Chimeric clotting factors
09-11-2021 дата публикации
Номер:
US0011168316B2
Автор: Joe Salas, Elena Kistanova, Vu Phong Hong, Adam R. Mezo, Robert T. PETERS, SALAS JOE, KISTANOVA ELENA, HONG VU PHONG, MEZO ADAM R, PETERS ROBERT T
Принадлежит: Bioverativ Therapeutics, Inc., BIOVERATIV THERAPEUTICS INC
Контакты:
Номер заявки: 44-81-1622
Дата заявки: 20-12-2018

























CPC - классификация
AA6A61A61KA61K3A61K38A61K38/A61K38/3A61K38/36A61K38/4A61K38/48A61K38/484A61K38/4846A61K4A61K47A61K47/A61K47/6A61K47/62A61PA61P7A61P7/A61P7/0A61P7/02A61P7/04CC1C12C12NC12N9C12N9/C12N9/6C12N9/64C12N9/643C12N9/6432C12N9/6437C12YC12Y3C12Y30C12Y304C12Y304/C12Y304/2C12Y304/21C12Y304/210C12Y304/2100C12Y304/21006C12Y304/2102C12Y304/21021IPC - классификация
AA6A61A61KA61K3A61K38A61K38/A61K38/3A61K38/36A61K38/4A61K38/48A61K38/5A61K38/58A61K4A61K47A61K47/A61K47/6A61K47/62A61PA61P7A61P7/A61P7/0A61P7/04CC0C07C07KC07K1C07K14C07K14/C07K14/8C07K14/81C07K14/815C1C12C12NC12N9C12N9/C12N9/6C12N9/64Цитирование НПИ
Andersen, L.M., et al., “Antibody-Induced Enhancement of Factor VIIa Activity Through Distinct Allosteric Pathways,” The Journal of Biological Chemistry 287(12):8994-9001, American Society for Biochemistry and Molecular Biology, United States (2012).Andrianomenjanahary, S., et al., “Synthesis of Novel Target Pro-Prodrugs of Anthracyclines Potentially Activated by a Monoclonal Antibody Galactosidase Conjugate (Part 1),” Bioorganic & Medicinal Chemistry Letters 2(9):1093-1096, Pergamon Press, England (1992).
Armour, K.L., et al., “Recombinant Human IgG Molecules Lacking Fc.gamma. Receptor I Binding and Monocyte Triggering Activities,” European Journal of Immunology 29(8):2613-2624, Wiley-VCH, Germany (1999).
Bajaj, S.P., et al., “Redetermination of the Rate-Limiting Step in the Activation of Factor IX by Factor XIa and by Factor VIIa/tissue Factor. Explanation for Different Electrophoretic Radioactivity Profiles Obtained on Activation of 3H- and 125I-labeled Factor IX,” Biochemistry 22(17):4047-4053, American Chemical Society, United States (1983).
Bertrand, P. and Gesson; J.P., “Click Chemistry with O-dimethylpropargylcarbamate for preparation of pH-sensitive functional groups. A Case Study,” The Journal of Organic Chemistry 72(9):3596-3599, American Chemical Society, United States (2007).
Biogen Idec, Hemophilia R&D Roundtable, phx.corporate-ir.net, accessed at http/www.google.de/url?sa=t&rct=j&q=&esrc=s&source=web&cd=9&ved=0ahU- KEwi9rODXvpDLAhZkbZoKHbeJDXIQFghfMAg&url=http%3A%2F%2Fphx.corporate-ir.net-%2FExternal.File%3Fitem% JDUGFyZW50SUQ9NDOwMDk1fENoaWxkSUQ9NDYxNzcxfFR5cGU9- MQ%3D%3D%26t% 3D1&usg=AFQjCNHEQPyuN7AIPzPikX2uAUL5fv5JoQ&sig2=8Ur9s6EFYDdNU-XKKaqwzQ, accessed on Feb. 24, 2016, 52 pages (2011).
Blencowe, C.A., et al., “Self-Immolative Linkers in Polymeric Delivery Systems,” Polymer Chemistry 2(4)773-790, Royal Society of Chemistry, England (2011).
Bovenschen N., et al., “LDL Receptor Cooperates with LDL Receptor-Related Protein in Regulating Plasma Levels of Coagulation Factor VIII in Vivo,” Blood 106(3):906-912, The American Society of Hematology, United States (2005).
Bovenschen, N., “LDL Receptor Polymorphisms Revisited,” Blood 116(25):5439-5440, The American Society of Hematology, United States (2010).
Brady, S.F., et al., “Design and Synthesis of a Pro-Drug of Vinblastine Targeted at Treatment of Prostate Cancer with Enhanced Efficacy and Reduced Systemic Toxicity,” Journal of Medicinal Chemistry 45(21):4706-4715, American Chemical Society, United States (2002).
