Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives
Reexamination Certificate
2005-11-15
2005-11-15
Nickol, Gary B. (Department: 1642)
Organic compounds -- part of the class 532-570 series
Organic compounds
Carbohydrates or derivatives
C435S069100, C435S320100, C435S325000
Reexamination Certificate
active
06965023
ABSTRACT:
In accordance with the present invention, there are provided novel Death Domain (DD), Death Effector Domain (DED) and NB-ARC domain proteins. The invention also provides nucleic acid molecules encoding DD, DED and NB-ARC domain proteins, vectors containing these nucleic acid molecules and host cells containing the vectors. The invention also provides antibodies that can specifically bind to invention DDs, DEDs or NB-ARC domains. Such DDs, DEDs and NB-ARC domains and/or anti-DD, anti-DED or anti-NB-ARC domain antibodies are useful for discovery of drugs that suppress infection, autoimmunity, inflammation, allergy, allograft rejection, sepsis, and other diseases.
REFERENCES:
patent: 6440663 (2002-08-01), Scanlan et al.
patent: WO 95/10630 (1995-04-01), None
patent: WO 97/00690 (1997-01-01), None
patent: WO 98/39429 (1998-09-01), None
patent: WO 99/27112 (1999-06-01), None
patent: WO00/20587 (2000-04-01), None
patent: WO 01/51641 (2001-07-01), None
Watanabe et al. (GenEmbl/PRI Database, Accession No. AK000528, Feb. 22, 2000).
EST Database, Accession No. AA114228, Nov. 13, 1996, IDS.
Matthews et al. (Anal.Biochem., vol. 169, Feb. 1988, pp. 1-25).
Berger et al., “The apoptosis mediator mDAP-3 is a novel member of a conserved family of mitochondrial proteins,”Journal of Cell Science,113:3603-3612 (2000).
Feinstein et al., “The death domain: a module shared by proteins with diverse Cellular functions,”Trends in Biochemical Sciences,20:342-344 (1995).
Han et al., “MRIT, a novel death-effector domain-containing protein, interacts with caspases and Bc1XLand initiates cell death,”Proc. Natl. Acad. Sci. USA,94:11333-11338 (1997).
Hofmann, K., “The modular nature of apoptic signaling proteins,”Cell. Mol. Life Sci.,55:1113-1123 (1999).
Kumar et al., “Identification of a Novel Tumor Necrosis Factor-α-inducible Gene, SCC-S2, Containing the Consensus Sequence of a Death Effector Domain of Fas-associated Death Domain-like Interleukin-1β-converting Enzyme-inhibitory Protein,”J. Biol. Chem.,275:2973-2978 (2000).
Liang and Fesik, “Three-dimensional Structures of Proteins Involved in Programmed Cell Death,”J. Mol. Biol.,274:291-302 (1997).
Park et al., “Establishment of a High-Throughput Screening System for Caspase-3 Inhibitors,”Arch. Pharm. Res.,23:246-251 (2000).
Reed and Tomaselli, “Drug discovery opportunities from apoptosis research,”Current Opin. Biotech.,11:586-592 (2000).
Altschul et al., “Basic local alignment search tool,”J. Mol. Biol.215:403-410 (1990).
Altschul et al., “Gapped BLAST and PSI-BLAST: a new generation of protein database search programs,”Nucleic Acids Res.25:3389-3402 (1997).
Ashkenazi and Dixit, “Death receptors: signaling and modulation,”Science281:1305-1308 (1998).
Boldin et al., “Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/Apo-1- and TNF receptor-induced cell death,”Cell,85: 803-815 (1996).
Campbell et al., “The development ofChlamydia trachomatisinclusions within the host eukaryotic cell during interphase and mitosis,”J. Gen. Micro.135:1153-1165 (1989).
Deveraux et al., “X-linked IAP is a direct inhibitor of cell death proteases,”Nature388:300-304 (1997).
Eberstadt et al., “NMR structure and mutagenesis of the FADD (Mort1) death-effector domain,”Nature392:941-945 (1998).
Estojak et al., “Correlation of two-hybrid affinity data with in vitro measurements,”Mol. Cell Biol.15:5820 (1995).
Fan et al., “Inhibition of apoptosis in Chlamydia-infected cells: blockade of mitochondrial cytochrome c release and caspase activation,”J. Exp. Med.187:487-497 (1998).
Gibellini et al., “Inhibition of apoptosis byChlamydia psittaciandChlamydia trachomatisinfection in tissue culture cells,”Zentralblatt fur Bakteriologie288:35-43 (1998).
