US RE30985E
· Cartaya
· 1982
[cited by applicant]
US 4560655A
· Baker
· 1985
[cited by applicant]
US 4657866A
· Kumar
· 1987
[cited by applicant]
US 4767704A
· Cleveland
· 1988
[cited by applicant]
US 4927762A
· Darfler
· 1990
[cited by applicant]
US 5122469A
· Mather
· 1992
[cited by applicant]
US 5223409A
· Ladner
· 1993
[cited by applicant]
US 5643768A
· Kawasaki
· 1997
[cited by applicant]
US 5856456A
· Whitlow
· 1999
[cited by applicant]
US 6172197B1
· McCafferty
· 2001
[cited by applicant]
US 6472147B1
· Janda
· 2002
[cited by applicant]
US 6582915B1
· Griffiths
· 2003
[cited by applicant]
US 6673901B2
· Koide
· 2004
[cited by applicant]
US 6969108B2
· Fukumoto
· 2005
[cited by applicant]
US 7842476B2
· McGregor
· 2010
[cited by applicant]
US 8278419B2
· Jacobs
· 2012
[cited by applicant]
US 8569227B2
· Jacobs
· 2013
[cited by applicant]
US 9644023B2
· Torres
· 2017
[cited by applicant]
US 20050287153A1
· Dennis
· 2005
[cited by applicant]
US 20110118144A1
· Hyun
· 2011
[cited by applicant]
US 20130226834A1
· Gannalo, II
· 2013
[cited by applicant]
WO 8700195A1
· 1987
[cited by applicant]
WO 9003430A1
· 1990
[cited by applicant]
WO 9013646A1
· 1990
[cited by applicant]
WO 9411026A2
· 1994
[cited by applicant]
WO 0034317A2
· 2000
[cited by applicant]
WO 2004003019A2
· 2004
[cited by applicant]
WO 2009085462A1
· 2009
[cited by applicant]
WO 2010051274A2
· 2010
[cited by applicant]
WO 2010093627A2
· 2010
[cited by applicant]
WO 2011150133A2
· 2011
[cited by applicant]
WO 2013049275A1
· 2013
[cited by applicant]
WO 2014081944A2
· 2014
[cited by applicant]
WO 2015089073A2
· 2015
[cited by applicant]
WO 2015143199A1
· 2015
[cited by applicant]
WO 2016197071A1
· 2016
[cited by applicant]
Alfthan, et al., “Properties of a single-chain antibody containing different linker peptides,” Protein Engineering, 8(7): 725-731 (1995).
[cited by applicant]
Altuvia et al., “Ranking Potential Binding Peptides to MHC Molecules by a Computational Threading Approach”, Journal of Molecular Biology, vol. 249, Issue 2, pp. 244-250, 1995.
[cited by applicant]
Andersen et al., “Extending Half-life by Indirect Targeting of the neonatal Fc Receptor (FcRn) Using a Minimal Albumin Binding Domain”, Journal of Biological Chemistry, vol. 286, No. 7, pp. 5234-5241, 2011.
[cited by applicant]
Barnes et al., “Methods for growth of cultured cells in serum-free medium” Analytical Biochemistry, vol. 102, Issue 2, pp. 255-270, Mar. 1980.
[cited by applicant]
Binz et al., “High-affinity binders selected from designed ankyrin repeat protein libraries,” Nature Biotechnology, vol. 22, No. 5, pp. 575-585 (May 2004).
[cited by applicant]
Birtalan et al., “The Intrinsic Contributions of Tyrosine, Serine, Glycine and Arginine to the Affinity and Specificity of Antibodies”, Journal of Molecular Biology, vol. 377, Issue 5, pp. 1518-1528, Apr. 2008.
[cited by applicant]
Bork et al., “Proposed acquisition of an animal protein domain by bacteria,” Proceedings of the National Academy of Science, USA, vol. 89, pp. 8990-8994 (1992).
[cited by applicant]
Breton et al., “Prolonged Half-Life in the Circulation of a Chemical Conjugate Between a Pro-Urokinase Derivative and Human Serum Albumin”, Eur. J. Biochem., vol. 231, pp. 563-569, 1995.
[cited by applicant]
Connell, “Expression Systems for use in actinomycetes and related organisms”, Curr. Opin. Biotechnol., vol. 12, pp. 446-449, 2001.
[cited by applicant]
Coppieters et al., “Formatted Anti-Tumor necrosis Factor a VHH Proteins Derived From Camelids Show Superior Potency and Targeting to inflamed Joints in a Murine Model of Collagen-Induced Arthritis”, Arthritis & Rheumati…
[cited by applicant]
Database Geneseq (online) Aug. 13, 2015 (Aug. 13, 2015), “Staphylococcal leukotoxin binding FN3 domain (Luk122), SEQ ID 145”, XP055768899, retrieved from EBI accession No. GSP:BCB11489 Database accession No. BCB11489 (1…
[cited by applicant]
Database Geneseq, “Staphylococcal LukE binding FN3 domain (Luk51), Seq ID 50”, XP002796459, Ebi accession No. GSP:BCB11394, *sequence*, (2015). (2 pages).