Brandstetter, H., et al., “X-Ray Structure of Clotting Factor IXa: Active Site and Module Structure Related to Xase Activity and Hemophilia B,” Proceedings of the National Academy of Sciences of the United States of America 92 (21):9796-9800, The National Academy of Sciences, United States (1995).
Brunetti-Pierri, N., et al., “Bioengineered Factor IX Molecules with Increased Catalytic Activity Improve the Therapeutic Index of Gene Therapy Vectors for Hemophilia B,” Human Gene Therapy 20(5)1479-485, Mary Ann Liebert, Inc., United States (2009).
Bunce, M.W., et al., “Zymogen-like: Factor Xa Variants Restore Thrombin Generation and Effectively Bypass the Intrinsic Pathway in vitro,” Blood 117(1): 290-298, The American Society of Hematology, United States (2011).
Burmeister, W.P., et al., “Crystal structure of the complex of rat neonatal Fc receptor with Fc,” Nature 372 (6504):379-383, Nature Publishing Group, England (1994).
Caliceti, P., et al., “Biopharmaceutical Properties of Uricase Conjugated to Neutral and Amphiphilic Polymers,” Bioconjugate Chemistry 10(4):638-646, American Chemical Society, United States (1999).
Capon, D.J., et al., “Designing CD4 Immunoadhesins for AIDS Therapy,” Nature 37(6207):525-531, Nature Publishing Group, England (1989).
Carl, P.L., et al., “A Novel Connector Linkage Applicable in Prodrug Design,” Journal of Medicinal Chemistry 24 (5):479-480, American Chemical Society, United States (1981).
Chang, J., et al., “Changing Residue 338 in Human Factor IX from Arginine to Alanine Causes an Increase in Catalytic Activity,” The Journal of Biological Chemistry 273(20):12089-12094, The American Society for Biochemistry and Molecular Biology, Inc., United States (1998).
Cho, J.W. and Troy, F A. II, “Polysialic Acid Engineering: Synthesis of Polysialylated Neoglycosphingolipids by using the Polysialyltransferase from Neuroinvasive Escherichia coli K1,” Proceedings of the National Academy of Sciences USA 91 (24):11427-11431, National Academy of Sciences, United States (1994).
Cripe, L.D., et al., “Structure of the gene for human coagulation factor V,” Biochemistry 31(15):3777-3785, American Chemical Society, United States (1992).
De Groot, F.M., et al., “Elongated Multiple Electronic Cascade and Cyclization Spacer Systems in Activatible Anticancer Prodrugs for Enhanced Drug Release,” The Journal of Organic Chemistry 66(26):8815-8830, American Chemical Society, United States (2001).
Delgado, C., et al., “The Uses and Properties of PEG-Linked Proteins,” Critical Reviews in Therapeutic Drug Carrier Systems 9(3-4):249-304, CRC Press, Inc., United States (1992).
Dennis, M.S., et al., “Albumin Binding as a General Strategy for Improving the Pharmacokinetics of Proteins,” The Journal of Biological Chemistry 277(38):35035-35043, The American Society for Biochemistry and Molecular Biology, Inc., United States (2002).
Doronina, S.O., et al., “Development of Potent Monoclonal Antibody Auristatin Conjugates for Cancer Therapy,” Nature Biotechnology 21(7):778-784, Nature America Publishing, United States (2003).
Dumont, J.A., et al., “Prolonged activity of a recombinant factor VIII-Fc fusion protein in hemophilia A mice and dogs,” Blood 119(13):3024-3030, The American Society of Hematology, United States (2012).
Eaton, D., et al., “Proteolytic Processing of Human Factor VIII. Correlation of Specific Cleavages by Thrombin, Factor Xa, and Activated Protein C with Activation and Inactivation of Factor VIII Coagulant Activity,” Biochemistry 25 (2):505-512, American Chemical Society, United States (1986).
Eaton, D.L., et al., “Construction and Characterization of an Active Factor VIII Variant Lacking the central One-Third of the Molecule,” Biochemistry 25(26):8343-8347, American Chemical Society, United States (1986).
English language Abstract of European Patent Publication No. EP0295597A2, European Patent office, Espacenet database—Worldwide (1988).
Everett, S.A., et al., “Bioreductively-Activated Prodrugs for Targeting Hypoxic Tissues: Elimination of Aspirin from 2-Nitroimidazole Derivatives,” Bioorganic & Medicinal Chemistry Letters 9(9):1267-1272, Elsevier, England (1999).
Extended European Search Report for EP Application No. 13799785.4, European Patent Office, Germany, dated Aug. 25, 2016, 15 pages (Outstanding EESR in 4159.389EP02).
Extended European Search Report for EP Application No. 13799824.1, European Patent Office, Germany, dated Jul. 7, 2016, 14 pages.
Fay, P.J., et al., “Human Factor VIIIa Subunit Structure. Reconstruction of Factor VIIIa from the Isolated A1/A3-C1-C2 Dimer and A2 Subunit,” The Journal of Biological Chemistry 266(14):8957-8962, The American Society for Biochemistry and Molecular Biology, Inc., United States (1991).
