Antibodies against MICA and/or MICB and uses thereof

CPC - классификация

AA6A61A61KA61K2A61K20A61K203A61K2039A61K2039/A61K2039/5A61K2039/50A61K2039/505A61PA61P3A61P35A61P35/A61P35/0A61P35/00CC0C07C07KC07K1C07K16C07K16/C07K16/2C07K16/28C07K16/281C07K16/2818C07K16/283C07K16/2833C07K2C07K23C07K231C07K2317C07K2317/C07K2317/3C07K2317/33C07K2317/34C07K2317/5C07K2317/52C07K2317/56C07K2317/565C07K2317/7C07K2317/72C07K2317/73C07K2317/732C07K2317/9C07K2317/92C07K2317/94C1C12C12NC12N1C12N15C12N15/C12N15/8C12N15/85

IPC - классификация

AA6A61A61PA61P3A61P35A61P35/A61P35/0A61P35/00A61P35/02A61P35/04A61P5A61P5/A61P5/3A61P5/32CC0C07C07KC07K1C07K16C07K16/C07K16/2C07K16/28C1C12C12NC12N1C12N15C12N15/C12N15/8C12N15/85

Цитирование НПИ

Alexander, A.J. and Hughes, D.E., “Monitoring of IgG Antibody Thermal Stability by Micellar Electrokinetic Capillary Chromatography and Matrix-assisted Laser Desorption/ionization Mass Spectrometry,” Analytical Chemistry 67(20):3626-3632, American Chemical Society, United States (1995).
Bauer, S., et al., “Activation of NK Cells and T Cells by NKG2D, a Receptor for Stress-inducible MICA,” Science 285(5428):727-729, American Association for the Advancement of Science, United States (Jul. 1999).
Berge, S.M., et al., “Pharmaceutical Salts,” Journal of Pharmaceutical Sciences 66(1):1-19, Wiley, United States (Jan. 1977).
Biotechnology, Chemical, Pharmaceutical (BCP) Partnership Meeting (SPE Dan Kolker, Sep. 17, 2020; pp. 1-36).
Bird, R.E., et al., “Single-chain Antigen-binding Proteins,” Science 242(4877):423-426, Association for the Advancement of Science, United States (Oct. 1988).
Bloemen, P.G., et al., “Adhesion Molecules: A New Target for Immunoliposome-mediated Drug Delivery,” FEBS Letters 357(2):140-144, John Wiley & Sons Ltd, England (1995).
Bonnafous, C., et al., “Targeting MICA with Therapeutic Antibodies for the Treatment of Cancer”, Journal for Immunotherapy of Cancer, Biomed Central Ltd, United Kingdom, Nov. 7, 2013, vol. 1 (1), pp. P41, XP021167251.
Bordusa, F, “F C_N Protease Catalyzed Bond Formation Using,” Highlights in Bioorganic Chemistry 389-403, (2004).
Brennan, M., et al., “Preparation of Bispecific Antibodies by Chemical Recombination of Monoclonal Immunoglobulin G1 Fragments,” Science 229(4708):81-83, American Association for the Advancement of Science, United States (Jul. 1985).
Briscoe.P, et al.,“Delivery of superoxide dismutase to pulmonary epithelium via pH-sensitive liposomes,” American Journal of Physiology 268:L374-380, American Physiology Society (1995).
Brummell, D.A., et al., “Probing the Combining Site of an Anti-Carbohydrate Antibody by Saturation-Mutagenesis: Role of the Heavy-Chain CDR3 Residues,” Biochemistry 32(4):1180-1187, American Chemical Society, United States (1993).
Burks, E.A., et al., “In vitro Scanning Saturation Mutagenesis of an Antibody Binding Pocket,” Proceedings of the National Academy of Sciences USA 94(2):412-417, Plenum Publishing Corporation , United States (1997).
Chen, B., et al., “Influence of Histidine on the Stability and Physical Properties of a Fully Human Antibody in Aqueous and Solid Forms,” Pharmaceutical Research 20(12):1952-1960, Kluwer Academic, United States (2003).
Chen, J., et al., “B Cell Development in Mice That Lack One or Both Immunoglobulin Kappa Light Chain Genes,” The EMBO Journal 12(3):821-830, Wiley Blackwell, England (1993).
Chen, J., et al., “Immunoglobulin Gene Rearrangement in B Cell Deficient Mice Generated by Targeted Deletion of the JH Locus,” International Immunology 5(6):647-656, Oxford University Press, England (1993).
Cheung, R.C., et al., “Epitope-specific Antibody Response to the Surface Antigen of Duck Hepatitis B Virus in Infected Ducks,” Virology 176(2):546-552, Academic Press, United States (1990).
