of Human Ribonucleotide Reductase Subunit M2 Gene in a Gemcitabine Resistant KB Clone,” Biochem. Pharmacol. 67:1499-1511 (2004).
Liu, X., et al., “The Ribonucleotide Reductase Subunit M2B Subcellular Localization and Functional Importance for DNA Replication in Physiological Growth of KB Cells,” Biochem. Pharmacol. 70:1288-1297 (2005).
Liu, X., et al., “Metastasis—Suppressing Potential of Ribonucleotide Reductase Small Subunit p53R2 in Human Cancer Cells,” Clin. Cancer Res. 12:6337-6344 (2006).
Lozano, G., et al., “p53 Sends Nucleotides to Repair DNA,” Nature 404:24-25 (2000).
Nakano, K., et al., “A Ribonucleotide Reductase Gene is a Transcriptional Target of p53 and p73,” Oncogene 19:4283-4289 (2000).
Nocentini, G., et al., “Ribonucleotide Reductase Inhibitors: New Strategies for Cancer Chemotherapy,” Crit. Rev. Oncol. Hematol. 22:89-126 (1996).
Nyholm, S., et al., “Reduction and Loss of the Iron Center in the Reaction of the Small Subunit of Mouse Ribonucleotide Reductase with Hydroxyurea,” Biochem. 32:11569-11574 (1993).
Ochiai, E.I., et al., “Tyrosyl Free Radical Formation in the Small Subunit of Mouse Ribonucleotide Reductase,” J. Biol. Chem. 265:15758-15761 (1990).
Shao, J., et al., “Determination of the Potency and Subunit-Selectivity of Ribonucleotide Reductase Inhibitors with a Recombinant-Holoenzyme-Based In Vitro Assay,” Biochem. Pharmacol. 69:627-634 (2005).
Tanaka, H., et al., “A Ribonucleotide Reductase Gene Involved in a p53—Dependent Cell-Cycle Checkpoint for DNA Damage,” Nature 404:42-49 (2000).
Thelander, L., et al., “Isolation and Characterization of Expressible cDNA Clones Encoding the M1 and M2 Subunits of Mouse Ribonucleotide Reductase,” Mol. Cell. Biol. 6:3433-3442 (1986).
Wright, J. A., et al., “Regulation and Drug Resistance Mechanisms of Mammalian Ribonucleotide Reductase, and the Significance of DNA Synthesis,” Biochem. Cell. Biol. 68:1364-1371 (1990).
Xue, L., et al., “Wild-Type p53 Regulates Human Ribonucleotide Reductase by Protein—Protein Interaction with p53R2 as well as hRRM2 Subunits,” Cancer Res. 63:980-986 (2003).
Yamaguchi, T., et al., “p53R2-Dependent Pathway for DNA Synthesis in a p53—Regulated Cell Cycle Checkpoint,” Cancer Res. 61:8256-8262 (2001).
Yen, Y., et al., “Characterization of a Hydroxyurea-Resistant Human KB Cell Line with Supersensitivity to 6-Thioguanine,” Cancer Res. 54:3686-3691 (1994).
Zhou, B.S., et al., “Overexpression of Ribonucleotide Redactase in Transfected Human KB Cells Increases Their Resistance to Hydroxyurea: M2 but not MI Is Sufficient to Increase Resistance to Hydroxyurea in Transfected Cells,” Cancer Res. 55:1328-1333 (1995).
Zhou, B.S., et al., “Overexpression of Transfected Human Ribonucleotide Reductase M2 Subunit in Human Cancer Cells Enhances Their Invasive Potential,” Clin. Exp. Metastasis 16:43-49 (1998).
Zhou, B.S., et al., “The Human Ribonucleotide Reductase Subunit hRRM2 Complements p53R2 in Response to UV-Induced DNA Repair in Cells with Mutant p53,” Cancer Res. 63:6583-6594 (2003).
Horne David
Perkins Harki Angela L
Su Leila
Yen Yun
Yuan Yate-Ching
Bianchi Kristin
City of Hope
Morris Patrick
Perkins Coie LLP
Saeed Kamal A
LandOfFree
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