Final Office Action dated Apr. 5, 2017, in U.S. Appl. No. 14/406,163, inventors Hong V., et al., filed Dec. 5, 2014.
Final Office Action dated Jan. 21, 2016, in U.S. Appl. No. 13/809,287, inventors Salas J., et al., filed Apr. 29, 2013.
Final Office Action dated Jun. 26, 2018, in U.S. Appl. No. 14/406,163, inventors Hong V., et al., filed Jun. 7, 2013.
Final Office Action dated May 16, 2012, in U.S. Appl. No. 12/949,564, inventors Rivera D., et al., filed Nov. 18, 2010.
Friend, P.J., et al., “Phase I Study of an Engineered Aglycosylated Humanized CD3 Antibody in Renal Transplant Rejection,” Transplantation 68(11):1632-1637, Lippincott Williams & Wilkins, Inc., United States (1999).
Gallwitz, M., et al., “The Extended Cleavage Specificity of Human Thrombin,” PLoS One 7(2):e31756, Public Library of Science, United States (2012).
Genbank, “Homo sapiens Transferrin (TF), mRNA,” Accession No. NM001063.1, accessed at http://www.ncbi.nlm.nih.gov/nuccore/NM_001063, accessed on Sep. 24, 2014, 5 pages.
Genbank, “Homo sapiens Transferrin (TF), mRNA,” Accession No. XM002793 published on May 13, 2002, accessed at https://www.ncbi.nlm.nih.gov/nuccore/XM_002793.7?report=genbank, accessed on Sep. 24, 2014, 2 pages.
Genbank, “Homo sapiens Transferrin (TF), mRNA,” Accession No. XM039845 published on Jul. 16, 2001, accessed at https://www.ncbi.nlm.nih.gov/nuccore/XM_039845.1?report=genbank, accessed on Sep. 24, 2014, 2 pages.
Genbank, “Homo sapiens Transferrin (TF), mRNA,” Accession No. XM039847 published on Jul. 16, 2001, accessed at https://www.ncbi.nlm.nih.gov/nuccore/XM_039847.1?report=genbank, accessed on Sep. 24, 2014, 2 pages.
Genbank, “Human Transferrin mRNA, Complete cds,” Accession No. M12530.1, published on Jan. 14, 1995, accessed at https://www.ncbi.nim.nih.gov/nuccore/M1253014, accessed on Jan. 15, 2015, 2 pages.
Genbank, “Human Transferrin: cDNA Characterization and Chromosomal Localization,” Accession No. AAA61140.1, published on Jan. 14, 1995, accessed at https://www.ncbi.nlm.nih.gov/protein/AAA61140, accessed on Jan. 15, 2015, 1 page.
Genbank, “Transferrin [human, liver, mRNA, 2347 nt],” Accession No. S95936.1 published on May 7, 1993, accessed at https://www.ncbi.nlm.nih.gov/nuccore/S95936, accessed on Sep. 24, 2014, 2 pages.
Geys, J., et al., “Acute Toxicity and Prothrombotic Effects of Quantum Dots: Impact of Surface Charge,” Environonmental Health Perspectives 116(12):1607-1613, National Institute of Environmental Health Sciences, United States (2008).
Gitschier, J., et al., “Characterization of the Human Factor VIII Gene,” Nature 312(5992):326-330, Nature Publishing Group, England (1984).
Greenwald, R.B., et al., “Drug Delivery Systems Based on Trimethyl Lock Lactonization: Poly(Ethylene Glycol) Prodrugs of Amino-Containing Compounds,” Journal of Medicinal Chemistry 43(3):475-487, American Chemical Society, United States (2000).
Hay M.P. and Denny W.A., “A New Synthesis of Carmethizole and Related Nitrogen Analogues,” Tetrahedron Letters 38(48):8425-8428, Elsevier, England (1997).
Hay, M.P., et al., “Substituent Effects on the Kinetics of Reductively-Initiated Fragmentation of Nitrobenzyl Carbamates Designed as for Bioreductive Prodrugs,” Journal of the Chemical Society, Perkins Transactions 1 19:2759-2770, Royal Society of Chemistry, England (1999).
Hay, M.P., et al., “Synthesis and Evaluation of Nitroheterocyclic Carbamate Prodrugs for Use With Nitroreductase-Mediated Gene-Directed Enzyme Prodrug Therapy,” Journal of Medicinal Chemistry 46(25):5533-5345, American Chemical Society, United States (2003).
Hoeben, R.C., et al., “Expression of Functionial Factor VIII in Primary Human Skin Fibroblasts after Retrovirus-mediated Gene Transfer,” The Journal of Biological Chemistry 265(13):7318-7323, The American Society for Biochemistry and Molecular Biology, United States (1990).
Holt, L.J., et al., “Anti-Serum Albumin Domain Antibodies for Extending the Half-Lives of Short Lived Drugs,” Protein Engineering, Design and Selection 21(5):283-288, Oxford University Press, England (2008).