Choi, T.K., et al., “Transgenic Mice Containing a Human Heavy Chain Immunoglobulin Gene Fragment Cloned in a Yeast Artificial Chromosome,” Nature Genetics 4(2):117-123, Nature Pub. Co., United States (1993).
Cox, J.P., et al., “A Directory of Human Germ-line V kappa Segments Reveals a Strong Bias in their Usage,” European Journal of Immunology 24(4):827-836, Verlag Chemie GmbH, Germany (Apr. 1994).
Dall Acqua, W.F., et al., “Increasing the Affinity of a Human IgG1 for the Neonatal Fc Receptor: Biological Consequences,” The Journal of Immunology 169(9):5171-5180, American Association of Immunologists, United States (Nov. 2002).
Dall'Acqua, W.F., et al., “Properties of Human IgG1s Engineered for Enhanced Binding to the Neonatal Fc Receptor (FcRn),” The Journal of Biological Chemistry 281(33):23514-23524, American Society for Biochemistry and Molecular Biology, United States (2006).
De Graaf, A.J., et al., “Nonnatural Amino Acids for Site-specific Protein Conjugation,” Bioconjugate Chemistry 20(7):1281-1295, American Chemical Society, United States (2009).
Diefenbach, A., et al., “Ligands for the Murine NKG2D Receptor: Expression by Tumor Cells and Activation of NK Cells and Macrophages,”Nature Immunology, 1(2):119-126, Nature America Inc, United States (Aug. 2000).
Doubrovina, E.S.,et al., “Evasion From Nk Cell Immunity by Mhc Class I Chain-related Molecules Expressing Colon Adenocarcinoma,” Journal of Immunology, 171(12):6891-6899, American Association of Immunologists, United States, (Dec. 2003).
Dranoff, G., et al., “Vaccination With Irradiated Tumor Cells Engineered to Secrete Murine Granulocyte-macrophage Colony-stimulating Factor Stimulates Potent, Specific, and Long-lasting Anti-tumor Immunity,” Proceedings of the National Academy of Sciences of the United States of America 90(8):3539-3543, National Academy of Sciences, United States (1993).
Duquesnoy, R.J., et al., “Structurally Based Epitope Analysis of Major Histocompatibility Complex Class I-related Chain a (MICA) Antibody Specificity Patterns,” Human Immunology, 69(12):826-832, Elsevier/North-Holland, United States (Dec. 2008).
Fishwild, D.M., et al., “High-Avidity Human IgG Kappa Monoclonal Antibodies from a Novel Strain of Minilocus Transgenic Mice,” Nature Biotechnology 14(7):845-851, Nature America Publishing, United States (1996).
Frese, M.A. and Dierks, T., “Formylglycine Aldehyde Tag-protein Engineering Through a Novel Post-translational Modification,” Chembiochem 10(3):425-427, Wiley-VCH Verlag, Germany (2009).
Fulda, S., et al., “Smac Agonists Sensitize for Apo2I/TRAIL- or Anticancer Drug-induced Apoptosis and Induce Regression of Malignant Glioma in Vivo,” Nature Medicine 8(8):808-815, Nature Publishing Company, United States (2002).
Gala, F.A. and Morrison, S.L., “V Region Carbohydrate and Antibody Expression,” The Journal of Immunology 172(9):5489-5494, Williams & Wilkins, United States (2004).
Gautier, A., et al., “An Engineered Protein Tag for Multiprotein Labeling in Living Cells,” Chemistry & Biology 15(2):128-136, Elsevier, United States (2008).
Ghadially, H., et al., “MHC Class I Chain-related Protein A and B (MICA and MICB) are Predominantly Expressed Intracellularly in Tumour and Normal Tissue,” British Journal of Cancer, 116(9):1208-1217, Nature Publishing Group on behalf of Cancer Research UK, England, (Apr. 2017).
Ghirlando, R., et al., “Glycosylation of Human IgG-Fc: Influences on Structure Revealed by Differential Scanning Micro-Calorimetry,” Immunology Letters 68(1):47-52, Elsevier/North-Holland Biomedical Press, Netherlands (1999).
Girlanda, S., et al., “MICA Expressed by Multiple Myeloma and Monoclonal Gammopathy of Undetermined Significance Plasma Cells Costimulates Pamidronate-activated Gammadelta Lymphocytes,” Cancer Research, 65(16):7502-7508, American Association for Cancer Research, United States (Aug. 2005).
Glennie, M.J., et al., “Preparation and Performance of Bispecific F(Ab' Gamma)2 Antibody Containing Thioether-linked Fab' Gamma Fragments,” Journal of Immunology 139(7):2367-2375, American Association of Immunologists, United States (1987).
Greenberg, P.D. and Riddell, S.R., “Deficient Cellular Immunity-Finding and Fixing the Defects,” Science 285(5427):546-551, American Association for the Advancement of Science, United States (1999).
