US 5122368A
· Greenfield
· 1992
[cited by applicant]
US 5622929A
· Willner
· 1997
[cited by applicant]
US 5824805A
· King
· 1998
[cited by applicant]
US 6214345B1
· Firestone
· 2001
[cited by applicant]
US 7223837B2
· De Groot
· 2007
[cited by applicant]
US 7521056B2
· Chang
· 2009
[cited by applicant]
US 7527787B2
· Chang
· 2009
[cited by applicant]
US 7534866B2
· Chang
· 2009
[cited by applicant]
US 7550143B2
· Chang
· 2009
[cited by applicant]
US 7666400B2
· Chang
· 2010
[cited by applicant]
US 7705045B2
· De Groot
· 2010
[cited by applicant]
US 7829531B2
· Senter
· 2010
[cited by applicant]
US 7837980B2
· Alley
· 2010
[cited by applicant]
US 7847105B2
· Gangwar
· 2010
[cited by applicant]
US 7851437B2
· Senter
· 2010
[cited by applicant]
US 7968586B2
· Gangwar
· 2011
[cited by applicant]
US 7989434B2
· Feng
· 2011
[cited by applicant]
US 8034787B2
· DuBois
· 2011
[cited by applicant]
US 8034959B2
· Ng
· 2011
[cited by applicant]
US 8039273B2
· Jeffrey
· 2011
[cited by applicant]
US 8067546B2
· McDonagh
· 2011
[cited by applicant]
US 20060024308A1
· Crea
· 2006
[cited by applicant]
US 20120156194A1
· Arron et al.
· 2012
[cited by applicant]
US 20120258108A1
· Ghayur
· 2012
[cited by examiner]
US 20140154710A1
· Pierce
· 2014
[cited by applicant]
EP 0453082A1
· 1991
[cited by applicant]
EP 2757376
· 2014
[cited by applicant]
WO 2002083180A1
· 2002
[cited by applicant]
WO 2003016471A2
· 2003
[cited by applicant]
WO 2004010957A2
· 2004
[cited by applicant]
WO 2004043493A1
· 2004
[cited by applicant]
WO 2005112919A2
· 2005
[cited by applicant]
WO 2006110476A2
· 2006
[cited by applicant]
WO 2007018431A2
· 2007
[cited by applicant]
WO 2007059404A2
· 2007
[cited by applicant]
WO 2007089149A2
· 2007
[cited by applicant]
WO 2009017394A2
· 2009
[cited by applicant]
WO 2010062171A2
· 2010
[cited by applicant]
WO 2015120171A1
· 2015
[cited by applicant]
WO 2016016265A1
· 2016
[cited by applicant]
WO 2016057890A1
· 2016
[cited by applicant]
WO 2017060482A1
· 2017
[cited by applicant]
Almagro & Fransson, Humanization of antibodies, Frontiers in Bioscience 2008; 13: 1619-33 (Year: 2008).
[cited by examiner]
Rudikoff et al., Single amino acid substitution altering antigen-binding specificity, PNAS, USA, 1982, 79: 1979-1983 (Year: 1982).
[cited by examiner]
Riemer et al., Matching of trastuzumab (Herceptin®) epitope mimics onto the surface of Her-2/neu—a new method of epitope definition, Mol Immunol, 2005 42(9): 1121-1124 (Year: 2005).
[cited by examiner]
Zhu, M. et al., “Neutralizing monoclonal antibody to periostin inhibits ovarian tumor growth and metastasis” Mol Cancer Ther. Aug. 2011;10(8):1500-8. doi: 10.1158/1535-7163.MCT-11-0046. Epub Jun. 13, 2011. PMID: 2167023…
[cited by applicant]
Field, S. et al., “Novel highly specific anti-periostin antibodies uncover the functional importance of the fascilin 1-1 domain and highlight preferential expression of periostin in aggressive breast cancer” (2016) Mole…
[cited by applicant]
Kyutoku, M. et al., “Role of periostin in cancer progression and metastasis: inhibition of breast cancer progression and metastasis by anti-periostin antibody in a murine model” (2011) Int J Mol Med 28(2):181-6. doi: 10…
[cited by applicant]
Tai, I.T et al., “Periostin induction in tumor cell line explants and inhibition of in vitro cell growth by anti-periostin antibodies” (2005) Carcinogenesis 26(5):908-915, https://doi.org/10.1093/carcin/bgi034.
[cited by applicant]
Orecchia, P. et al., “Identification of a novel cell binding site of periostin involved in tumour growth” (2011) Eur J Cancer 47(14):2221-9. doi: 10.1016/j.ejca.2011.04.026.
