Activatable recombinant neurotoxins

Details Activatable recombinant neurotoxins Activatable recombinant neurotoxins

2006-11-07

2006-11-07

Bugaisky, Gabriele (Department: 1656)

Chemistry: molecular biology and microbiology

Micro-organism, tissue cell culture or enzyme using process...

Recombinant dna technique included in method of making a...

C435S069700, C435S212000, C435S220000, C435S252300, C435S320100, C536S023200

Reexamination Certificate

active

07132259

ABSTRACT:
The invention provides, in part, compositions comprising activatable recombinant neurotoxins and polypeptides derived therefrom. The invention also provides, in part, nucleic acid molecules encoding such polypeptides, and methods of making such polypeptides and nucleic acid molecules.

REFERENCES:
patent: 4683202 (1987-07-01), Mullis
patent: 4800159 (1989-01-01), Mullis
patent: 5919665 (1999-07-01), Williams
patent: 5989545 (1999-11-01), Foster et al.
patent: 6461617 (2002-10-01), Shone et al.
patent: 6962703 (2005-11-01), Foster et al.
patent: WO 95/32738 (1995-12-01), None
patent: WO 96/33273 (1996-10-01), None
patent: WO 98/07864 (1998-02-01), None
patent: WO 98/08540 (1998-03-01), None
patent: WO 99/17806 (1999-04-01), None
patent: WO 99/55359 (1999-11-01), None
Borodic et al, “Pharmacology and Histology of the Therapeutic Application of Botulinum Toxin Application of Botulinum Toxins”, pp. 119-157 (1994).
Tonello et al, “Tetanus and Botulinum Neurotoxins a Novel Group of Zinc-Endopeptidases”, Intracellular Protein Catabolism, Adv. Exp. Med. & Biol. 389, pp. 251-260 (1996).
Coffield et al, The Site and Mechanism of Action of Botulinum Neurotoxin in Therapy with Botulinum Toxin, pp. 3-13 (1994).
Dolly et al, “Probing the process of transmitter release with botulinum and tetanus neurotoxins” Seminars in Neuroscience, 6 (3): pp. 149-158 (1994).
Foran et al, “Botulinum Neurotoxin C1 Cleaves both Syntaxin and SNAP-25 in Intact and Permeabilized Chromaffin Cells: Correlation with Its Blockade of Catecholamine Release”, Biochem. 35: pp. 2630-2636 (1996).
Li et al, “A Single Mutation in the Recombinant Light Chain of Tetanus Toxin Abolishes Its Proteolytic Activity and Removes the Toxicity Seen After Reconstitution with Native Heavy Chain”, Biochemistry 33, No. 22: pp. 7014-7020 (1994).
Zhou et al, “Expression and Purification of the Light Chain of Botulinum Neurotoxin A: A Single Mutation Abolishes Its Cleavage of SNAP-25 and Neurotoxicity after Reconstruction with the Heavy Chain”, Biochemistry 34: pp. 15175-15181 (1995).
Lacy et al, “Crystal structure of botulinum neurotoxin type A and implications for toxicity” Nature Struct. Biol. Oct.; 5(10): pp. 898-902 (1998).
Kurazono et al, “Minimal Essential Domains Specifying Toxicity of the Light Cahins of Tetanus Toxin and Botulinum Neurotoxin Type A”, J. Biol. Chem.: pp. 14721-14729 (1992).
Hutchinson et al, “Mutagenesis at a Specific Position in a DNA Sequence”,J. Biol. Chem. 253: No. 18, Sep. 25 issue, pp. 6651-6560 (1978).
Li et al, “Expression and Characterisation of the Heavy Chain of Tetanus Toxin: Reconstitution of the Fully-Recombinant Dichain Protein in Active Form”, J. Biochem. 125: pp. 1200-1208 (1999).

Affiliated with

Also associated with

Rating

Activatable recombinant neurotoxins does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Activatable recombinant neurotoxins, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Activatable recombinant neurotoxins will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-3623750