Groh, V., et al., “Broad Tumor-associated Expression and Recognition by Tumor-derived Gamma Delta T Cells of MICA and MICB,” Proceedings of the National Academy of Sciences of the United States of America, 96(12):6879-6884, National Academy of Sciences, United States (Jun. 1999).
Groh, V., et al., “Cell Stress-regulated Human Major Histocompatibility Complex Class 1 Gene Expressed in Gastrointestinal Epithelium,” Proceedings of the National Academy of Sciences of the United States of America, 93(22):12445-12450, National Academy of Sciences, United States (Oct. 1996).
Groh, V., et al., “Costimulation of Cd8alphabeta T Cells by NKG2D via Engagement by Mic Induced on Virus-infected Cells,” Nature immunology, 2(3):255-260, Nature America Inc, United States , (Mar. 2001).
Groh, V., et al., “Efficient Cross-priming of Tumor Antigen-specific T Cells by Dendritic Cells Sensitized With Diverse Anti-mica Opsonized Tumor Cells,” Proceedings of the National Academy of Sciences of the United States of America, 102(18):6461-6466, National Academy of Sciences, United States, (May 2005).
Groh, V., et al., “Recognition of Stress-induced MHC Molecules by Intestinal Epithelial Gammadelta T Cells,” Science, 279(5357):1737-1740, American Association for the Advancement of Science, United States (Mar. 1998).
Groh, V., et al., “Tumour-derived Soluble MIC ligands Impair expression of NKG2D and T-cell Activation,” Nature, 419(6908):734-738, Nature Publishing Group, England (Oct. 2002).
Hackenberger, C.P. and Schwarzer, D., “Chemoselective Ligation and Modification Strategies for Peptides and Proteins,” Angewandte Chemie 47(52):10030-10074, Wiley-VCH, Germany (2008).
Hahne, M., et al., “Melanoma Cell Expression of Fas(Apo-1/CD95) Ligand: Implications for Tumor Immune Escape,” Science 274(5291):1363-1366, American Association forthe Advancement of Science, United States (1996).
Harding, F.A. and Lonberg, N., “Class Switching in Human Immunoglobulin Transgenic Mice,” Annals of the New York Academy of Sciences 764:536-546, The Academy, United States (1995).
He, Y-F., et al., “Blocking Programmed Death-1 Ligand-PD-1 Interactions by Local Gene Therapy Results in Enhancement of Antitumor Effect of Secondary Lymphoid Tissue Chemokine,” The Journal of Immunology 173(8):4919-4928, The American Association of Immunologists, United States (Oct. 2004).
Herbst, R.S., et al., “A Study of MPDL3280A, an Engineered PD-L1 Antibody in Patients with Locally Advanced or Metastatic Tumors,” Journal of Clinical Oncology 31 (Suppl):Abstract 3000, American Society of Clinical Oncology, United States (2013).
Hinton, P.R., et al., “An Engineered Human IgG1 Antibody with Longer Serum Half-Life,” Journal of Immunology 176(1):346-356, American Association of Immunologists, United States (2006).
Hinton, P.R., et al., “Engineered Human IgG Antibodies With Longer Serum Half-lives in Primates,” The Journal of Biological Chemistry 279(8):6213-6216, American Society for Biochemistry and Molecular Biology, United States (2004).
Howard, M. and Ogarra, A., “Biological Properties of Interleukin 10,” Immunology Today 13(6):198-200, Elsevier Science Publishers, England (1992).
Huang et al. (Analytical and Bioanalytical Chemistry (2020) 412:1693-1700).
Hue, S., et al., “Potential Role of NKG2D/MHC Class I-related Chain a Interaction in Intrathymic Maturation of Single-positive CD8 T Cells,” Journal of Immunology, 171(4):1909-1917, American Association of Immunologists, United States (Aug. 2003).
Huston, J.S., et al., “Protein Engineering of Antibody Binding Sites: Recovery of Specific Activity in an Anti-digoxin Single-chain Fv Analogue Produced in Escherichia coli,” Proceedings of the National Academy of Sciences USA 85(16):5879-5883, National Academy of Sciences, United States (Aug. 1988).
Hutloff, A., et al., “ICOS is an Inducible T-cell Co-stimulator Structurally and Functionally Related to CD28,” Nature 397(6716):263-266, Nature Publishing Group, England (Jan. 1999).
Hyer, M.L., et al., “Synthetic Triterpenoids Cooperate With Tumor Necrosis Factor-related Apoptosis-inducing Ligand to Induce Apoptosis of Breast Cancer Cells,” Cancer Research 65(11):4799-4808, American Association for Cancer Research, United States (2005).
Idusogie, E.E., et al., “Engineered Antibodies with Increased Activity to Recruit Complement,” The Journal of Immunology 166(4):2571-2575, American Association of Immunologists, United States (2001).