[cited by applicant]
Extended European Search Report for European Patent Application No. 19772550.0 dated Jul. 6, 2022.
[cited by applicant]
Sorensen, A. L. et al. Chemoenzymatically synthesized multimeric Tn/STn MUC1 glycopeptides elicit cancer-specific anti-MUC1 antibody responses and override tolerance. Glycobiology 16, 96-107, doi:10.1093/glycob/cwj044 (…
[cited by applicant]
Staerz et al., “Hybrid antibodies can target sites for attack by T cells.” Nature 314.6012 (1985): 628-631.
[cited by applicant]
Steffensen, K.D., et al., Prevalence of epithelial ovarian cancer stem cells correlates with recurrence in early-stage ovarian cancer. J Oncol. 2011: p. 620523.
[cited by applicant]
Swers, J.S., et al., Shuffled antibody libraries created by in vivo homologous recombination and yeast surface display. Nucleic Acids Res, 2004. 32(3): p. e36.
[cited by applicant]
Tang, Y. et al. Periostin promotes migration and osteogenic differentiation of human periodontal ligament mesenchymal stem cells via the Jun amino-terminal kinases (JNK) pathway under inflammatory conditions. Cell proli…
[cited by applicant]
Weaver-Feldhaus, J. M., et al. Directed evolution for the development of conformation-specific affinity reagents using yeast display. Protein engineering, design & selection : PEDS 18, 527-536, doi: 10.1093/protein/gzi0…
[cited by applicant]
Yang, X., et al., Structures and biosynthesis of the N- and O-glycans of recombinant human oviduct-specific glycoprotein expressed in human embryonic kidney cells. Carbohydr Res, 2012. 358: p. 47-55.
[cited by applicant]
Yun, H., et al. (1)H, (13)C, and (15)N resonance assignments of FAS1-IV domain of human periostin, a component of extracellular matrix proteins. Biomolecular NMR assignments 12, 95-98, doi: 10.1007/s12104-017-9786-z (20…
[cited by applicant]
Zhao, A., et al., Rapid isolation of high-affinity human antibodies against the tumor vascular marker Endosialin/TEM1, using a paired yeast-display/secretory scFv library platform. J Immunol Methods, 2011. 363(2): p. 22…
[cited by applicant]
Shusta, E.V., et al., Directed evolution of a stable scaffold for T-cell receptor engineering. Nat Biotechnol, 2000. 18(7): p. 754-9.
[cited by applicant]
Siegel, R.W., Antibody affinity optimization using yeast cell surface display. Methods Mol Biol, 2009. 504: p. 351-83.
[cited by applicant]
Abbott, K. L. et al. Focused glycomic analysis of the N-linked glycan biosynthetic pathway in ovarian cancer. Proteomics 8, 3210-3220, doi:10.1002/pmic.200800157 (2008).
[cited by applicant]
Abbott, K. L. et al. Identification of candidate biomarkers with cancer-specific glycosylation in the tissue and serum of endometrioid ovarian cancer patients by glycoproteomic analysis. Proteomics 10, 470-481, doi:10.1…
[cited by applicant]
Abbott, K. L. et al. Targeted glycoproteomic identification of biomarkers for human breast carcinoma. Journal of proteome research 7, 1470-1480, doi: 10.1021/pr700792g (2008).
[cited by applicant]
Allam, H. et al. “Glycomic Analysis of Membrane Glycoproteins with Bisecting Glycosylation from Ovarian Cancer Tissues Reveals Novel Structures and Functions.” Journal of Proteome Research 14.1 (2015): 434-446.
[cited by applicant]
Allam, H. et al. The glycosyltransferase GnT-III activates Notch signaling and drives stem cell expansion to promote the growth and invasion of ovarian cancer. The Journal of biological chemistry, doi: 10.1074/jbc.M117.…
[cited by applicant]
Alvero, A.B., et al., Molecular phenotyping of human ovarian cancer stem cells unravels the mechanisms for repair and chemoresistance. Cell Cycle, 2009. 8(1): p. 158-66.
[cited by applicant]
Bapat, S.A., et al., Stem and progenitor-like cells contribute to the aggressive behavior of human epithelial ovarian cancer. Cancer Res, 2005. 65(8): p. 3025-9.
[cited by applicant]
Bergan, L., et al. Development and in vitro validation of anti-mesothelin biobodies that prevent CA125/Mesothelin-dependent cell attachment. Cancer letters 255, 263-274, doi: 10.1016/j.canlet.2007.04.012 (2007).