[cited by applicant]
David et al., “Protein iodination with solid state lactoperoxidase” Biochemistry, vol. 13, No. 5, pp. 1014-1021, 1974.
[cited by applicant]
Dennis “Albumin Binding as a General Strategy for Improving the Pharmacokinetics of Proteins”, Journal of Biological Chemistry, vol. 277, No. 38, pp. 35035-35043, 2002.
[cited by applicant]
Dennis et al., “Imaging Tumors with an Albumin-Binding Fab, a Novel Tumor-Targeting Agent”, Cancer Research, vol. 67, pp. 254-261, Jan. 2007.
[cited by applicant]
Duttaroy et al., “Development of a Long-Acting Insulin Analog Using Albumin Fusion Technology”, Diabetes, vol. 54, pp. 251-258, Jan. 2005.
[cited by applicant]
Flisiak et al., “Albinterferon-alfa 2b: a new treatment option for hepatitis C”, Expert Opinion on Biological therapy, vol. 10, issue 10, pp. 1509-1515, 2010.
[cited by applicant]
Hallewell et al., “Genetically Engineered Polymers of Human CuZN Superoxide Dismutase,” The Journal of Biological Chemistry, vol. 264, No. 9, pp. 5260-5268 (1989).
[cited by applicant]
Ham et al., “Media and growth requirements”, Methods in Enzymology, vol. 58, pp. 44-93, 1979.
[cited by applicant]
Hanes et al., “In vitro selection and evolution of functional proteins by using ribosome display,” Proceedings of the National Academy of Sciences USA, vol. 94, pp. 4937-4942 (1997).
[cited by applicant]
Holt et al., “Anti-serum albumin domain antibodies for extending the half-lives of short lived drugs”, Protein Engineering Design & Selection, vol. 21, No. 5, pp. 283-288, 2008.
[cited by applicant]
Hunter, “Preparation of lodine-131 Labelled Human Growth Hormone of High Specific Activity”, Nature, vol. 194, 1962.
[cited by applicant]
Jacobs et al, “Fusion to a highly stable consensus albumin binding domain allows for tunable pharmacokinetics”, Protein Engineering, Design and Selection, vol. 28, No. 10, pp. 385-393 (2015).
[cited by applicant]
Jacobs et al., “Design of novel FN3 domains with high stability by a consensus sequence approach,” Protein Engineering, Design & Selection, vol. 25, No. 3, pp. 107-117 (2012).
[cited by applicant]
Koide et al., “High-affinity single-domain binding proteins with a binary-code interface,” PNAS, vol. 104, No. 16, pp. 6632-6637 (Apr. 17, 2007).
[cited by applicant]
Koide, et al., Teaching an Old Scaffold New Tricks: Monobodies Constructed Using Alternative Surfaces of the FN3 Scaffold, Journal of Molecular Biology, 415: 393-405 (2012).
[cited by applicant]
Kontermann et al., “Strategies for extended serum half-lite of protein therapeutics” Current Opinion in Biotechnology, vol. 22, pp. 868-876, 2011.
[cited by applicant]
Lehmann et al., “Engineering proteins for thermostability: the use of sequence alignments versus rational design and directed evolution,” Current Opinion in Biotechnology, vol. 12, pp. 371-375 (2001).
[cited by applicant]
Luckow et al., “Trends in the Development of Baculovirus Expression Vetors”, Biotechnology, vol. 6, pp. 47-55, 1988.
[cited by applicant]
Makrides “Strategies for Achieving High-Level Expression of Genes in
[cited by applicant]
Malm et al., “Engineering of bispecific affibody molecule towards HER2 and HER3 by addition of an albumin-binding domain allows for affinity purification and in vivo half-life extension”, Biotechnology Journal, vol. 9, …
[cited by applicant]
Mayfield et al., Expression and assembly of a fully active antibody in algae, PNAS, vol. 100, No. 2, pp. 438-442, Jan. 2003.
[cited by applicant]
Meinke et al., “Cellulose-Binding Polypeptides from Cellulomonas fimi: Endoglucanase D (CenD), a Family A b-1,4-Glucanase,” Journal of Bacteriology, vol. 175, No. 7, pp. 1910-1918 (1993).
[cited by applicant]
Metzner et al., “Genetic fusion to albumin improves the pharmacokinetic properties of factor IX”, Thromb. Haemost. vol. 102, pp. 634-644, 2009.
