Chemistry: molecular biology and microbiology – Animal cell – per se ; composition thereof; process of... – Animal cell – per se – expressing immunoglobulin – antibody – or...
Reexamination Certificate
2006-03-28
2006-03-28
Turner, Sharon (Department: 1649)
Chemistry: molecular biology and microbiology
Animal cell, per se ; composition thereof; process of...
Animal cell, per se, expressing immunoglobulin, antibody, or...
C530S300000
Reexamination Certificate
active
07018839
ABSTRACT:
The acetylcholinesterase 14-mer peptide AEFHRWSSYMVHWK acts alone or in synergism with2-amyloid to contribute to neuronal degeneration, e.g. in Parkinson's and Alzheimer's diseases, perhaps by exerting calcium channel opening activity. Antibodies and other compounds which inhibit the biological activity are useful for prophylaxis or treatment.
REFERENCES:
patent: 5932780 (1999-08-01), Soreq et al.
patent: 0 288 243 (1988-10-01), None
de Serres et al., Cellular and Molecular Neurobiology, 13(3):279-87, 1993.
Moran et al., Acta Neuropatthologica 85(4):362-9, 1993.
Skolnick et al., Trends in Biotech 18(1):34-39, 2000.
Dagerlind et al., 62(1):217-39, 1994.
S. Bon et al., “Identical N-terminal peptide sequences of asymmetric forms and of low-salt-Soluble and detergent-soluble amphiphilic dimers of Torpedo acetylcholinesterase”. FEBS Letters, vol. 209, No. 2, Dec. 1986, pp. 206-212.
H.I. Ziltener et al., “Monoclonal antipeptide antibodies recognize IL-3 and neutralize its bioactivity in vivo”, Journal of Immunology, vol. 140, No. 4, Feb. 15, 1998, Baltimore US, pp. 1182-1187.
T.L. Leto et al., “Characterization of the calmodulin-binding site of nonerythroid α-spectrin”. The Journal of Biological Chemistry, vol. 264, No. 10, Apr. 5, 1989, MD US, pp. 5826-5830.
Chemical Abstracts, vol. 118, No. 23, Jun. 7, 1993, Columbus, Ohio, US, Abstract No. 227311, XP002035623 & J. Bacteriology, vol. 174, No. 13, 1992, pp. 4361-4373, J.P. Mueller et al., “Teranscriptional regulation ofBacillus subtilisglucose starvation-inducible genes; control of gsiA by the comP-comA transduction systems”.
Chemical Abstracts, vol. 121, No. 19, Nov. 7, 1994, Columbus, Ohio, US, Abstract No. 222683, XP002035624 & Neuroscience, vol. 62, No. 1, 1994, Oxford, pp. 217-239, A. Dagerlind et al., “Immunologically induced sympathectomy of preganglion nerves by antibodies against acetylcholinesterase: increased levels of peptides and their messenger RNAs in rat adrenal chromaffin cells”.
Chemical Abstracts, vol. 102, No. 25, Jun. 24, 1985, Columbus, Ohio, US; Abstract No. 217461, XP002035625 & J. Neurochem., vol. 44, No. 5, 1985, D.J. Marsh & J. Massoulie: “Proteolytic digestion patterns of soluble and detergent-soluble bovine caudate necleus acetylcholinesterases”.
S. Budavari et al., “The Merck Index”, 1996, Merck & Co., Whitehouse Station, New Jersey, USA XP002035622 408196.
Greenfield Susan Adele
Vaux David John Talbutt
Synaptica Limited
Turner Sharon
LandOfFree
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