Gish and States, “Identification of protein coding regions by database similarity search,”Nature Genet.3:266-272 (1993).
Grutter, “Caspases: key player in programmed cell death,”Curr. Opin. Struct. Biol.10:649-655 (2000).
Haraguchi et al., “Apoptotic protease activating factor 1 (Apfa-1)—independent cell death suppression by Bcl-2,”J. Exp. Med.191:1709-1720 (2000).
Hauser and Engel, “Pseudomonas aeruginosainduces type-III-secretion-mediated apoptosis of macrophages and epithelial cells,”Infect. Immun.67:5530-5537 (1999).
Hersh et al., “The Salmonella invasion SipB induces macrophage apoptosis by binding to caspase-1”Proc. Natl. Acad. Sci. USA96:2396-2401 (1999).
Jaroszewski et al., “Fold prediction by a hierarchy of sequence threading and modeling methods,”Protein Sciences7:1431-1440 (1998).
Juo et al., “Essential requirement for caspase-8/FLICE in the initiation of the Fas-induced apoptotic cascade,”Curr. Biol.8:1001-1008 (1998).
Kischkel et al., “Apo2L/TRAIL-dependent recruitment of endogenous FADD and caspase-8 death receptors 4 and 5,”Immunity,12:611-620 (2000).
Kissil et al., “Isolation of DAP3, a novel mediator of interferon-Y-induced cell death,”J. Biol. Chem.270:27932-27936 (1995).
Kissil et al., “Structure-function analysis of an evolutionary conserved protein, DAP3, which mediates TNF-α- and Fas-induced cell death,”EMBO J.18:353-362 (1999).
Leo et al., “Differential requirements for tumor necrosis factor receptor-associated factor family proteins in CD40-mediated induction of NF-kB and jun N-terminal activation,”J. Biol. Chem.274:22414-11422 (1999).
Li et al., “Saturated BLAST: an automated multiple intermediate sequence search used to detect distant homology,”Bioinformaticts16:1105-1110 (2000).
Madden et al., “Applications of Network BLAST server,”Meth. Enzymol.266: 131-141 (1996).
Matsuzawa et al., “p53-inducible human homologue ofDrosophila seveninabsentia(Siah) inhibits cell growth: suppression of BAG-1,”EMBO J.17:2736-2747 (1998).
Muzio et al. “An induced proximity model for caspase-8 activation,”J. Biol. Chem.273:2926-2930 (1998).
Muzio et al., “FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex,”Cell85:817-827 (1996).
Nagata, S., “Fas-induced apoptosis, a disease caused by abnormality,”Genes Cells1:873-879 (1996).
Oddo et al., “Fas ligand-induced apoptosis of infected human macrophages reduces the viability of intracellularMycobacterium tuberculosis,” J. Immunol.160:5448-5454 (1998).
Ojcius et al., “Apoptosis of epithelial cells and macrophages due to infection with the obligate intracellular pathogenChlamydia psittaci,” J. Immunol.161:4220-4226 (1998).
Ojcius et al., “Enhancement of ATP levels and glucose metabolism during an infection by Chlamydia,”J. Biol. Chem.273:7052-7058 (1998).
Sali, A. and Blundell, T., “Comperative protein modelling by satisfaction of spatial restraints,”J. Mol. Biol.234:779-815 (1993).
Salvesen and Dixit, “Caspase activation: the induced-proximity model,”Proc. Natl. Acad. Sci. USA96:10964-10967 (1999).
Salvasen et al., “Caspase 8: igniting the death machine,”Structure Fold. Des.7:R225-229 (1999).
Sato et al., “A novel member of TRAF family of putative signal transducing proteins binds to the cytosolic domain of CD40,”FEBS Lett.358:113-118 (1995).
Sato et al., “FAP-1: A protein tyrosine phosphatase that associates with Fas,”Science268:411-415 (1995).
Sato et al., “Interactions among members of the Bcl-2 protein family analyzed with a yeast two-hybrid system,”Proc. Natl. Acad. Sci. USA91:9238-9242 (1994).
Scanlan et al., “Antigens recognized by autologous antibody in patients with renal-cell carcinoma,”Int. J. Cancer83: 456-464 (1999).
Schneider et al., “Characteri
Fiorentino Loredana
Godzik Adam
Lee Sug Hyung
Pawlowski Krzysztof
Reed John C.
Nickol Gary B.
The Burnham Institute
LandOfFree
Death domain proteins does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Death domain proteins, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Death domain proteins will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3483593