US 5643768A
· Kawasaki
· 1997
[cited by applicant]
US 6018030A
· Ferrari
· 2000
[cited by applicant]
US 6355776B1
· Ferrari
· 2002
[cited by applicant]
US 6462189B1
· Koide
· 2002
[cited by applicant]
US 6521427B1
· Evans
· 2003
[cited by applicant]
US 6673901B2
· Koide
· 2004
[cited by applicant]
US 6703199B1
· Koide
· 2004
[cited by applicant]
US 6818418B1
· Lipovsek
· 2004
[cited by applicant]
US 6846655B1
· Wagner
· 2005
[cited by applicant]
US 7078490B2
· Koide
· 2006
[cited by applicant]
US 7115396B2
· Lipovsek
· 2006
[cited by applicant]
US 7119171B2
· Koide
· 2006
[cited by applicant]
US 7153661B2
· Koide
· 2006
[cited by applicant]
US 7842476B2
· McGregor
· 2010
[cited by applicant]
US 8278419B2
· Jacobs
· 2012
[cited by applicant]
US 20040259781A1
· Chiquet-Ehrismann
· 2004
[cited by applicant]
US 20050255548A1
· Lipovsek
· 2005
[cited by applicant]
US 20060040278A1
· Cojocaru
· 2006
[cited by applicant]
US 20060246059A1
· Lipovsek
· 2006
[cited by applicant]
US 20060270604A1
· Lipovsek
· 2006
[cited by applicant]
US 20080220049A1
· Chen
· 2008
[cited by applicant]
US 20090176654A1
· Cappuccilli
· 2009
[cited by applicant]
CA 2293632A1
· 1998
[cited by applicant]
CA 2418835A1
· 2002
[cited by applicant]
EP 1266025A1
· 2002
[cited by applicant]
EP 0985039B1
· 2008
[cited by applicant]
EP 1137941B1
· 2009
[cited by applicant]
WO 0164942A1
· 2001
[cited by applicant]
WO 0204523
· 2002
[cited by applicant]
WO 0232925A2
· 2002
[cited by applicant]
WO 03104418A2
· 2003
[cited by applicant]
WO 2004029224A2
· 2004
[cited by applicant]
WO 2004058821A2
· 2004
[cited by applicant]
WO 2005056754A2
· 2005
[cited by applicant]
WO 2007085815A2
· 2007
[cited by applicant]
WO 2008079973A2
· 2008
[cited by applicant]
WO 2008156642A1
· 2008
[cited by applicant]
WO 2009023184A2
· 2009
[cited by applicant]
WO 2009058379A2
· 2009
[cited by applicant]
WO 2009086116A2
· 2009
[cited by applicant]
WO 2009133208A1
· 2009
[cited by applicant]
WO 2010051274A2
· 2010
[cited by applicant]
WO 2010060095A1
· 2010
[cited by applicant]
WO 2011005133A1
· 2011
[cited by applicant]
WO 2012016245A2
· 2012
[cited by applicant]
Koide et al., “Monobodies: antibody mimics based on the scaffold of the fibronectin type III domain,” Methods Mol. Biol. 352:95-109 (2007) Abstract Only.
[cited by applicant]
Alexey Teplyakov et al, “C-terminal [beta]-strand swapping in a consensus-derived fibronectin Type III scaffold”, Proteins: Structure, Function, and Bioinformatics, US, (Feb. 12, 2014), vol. 82, No. 7, doi:10.1002/prot.…
[cited by applicant]
Bass et al., “Hormone Phage: An Enrichment Method for Variant Proteins with Altered Binding Properties,” Proteins: Structure, Function, and Genetics, 8: 309-314 (1990).
[cited by applicant]
Binz et al, “Engineered proteins as spedific binding reagents”, Current opinion in Biotchnology, 16, pp. 459-469, 2005.
[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]
Bork et al., “Proposed acquisition of an animal protein domain by bacteria”, Proc. Natl. Acad, Sci, vol. 89, pp. 8990-8994, Oct. 1992.
[cited by applicant]
C.N. Pace, “Determination and Analysis of Urea and Guanidine Hydrochloride Denaturation Curves,” Methods in Enzymology, 131: 266-280 (1986).
[cited by applicant]
Clarke et al., “Folding and Stability of a Fibronectin Type III Domain of Human Tenascin,” Journal of Molecular Biology, 270: 771-778 (1997).
[cited by applicant]
Dehouck, et al., “Fast and accurate predictions of protein stability changes upon mutations using statistical potentials and neural networks: PoPMuSiC-2.0,” Bioinformatics, 25(19): 2537-2543 (2009).
[cited by applicant]
Diem et al., “Selection of high-affinity Centyrin FN3 domains from a simple library diversified at a combination of strand and loop positions”, Protein Engineering, Design and Selection, vol. 27, No. 10, pp. 419-429, (2…
[cited by applicant]
Dineen et al., “The Adnectin CT-322 is a novel VEGF receptor 2 inhibitor that decreases tumor burden in an orthotopic mouse model of pancreatic cancer,” BMC Cancer, 8: 352-361 (2008).
