Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Having -c- – wherein x is chalcogen – bonded directly to...
Reexamination Certificate
2011-06-28
2011-06-28
Hui, San-ming (Department: 1628)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Having -c-, wherein x is chalcogen, bonded directly to...
C546S078000
Reexamination Certificate
active
07968561
ABSTRACT:
There is provided a compound having Formula Iwherein G is a fluorocarbyl group, and wherein R1is any one of a sulphamate group, a phosphonate group, a thiophosphonate group, a sulphonate group or a sulphonamide group.
REFERENCES:
patent: 7276513 (2007-10-01), Potter et al.
patent: WO 91/13083 (1991-09-01), None
patent: WO 93/05063 (1993-03-01), None
patent: WO 96/15257 (1996-05-01), None
patent: WO 98/05635 (1998-02-01), None
patent: WO 98/07859 (1998-02-01), None
patent: WO 98/09985 (1998-03-01), None
patent: WO 99/52890 (1999-10-01), None
patent: WO 02/32409 (2002-04-01), None
patent: WO 03/033518 (2003-04-01), None
Yale HL, “The Trifluoromethyl Group in Medicinal Chemistry,” Journal of Medicinal and Pharmaceutical Chemistry, 1959, 1(2), 5-11.
Wakefield B, “Fluorinated pharmaceuticals,” Innovations in Pharmaceutical Technology, Jan. 2000, 74-77.
Delphine S. Fischer, et al., D-Ring Modified Estrone Derivatives As Novel Potent Inhibitors of Steroid Sulfatase, Bioorganic & Medicinal Chemistry (2003) vol. 11, p. 1685-1700.
Jerzy Adamski, et al., Molecular Cloning of a Novel Widely Expressed Human 80 kDA 17β-hydroxysteroid Dehydrogenase IV, Biochem. J. (1995) vol. 311, p. 437-443.
D. Agnusdei, et al., Results of International Clinical Trials With Raloxifen, Annales d'Endocrinologie (1999) vol. 60, p. 242-246.
Rolf Appel, et al., Hydrazinesulfonic Acid Amide, Chemische Berichte (1958) vol. 91, p. 1339-1341.
Marion M. Bradford, A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding, Analytical Biochemistry (1976) vol. 72, p. 248-254.
Rock Breton, et al., The Structure of a Complex of Human 17β-Hydroxysteroid Dehydrogenase With Estradiol and NADP+Identifies Two Principal Targets for the Design of Inhibitors, Structure (1996) vol. 4, No. 8, p. 905-915.
M. Castiglione-Gertsch, New Aromatase Inhibitors: More Selectivity, Less Toxicity, Unfortunately, The Same Activity, European Journal of Cancer (1996) vol. 32A, No. 3, p. 393-395.
A. Claussner, et al., 11β-Amidoallcyl Estradiols, A New Series of Pure Antiestrogens, J. Steroid Biochem. Molec. Biol. (1992) vol. 41, No. 3-8, p. 609-614.
N.G. Coldham, et al., A Possible Mechanism for Increased Breast Cell Proliferation by Progestins Through Increased Reductive 17β-Hydroxysteroid Dehydrogenase Activity, Int. J. Cancer (1990) vol. 45, p. 174-178.
Bridgette M. Collins, et al., The Estrogenic and Antiestrogenic Activities of Phytochemicals With the Human Estrogen Receptor Expressed in Yeast, Steroids (1997) vol. 62, p. 365-372.
L. Duncan, et al., Inhibition of Estrone Sulfatase Activity by Estrone-3-Methylthiophosphonate: A Potential Therapeutic Agent in Breast Cancer, J. Cancer Research (1993) vol. 53, p. 298-303.
Wayne M. Geissler, et al., Male Pseudohermaphroditism Caused by Mutations of Testicular 17β-Hydroxysteroid Dehydrogenase 3, Nature Generics (1994) vol. 7, p. 34-39.
Debashis Ghosh, et al., Structure of Human Estrogenic 17β-Hydroxysteroid Dehydrogenase at 2.20 Resolution, Structure (1995) vol. 3, p. 503-513.
Jack Gorski, et al., Current Models of Steroid Hormone Action: A Critique, Annu. Rev. Physiol. (1976) vol. 38, p. 425-450.
Jack Gorski, et al., Hormone Receptors: Studies on the Interaction of Estrogen With the Uterus1, Recent Progress in Hormone Research (1967) vol. 24, p. 45-80.
Ranju Gupta, et al., Synthesis and Biological Activity of Some D-Ring Modified Estrone Derivatives, Indian Journal of Chemistry (1999) vol. 38B, p. 563-571.
J. Heer, et al., Steroids XL. Marrianolic and Diosynolic Acids. Estrogenic Carboxylic Acids II, Helvetica Chemica Acta (1945) vol. 28, p. 156-65.
K. Holli, et al., Lumpectomy With or Without Postoperative Radiotherapy for Breast Cancer With Favourable Prognostic Features: Results of a Randomized Study, British Journal of Cancer (2001) vol. 84, No. 2, p. 164-169.
Charles A. Horiuchi, et al., Novel regioslective Iodination of Estradiol, Estriol, and Estrone Using Iodine-Copper (II) Acetate, J. Chem. Soc. Chem. Commun. (1982) p. 671-672.
Kathryn B. Horowitz, et al., Nuclear Mechanisms of Estrogen Action, The Journal of Biological Chemistry (1978) vol. 253, No. 22, p. 8185-8193.