International Preliminary Reporton Patentability for International Application No. PCT/US2013/044841, International Bureau of WIPO, Switzerland, dated Dec. 9, 2014, 14 pages.
International Preliminary Reporton Patentability for International Application No. PCT/US2013/044842, International Bureau of WIPO, Switzerland, dated Dec. 9, 2014, 8 pages.
International Search Report and Written Opinion for International Application No. PCT/US2011/48517, ISA, United States, dated Mar. 14, 2012.
International Search Report and Written Opinion for International Application No. PCT/US2013/044841, International Searching Authority, Alexandria, Virginia, USA, dated Nov. 20, 2013, 18 pages.
International Search Report for International Application PCT/US2013/044842, ISA, United States, dated Nov. 25, 2013.
Israel, E.J., et al., “Expression of the neonatal Fc receptor, FcRn, on human intestinal epithelial cells,” Immunology 92 (1):69-74, Blackwell Sciences, England (1997).
Izquierdo, C. and Burguillo, F.J., “Synthetic Substrates for Thrombin,” International Journal of Biochemistry 21 (6):579-592 Pergamon Press, England (1989).
Jaffer, F.A., et al., “In Vivo Imaging of Thrombin Activity in Experimental Thrombi With Thrombin-Sensitive Near-Infrared Molecular Probe,” Arteriosclerosis, Thrombosis and Vascular Biology 22(11):1929-1935, Lippincott Williams & Wilkins, United States (2002).
Jenny, R.J., et al., “Complete cDNA and Derived Amino acid Sequence of Human Factor V,” Proceedings of the National Academy of Sciences USA 84(14):4846-4850, National Academy of Sciences, United States (1987).
Kane, W.H. and Davie, E.W., “Cloning of a cDNA Coding for Human Factor V, a Blood Coagulation Factor Homologous to Factor VIII and Ceruloplasmin,” Proceedings of the National Academy of Sciences USA 83 (18):6800-6804, National Academy of Sciences, United States (1986).
Kobayashi, N., et al., “FcRn-Mediated Transcytosis of Immunoglobulin G in Human Renal Proximal Tubular Epithelial Cells,” American Journal of Physiology 282(2):F358-F365, American Physiological Society, United States (2002).
Kohchi, Y., et al., “Design and Synthesis of Novel Prodrugs of 2'-Deoxy-2'-Methylidenecytidine Activated by Membrane Dipeptidase Overexpressed in Tumor Tissues,” Bioorganic & Medicinal Chemistry Letters 17(8):2241-2245, Elsevier Science Ltd, England (2007).
Konig, T. and Skerra, A., “Use of an Albumin-Binding Domain for the Selective Immobilisation of Recombinant Capture Antibody Fragments on ELISA Plates,” Journal of Immunological Methods 218(1-2):73-83, Elsevier Science B.V., Netherlands (1998).
Kraulis, P.J., et al., “The Serum Albumin-Binding Domain of Streptococcal Protein G is a Three-Helical Bundle: a Heteronuclear NMR study,” FEBS Letters 378(2):190-194, Federation of European Biochemical Societies, England (1996).
Langner, K-D., et al., “Synthesis of Biologically Active Deletion Mutants of Human Factor VIII:C,” Behring Institute Mitteilungen 82: 16-25, Behringwerke AG, Germany (1988).
Lenting, P.J., et al., “Biochemistry of FVIII and Inhibitors: The Disappearing Act of Factor VIII,” Haemophilia 16 (102):6-15, Blackwell Publishing Ltd, England (2010).
Lin, C.N., et al., “Generation of a Novel Factor IX with Augmented Clotting Activities in Vitro and in Vivo,” Journal of Thrombosis and Haemostasis 8(8): 1773-1783, International Society on Thrombosis and Haemostasis, England (2010).
Linhult, M., et al., “Mutational Analysis of the Interaction Between Albumin-Binding Domain from Streptococcal Protein G and Human Serum Albumin,” Protein Science 11(2):206-213, Cold Spring Harbor Laboratory Press, United States (2002).
Lollar, P. and Parker, E.T., “Structural Basis for the Decreased Procoagulant Activity of Human Factor VIII Compared to the Porcine Homolog,” Journal of Biological Chemistry 266(19):12481-12486, The American Society for Biochemistry and Molecular Biology, Inc., United States (1991).
Louvain-Quintard, V.B., et al., “Thrombin-activable Factor X Re-establishes an Intrinsic Amplification in Tenase-deficient Plasmas,” The Journal of Biological Chemistry 280(50):41352-41359, The American Society for Biochemistry and Molecular Biology, Inc., United States (2005).
Lusson, J., et al., “cDNA Structure of the Mouse and Rat Subtilisin/kexin-like PC5: a Candidate Proprotein Convertase Expressed in Endocrine and Nonendocrine Cells,” Proceedings of the National Academy of Sciences USA 90 (14):6691-6695, National Academy of Sciences, United States (1993).
