Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Hormones – e.g. – prolactin – thymosin – growth factors – etc.
Reexamination Certificate
2006-08-22
2006-08-22
Carlson, Karen Cochrane (Department: 1653)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
Hormones, e.g., prolactin, thymosin, growth factors, etc.
C530S350000, C435S320100, C536S023100
Reexamination Certificate
active
07094884
ABSTRACT:
The present invention relates to the diagnosis of Alzheimer's Disease. It especially teaches the production of a soluble Aβ-chaperone complex and the advantageous use of such chaperone-Aβ complex, especially in the detection of Aβ in an immunoassay, as well as its use as an immunogen.
REFERENCES:
patent: 4735896 (1988-04-01), Wang et al.
patent: 4879212 (1989-11-01), Wang et al.
patent: 4945042 (1990-07-01), Geiger et al.
patent: 6207420 (2001-03-01), Harrison et al.
patent: 6316405 (2001-11-01), Rich et al.
patent: 597884 (1986-04-01), None
patent: 0 280 211 (1994-11-01), None
patent: 0 396 559 (1996-08-01), None
patent: 1 077 262 (2001-02-01), None
patent: WO 92/22573 (1992-12-01), None
patent: WO 93/21346 (1993-10-01), None
patent: WO 94/08012 (1994-04-01), None
patent: WO 98/13496 (1998-04-01), None
patent: WO/00/20606 (2000-04-01), None
patent: WO 00/26251 (2000-05-01), None
Bardwell, J.,Building Bridges: Disulphide Bond Formation in Cell, Molecular Microbiology (1994) 14(2), 199-205.
Bessinger, M., et al.,How Chaperones Fold Proteins, Biol. Chem., vol. 379, pp. 245-259, Mar. 1998.
Bothmann, H., et al.,The Periplasmic Escherichia coli Peptidylprolyl cis,trans-Isomerase FkpA, The Journal of Biological Chemistry, vol. 275, No. 22, Issue of Jun. 2, pp. 17100-17105, 2000.
Braden, B., et al.,Structural Features of the Reactions Between Antibodies and Protein Antigens, The FASEB Journal, pp. 9-16, vol. 9, Jan. 1995.
Buchner, J.,Supervising The Fold: Functional Principles of Molecular Chaperones, The FASEB Journal, pp. 10-19, vol. 10, Jan. 1996.
Butler, J.E., et al.,The Physical and Functional Behavior of Capture Antibodies Adsorbed on Polystyrene, Journal of Immunological Methods, 150 (1992), 77-90.
Caffrey, M., et al.,Biophysical Characterization of gp41 Aggregates Suggests a Model for the Molecular Mechanism of HIV-Associated Neurological Damage and Dementia, The Journal of Biological Chemist, vol. 275, No. 26, Issue of Jun. 30, pp. 19877-19882, 2000.
Chan, D., et al.,Core Structure of gp41 From The HIV Envelope Glycoprotein, Cell, vol., 89, 263-273, Apr. 18, 1997.
Crooke, E., et al., Trigger Factor:A Soluble Protein That Folds Pro-OmpA Into A Membrane-Assembly-Competent Form, Biochemistry, vol. 84, pp. 5216-5220, Aug. 1987.
Danese, P., et al.,The Cpx Two-Component Signal Transduction Pathway of Escherichia coli Regulates Transcription of the Gene Specifying the Stress-Inducible Periplasmic Protease, DegP, Genes & Development, pp. 387-398 (1995).
Dartigalongue, C., et al.,A New Heat-Shock Gene, ppiD, Encodes A Peptidyl-Prolyl Isomerase Required For Foling of Other Membrane Proteins in Escherichia Coli, The EMBO Journal, vol. 17, No. 14, pp. 3968-2980, 1998.
Dent, A., et al.,The Preparation of Protein—Protein Conjugates, Heterobifunctional Reagents Based on the Biotin-Avidin Interaction, Chapter 5, pp. 261-263.
Doms, R., et al., HIV-1 Membrane Fusion: Targets of Opportunity, The Journal of Cell Biology, pp. F9-F13, vol. 151, No. 2, Oct. 16, 2000.
Egan, D.A., et al.,Equilibruim Denaturation of Recombinant Human FK Binding Protein in Urea, Biochemistry, pp. 1920-1927, vol. 32, No. 8, 1993.
Ehrnsperger, Monika, et al.,Stabilization of Proteins and Peptides in Diagnostic Immunological Assays by the Molecular Chaperone Hsp25, Analytical Biochemistry 259 (1998), pp. 218-225.
Endrich, et al.,The V3 Loop of a Human Immunodeficiency Virus Type-1 Envelope Protein is a High-Affinity Ligand for Immunophilins Present in Human Blood, Eur. J. Biochem., 252-441-446 (1998).
Fischer, G.,Cyclophilin and Peptidyl-Prolyl Cis-Trans Isomerase are Probably Identical Proteins, Nature, vol. 337 Feb. 2, 1989.
Frech, C., et al.Preferential Binding of an Unfolded Protein to DsbA, The EMBO Journal, vol. 15, No. 2, pp. 392-398, 1996.
Gething, M.,Protein Folding in the Cell, Nature, vol. 355, Jan. 2, 1992.
Goethel, S.F., et al.,Peptide-Proly Cis-Trans Isomerases, a Superfamily of Ubiquitous Folding Catalysts, Cellular and Molecullar Life Sciences (CMLS), pp. 423-436, vol. 55, 1999.