[cited by applicant]
Bhaumik, M., et al. Cloning and chromosomal mapping of the mouse Mgat3 gene encoding N-acetylglucosaminyltransferase III. Gene 164, 295-300 (1995).
[cited by applicant]
Boder, E. T., et al. Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity. Proceedings of the National Academy of Sciences of the United States of America 97, 10701-10705, doi:10.…
[cited by applicant]
Boder, E. T., et al. Yeast surface display for screening combinatorial polypeptide libraries. Nat Biotechnol, 1997. 15(6): p. 553-7.
[cited by applicant]
Bowley, D.R., et al., Antigen selection from an HIV-1 immune antibody library displayed on yeast yields many novel antibodies compared to selection from the same library displayed on phage. Protein Eng Des Sel, 2007. 20…
[cited by applicant]
Chandler, K. B., et al. Site-Specific N-Glycosylation of Endothelial Cell Receptor Tyrosine Kinase VEGFR-2. Journal of proteome research 16, 677-688, doi: 10.1021/acs.jproteome.6b00738 (2017).
[cited by applicant]
Christiansen, M. N. et al. Cell surface protein glycosylation in cancer. Proteomics 14, 525-546, doi: 10.1002/pmic.201300387 (2014).
[cited by applicant]
Colby, D. W. et al. Development of a human light chain variable domain (V(L)) intracellular antibody specific for the amino terminus of huntingtin via yeast surface display. Journal of molecular biology 342, 901-912, do…
[cited by applicant]
Colby, D. W. et al. Potent inhibition of huntingtin aggregation and cytotoxicity by a disulfide bond-free single-domain intracellular antibody. Proceedings of the National Academy of Sciences of the United States of Ame…
[cited by applicant]
Conway, S. J. et al. The role of periostin in tissue remodeling across health and disease. Cellular and molecular life sciences : CMLS 71, 1279-1288, doi: 10.1007/s00018-013-1494-y (2014).
[cited by applicant]
Dangaj, D., et al. “Novel recombinant human b7-h4 antibodies overcome tumoral immune escape to potentiate T-cell antitumor responses.” Cancer research 73.15 (2013): 4820-4829.
[cited by applicant]
Dangaj, D., et al. Isolation and Validation of Anti-B7-H4 scFvs from an Ovarian Cancer scFv Yeast-Display Library. Methods in molecular biology 1319, 37-49, doi:10.1007/978-1-4939-2748-7_2 (2015).
[cited by applicant]
Dangaj, D., et al. Mannose receptor (MR) engagement by mesothelin GPI anchor polarizes tumor-associated macrophages and is blocked by anti-MR human recombinant antibody. PLoS One, 2011. 6(12): p. e28386.
[cited by applicant]
Doronina, S. O., et al. “Enhanced activity of monomethylauristatin F through monoclonal antibody delivery: effects of linker technology on efficacy and toxicity.” Bioconjugate chemistry 17.1 (2006): 114-124.
[cited by applicant]
Ghajar, C.M., et al., The perivascular niche regulates breast tumour dormancy. Nat Cell Biol, 2013. 15(7): p. 807-17.
[cited by applicant]
Hakomori, S., et al. Isoantigenic expression of Forssman glycolipid in human gastric and colonic mucosa: its possible identity with “A-like antigen” in human cancer. Proceedings of the National Academy of Sciences of th…
[cited by applicant]
Hu, L., et al., Ovarian cancer stem-like side-population cells are tumourigenic and chemoresistant. Br J Cancer. 102(8); p. 1276-83. 2010.
[cited by applicant]
International Searching Authority. International Search Report and Written Opinion for application PCT/US2019/023020. Mailed on Jun. 25, 2019.
[cited by applicant]
Jia, L., et al., Proteomic analysis reflects different histologic subtypes of epithelial ovarian cancer. Med Hypotheses, 2012. 78(3): p. 407-9.
[cited by applicant]
Kieke, M. C. et al. Selection of functional T cell receptor mutants from a yeast surface-display library. Proceedings of the National Academy of Sciences of the United States of America 96, 5651-5656 (1999).
[cited by applicant]
Kohler, R. S. et al. Epigenetic activation of MGAT3 and corresponding bisecting GlcNAc shortens the survival of cancer patients. Oncotarget 7, 51674-51686, doi:10.18632/oncotarget. 10543 (2016).
