Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...
Reexamination Certificate
2003-08-17
2008-11-25
Carlson, Karen Cochrane (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...
Reexamination Certificate
active
07455989
ABSTRACT:
A polynucleotide encoding a chimeric polypeptide is provided. The chimeric polypeptide includes (a) a first polypeptide region being capable of specifically binding at least one detectable molecule; and (b) a second polypeptide region being capable of specifically binding a biological component or macromolecule or targeting a cellular compartment. Methods utilizing the polynucleotide or the chimeric polypeptide for highlighting a cell compartment, a biological component or macromolecule are also provided.
REFERENCES:
patent: 2002/0025536 (2002-02-01), Gyuris et al.
patent: WO 91/17271 (1991-11-01), None
patent: WO 92/01047 (1992-01-01), None
patent: WO 92/09690 (1992-06-01), None
patent: WO 92/15679 (1992-09-01), None
patent: WO 92/18619 (1992-10-01), None
patent: WO 92/20791 (1992-11-01), None
patent: WO 93/01288 (1993-01-01), None
patent: WO 97/08553 (1997-06-01), None
Prufer et al. 2000; Dimerization with retinoid X receptors promotes nuclear localization and subnuclear targeting of vitamin D receptors. J. Biol. Chem. 275 (52): 41114-41123.
Day et al. Sep. 2001; Fluorescence resonance energy transfer microscopy of localized protein interactions in the living cell nucleus. Methods 25: 4-18.
Xu et al. 1998; A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins. Proc Natl Acad Sci U S A. Jan. 5, 1999; 96(1): 151-156.
Furusawa Makoto et al. “AMY-1, A C-Myc-Binding Protein, Is Localized in the Mitochondria of Sperm by Association With S-AKAP84, An Anchor Protein of cAMP-Dependent Protein Kinase”, The Journal of Biological Chemistry, 276(39):36647-36651, 2001.
Alam et al. “Germ Line Transmission and Expression of A LacZ Containing Transgene in Tilapia (Oreochromis Niloticus)”, Transgenic Research, 5: 87-95, 1996.
Jockusch et al. “The Molecular Architecture of Focal Adhesions”, Annual Reviews of Cell Development Biology, 11: 379-416, 1995.
Janmey “Phosphoinositides and Calcium as Regulators of Cellular Actin Assembly and Disassembly”, Annual Reviews of Physiology, 56: 169-191, 1994.
Barras III “Assembly of Combinatorial Antibody Libraries on Phage Surfaces: The Gene III Site”, Proc. Natl. Acad. Sci. USA, 88: 7978-7982, 1991.
Bilang et al. “The 3'-Terminal Region of the Hygromycin-B-Resistance Gene Is Important for Its Activity inEscherichia coliandNicotiana tabacum”, Gene, 100: 247-250, 1991.
Brinkly “A Brief Survey of Methods for Preparing Protein Conjugates With Dyes, Haptens, and Cross-Linking Reagents”, Bioconjugate Chemistry, 3: 2-13, 1992.
Brousseau et al. “Hyperalphalipoproteinemia in Human Lecithin Cholesterol Acyltransferase Transgenic Rabbits”, The Journal of Clinical Investigation, 97(8): 1844-1851, 1996.
Geiger et al. “The Cytoplasmic Domain of Adherens-Type Junctions”, Cell Motility and the Cytoskeleton, 20: 1-6, 1991.
Clackson et al. “Making Antibody Fragments Using Phage Display Libraries”, Nature, 352: 624-628, 1991.
Cozzi et al. “Longitudinal Analysis of the Expression of Human Decay Accelerating Factor (HDAF) on Lymphocytes, in the Plasma, and in the Skin Biopsies of Transgeinc Pigs”, Xenotransplantation, 3: 128-133, 1996.
Tsukita et al. “Molecular Linkage Between Cadherins and Actin Filaments in Cell-Cell Adherens Junctions”, Current Opinion in Cell Biology, 4: 834-839, 1992.
Damak et al. “Improved Wool Production in Transgenic Sheep Expressing Insulin-Like Growth Factor 1”, Bio/Technology, 14: 185-188, 1996.
Danon et al. “Light Regulated Translational Activators: Identification of Chloroplast Gene Specific mRNA Binding Proteins”, The EMBO Journal, 10(13): 3993-4001, 1991.
De Block et al. “Transformation ofBrassica napusandBrassica oleraceaUsingAgrobacterium tumefaciensand the Expression of the Bar and Neo Genes in the Transgenic Plants”, Plant Physiology, 91: 694-701, 1989.
