Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues
Reexamination Certificate
2007-04-04
2010-11-23
Noakes, Suzanne M. (Department: 1656)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
Reexamination Certificate
active
07838629
ABSTRACT:
The present invention relates to conjugates containing a covalent linkage between one or more polypeptide molecules based on gamma-crystallin or ubiquitin and one or more functional components. Furthermore, the present invention relates to a method for the preparation of such a conjugate as well as to the use of the conjugate in diagnostics, therapy and chromatography.
REFERENCES:
patent: 4873192 (1989-10-01), Kunkel
patent: 5789166 (1998-08-01), Bauer et al.
patent: 5958684 (1999-09-01), Van Leeuwen et al.
patent: 6673901 (2004-01-01), Koide
patent: 7601803 (2009-10-01), Fiedler et al.
patent: 2004/0043386 (2004-03-01), Pray et al.
patent: 2006/0058510 (2006-03-01), Skerra et al.
patent: 2006/0099686 (2006-05-01), Fiedler et al.
patent: 2007/0111287 (2007-05-01), Fiedler et al.
patent: 2008/0171851 (2008-07-01), Fiedler et al.
patent: 2 761 688 (1998-10-01), None
patent: WO 97/16556 (1997-05-01), None
patent: WO 98/44121 (1998-10-01), None
patent: WO 98/54312 (1998-12-01), None
patent: WO 99/16873 (1999-04-01), None
patent: WO 01/04144 (2001-01-01), None
patent: WO2004/106368 (2004-12-01), None
patent: WO2006/040129 (2006-04-01), None
Baker et al. Journal of Biological Chemistry, 1994, 269(41 ):25381-25386.
Ubiquitin-like Superfamily Statistics from <http://supfam.cs.bris.ac.uk/SUPERFAMILY/cgi-bin/scop.cgi?sunid=54236> obtained on Mar. 16, 2010—from Superfamily v. 1.73—HMM library and genome assignments server.
International Search Report corresponding to PCT Application No. PCT/EP2005/010932 dated Nov. 4, 2006.
Yeh et al.Ubiquitin-like proteins: new wines in new bottles. Gene,vol. 248, (2000), pp. 1-14.
Notification of Transmittal of Translation of the International Preliminary Report on Patentability (Chapter I or Chapter II of the Patent Cooperation Treaty) corresponding to International Application No. PCT/EP2005/010932 dated May 3, 2007.
Abedi et al, “Green fluorescent protein as a scaffold for intracellular presentation of peptides,” Nucleic Acids Research, vol. 26, No. 2 pp. 623-630 (1998).
Advisory Action corresponding to U.S. Appl. No. 10/030,605 dated Oct. 13, 2006.
Advisory Action corresponding to U.S. Appl. No. 12/072,959 dated May 18, 2010.
Bazarsuren et al., “In vitro folding, functional characterization, and disulfide pattern of the extracellular domain of human GLP-1 receptor,” Biophysical Chemistry. vol. 96 pp. 305-318 (2002).
Beal et al., “Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting,” PNAS. vol. 93 pp. 861-866 (1996).
Berman et al., “The Protein Data Bank,” Nucleic Acid Res. vol. 28, No. 1 pp. 235-242 (2000).
Beste, et al., “Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold,” PNAS. vol. 96 pp. 1898-1903 (1999).
Bird et al., “Single-Chain Antigen-Binding Proteins,” Science. vol. 242 pp. 423-426 (1988).
Bowie et al., “Deciphering the Message in Protein Sequences: Tolerance to Amino Acid Substitutions,” Science. vol. 247 pp. 1306-1310 (1990).
Brinkmann et al., “A recombinant immunotoxin containing a disulfide-stabilized Fv-fragment,” PNAS. vol. 90 pp. 7538-7542 (1993).
Brinkmann et al., “Stabilization of a Recombinant Fv Fragment by Base-Loop Interconnection and Vh-VLPermutation,” Journal of Molecular Biology. vol. 268 pp. 107-117 (1997).
Buchberger et al., “The UBX Domain: A Widespread Ubiquitin-Like Module,” Journal of Molecular Biology. vol. 307, No. 1 pp. 17-24 (2001).
Burch, T.J., and Haas, A.L., “Site-directed mutagenesis of ubiquitin, Differential roles for arginine in the interaction with ubiquitin-activating enzyme,” Biochemistry. vol. 33, No. 23 pp. 7300-7308 (1994) [Abstract].
Butt et al., “Ubiquitin fusion augments the yield of cloned gene products inEscherichia coli,” PNAS. vol. 86 pp. 2540-2544 (1989).
Campion et al., “Biochemical Properties of Site-Directed Mutants of Human Epidermal Growth Factor: Importance of Solvent-Exposed Hydrophobic Residues of the Amino-Terminal Domain in Receptor Binding,” Biochemistry. vol. 29, No. 42 pp. 9988-9993 (1990).
