Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Blood proteins or globulins – e.g. – proteoglycans – platelet...
Reexamination Certificate
2007-10-30
2011-11-01
Kim, Alexander (Department: 1656)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
Blood proteins or globulins, e.g., proteoglycans, platelet...
C530S350000, C435S013000
Reexamination Certificate
active
08048990
ABSTRACT:
The invention provides vitamin K-dependent polypeptides with enhanced membrane binding affinity. These polypeptides can be used to modulate clot formation in mammals. Methods of modulating clot formation in mammals are also described.
REFERENCES:
patent: 4784950 (1988-11-01), Hagen et al.
patent: 4904584 (1990-02-01), Shaw
patent: 5009889 (1991-04-01), Taylor, Jr. et al.
patent: 5041376 (1991-08-01), Gething et al.
patent: 5093317 (1992-03-01), Lewis et al.
patent: 5180583 (1993-01-01), Hedner
patent: 5225537 (1993-07-01), Foster
patent: 5258288 (1993-11-01), Wydro et al.
patent: 5288629 (1994-02-01), Berkner
patent: 5374617 (1994-12-01), Morrissey et al.
patent: 5460950 (1995-10-01), Barr et al.
patent: 5504064 (1996-04-01), Morrissey et al.
patent: 5516640 (1996-05-01), Watanabe et al.
patent: 5580560 (1996-12-01), Nicolaisen et al.
patent: 5648254 (1997-07-01), Mulvihill et al.
patent: 5788965 (1998-08-01), Berkner et al.
patent: 5817788 (1998-10-01), Berkner et al.
patent: 5824639 (1998-10-01), Berkner
patent: 5833982 (1998-11-01), Berkner et al.
patent: 5837843 (1998-11-01), Smirnov et al.
patent: 5847085 (1998-12-01), Esmon et al.
patent: 5861374 (1999-01-01), Berkner et al.
patent: 5891843 (1999-04-01), Turecek et al.
patent: 5965425 (1999-10-01), Barr et al.
patent: 5986079 (1999-11-01), Barr et al.
patent: 6013620 (2000-01-01), Turecek et al.
patent: 6017882 (2000-01-01), Nelsestuen
patent: 6071514 (2000-06-01), Grinnell et al.
patent: 6100061 (2000-08-01), Reiter et al.
patent: 6423826 (2002-07-01), Nelsestuen et al.
patent: 6475725 (2002-11-01), Reiter et al.
patent: 6693075 (2004-02-01), Nelsestuen
patent: 6747003 (2004-06-01), Nelsestuen
patent: 6762286 (2004-07-01), Nelsestuen
patent: 6806063 (2004-10-01), Pedersen et al.
patent: 6903069 (2005-06-01), Pingel et al.
patent: 7026524 (2006-04-01), Persson et al.
patent: 7160540 (2007-01-01), Nelsestuen
patent: 7176288 (2007-02-01), Persson et al.
patent: 7220837 (2007-05-01), Nelsestuen
patent: 7247708 (2007-07-01), Nelsestuen
patent: 7294699 (2007-11-01), Nelsestuen
patent: 7314917 (2008-01-01), Nelsestuen
patent: 2003/0211094 (2003-11-01), Nelsestuen
patent: 0 296 413 (1988-12-01), None
patent: 0 354 504 (1990-02-01), None
patent: 0 512 011 (1994-04-01), None
patent: 0 370 205 (1998-07-01), None
patent: 64-085096 (1989-03-01), None
patent: WO 88/10295 (1988-12-01), None
patent: WO 91/11514 (1991-08-01), None
patent: WO 92/15686 (1992-09-01), None
patent: WO 94/27631 (1994-12-01), None
patent: WO 96/00577 (1996-01-01), None
patent: WO 98/32466 (1998-07-01), None
patent: WO 98/35026 (1998-08-01), None
patent: WO 99/03498 (1999-01-01), None
patent: WO 99/03887 (1999-01-01), None
patent: WO 99/20767 (1999-04-01), None
patent: WO 99/66031 (1999-12-01), None
patent: WO 00/26230 (2000-05-01), None
patent: WO 00/26354 (2000-05-01), None
patent: WO 00/28065 (2000-05-01), None
patent: WO 00/54787 (2000-09-01), None
patent: WO 00/66753 (2000-11-01), None
patent: WO 01/58935 (2001-08-01), None
patent: WO 01/83725 (2001-11-01), None
patent: WO 02/02764 (2002-01-01), None
patent: WO 02/03075 (2002-01-01), None
patent: WO 02/22776 (2002-03-01), None
patent: WO 02/29025 (2002-04-01), None
patent: WO 02/38162 (2002-05-01), None
patent: WO 02/077218 (2002-10-01), None
patent: WO 03/027147 (2003-04-01), None
patent: WO 03/037932 (2003-05-01), None
patent: WO 03/055512 (2003-07-01), None
patent: WO 03/093465 (2003-11-01), None
patent: WO 2004/029091 (2004-04-01), None
patent: WO 2004/083361 (2004-09-01), None
patent: 9809597 (1999-04-01), None
P04070 the human protein C (last viewed on Sep. 18, 2010).