Deng et al. “Selection of Antibody Single-Chain Variable Fragments With Improved Carbohydrate Binding by Phage Display”, The Journal of Biological Chemistry, 269(13): 9533-9538, 1994.
Dower “Electroporation of Bacteria: A General Approach to Genetic Transformation”, Genetic Engineering, Principles and Methods, 12: 275-296, 1990.
Duncker et al. “Expression of A Cystine-Rich Fish Antifreeze in Transgenic Drosophila Melanogaster”, Transgenic Research, 5: 49-55, 1996.
Duncker et al. “Antifreeze Protein Does Not Confer Cold Tolerance to Transgenic Drosophila Melanogaster”, Cryobiology, 32: 521-527, 1995.
Dziadek “Transgenic Animals: How They Are Made and Their Role in Animal Production and Research”, Australian Veterinary Journal, 73(5): 182-187, 1996.
Faux et al. “Molecular Glue: Kinase Anchoring and Scaffold Proteins”, Cell, 85: 9-12, 1996.
Fuchs et al. “Targeting Recombinant Antibodies to the Surface ofEscherichia coli: Fusion to A Peptidoglycan Associated Lipoprotein”, Bio/Technology, 9: 1370-1372, 1991.
Garrard et al. “Fab Assembly and Enrichment in A Monovalent Phage Display System”, Bio/Technology, 9: 1373-1377, 1991.
Garrard et al. “Selection of An Anti-IGF-1 Fab From A Fab Phage Library Created by Mutagenesis of Multiple CDR Loops”, Gene, 128: 103-109, 1993.
Glatz et al. “Cellular Fatty Acid-Binding Proteins: Their Function and Physiological Significance”, Progressive Lipid Research, 35(3): 243-282, 1996.
Gram et al “In Vitro Selection and Affinity Maturation of Antibodies From A Naive Combinatorial Immunoglobulin Library”, Proc. Natl. Acad. Sci. USA, 89: 3576-3580, 1992.
Griffiths et al. “Human Anti-Self Antibodies With High Specificity From Phage Display Libraries”, The EMBO Journal, 12(2): 725-734, 1993.
Guerche et al. “Direct Gene Transfer by Electroporation inBrassica napus”, Plant Science, 52: 111-116, 1987.
Hanahan et al. “Plasmid Transformation ofEscherichia coliand Other Bacteria”, Methods in Enzymology, 204: 63-113, 1991.
Hawkins et al. “Selection of Phage Antibodies by Binding Affinity. Mimicking Affinity Maturation”, Journal of Molecular Biology, 226: 889-896, 1992.
Hawkins et al. “The Contribution of Contact and Non-Contact Residues of Antibody in the Affinity of Binding to Antigen. The Interaction of Mutant D1.3 Antibodies With Lysozyme”, Journal of Molecular Biology, 234: 958-964, 1993.
Hay et al. “Bacteriophage Cloning andEscherichia coliExpression of A Human IgM Fab”, Human Antibody Hybridomas, 3: 81-85, 1992.
Hoogenboom et al. “Multi-Subunit Proteins on the Surface of Filamentous Phage: Methodologies for Displaying Antibody (Fab) Heavy and Light Chains”, Nucleic Acids Research, 19(15): 4133-4137, 1991.
Horsch et al. “A Simple and General Method for Transferring Genes Into Plants”, Science, 277: 1229-1231, 1985.
Howell et al. “Cloned Cauliflower Mosaic Virus DNA Infects Turnips (Brassica rapa)”, Science, 208: 1265-1267, 1980.
Huse et al. “Generation of A Large Combinatorial Library of the Immunoglobulin Repertoire in Phage Lambda”, Science, 246(4935): 1275-1281, 1989.
Knudsen et al. “Interction of α-Actinin With the Cadherin/Catenin Cell-Cell Adhesion Complex Via α-Catenin”, The Journal of Cell Biology, 130(1): 67-77, 1995.
Itoh et al. “Involvement of ZO-1 in Cadherin-Based Cell Adhesion Through Its Direct Binding to a Catenin and Actin Filaments”, The Journal of Cell Biology, 138(1): 181-192, 1997.
Kang et al. “Linkage of Recognition and Replication Functions by Assembling Combinatorial Antibody Fab Libraries Along Phage Surfaces”, Proc. Natl. Acad. Sci. USA, 88: 4363-4366, 1991.
Keller et al. “In Vivo Particle-Mediated Cytokine Gene Transfer Into Canine Oral Mucosa and Epidermis”, Cancer Gene Therapy, 3(3): 186-191, 1996.
Kim et al. “Neuron-Spe
Carlson Karen Cochrane
Yeda Research and Development Co. Ltd.
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