International Search Report and Written Opinion for Application No. PCT/US2019/023693, dated Sep. 13, 2019, 23 pages.
Jefferis, R., et al., “Human Immunoglobulin Allotypes: Possible Implications for Immunogenicity,” Mabs 1(4):332-338, Taylor & Francis, United States (Jul.-Aug. 2009).
Jinushi, M., et al., “Therapy-Induced Antibodies to MHC Class I Chain-Related Protein A Antagonize Immune Suppression and Stimulate Antitumor Cytotoxicity,” Proceedings of the National Academy of Sciences of the United States of America, 103(24):9190-9195, National Academy of Sciences, United States, (Jun. 2006).
Jones, P.T., et al., “Replacing the Complementarity-determining Regions in a Human Antibody with those from a Mouse,” Nature 321(6069):522-525, Nature Publishing Group, England (May 1986).
Jordan, P.A., et al., “A role for the Thiol Isomerase Protein ERP5 in Platelet Function,” Blood, 105(4):1500-1507, American Society of Hematology, United States (Feb. 2005).
Kabat, E.A., et al., “Sequences of Proteins of Immunological Interest,” 5th Edition, U.S. Department of Public Health and Human Services, Public Health Service, NIH publication No. 91-3242, National Institutes of Health, Bethesda (1991).
Kaiser, BK., et al., “Disulphide-isomerase-enabled Shedding of tumour-associated NKG2D ligands,”Nature, 447(7143):482-486, Nature Publishing Group, England (May 2007).
Karpovsky, B., et al., “Production of Target-specific Effector Cells Using Hetero-cross-linked Aggregates Containing Anti-target Cell and Anti-fc Gamma Receptor Antibodies,” The Journal of Experimental Medicine 160(6):1686-1701, Rockefeller University Press, United States (1984).
Kaufman, R.J. and Sharp, P.A., “Amplification and Expression of Sequences Cotransfected with a Modular Dihydrofolate Reductase Complementary DNA Gene,” Journal of Molecular Biology 159(4):601-621, Academic Press, Inc. Ltd., England (Aug. 1982).
Kehrl, J.H., et al., “Production of Transforming Growth Factor Beta by Human T Lymphocytes and its Potential Role in the Regulation of T Cell Growth,” The Journal of Experimental Medicine 163(5):1037-1050, Rockefeller University Press, United States (1986).
Keinanen, K. and Laukkanen, M.L., “Biosynthetic Lipid-tagging of Antibodies,” FEBS Letters 346(1):123-126, John Wiley & Sons Ltd, England (1994).
Killion, J.J. and Fidler, I.J., “Systemic Targeting of Liposome-encapsulated Immunomodulators to Macrophages for Treatment of Cancer Metastasis,” ImmunoMethods 4(3):273-279, Academic Presss, United States (1994).
Kim, N.W., et al., “Specific Association of Human Telomerase Activity With Immortal Cells and Cancer,” Science 266(5193):2011-2015, American Association for the Advancement of Science, United States (1994).
Kirkland, T.N., et al., “Analysis of the Fine Specificity and Cross-reactivity of Monoclonal Anti-lipid A Antibodies,” Journal of Microbiology 137(11):3614-3619, Microbiological Society of Korea, Korea (1986).
Kobayashi, H., et al., “Tryptophan H33 Plays an Important Role in Pyrimidine (6-4) Pyrimidone Photoproduct Binding by a High-Affinity Antibody,” Protein Engineering Design and Selection 12(10):879-884, Oxford University Press, United States (1999).
Koguchi, Y., et al., “Serum Immunoregulatory Proteins as Predictors of Overall Survival of Metastatic Melanoma Patients Treated With Ipilimumab,” Cancer Research, 75(23):5084-5092, American Association for Cancer Research, United States (Dec. 2015).
Kohler, G. and Milstein, C., “Continuous Cultures of Fused Cells Secreting Antibody of Predefined Specificity,” Nature 256(5517):495-497, Macmillan Journals Ltd., England (Aug. 1975).
Kostelny, S.A., et al., “Formation of a Bispecific Antibody by the Use of Leucine Zippers,” The Journal of Immunology 148(5):1547-1553, American Association of Immunologists, United States (Mar. 1992).
Krishnamurthy, R. and Manning, M.C., “The Stability Factor: Importance in Formulation Development,” Current Pharmaceutical Biotechnology 3(4):361-371, Bentham Science Publishers, Netherlands (2002).
Kugler, A., et al., , “Regression of Human Metastatic Renal Cell Carcinoma After Vaccination with Tumor Cell-Dendritic Cell Hybrids,” Nature Medicine 6(3):332-336, Nature Publishing Company, United States (2000).
Kuroiwa, Y., et al., “Cloned Transchromosomic Calves Producing Human Immunoglobulin,” Nature Biotechnology 20(9):889-894, Nature America Publishing, United States (2002).