Martinelli, N., et al., “Polymorphisms atLDLRLocus may be Associated with Coronary Artery Disease through Modulation of Coagulation Factor VIII Activity and Independently from Lipid Profile,” Blood 116(25):5688-5697, The American Society of Hematology, United States (2010).
McKnight, G.S., et al., “Expression of the Chicken Transferrin Gene in Transgenic Mice,” Cell 34(2):335-341, Cell Press, United States (1983).
Mei, B., et al., “Rational Design of a Fully active, Long-Acting PEGylated Factor VIII for Hemophilia A Treatment,” Blood 116(2):270-279, The American Society of Hematology, United States (2010).
Meulien, P., et al., “A New Recombinant Procoagulant Protein Derived from the cDNA Encoding Human Factor VIII,” Protein Engineering 2(4):301-306, IRL Press Ltd., England (1988).
Meyer, Y., et al., “A Comparative Study of the Self-Immolation ofpara-Aminobenzylalcohol and Hemithioaminal-Based Linkers in the Context of Protease-Sensitive Fluorogeinc Probes,” Organic & Biomolecular Chemistry 8(8):1777-1780, Royal Society of Chemistry, England (2010).
Morpurgo, M., et al., “Covalent modification of mushroom tyrosinase with different amphiphic polymers for pharmaceutical and biocatalysis applications,” Applied Biochemistry and Biotechnology 56(1):59-72, Humana Press, Inc., United States (1996).
Mount, J.D., et al., “Sustained Phenotypic Correction of Hemophilia B dogs with a Factor IX Null Mutation by Liver-Directed Gene Therapy,” Blood 99(8):2670-2676, The American Society of Hematology, United States (2002).
Muller, D. and Kontermann, R.E., “Recombinant Bispecific Antibodies for Cellular Cancer Immunotherapy,” Current Opinion in Molecular Therapeutics 9(4):319-326, Current Drugs Ltd, England (2007).
Nakagawa, T., et al., “Identification and Functional Expression of a New Member of the Mammalian Kex2-like Processing Endoprotease Family: its Striking Structural Similarity to PACE4,” The Journal of Biochemistry 113(2):132-135, Oxford University Press, England (1993).
Nakayama, K., “Furin: A Mammalian Subtilisin/Kex2p-like Endoprotease Involved in Processing of a Wide Variety of Precursor Proteins,” Biochemical Journal 327:625-635, Biochemical Society, England (1997).
Narita, M., et al., “The Low-Density Lipoprotein Receptor-Related Protein (LRP) Mediates Clearance of Coagulation Factor Xa In Vivo,” Blood 91(2):555-560, The American Society of Hematology, United States (1998).
Noel, M.J., “Nucleotide sequence of the coat protein gene and flanking regions of cucumber virus (CMV) strain 117F,” Nucleic Acids Research 18(5):1332, Oxford University Press, England (1990).
Non-Final Office Action dated Dec. 22, 2017, in U.S. Appl. No. 14/406,163, inventors Hong V., et al., filed Dec. 5, 2014.
Non-Final Office Action dated Dec. 27, 2011, in U.S. Appl. No. 12/949,564, inventors Rivera D., et al., filed Nov. 18, 2010.
Non-Final Office Action dated Dec. 8, 2016, in U.S. Appl. No. 14/406,163, inventors Hong V., et al., filed Dec. 5, 2014.
Non-Final Office Action dated Jul. 20, 2015, in U.S. Appl. No. 13/809,287, inventors Salas J., et al., filed Apr. 29, 2013.
Non-Final Office Action dated Nov. 13, 2015, in U.S. Appl. No. 14/125,040, inventors Thorn K., et al., filed May 13, 2014.
Non-Final Office Action dated Sep. 28, 2016, in U.S. Appl. No. 13/809,287, inventors Salas J., et al., filed Apr. 29, 2013.
Osterlund, M., et al., “Sequential coagulation factor Vlla domain binding to tissue factor,” Biochemcial and Biophysical Research Communications 337(4):1276-1282, Elsevier, United States (2005).
Pan, J., et al., “Enhanced Efficacy of Recombinant FVIII in Noncovalent Complex with PEGylated Liposome in HemophiliaA Mice,” Blood 114(13):2802-2811, The American Society of Hematology, United States (2009).
Partial Supplementary European Search Report for EP Application No. 13799785.4, European Patent Office, Germany, dated May 3, 2016, 7 pages.
Perry-Feigenbaum, R., et al., “The Pyridinone-Methide Elimination,” Organic & Biomolecular Chemistry 7 (23):4825-4828, Royal Society of Chemistry, England (2009).
Persson, E., et al., “Rational Design of Coagulation Factor VIIa Variants with Substantially Increased Intrinsic Activity,” Proceedings of the National Academy of Sciences USA 98(24): 13583-13588, The National Academy of Sciences, United States (2001).