Kathryn B. Horowitz, et al., Estrogen Control of Progestrone Receptor in Human Breast Cancer: Role of Estradiol and Antiestrogen*, Endocrinology (1978) vol. 103, p. 1742-1751.
Jiu-Zhen Jin, et al., Human Estrogenic 17β-Hydroxysteroid Dehydrogenase: Predominance of Estrone Reduction and Its Induction by NADPH, Biochemical and Biophysical Research Communications (1999) vol. 259, p. 489-493.
V. Craig Jordan, The Strategic Use of Antiestrogens to Control the Development and Growth of Breast Cancer, Cancer (1992) vol. 70, p. 977-982.
Fernand Labrie, At the Cutting Edge Intracrinology, Molecular and Cellular Endocrinology (1991) vol. 78, p. C113-C118.
J.C. Le Bail, et al., Aromatase and 17β-Hydroxysteroid Dehydrogenase Inhibition by Flavonoids, Cancer Letters (1998) vol. 133, p. 101-106.
Isabelle Le Roy, et al., Genetic Correlation Between Steroid Sulfatase Concentration and Initiation of Attack Behavior in Mice1, Behavior Genetics (1999) vol. 29, No. 2, p. 131-136.
Pui-Kai Li, et al., Development of Potent Non-Estrogenic Estrone Sulfatase Inhibitors, Steroids (1998) vol. 63, p. 425-432.
Lodish, et al., Cell Division and the Cell Cycle, Molecular Cell Biology (1995) 3rdEdition, p. 177-181.
Bernard Loev, et al., Alkenylphenols Related to the Poison Ivy Principle. An Improved Method of Synthesis Involving the Na-Butanol Cleavage of Benzyl Ethers, J. Am Chem. Soc. (1956) vol. 78, No. 23, p. 6095-6098.
J. H. MacIndoe, et al., The Hydrolysis of Estrone Sulfate and Dehydroepiandrosterone Sulfate by MCF-7 Human Breast Cancer Cells*, Endocrinology (1988) vol. 123, p. 1281-1287.
Mitsuteru Numazawa, et al., Efficient Synthesis of 2-Methoxy- and 4-Methoxy-Estrogens, J. Chem. Soc. Chem. Commun. (1983) p. 533-534.
Makoto Okada, et al., Efficient General Method for Sulfamoylation of a Hydroxyl Group, Tetrahedron Letters (2000) vol. 41, p. 7047-7051.
Philip C. Bulman Page., et al., Efficient Regioselective A-Ring Functionalization of Oestrogens, Tetrahedron (1990) vol. 46, No. 6, p. 2059-2068.
H. Peltoketo, et al., Complete Amino Acid Sequence of Human Placental 17β-Hydroxysteroid Dehydrogenase Deduced From cDNA, FEBS Letters (1988) vol. 239, No. 1, p. 73-77.
H. Peltoketo, et al., 17β-Hydroxysteroid Dehydrogenase (HSD)/17-Kesosteroid Reductase (KSR) Family; Nomenclature and Main Characteristics of the 17HSD/KSR Enzymes, Journal of Molecular Endocrinology (1999) vol. 23, p. 1-11.
Trevor M. Penning, et al., Molecular Endocrinology of Hydroxysteroid Dehydrogenases*, Endocrine Reviews (1997) vol. 18, No. 3, p. 281-305.
Atul Purohit, et al., The Effect of 2-Methoxyoestrone-3-O-Sulphamate on the Growth of Breast Cancer Cells and Induced Mammary Tumours, Int. J. Cancer (2000) vol. 85, p. 584-589.
Atul Purohit, et al., In Vivo Inhibition of Oestrone Sulphatase and Dehydroepiandrosterone Sulphatase by Oestrone-3-O-Sulphamate, Int. J. Cancer (1995) vol. 63, p. 106-111.
Atul Purohit, et al., Inactivation of Steroid Sulfatase by an Active Site-Directed Inhibitor, Estrone-3-O-Sulfamate, Biochemistry (1995) vol. 34, p. 11508-11514.
Atul Purohit, et al., In Vivo Activity of 4-Methylcoumarin-7-O-Sulfamate, A Nonsteroidal, Nonestrogenic Steroid Sulfatase Inhitbitor, Cancer Research (1996) vol. 56, p. 4950-4955.
Atul Purohit, et al., In Vivo Inhibition of Estrone Sulfatase Activity and Growth of Nitrosomethylurea-induced Mammary Tumors by 667 COUMATE1, Cancer Research (2000) vol. 60, p. 3394-3396.
Atul Purohit, et al., Oestrogen Sulphatase Activity in Hormone-Dependent and Hormone-Independent Breast-Cancer Cells: Modulation by Steroidal and Non-Steroidal Therapeutic Agents, Int. J. Cancer (1992) vol. 50, p. 901-905.
Richard Poulin, et al., Stimulation of Cell Proliferation and Estrogenic Response by Adrenal C19-Δ5-Steroids in the ZR-75-1 Human Breast Cancer Cell Line', Cancer Research (1986) v
Foster Paul
Lloyd Potter Barry Victor
Purohit Atul
Reed Michael John
Woo Lok Wai Lawrence
Frommer & Lawrence & Haug LLP
Garman Russell A.
Hui San-ming
Kuzmich Sandra
Sterix Limited
LandOfFree
Steroidal compounds as steroid sulphatase inhibitors does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Steroidal compounds as steroid sulphatase inhibitors, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Steroidal compounds as steroid sulphatase inhibitors will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-2689865