Liu, G., et al., “Perturbation of NK Cell Peripheral Homeostasis Accelerates Prostate Carcinoma Metastasis,” Journal of Clinical Investigation, 123(10):4410-4422, American Society for Clinical Investigation, United States, (Oct. 2013).
Liu, G., et al., “Perturbation of NK Cell Peripheral Homeostasis Accelerates Prostate Carcinoma Metastasis,” Journal of Clinical Investigation, 123(10):Supplement Material, American Society for Clinical Investigation, United States, (Oct. 2013), 13 pages.
Liu, M.A., et al., “Heteroantibody Duplexes Target Cells for Lysis by Cytotoxic T Lymphocytes,” Proceedings of the National Academy of Sciences of the United States of America 82(24):8648-8652, National Academy of Sciences, United States (1985).
Liu, S.Y., et al., “Ongoing Clinical Trials of PD-1 and PD-L1 Inhibitors for Lung Cancer in China,”Journal of Hematology & Oncology, 10(1):136, Biomed Central, England (Jul. 2017).
Lonberg, N. and Huszar, D., “Human Antibodies from Transgenic Mice,” International Reviews of Immunology 13(1):65-93, Informa Healthcare, England (1995).
Lonberg, N., et al., “Antigen-specific Human Antibodies from Mice Comprising Four Distinct Genetic Modifications,” Nature 368(6474):856-859, Nature Publishing Group, United States (Apr. 1994).
Lonberg, N., “Handbook of Experimental Pharmacology,” The Pharmacology of Monoclonal Antibodies 113:49-101 (1994).
Lonberg, N., “Human Antibodies from Transgenic Animals,” Nature Biotechnology 23(9):1117-1125, Nature Publishing Group, United Kingdom (2005).
Marshall, R.D., “Glycoproteins,” Annual Review of Biochemistry 41:673-702, Annual Reviews, United States (1972).
Marten, A., et al., “Soluble MIC is Elevated in the Serum of Patients with Pancreatic Carcinoma Diminishing γδ T Cell Cytotoxicity,” International Journal of Cancer, 119(10):2359-2365, Wiley-Liss, Inc, United States (Nov. 2006).
McCafferty, J., et al., “Phage Antibodies: Filamentous Phage Displaying Antibody Variable Domains,” Nature 348(6301):552-554, Nature Publishing Group, London (Dec. 1990).
Melero, I., et al., “Monoclonal Antibodies Against the 4-1BB T-cell Activation Molecule Eradicate Established Tumors,” Nature Medicine 3(6):682-685, Nature Publishing Company, United States (1997).
Meyers, E., et al., “Optical Alignments in linear space,” Computer Applications in the Biosciences 4(1):11-17, Oxford University Press, England (1989).
Mimura, Y., et al., “The Influence of Glycosylation on the Thermal Stability and Effector Function Expression of Human IgG1-Fc: Properties of a Series of Truncated Glycoforms,” Molecular Immunology 37(12-13):697-706, Pergamon Press, England (2000).
Mokyr, M.B., et al., “Realization of the Therapeutic Potential of CTLA-4 Blockade in Low-dose Chemotherapy-treated Tumor-bearing Mice,” Cancer Research 58(23):5301-5304, American Association for Cancer Research, United States (1998).
Moldenhauer, G., et al., “Identity of HML-1 Antigen on Intestinal Intraepithelial T Cells and of B-ly7 Antigen on Hairy Cell Leukaemia,” Scandinavian Journal of Immunology 32(2):77-82, Blackwell Scientific Publications, England (1990).
Morel, G.A., et al., “Monoclonal Antibodies to Bovine Serum Albumin: Affinity and Specificity Determinations,” Molecular Immunology 25(1):7-15, Pergamon Press, England (1988).
Morrison, S.L., “Transfectomas Provide Novel Chimeric Antibodies,” Science 229(4719):1202-1207, Association for the Advancement of Science, United States (Sep. 1985).
Mossner, E., et al., “Increasing the Efficacy of CD20 Antibody Therapy through the Engineering of a NewType II anti-CD20 Antibody with Enhanced Direct and Immune Effector Cell-Mediated B-Cell Cytotoxicity,” Blood 115(22):4393-4402, American Society of Hematology, United States (2010).
Murray, A., et al., “Epitope Affinity Chromatography and Biophysical Studies of Monoclonal Antibodies and Recombinant Antibody Fragments,” Journal of Chromatographic Science 40(6):343-349, Oxford University Press, United States (2002).
Natsume, A., et al., “Improving Effector Functions of Antibodies for Cancer Treatment: Enhancing ADCC and CDC,” Drug Design, Development and Therapy 3:7-16, Dove Press Limited, New Zealand (2009).