Persson, E., et al., “Substitution of Valine for Leucine 305 in Factor VIIa Increases the Intrinsic Enzymatic Activity,” The Journal of Biological Chemistry 276(31):29195-29199, The American Society for Biochemistry and Molecular Biology, Inc., United States (2001).
Persson, E., “Novel molecules for the correction of factor Xa generation and phenotype in hemophilia,” Thrombosis Research 129(Suppl 2):S51-S53, Elsevier Ltd., England (2012).
Peters, R.T., et al., “Prolonged activity of factor IX as a monomeric Fc fusion protein,” Blood 115(10)12057-2064, American Society of Hematology, United States (2010).
Peterson, J.A., et al., “A site Involving the “hybrid” and PSI Homology Domains of GPIIIa (beta 3-integrin subunit) is a Common Target for Antibodies Associated with Quinine-Induced Immune Thrombocytopenia,” Blood 101(3):937-942, The American Society of Hematology, United States (2003).
Petrovan, R.J. and Ruf, W., “Residue Met156 Contributes to the Labile Enzyme Conformation of Coagulation Factor VIIa,” The Journal of Biological Chemistry 276(9):6616-6620, The American Society for Biochemistry and Molecular Biology, Inc., United States (2001).
Peyvandi, F., et al., “Genetic Diagnosis of Gaemophilia and Other Inherited Bleeding Disorders,” Haemophilia 12 (Suppl 3):82-89, Blackwell Publishing Ltd., England (2006).
Rautio, J., et al., “Prodrugs: Design and Clinical Applications,” Nature Reviews. Drug Discovery 7(3):255-270, Nature Publishing Group, England (2008).
Rehemtulla, A., et al., “PACE4 is a Member of the Mammalian Propeptidase Family that has Overlapping but not Identical Substrate Specificity to PACE,” Biochemistry 32(43):11586-11590, American Chemical Society, United States (1993).
Rijkers, D.T., et al., “Design and Synthesis of Thrombin Substrates With Modified Kinetic Parameters,” Thrombosis Research 79(5-6):491-499, Pergamon Press., United States (1995).
Ritchie, K.A., et al., “Allelic Exclusion and Control of Endogenous Immunoglobulin Gene Rearrangement in Kappa Transgenic Mice,” Nature 312(5994):517-520, Nature Publishing Group, England (1984).
Roovers, R.C., et al., “Efficient Inhibition of EGFR Signaling and of Tumour Growth by Antagonistic Anti-EGFR Nanobodies,” Cancer Immunology, Immunotherapy 56(3):303-317, Springer Verlag, Germany (2007).
Rostin, J., et al., “B-Domain Deleted Recombinant Coagulation Factor VIII Modified with Monomethoxy Polyethylene Glycol,” Bioconjugate Chemistry 11(3):387-396, American Chemical Society, United States (2000).
Roth, J. et al., “From Microbes to Man” in Polysialic Acid, Roth J., Rutishauser U., Troy F.A , eds , pp. 335-348, BirkhauserVerlag, Basel, Switzerland (1993).
Routledge, E.G., et al.,“The Effect of Aglycosylation on the Immunogenicity of a Humanized Therapeutic CD3 Monoclonal Antibody,” Transplantation 60(8)1847-853, Williams & Wilkins, United States (1995).
Salas, J., et al., “Enhanced pharmacokinetics of factor VIIA as a monomeric Fc fusion,” Journal of Thrombosis and Haemostasis 9(Suppl 2):268, Abstract O-TU-026, International Society on Thrombosis and Haemostasis, United States (2011).
Salas, J., et al., “Enhanced pharmacokinetics of factor VIIA as a monomeric Fc fusion,” Thrombosis Research 135:970-976, Elsevier Ltd., England (Jan. 2015).
Salas, J., et al., “Targeting factor VIIa to platelet receptors results in enhanced activity,” Journal of Thrombosis and Haemostasis 9(Suppl 2):285, Abstract O-TU-078, International Society on Thrombosis and Haemostasis, United States (2011).
Sarver, N., et al., “Stable Expression of Recombinant Factor VIII Molecules Using a Bovine Papillomavirus Vector,” DNA 6(6):553-564, Mary Ann Liebert, Inc., United States (1987).
Schulte, S., “Use of Albumin: Fusion. Technology to Prolong the Half-Life of Recombinant Factor VIIa,” Thrombosis Research 122(Suppl 4):S14-S19, Pergamon Press, United States (2008).
Schwarz, M., et al., “Conformation-Specific Blockade of the Integrin GPIIb/IIIa: a Novel Antiplatelet Strategy that Selectively Targets Activated Platelets,” Circulation Research 99(1 ):25-33, American Heart Association, Inc., United States (2006).
Senter, P.D., et al., “Development of Drug-Release Strategy Based on the Reductive Fragmentation of Benzyl Carbamate Disulfides,” The Journal of Organic Chemistry 55(9):2975-2978, American Chemical Society, United States (1990).
