Methods of modulating tubulin deacetylast activity

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Carbohydrate doai

Reexamination Certificate

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C514S220000, C514S230500, C435S183000, C435S375000, C435S018000, C435S019000, C435S007100

Reexamination Certificate

active

07884081

ABSTRACT:
The present invention provides methods for identifying agents that modulate a level or an activity of tubulin deacetylase polypeptide, as well as agents identified by the methods. The invention further provides methods of modulating tubulin deacetylase activity in a cell. The invention further provides methods of modulating cellular proliferation by modulating the activity of tubulin deacetylase.

REFERENCES:
patent: WO 89/06132 (1989-07-01), None
patent: WO 03/004621 (2003-01-01), None
patent: WO 03/046207 (2003-06-01), None
Finnin et al. Structure of the histone deacetylase SIRT2. Nature Structural Biology. 2001, vol. 8, pp. 621-625.
Frye, R.A. Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochemical and Biophysical Research Communications. 1999, vol. 260, pp. 273-279.
Grozinger, et al. Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deactylases by phenotypic screening. Journal of Biological Chemistry. 2001, vol. 276, No. 42, pp. 38837-38843.
Landry et al. Role of NAD(+) in the deacetylase activity of the SIR2-like proteins. Biochemical and Biophysical Research Communications. 2000, vol. 278, pp. 685-690.
Ledizet et al. Identification of an acetylation site of Chlamydomonas alpha-tubulin. Proc Natl Acad Sci USA. 1987, vol. 84, No. 16, pp. 5720-5724.
Li, Q., et al. Discovery and developments of antimitotic agents that inhibit tubulin polymerization for the treatment of cancer. Expert Opinion on Therapeutic Patents, Ashely Publications, GB, vol. 12, No. 11, Nov. 1, 2002, pp. 1663-1702.
Macrae, T. Tubulin post-translational modifications—enzymes and their mechanisms of action. European Journal of Biochemistry. 1997, vol. 244, pp. 265-278.
Maruta, H., et al. The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules. Journal of Cell Biology. 1986, vol. 103, No. 2, pp. 571-579.
North, B., et al. The human Sir2 ortholog, SIRT2, is an NAD+- dependent tubulin deacetylase. Molecular Cell. 2003, vol. 11, No. 2, pp. 437-444.
Tanner et al. Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose. Proc Natl Acad Sci USA. 2000, vol. 97, pp. 14178-14182.
Smith et al. A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family. Proc Natl Acad Sci USA. 2000, vol. 97, pp. 6658-6663.

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