[cited by applicant]
Muller et al., “Improved Pharmacokinetics of Recombinant bispecific Antibody Molecules by Fusion to Human Serum Albumin”, Journal of Biological Chemistry, vol. 282, No. 17, pp. 12650-12660, Apr. 2007.
[cited by applicant]
Muller et al., “Superior serum half life of albumin tagged TNF ligands”, Biochemical and Biophysical Research Communications, vol. 396, pp. 793-799, 2010.
[cited by applicant]
Nygren, “Conjugation of Horseradish Peroxidase to Fab Fragments with Different Homobifunctional and Heterobifunctional Cross-Linking Reagents”, Journal of Histochemistry and Cytochemistry, vol. 30, No. 5, pp. 407-412, 1…
[cited by applicant]
Odegrip et al., “CIS display: In vitro selection of peptides from libraries of protein-DNA complexes”, Proc Natl Acad Sci USA, vol. 101, No. 9, pp. 2806-2810, Mar. 2004.
[cited by applicant]
Olson et al., “Design, expression, and stability of a diverse protein library based on the human fibronectin type III domain,” Protein Science, vol. 16, 476-484 (2007).
[cited by applicant]
Orlova et al., “Site-Specific Radiometal labeling and Improved Biodistribution Using ABY-027, A Novel HER2-Targeting Affibody Molecule-Albumin-Binding Domain Fusion Protein”, J. Nucl Med, vol. 54, No. 6, pp. 961-968, Ju…
[cited by applicant]
Osborn et al., “Albutropin: a growth hormone-albumin fusion with improved pharmacokinetics and pharmacodynamics in rats and monkeys”, European Journal of Pharmacology, vol. 456, pp. 149-158, 2002.
[cited by applicant]
Pain et al., “Preparation of Protein A-Peroxidase monoconjugate Using a Heterobifunctional Reagent, and its use in Enzyme Immunoassays”, Journal of Immunological Methods, vol. 40, pp. 219-230, 1981.
[cited by applicant]
Raju et al., “Glycoengineering of Therapeutic Glycoproteins: In Virto Galactosylation and Sialylation of Glycoproteins with Terminal N-Acetylglucosamine and Galactose Residues”, Biochemistry, vol. 40, pp. 8868-8876, 200…
[cited by applicant]
Roberts et al., “RNA-peptide fusions for the in vitro selection of peptides and proteins”, Proc. Natl. Acad Sci, USA. vol. 94, pp. 12297-12302, Nov. 1997.
[cited by applicant]
Robinson et al., “Covalent Attachment of Arc Repressor Subunits by a Peptide Linker Enhances Affinity for Operator DNA,” Biochemistry, vol. 35, pp. 109-116 (1996).
[cited by applicant]
Schulte “Use of albumin fusion technology to prolong the half-life of recombinant factor Vila”, Thrombosis Research, 122, Suppl. 4, pp. S14-S19, 2008.
[cited by applicant]
Sharp et al., “Synonymous codon usage in Saccharomyces Cerevisiae”, Yeast, vol. 7, pp. 657-678, 1991.
[cited by applicant]
Sheffield et al., “Prolonged in vivo anticoagulant activity of a hirudin-albumin fusion protein secreted from Pichia pastoris” Blood Coagulation and Fibrinolysis, vol. 12, pp. 433-443, 2001.
[cited by applicant]
Sinclair et al., “Synonymous codon usage bias and the expression of human glucocerebrosidase in the methylotrophic yeast, Pichia pastoris”, Protein Expression and Purification, vol. 26, pp. 96-105, 2002.
[cited by applicant]
Tijink et al., “Improved tumor targeting of anti-epidermal growth factor receptor nanobodies through albumin binding: taking advantage of modular Nanobody technology”, Mol Cancer Ther, 7(8), pp. 2288-2297, 2008.
[cited by applicant]
Walker et al., “Anti-serum albumin domain antibodies in the development of highly potent, efficacious and long-acting interferon”, Protein Engineering, Design & Selection, vol. 23, No. 4, pp. 271-278,2010.
[cited by applicant]
Watanabe et al., “Gene Cloning of Chitinase A1 from Bacillus circulans WL-12 Revealed Its Evolutionary Relationship to Serratia Chitinase and to the Type III Homology Units of Fibronectin,” Journal of Biological Chemist…
[cited by applicant]
Wunder et al., “Albumin-based Drug Delivery as Novel Therapeutic Approach for Rheumatoid Arthritis”, Journal of immunology, vol. 170, pp. 4793-4801, 2003.
[cited by applicant]
Zhang et al., “PKSolver: An add-in program for pharmacokinetic and pharmacodynamic data analysis in Microsoft Excel”, Computer Methods and Programs in Biomedicine, vol. 99, pp. 306-314, 2010.
[cited by applicant]
Zola, “Monoclonal Antibodies”, Encyclopedia of Life Sciences, vol. 9 pp. 147-158, 2010.
[cited by applicant]