Carter et al., “High levelEscherichia coilexpression and production of a bivalent humanized antibody fragment,” Nature Biotechnology. vol. 10 pp. 163-167 (1992).
Chen et al., “Direct Interaction of Hepatitis C Virus Core Protein with the Cellular Lymphotoxin-β Receptor Modulates the Signal Pathway of the Lymphotoxin-β Receptor,” Joumal of Virology. vol. 71, No. 12 pp. 9417-9426 (1997).
Chirgadze et al., “Structure fo the Bovine Eye Lens γD (γIIIb)-Crystallin at 1.95 Å,” Acta Cryst. vol. D52 pp. 712-721 (1996).
Choo, Y., and Klug, A., “Designing DNA-binding proteins on the surface of filamentous phage,” Current Opinion in Biotechnology. vol. 6 pp. 431-436 (1995).
Colcher et al., “Pharmacokinetics and biodistribution of genetically-engineered antibodies,” Q.J. Nucl. Med. vol. 42 pp. 225-241 (1998).
Connolly, “Solvent-Accessible Surfaces of Proteins and Nucleic Acids.” Science. vol. 221, No. 4612 pp. 709-713 (1983).
Cortese et al., “Selection of biologically active peptides by phage display of random peptide libraries,” Current Opinion in Biotechnology. vol. 7 pp. 616-621 (1996).
Crameri et al., “Molecular evolution of an arsenate detoxification pathway by DNA shuffling,” Nature Biotechnology. vol. 5 pp. 436-438 (1997).
Cumber et al., “Comparative stabilities in vitro and in vivo of a recombinant mouse antibody FvCys fragment and a bisFvCys conjugate,” Journal of Immunology. vol. 149, No. 1 pp. 120-126 (1992).
Daugherty et al., “Antibody affinity maturation using bacterial surface display,” Protein Engineering. vol. 11, No. 9 pp. 825-832 (1998).
de Kruif et al., “Selection and Application of Human Single Chain Fv Antibody Fragments from a Semi-synthetic Phage Antibody Display Library with Designed CDR3 Regions,” Journal of Molecular Biology. vol. 248 pp. 97-105 (1995).
den Dunnen et al., Database PIR—79, Accession No. A24060; Gene. vol. 38 pp. 197-204 (1985).
den Dunnen et al., Database PIR—79, Accession No. B24060; J. Mol. Biol. vol. 189 pp. 37-46 (1986).
Ebersbach et al., “Affilin-Novel Binding Molecules Based on Human γ-B-Crystallin, an All 62 -Sheet Protein,” Journal of Molecular Biology. Vol. 372 pp. 172-185 (2007).
Ecker et al., “Gene Synthesis, Expression, Structures, and Functional Activities of Site-specific Mutants of Ubiquitin,” The Journal of Biological Chemistry, vol. 262, No. 29 pp. 14213-14221 (1987).
European Office Action corresponding to European Patent Application No. 00 944 034.8-2401 dated Oct. 7, 2004.
European Patent Office Examination Report corresponding to Euopean Patent Application No. 06118519.5-2401 dated Apr. 2, 2007.
Exley, D., and Woodhams, B., “The Specificity of Antisera Raised by Oestradiol-17β-3-Hemisuccinyl-Bovine Serum Albumin,” Steroids. vol. 27, No. 6 pp. 813-820 (1976).
Filippi et al., “Linkage and Sequence Conservation of the X-Linked Genes DX253E (P3) and DXS254E (GdX) in Mouse and Man,” Genomics. vol. 7 pp. 453-457 (1990).
Finucane, F.D., and Woolfson, D.N., “Core-Directed Protein Design. II. Rescue of a Multiply Mutated and Destabilized Variant of Ubiquitin.” Biochemistry. vol. 38, No. 36 pp. 11613-11623 (1999).
“Fold: beta-Grasp (ubiquitin-like),” http://scop.mrc-Imb.cam.ac.uk/scop/data/scop.b.e.ca.html, Mar. 15, 2004. [Abstract].
Folgori et al., “Vaccine-Induced T-Cell Responses Against HCV: One Step Taken, More to Follow,” Gastroenterology. vol. 132, No. 4 pp. 1626-1628.
Genbank Accession No. lUBQ. Schlesinger,D.H. and Goldstein,G., “Hybrid troponin reconstituted from vertebrate and arthropod subunits,” Nature. vol. 255, No. 5507 pp. 423-424 (19
Ebersbach Hilmar
Fiedler Erik
Fiedler Ulrike
Hey Thomas
Jenkins Wilson Taylor & Hunt, P.A.
Noakes Suzanne M.
Scil Proteins GmbH
LandOfFree
Ubiquitin or gamma-crystalline conjugates for use in... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Ubiquitin or gamma-crystalline conjugates for use in..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Ubiquitin or gamma-crystalline conjugates for use in... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-4162600