Guyader, M., et al.Genome Organization and Transactivation of the Human Immunodeficiency Virus Type 2, Nature, vol. 326 Apr. 16, 1987.
Hottenrott, S., et al.,The Escherichia Coli SlyD is a Metal-Ion-Regulate Peptidyl-Prolyl Cis/Trans-Isomerase, The Journal of Biological Chemistry, vol. 272, No. 25, Issue of Jun. 20, pp. 15697-15701, 1997.
Ivery, M.T.G.,Immunophilins: Switched on Protein Binding Domains? Med Res Rev., Nov. 2000, pp. 452-484.
Kay, J.E.,Structure-Function Relationships in the FK506-Binding Proteing(FKBP)Family of Peptidylprolyl Cis-Trans Isomerases, Biochem. J., (1996), 314, 361-385.
Kojouharova, M.S., et al.,Differential Binding of IgG and of a HIV gp41 Peptide by the B Chain and A Chain Globular Head Sequences of C1q, Respectively, Journal of Immunology, 161:4352-4331.
Lane, W.S.,Complete Amino Acid Sequence of the FK506 and Rapamycin Binding Protein, FKBP, Isolated from Calf Thymus, Journal of Protein Chemistry, pp. 151-160, vol. 10, No. 2, 1991.
Lu, Min., et al.,A Trimeric Structured Domain of the HIV-1 Transmembrane Glycoprotein, Nature Structural Biology, pp. 1-8, vol. 2, No. 12, Dec. 1995.
Matsubara, Etsuro, et al.,Apolipoprotein J and Alzheimer's Amyloid β Solubility, Biochem J. 316 (1996), pp. 671-679.
Meister, S., et al.,Basic Amino Acid Residues in the V3 Loop of Simian Immunodificiency Virus Envelope Alter Viral Coreceptor Tropism and Infectivity but Do Not Allow Efficient Utilization of CXCR4 as Entry Cofactor, Virology, 284, 287-296 (2001).
Missiakas, D., et al.,Identification and Characterization of a New Disulfide Isomerase-Like Protein(DsbD)in Escherichia Coli, The EMBO Journal, vol. 14, No. 14, pp. 3415-3424, 1995.
Missiakas, D., et al.,New Components of Protein Foling in Extracytoplasmic Compartments of Escherichia Coli SurA, FkpA and Skp/OmpH, Molecular Microbiology, (1996) 21(4), pp. 871-884.
Otteken, et al.Calreticulin Interacts With Newly Synthesized Human Immunodeficiency Virus Type 1 Envelope Gylcoprotein, Suggesting A Chaperone Function Similar To That Of Calnexin, The Journal of Biological Chemistry , vol. 271, No. 1, Jan. 5, 1996, pp. 97-103.
Pennisi, Elizabeth,Expanding the Eukaryote's Cast of Chaperones, Science, vol. 274, Dec. 1996 pp. 1613-1614.
Prusiner, S.B.,Prions, Nobel Lecture, vol. 95, pp. 13363-1383, Nov. 1998.
Rahfeld, J., et al.,Confirmation of the Existence of a Third Family Among Peptidyl-Prolyl Cisltrans Isomerases Amino Acid Sequence and Recombinant Production of Parvulin, FEBS Letters, 352 (1994) pp. 180-184.
Ramm, K., et al.,The Periplasmic Escherichia Coli Peptidylprolyl Cis, Trans-Isomerase FkpA, The Journal of Biological Chemistry, vol., 275, No. 22, Issue of Jun. 2, pp. 17106-17113, 2000.
Ratner, L., et al.,Complete Nucleotide Sequence of the AIDS Virus, HTLV-III, Nature, pp. 277-284, vol. 313-Jan. 24, 1985.
Rool, M.J., et al.,Protein Design of an HIV-1 Entry Inhibitor, Science, pp. 884-888, vol., 291, Feb. 2, 2001.
Scholz, C., et al.,Cooperation of Enzymatic and Chaperone Functions of Trigger Factor in the Catalysis of Protein Folding, The EMBO Journal. vol. 16, No. 1, pp. 54-58, 1997.
Scholz, C.,Autocatalytic Folding of the Folding Catalyst FKBP12, The Journal of Biological Chemistry, vol., 271, No. 22, Issue of May 31, pp. 12703-12707, 1996.
Speth, C., et al.,A 60 kD Heat-Shock Protein-Like Molecular Interacts with the HIV Transmembrane Glycoprotein gp41, Molecular Immunology, 36 (1999) 619-628.
Stoller, G., et al., A Ribosome-Associated Peptidyl-Prolyl Cis/Trans Isomerase Identified As the Trigger Factor, The EMBO Journal, vol. 14, No. 20, pp. 4939-4948, 1995.
Tijssen, P.,Preparation of Enzyme-Antibody of Other Enzyme-Macromolecule Conjugates, Practice and Theory of Enzyme Immunoassays, Chapter 11, pp. 221-279, 1985.
Wang, C., et al.,Protein Disulfide Isomerase is Both an Enzyme and a Chaperone, The FASEB Journal, vol. 7, pp. 1515-1517, Dec. 1993.
Wild, C., et al.,A Synthetic Peptide Inhibitor of Human Immunodeficiency Virus Replication: Correlation Between Solution Structure and Viral Inhibition, Proc. Natl. Acad. Sci., vol.
Faatz Elke
Schaarschmidt Peter
Scholz Christian
Brinks Hofer Gilson & Lione
Roche Diagnostics Corporation
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