Needleman, S.B and Wunsch, C.D, “A General Method Applicable to the Search for Similarities in the Amino Acid Sequence of Two Proteins,” Journal of Molecular Biology, 48(3):443-453, Elsevier, England, (Mar. 1970).
Nestle, F.O., et al., “Vaccination of Melanoma Patients with Peptide- or Tumor Lysate-Pulsed Dendritic Cells,” Nature Medicine 4(3):328-332, Nature Publishing Company, United States (1998).
Nimmerjahn, F. and Ravetch, J.V., “Divergent Immunoglobulin G Subclass Activity Through Selective Fc Receptor Binding,” Science 310(5753):1510-1512, American Association for the Advancement of Science, United States (2005).
Norberto, W., et al., “Identification of MICA as a New Polymorphic Alloantigen Recognized by Antibodies in Sera of Organ Transplant Recipients,” Human Immunology, 61(9): 917-924,Elsevier Science INC, United States (Sep. 2000).
Nordstrom, J. L., et al., “Anti-Tumor Activity and Toxicokinetics Analysis of MGAH22, an Anti-HER2 Monoclonal Antibody with Enhanced Fcγ Receptor Binding Properties,” Breast Cancer Research 13(6):R123, BioMed Central Ltd, England (2011).
Owais, M., et al., “Chloroquine Encapsulated in Malaria-infected Erythrocyte-specific Antibody-bearing Liposomes Effectively Controls Chloroquine-resistant Plasmodium Berghei Infections in Mice,” Antimicrobial Agents and Chemotherapy 39(1):180-184, American Society for Microbiology, United States (1995).
Parekh, R.B., et al., “Association of Rheumatoid Arthritis and Primary Osteoarthritis with Changes in the Glycosylation Pattern of Total Serum IgG,” Nature 316(6027):452-457, Nature Publishing Group, England (1985).
Paulus, H., et al., “Preparation and Biomedical Applications of Bispecific Antibodies,” Behring Institute Mitteilungen 78:118-132, Behringwerke Ag, Germany (1985).
Queen, C., et al., “A Humanized Antibody that Binds to the Interleukin 2 Receptor,” Proceedings of the National Academy of Sciences USA 86(24):10029-10033, National Academy of Sciences, United States (Dec. 1989).
Ranade. V,V., “Drug Delivery Systems. 1. Site-specific Drug Delivery Using Liposomes as Carriers,” Journal of Clinical Pharmacology 29(8):685-694, Wiley, England (1989).
Ren, H., et al., “A Biocompatible Condensation Reaction for the Labeling of Terminal Cysteine Residues on Proteins,” Angewandte Chemie 48(51):9658-9662, Wiley-VCH, Germany (2009).
Restifo, N. and Sznol, M., “Cancer: Principles and Practice of Oncology,” Cancer Vaccines, Chapter 61, 5th ed., pp. 3023-3043, DeVita et al. (ed.) 1997.
Ribas, A., “Anti-CTLA4 Antibody Clinical Trials in Melanoma,” Update on Cancer Therapeutics 2(3):133-139, Elsevier, Ltd, England (Sep. 2007).
Richards, J.O., et al., “Optimization of Antibody Binding to FcgammaRIIa Enhances Macrophage Phagocytosis of Tumor Cells,” Molecular Cancer Therapeutics 7(8):2517-2527, American Association for Cancer Research, United States (2008).
Ridge J.P., et al., “A Conditioned Dendritic Cell can be a Temporal Bridge Between a CD4+ T-helper and a T-killer Cell,” Nature 393(6684):474-478, Nature Publishing Group, England (1998).
Riechmann, L., et al., “Reshaping Human Antibodies for Therapy,” Nature 332(6162):323-327, Nature Publishing Group, United States (Mar. 1988).
Rosenberg, S.A., “A New Era for Cancer Immunotherapy Based on the Genes That Encode Cancer Antigens,” Immunity 10(3):281-287, Cell Press, United States (1999).
Salih, H.R., et al., “Functional Expression and Release of Ligands for the Activating Immunoreceptor NKG2D in Leukemia,” Blood, 102(4):1389-1396, American Society of Hematology, United States (Aug. 2003).
Salih, HR., et al., “Cutting Edge: Down-regulation of MICA on Human Tumors by Proteolytic Shedding,” Journal of Immunology, 169(8):4098-4102, American Association of Immunologists, United States , (Oct. 2002).
Sarmay, G., et al., “Mapping and Comparison of the Interaction Sites on the Fc Region of IgG Responsible for Triggering Antibody Dependent Cellular Cytotoxicity (ADCC) Through Different Types of Human Fc Gamma Receptor,” Molecular Immunology 29(5):633-639, Pergamon Press, England (1992).