[cited by applicant]
Kubota, T., et al. Novel anti-Tn single-chain Fv-Fc fusion proteins derived from immunized phage library and antibody Fc domain. Anticancer research 30, 3397-3405 (2010).
[cited by applicant]
Kurrey, N.K., et al., Snail and slug mediate radioresistance and chemoresistance by antagonizing p53-mediated apoptosis and acquiring a stem-like phenotype in ovarian cancer cells. Stem Cells, 2009. 27(9): p. 2059-68.
[cited by applicant]
Kusumbe, A.P., et al., CD133-expressing stem cells associated with ovarian metastases establish an endothelial hierarchy and contribute to tumor vasculature. Stem Cells, 2009. 27(3): p. 498-508.
[cited by applicant]
Lakshminarayanan, V. et al. Immune recognition of tumor-associated mucin MUC1 is achieved by a fully synthetic aberrantly glycosylated MUC1 tripartite vaccine. Proceedings of the National Academy of Sciences of the Unit…
[cited by applicant]
Lee, K. J. et al. Phage-display selection of a human single-chain fv antibody highly specific for melanoma and breast cancer cells using a chemoenzymatically synthesized G(M3)-carbohydrate antigen. Journal of the Americ…
[cited by applicant]
Li, W. et al. Periostin: its role in asthma and its potential as a diagnostic or therapeutic target. Respiratory research 16, 57, doi: 10.1186/s12931-015-0218-2 (2015).
[cited by applicant]
Li, Y., et al., Validation of glypican-3-specific scFv isolated from paired display/secretory yeast display library. BMC Biotechnol, 2012. 12: p. 23.
[cited by applicant]
Liu, J. et al. Structural characterizations of human periostin dimerization and cysteinylation. FEBS letters 592, 1789-1803, doi:10.1002/1873-3468.13091 (2018).
[cited by applicant]
Lu, Z., et al. “Generation of a fully human scFv that binds tumor-specific glycoforms.” Scientific reports 9.1 (2019): 1-11.
[cited by applicant]
Mao, S. et al. Phage display library selection of high-affinity human single-chain antibodies to tumor-associated carbohydrate antigens sialyl Lewisx and Lewisx. Proceedings of the National Academy of Sciences of the Un…
[cited by applicant]
Milstein, et al. “Hybrid hybridomas and their use in immunohistochemistry.” Nature 305.5934 (1983): 537-540.
[cited by applicant]
Nitta et al. “Preliminary trial of specific targeting therapy against malignant glioma.” The Lancet 335.8686 (1990): 368-371.
[cited by applicant]
North, S.J., et al., Glycomics profiling of Chinese hamster ovary cell glycosylation mutants reveals N-glycans of a novel size and complexity. J Biol Chem, 2010. 285(8): p. 5759-75.
[cited by applicant]
Posey Jr, A. D., et al. “Engineered Car T cells targeting the cancer-associated Tn-glycoform of the membrane mucin MUC1 control adenocarcinoma.” Immunity 44.6 (2016): 1444-1454.
[cited by applicant]
Prantner, A. M. et al. Molecular Imaging of Mesothelin-Expressing Ovarian Cancer with a Human and Mouse Cross-Reactive Nanobody. Molecular pharmaceutics 15, 1403-1411, doi: 10.1021/acs.molpharmaceut.7b00789 (2018).
[cited by applicant]
Ragupathi, G. Carbohydrate antigens as targets for active specific immunotherapy. Cancer immunology, immunotherapy : CII 43, 152-157 (1996).
[cited by applicant]
Rosenberg SA et al. “Adoptive cell transfer: a clinical path to effective cancer immunotherapy.” Nature Reviews Cancer 8.4 (2008): 299-308.
[cited by applicant]
Scholler, N., et al., Bead-based ELISA for validation of ovarian cancer early detection markers. Clin Cancer Res, 2006. 12(7 Pt 1): p. 2117-24.
[cited by applicant]
Scholler, N., et al., Method for generation of in vivo biotinylated recombinant antibodies by yeast mating. J Immunol Methods, 2006. 317(1-2): p. 132-43.
[cited by applicant]
Scholler, N., Selection of antibody fragments by yeast display. Methods Mol Biol, 2012. 907: p. 259-80.
[cited by applicant]
Siegel RW. et al., High efficiency recovery and epitope-specific sorting of an scFv yeast display library, J Immunol Methods, 2004, vol. 286, pp. 141-153.
[cited by applicant]
Almagro et al., Humanization of antibodies, Frontiers in Bioscience, 2008, vol. 13, pp. 1619-1633.
[cited by applicant]