Tokunaga et al., Cellular Basis for Protein C Deficiency Caused by a Single Amino Acid Substitution at Argl5 in the γ-Carboxyglutamic Acid Domain, J. Biochem (1996) 120 (2): 360-368.
Guo et al., Protein tolerance to random amino acid change, 2004, Proc. Natl. Acad. Sci. USA 101: 9205-9210.
Lazar et al., Transforming Growth Factor α: Mutation of Aspartic Acid 47 and Leucine 48 Results in Different Biological Activity, 1988, Mol. Cell. Biol. 8:1247-1252.
Hill et al., Functional Analysis of conserved Histidines in ADP-Glucose Pyrophosphorylase fromEscherichia coli, 1998, Biochem. Biophys. Res. Comm. 244:573-577.
Zhang et al., Influence of specific gamma-carboxyglutamic acid residues on the integrity of the calcium-dependent conformation of human protein C., J. Biochem, 1996, vol. 267, pp. 26078-26084.
EMBL Accession No. AF465270 dated Feb. 2, 2003, pages.
GenBank Accession No. M13232 dated Feb. 13, 1996, 3 pages.
UNIPROT Accession No. P22457 dated Dec. 4, 2007, 7 pages.
“Docking of Tissue Factor and Factor VIIa Initiates Blood Coagulation,” at http://www.sdsc.edu.IOTW/week46.96, 1996, 1 page.
Arnlijots et al., “Prevention of experimental arterial thrombosis by topical administration of active site-inactivated factor VIIa,”J. Vasc. Surg., 1997, 25(2):341-346.
Bauer, “Treatment of factor VII deficiency with recombinant factor VIIa,”Haemostasis, 1996, 26(Suppl. 1):155-158.
Bharadwaj et al., “Factor VII Central. A novel mutation in the catalytic domain that reduces tissue factor binding, impairs activation by factor XA, and abolishes amidolytic and coagulant activity,”J. Biol. Chem., 1996, 271:30685-30691.
Bjoern et al., “Human Plasma and Recombinant Factor VII. Characterization ofO-glycosylations at serine residues 52 and 60 and effects of site-directed mutagenesis of serine 52 to alanine,”J. Biol. Chem., 1991, 266(17):11051-11057.
Broze et al., “Monoclonal anti-human factor VII antibodies. Detection in plasma of a second protein antigenically and genetically related to factor VII,”J. Clin. Invest., 1985, 76:937-946.
Chang et al., “Engineered Recombinant Factor VII Q217Variants with Altered Inhibitor Specificities,”Biochemistry, 1999, 38:10940-10948.
Chang et al., “Replacing the First Epidermal Growth Factor-like Domain of Factor IX with That of Factor VII Enhances Activity In Vitro and in Canine Hemophilia B,”J. Clin. Invest., 1997, 100(4): 886-892.
Cheung et al., “Localization of a metal-dependent epitope to the amino terminal residues 33-40 of human factor IX,”Thromb. Res., 1995, 80(5):419-427.
Cheung et al., “Localization of an Epitope of a Calcium Dependent Monoclonal Antibody to the N Terminal Region of the GLA domain of Human Factor VII,”Thromb. Res., 1995, 79(2):199-206.
Choudhri et al., “Targeted Inhibition of Intrinsic Coagulation Limits Cerebral Injury in Stroke without Increasing Intracerebral Hemorrhage,”J. Exp. Med., 1999, 190:91-99.
Christiansen et al., “Hydrophobic Amino Acid Residues of Human Anticoagulation Protein C that Contribute to its Functional Binding to Phospholipid Vesicles,”Biochemistry, 1995, 34:10376-10382.
Dackiw et al., “Prevention of endotoxin-induced mortality by antitissue factor immunization,”Arch. Surg., 1996, 131 :1273-1278.
Dahlback, “Inherited Thrombophilia: Resistance to Activated Protein C as a Pathogenic Factor of Venous Thromboemolism,”Blood, 1995, 85:607-614.
Dickinsin and Ruf, “Active Site Modification of Factor VIIa Affects Interactions of the Protease Domaine with Tissue Factor,”J. Biol. Chem., 1997, 272(32):19875-19879.
Dickinson et al., “Influence of Cofactor Binding and Active Site Occupancy on the Conformation of the Macromolecular Substrate Exosite of Factor VIIa,”J. Mol. Biol., 1998, 277:959-971.
Dickinson et al., “Identification of surface residues mediating tissue factor binding and catalytic function of the serine protease factor VIIa,”Proc. Natl. Acad. Sci. USA, 1996, 93:14379-14384.
Esmon et al., “Isolation of a membrane-bound cofactor for thrombin-catalyzed activation of protein C,”J. Biol. Chem., 1982, 257:859-864.
Evans, Jr. and Nelsestuen, “Importance ofcis-Proline 22 in the Membrane-Binding Conformation of Bovine Prothrombin,”Biochemistry, 1996, 35:8210-8215.
Evans and Nelsestuan, “Importance of Cis
Fish & Richardson P.C.
Kim Alexander
Regents of the University of Minnesota
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