Shields, R.L., et al., “High Resolution Mapping of the Binding Site on Human IgG1 for Fc.gamma.RI, Fc.gamma.RII, Fc.gamma.RIII, and FcRn and Design of IgG1 Variants with Improved Binding to the Fc.gamma.R,” The Journal of Biological Chemistry 276(9):6591-6604, The American Society for Biochemistry and Molecular Biology, Inc., United States (2001).
Sichler, K., et al., “Physiological fIXa Activation Involves a Cooperative Conformational Rearrangement of the 99-Loop,” The Journal of Biological Chemistry 278(6):4121-4126, The American Society for Biochemistry and Molecular Biology, Inc., United States (2003).
Simioni, P., et al., “X-Linked Thrombophilia with a Mutant Factor IX (factor IX Padua),” The New England Journal of Medicine 361(17):1671-1675, Massachusetts Medical Society, United States (2009).
Simplicio, A.L., et al., “Prodrugs for Amines,” Molecules 13(3):519-547, MDPI, Switzerland (2008).
Singh, Y., et al., “Recent Trends in Targeted Anticancer Prodrug and Conjugate Design,” Current Medicinal Chemistry 15(18):1802-1826, Bentham Science Publishers, Netherlands (2008).
Soejima, K., et al., “Factor VIIa Modified in the 170 Loop Shows Enhanced Catalytic Activity but Does Not Change the Zymogen-like Property,” The Journal of Biological Chemistry 276(20):17229-17235, The American Society for Biochemistry and Molecular Biology, Inc., United States (2001).
Soejima, K., et al.,“ The 99 and 170 Loop-Modified Factor VIIa Mutants Show Enhanced Catalytic Activity Without Tissue Factor,” The Journal of Biological Chemistry 277(50):49027-49035, The American Society for Biochemistry and Molecular Biology, Inc., United States (2002).
Sommermeyer, V.K., et al., “Klinisch Verwendte Hydroxyethylstarke: Physikalisch-Chemische Charakterisierung,” Krankenhauspharmazie 8(8):271-278, Deutscher Apotheker Verlag, Birkenwaldstr, Germany (1987).
Spicer, E.K., et al., “Isolation of CDNA Clones Coding for Human Tissue Factor: Primary Structure of the Protein and CDNA,” Proceedings of the National Academy of Sciences USA 84(15):5148-5152, National Academy of Sciences, United States (1987).
Spira, J., et al., “Prolonged Bleeding-Free Period Following Prophylactic Infusion of Recombinant Factor VIII Reconstituted With Pegylated Liposomes,” Blood 108(12):3668-3673, The American Society of Hematology, United States (2006).
Spitzer, S.G., et al., “Replacement of Isoleucine-397 by Threonine in the Clotting Proteinase Factor IXa (Los Angeles and Long Beach variants) Affects Macromolecular Catalysis but not L-Tosylarginine Methyl Ester Hydrolysis. Lack of Correlation between the ox Brain Prothrombin Time and the Mutation Site in the Variant Proteins,” The Journal of Biological Chemistry 265(1):219-225, The American Society of Biochemistry and Molecular Biology, Inc., United States (1990).
Stennicke, H.R., et al., “Generation and Biochemical Characterization of GlycoPEGylated Factor VIIa Derivatives,” Thrombosis and Haemostasis 100(5):920-928, Schattauer GmbH, Germany (2008).
Story, C.M., et al., “A Major Histocompatibility Complex Class I-like Fc Receptor Cloned from Human Placenta Possible Role in Transfer of Immunoglobin G from Mother to Fetus,” The Journal of Experimental Medicine 180 (6):2377-2381, The Rockefeller University Press, United States (1994).
Strickland, D.K. and Medved, L., “Low-Density Lipoprotein Receptor-Related Protein (LRP)-Mediated Clearance of Activated Blood Coagulation Co-Factors and Proteases: Clearance Mechanism or Regulation?,” Journal of Thrombosis and Haemostasis 4(7):1484-1486, International Society on Thrombosis and Haemostasis, England (2006).
Stubbs, J.D., et al., “cDNA Cloning of a Mouse Mammary Epithelial Cell Surface Protein Reveals the Existence of Epidermal Growth Factor-like Domains Linked to Factor VIII-Like Sequences,” Proceedings of the National Academy of Sciences 87(21):8417-8421, The National Academy of Sciences of the United States (1990).
Sturzebecher, J., et al., “Dramatic Enhancement of the Catalytic Activity of Coagulation Factor IXa by Alcohols,” FEBS Letters 412(2):295-300, Federation of European Biochemical Societies, Netherlands (1997).
Supplementary Partial European Search Report for EP Application No. 13799824.1, European Patent Office, Bermany, dated Mar. 10, 2016, 11 pages.
Sykes, B.M., et al., “Leaving Group Effects in Reductively Triggered Fragmentation of 4-Nitrobenzyl Carbamates,” Journal of the Chemical Society, Perkin Transactions 1 10:1601-1608, Royal Society of Chemistry, England (2000).