[cited by applicant]
Dutta et al., “High-affinity fragment complementation of a fibronectin type III domain and its application to stability enhancement”, Protein Sci., (2005), vol. 14, No. 11, pp. 2838-2848, XP009154599.
[cited by applicant]
European Search Report for App. No. EP16176749 dated Oct. 24, 2016 and sent by agent Nov. 2, 2016.
[cited by applicant]
Garrard et al., “Selection of an anti-IGF-1 Fab from a Fab phage library created by mutagenesis of multiple CDR loops,” Gene, 128:103-109 (1993).
[cited by applicant]
GenBank Accession No. NP 002151, (2013).
[cited by applicant]
Getmanova et al., “Antagonists to Human and Mouse Vascular Endothelial Growth Factor Receptor 2 Generated by Directed Protein Evolution in Vitro,” Chemistry & Biology, 13: 549-556 (2006).
[cited by applicant]
Hackel et al., “Picomolar Affinity Fibronectin Domains Engineered Utilizing Loop Length Diversity, Recursive Mutagenesis, and Loop Shuffling,” Journal of Molecular Biology, 381: 1238-1252 (2008).
[cited by applicant]
Hackel et al., “Stability and CDR Composition Biases Enrich Binder Functionality Landscapes,” Journal of Molecular Biology, 401: 84-96 (2010).
[cited by applicant]
Hanes et al., “In vitro selection and evolution of the functional proteins by using ribosome display”, Proc Natl. Acad. Sci,. USA, vol. 94, pp. 4937-4942, May 1997.
[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]
Jain, et al., “Designing Protein Denaturants: Synthetic Agents Induce Cytochrome c Unfolding at Low concentrations and Stoichiometries,” Agnew. Chem., 114(4): 663-665 (2002).
[cited by applicant]
Jones et al., “A cDNA clone for cytotactin contains sequences similar to epidermal growth factor-like repeats and segments of fibronectin and fibrinogen”, Proc. Natl. Acad. Sci., vol. 85, pp. 2186-2190, Apr. 1988.
[cited by applicant]
Karatan, et al., “Molecular Recognition Properties of FN3 Monobodies that Bind the Src SH3 Domain,” Chemistry & Biology, 11: 835-844 (2004).
[cited by applicant]
Knappik, et al., “Fully Synthetic Human Combinatorial Antibody Libraries (HuCAL) Based on Modular Consensus Frameworks and CDRs Randomized with Trinucleotides,” Journal of Molecular Biology, 296: 57-86 (2002).
[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, Academic Press, vol. 415, No. 3, pp. 393-405 (2011).
[cited by applicant]
Koide, et al., “The Fibronectin Type III Domain as a Scaffold for Novel Binding Proteins,” Journal of Molecular Biology, 284(4): 1141-1151 (1998).
[cited by applicant]
Kunkel, et al., “Rapid and Efficient Site-Specific Mutagenesis without Phenotypic Selection,” Methods Enzymology, 154: 367-382 (1987).
[cited by applicant]
Lehmann et al., “Engineering proteins for theromostability: the use of sequence alignments versus rational design and directed evolution”, Current Opinion in Biotechnology, vol. 12, pp. 371-375, 2001.
[cited by applicant]
Lipovŝek, et al., “Evolution of an Interloop Disulfide Bond in High-Affinity Antibody Mimics Based on Fibronectin Type III Domain and Selected by Yeast Surface Display: Molecular Convergence with Single-Domain Camelid a…
[cited by applicant]
Luo et al., “N-terminal [beta]-strand swapping in a consensus-derived alternative scaffold driven by stabilizing hydrophobic interactions”, Proteins: Structure, Function, and Bioinformatics, US, (Jul. 1, 2014), vol. 82,…
[cited by applicant]
Meinke, et al., “Cellulose-Binding Polypeptides from Cellulomonas fimi: Endoglucanase D (CenD), a Family A β-1,4-Glucanase,” Journal of Bacteriology, 175(7): 1910-1918 (1993).
[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, No. 3, pp. 476-484, 2007.
[cited by applicant]
Parker, et al., “Antibody mimics based on human fibronectin type three domain engineered for thermostability and high-affinity binding to vascular endothelial growth factor receptor two,” Protein Engineering, Design & S…
[cited by applicant]
PCT International Search Report for PCT/US 09/62367, dated Sep. 27, 2010.
[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]
Skerra, et al., “Engineered protein scaffolds for molecular recognition,” Journal of Molecular Recognition, 13: 167-187 (2000).
[cited by applicant]
Steiner, et al., “Efficient Selection of DARPins with Sub-nonomolar Affinities using SRP Phage Display,” Journal of Molecular Biology, 382: 1211-1227 (2008).
[cited by applicant]
UniProt Accession No. P10039. (2013).
[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 United of Fibronectin,” The Journal of Biological C…
[cited by applicant]
Xu, et al., “Directed Evolution of High-Affinity Antibody Mimics Using mRNA Display,” Chemistry & Biology, 9: 933-942 (2002).
[cited by applicant]