Schaer, D.A., et al., “Modulation of GITR for Cancer Immunotherapy,” Current Opinion in Immunology 24(2):217-224, Elsevier Ltd., England (Apr. 2012).
Schreier, H., et al., “Targeting of Liposomes to Cells Expressing CD4 Using Glycosylphosphatidylinositol-anchored gp120. Influence of Liposome Composition on Intracellular Trafficking,” The Journal of Biological Chemistry 269(12):9090-9098, American Society for Biochemistry and Molecular Biology, United States (1994).
Senter, P.D., “Potent Antibody Drug Conjugates for Cancer Therapy,” Current Opinion in Chemical Biology 13(3):235-244, Elsevier, England (2009).
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, American Society for Biochemistry and Molecular Biology, United States (Mar. 2001).
Shields, R.L., et al., “Lack of Fucose on Human IgG1 N-linked Oligosaccharide Improves Binding to Human Fcgamma RIII and Antibody-Dependent Cellular Toxicity,” The Journal of Biological Chemistry 277(30):26733-26740, American Society for Biochemistry and Molecular Biology, United States (2002).
Smith,P., et al., “Mouse Model Recapitulating Human Fcγ Receptor Structural and Functional Diversity,” Proceedings of the National Academy of Sciences of the United States of America 109(16):6181-6186, National Academy of Sciences, United States (2012).
Songsivilai, S. and Lachmann, P.J., “Bispecific Antibody: A Tool for Diagnosis and Treatment of Disease,” Clinical and Experimental Immunology 79(3):315-321, Blackwell Scientific Publications, England (1990).
Spear, P., et al., “NKG2D Ligands as Therapeutic Targets,” Cancer Immunology, 13: 8, Cancer Research Institute, United States (May 2013).
Spiro, R.G., “Protein Glycosylation: Nature, Distribution, Enzymatic Formation, and Disease Implications of Glycopeptide Bonds,” Glycobiology 12(4):43R-56R, IRL Press at Oxford University Press, England (2002).
Stahli, C., et al., “Distinction of Epitopes by Monoclonal Antibodies.,” Methods in Enzymology 92:242-253, Academic Press, United States (1983).
Stavenhagen, J.B., et al., “Fc Optimization of Therapeutic Antibodies Enhances Their Ability to Kill Tumor Cells in Vitro and Controls Tumor Expansion in Vivo via Low-affinity Activating Fcgamma Receptors,” Cancer Research 67(18):8882-8890, American Association for Cancer Research, United States (2007).
Steinle, A., et al., “Diversification, Expression, and γδ T Cell Recognition of Evolutionarily Distant Members of the MIC Family of Major Histocompatibility Complex Class I-related Molecules,” Immunology and Proceedings of the National Academy of Sciences of the United States of America, 95(21):12510-12515, National Academy of Sciences,United States (Oct. 1998).
Steinle, A., et al., “Interactions of Human NKG2D with its Ligands MICA, MICB, and Homologs of the Mouse RAE-1 Protein Family,” Immunogenetics, 53(4):279-287, Springer-Verlag, United States (May-Jun. 2001).
Strohl, W.R., “Optimization of Fc-mediated Effector Functions of Monoclonal Antibodies,” Current Opinion in Biotechnology 20(6):685-691, Elsevier, England (2009).
Sunbul, M. and Yin, J., “Site Specific Protein Labeling by Enzymatic Posttranslational Modification,” Organic & Biomolecular Chemistry 7(17):3361-3371, Royal Society of Chemistry, England (2009).
Suto, R. and Srivastava, P.K., “A Mechanism for the Specific Immunogenicity of Heat Shock Protein-chaperoned Peptides,” Science 269(5230):1585-1588, American Association for the Advancement of Science, United States (1995).
Takebe, T., et al., “SR Alpha Promoter: An Efficient and Versatile Mammalian Cdna Expression System Composed of the Simian Virus 40 Early Promoter and the R-U5 Segment of Human T-Cell Leukemia Virus Type 1 Long Terminal Repeat,” Molecular and Cell Biology 8(1):466-472, American Society for Microbiology, United States (1988).
Taki, M., et al., “Transglutaminase-mediated N- and C-terminal Fluorescein Labeling of a Protein can Support the Native Activity of the Modified Protein,” Protein Engineering, Design & Selection 17(2):119-126, Oxford University Press, England (2004).
Tamura, Y., et al., “Immunotherapy of Tumors with Autologous Tumor-derived Heat Shock Protein Preparations,” Science 278(5335):117-120, American Association for the Advancement of Science, United States (1997).
Tarentino, A.L., et al., “The Isolation and Structure of the Core Oligosaccharide Sequences of IgM,” Biochemistry 14(25):5516-5523, American Chemical Society, United States (Dec. 1975).
Taylor, E.V., et al., , “Native Chemical Ligation: SemiSynthesis of Post-translationally Modified Proteins and Biological Probes,” Protein Engineering, 22:65-96, (2009).