Takahashi, N., et al., “Single-Chain Structure of Human Ceruplasmin: the Complete Amino Acid Sequence of the Whole Molecule,” Proceedings of the National Academy of Sciences 81(2):390-394, National Academy of Sciences, United States (1984).
Tan, S., et al., “Enhancing the Acute Hemostatic Efficacy in Cynomolgus Monkeys by Targeting Activated Coagulation Factor VII to Platelets,” Abstract 1488, 56.sup.th ASH Annual Meeting and Exposition, San Francisco, CA, Dec. 6-9, 2014, American Society of Hematology, United States, 1 page (Dec. 2014).
Tanihara, M., et al., “Thrombin-Sensitive Peptide Linkers for Biological Signal-Responsive Drug Release Systems,” Peptides 19(3):421-425, Elsevier Science Inc., United States (1998).
Taylor, L.D., et al., “Use of O- and P-Hydroxybenzyl Functions as Blocking Groups Which are Removable with Base,” Journal of Organic Chemistry 43(6): 1197-1200, American Chemical Society, United States (1978).
Toole, J.J., et al., “A Large Region (.apprxeq.95 kDa) of Human Factor VIII is Dispensable for in vitro Procoagulant Activity,” Proceedings of the National Academy of Sciences USA 83(16):5939-5942, National Academy of Sciences, United States (1986).
Toole, J.J., et al., “Molecular Cloning of a cDNA Encoding Human Antihaemophilic Factor,” Nature 312(5992):342-347, Nature Publishing Group, England (1984).
Trussel, S., et al., “New Strategy for the Extension of the Serum Half-Life of Antibody Fragments,” Bioconjugate Chemistry 20(12):2286-2292, American Chemical Society, United States (2009).
Tung, C.H., et al., “A Novel Near-Infrared Fluorescence Sensor for Detection of Thrombin Activation in Blood,” European Journal of Chemical Biology 3(2-3):207-211, Wiley-VCH Verlag, Germany (2002).
Uniprot KB, accession No. P12259, Coagulation factor V, Homo sapiens (Human), accessed at http://www.uniprot.org/uniprot/P12259, accessed on May 15, 2015, 26 pages.
UniprotKB, accession No. P13726-1, Tissue factor, Homo sapiens (Human), accessed at http://www.uniprot.org.uniprot/P13726, accessed on May 15, 2015, 18 pages.
Van Den Ouweland, A.M., et al., “Structural Homology between the Human Fur Gene Product and the Subtilisin-like Protease Encoded by Yeast KEX2,” Nucleic Acids Research 18(3):664, Oxford University Press, England (1990).
Vehar, G.A., et al., “Structure of Human Factor VIII,” Nature 312(5992)1337-342, Nature Publishing Group, England (1984).
Vorobjev, P.E., et al., “Oligonucleotide Conjugated to Linear and Branched High Molecular Weight Polyethylene Glycol as Substrates for RNase H,” Nucleosides & Nucleotides 18(11-12):2745-2750, Marcel Dekker, Inc., United States (1999).
Vysotchin, A., et al., “Domain structure and domain-domain interactions in human coagulation factor IX,” The Journal of Biological Chemistry 268(12)18436-8446, The American Society for Biochemistry and Molecular Biology, Inc., United States (1993).
Wajima, T., et al., “A Comprehensive Model for the Humoral Coagulation Network in Humans,” Clinical Pharmacology & Therapeutics 86(3):290-298 (2009).
Ward, E.S. and Ghetie V., “The Effector Functions of Immunoglobins: Implications for Therapy,” Therapeutic Immunology 2(2):77-94, Blackwell Science Ltd., England (1995).
Wasley, L.C., et al., “PACE/Furin Can Process the Vitamin K-Dependent Pro-Factor IX Precursor with the Secretory Pathway,” The Journal of Biological Chemistry 268(12):8458-8465, The American Society for Biochemistry and Molecular Biology, Inc., United States (1993).
Weidler, B., et al., “Pharmakokinetische Merkmale als Kriterien fur den klinischen Einsatz von Hydroxyethylstarke,” Arzneimittel-Forschung 41(5):494-498, Editio Cantor, Germany (1991).
Weinstain, R., et al., “Real-Time Monitoring of Drug Release,” Chemical Communications 46(4):553-555, Royal Society of Chemistry, England (2010).
Wolberg, A.S. and Mast, A.E., “Tissue factor and factor VIIa-Hemostasis and Beyond,” Thrombosis Research 129 (Suppl 2):S1-S4, Elsevier Ltd , England (2012).
Wolf, D.L et al. “Procoagulant Activity of Reversibly Acylated Human Factor Xa,” Blood 86(11)14153-4157, The American Society of Hematology, United States (1995).
Zogg, T. and Branstetter, H., “Structural Basis of the Cofactor- and Substrate-Assisted Activation of Human Coagulation Factor IXa,” Structure 17(12):1669-1678, Cell Press, United States (2009).