Taylor, L.D., et al., “A Transgenic Mouse that Expresses a Diversity of Human Sequence Heavy and Light Chain Immunoglobulins,” Nucleic Acids Research 20(23):6287-6295, Oxford University Press, England (1992).
Taylor, L.D., et al., “Human Immunoglobulin Transgenes Undergo Rearrangement, Somatic Mutation and Class Switching in Mice that Lack Endogenous IgM,” International Immunology 6(4):579-591, University Press, England (1994).
Tomizuka, K., et al., “Double Trans-chromosomic Mice: Maintenance of Two Individual Human Chromosome Fragments Containing lg Heavy and kappa loci and Expression of Fully Human Antibodies,” Proceedings of the National Academy of Sciences USA 97(2):722-727, National Academy of Sciences, United States (Jan. 2000).
Tomlinson, I.M., et al., “The Repertoire of Human Germline VH Sequences Reveals about Fifty Groups of VH Segments with Different Hypervariable Loops,” Journal of Molecular Biology 227(3):776-798, Elsevier, Netherlands (Oct. 1992).
Tuaillon, N., et al., “Biased Utilization of DHQ52 and JH4 Gene Segments in a Human Ig Transgenic Minilocus is Independent of Antigenic Selection,” The Journal of Immunology 152(6):2912-2920, Williams & Wilkins, United States (1994).
Tuaillon, N., et al., “Human Immunoglobulin Heavy-chain Minilocus Recombination in Transgenic Mice: Gene-segment Use in Mu and Gamma Transcripts,” Proceedings of the National Academy of Sciences of the United States of America 90(8):3720-3724, National Academy of Sciences, United States (1993).
Umana, P., et al., “Engineered Glycoforms of an Antineuroblastoma IgG1 with Optimized Antibody-Dependent Cellular Cytotoxic Activity,” Nature Biotechnology 17(2):176-180, Nature America Publishing, United States (1999).
Umezawa, F. and Eto. Y., “Liposome Targeting to Mouse Brain: Mannose as a Recognition Marker,” Biochemical and Biophysical Research Communications 153(3):1038-1044, Elsevier, United States (1988).
Urlaub, G. and Chasin, L.A., “Isolation of Chinese Hamster Cell Mutants Deficient in Dihydrofolate Reductase Activity,” Proceedings of the National Academy of Sciences USA 77(7):4216-4220, National Academy of Sciences, United States (Jul. 1980).
Wallick, S.C., et al., “Glycosylation of a Vh Residue of a Monoclonal Antibody Against Alpha (1—-6) Dextran Increases its Affinity for Antigen,” The Journal of Experimental Medicine 168(3):1099-1109, Rockefeller University Press, United States (1988).
Wang, C., et al., “In Vitro Characterization of the Anti-PD-1 Antibody Nivolumab, BMS-936558, and in Vivo Toxicology in Non-human Primates,” Cancer Immunology Research 2(9):846-856, American Association for Cancer Research, United States (Sep. 2014).
Ward, E.S., et al., “Binding Activities of a Repertoire of Single Immunoglobulin Variable Domains Secreted from Escherichia coli,” Nature 341(6242):544-546, Nature Publishing Group, England (Oct. 1989).
Weinberg, A.D., et al., “Engagement of the OX-40 Receptor in Vivo Enhances Antitumor Immunity,” Journal of Immunology 164(4):2160-2169, American Association of Immunologists, United States (2000).
Yamane-Ohnuki, N., et al., “Establishment of FUT8 Knockout Chinese Hamster Ovary Cells: An Ideal Host Cell Line for Producing Completely Defucosylated Antibodies with Enhanced Antibody-Dependent Cellular Cytotoxicity,” Biotechnology and Bioengineering 87(5):614-622, Wiley, United States (2004).
Yeung, Y.A., et al., “Engineering Human IgG1 Affinity to Human Neonatal Fc Receptor: Impact of Affinity Improvement on Pharmacokinetics in Primates,” Journal of Immunology 182(12):7663-7671, American Association of Immunologists, United States (2009).
Zhang, F., et al., “Structural Basis of a Novel PD-L1 Nanobody for Immune Checkpoint Blockade,”Cell Discovery, 3:17004, Nature Publishing Group, England (Mar. 2017).
Zhang, J., et al., “Antibody-Mediated Neutralization of Soluble MIC Significantly Enhances CTLA4 Blockade Therapy,” Science Advances, 3(5):e1602133, American Association for the Advancement of Science, United States (May 2017).
Zou, Y., et al., “MICA is a Target for Complement-Dependent Cytotoxicity With Mouse Monoclonal Antibodies and Human Alloantibodies,” Human Immunology, 63(1):30-39,Elsevier/North-Holland, United States (Jan. 2002).