BR112019010604A2 - proteína de ligação ao antígeno da membrana próstata-específico - Google Patents
proteína de ligação ao antígeno da membrana próstata-específico Download PDFInfo
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- BR112019010604A2 BR112019010604A2 BR112019010604A BR112019010604A BR112019010604A2 BR 112019010604 A2 BR112019010604 A2 BR 112019010604A2 BR 112019010604 A BR112019010604 A BR 112019010604A BR 112019010604 A BR112019010604 A BR 112019010604A BR 112019010604 A2 BR112019010604 A2 BR 112019010604A2
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- binding protein
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- prostate
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- membrane antigen
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| EP3589662A4 (en) | 2017-02-28 | 2020-12-30 | Harpoon Therapeutics, Inc. | INDUCTIBLE MONOVALENT ANTIGEN BINDING PROTEIN |
| CN113896792B (zh) | 2017-05-12 | 2025-08-22 | 哈普恩治疗公司 | 间皮素结合蛋白质 |
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| KR102425983B1 (ko) | 2017-10-13 | 2022-07-29 | 하푼 테라퓨틱스, 인크. | 삼중특이적 단백질 및 사용 방법 |
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| IL299748A (en) * | 2020-07-08 | 2023-03-01 | Lava Therapeutics N V | Antibodies that bind PSMA and T gamma delta receptors |
| CN117957256A (zh) | 2021-06-17 | 2024-04-30 | 勃林格殷格翰国际有限公司 | 新颖三特异性结合分子 |
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|---|---|---|---|---|
| FR901228A (fr) | 1943-01-16 | 1945-07-20 | Deutsche Edelstahlwerke Ag | Système d'aimant à entrefer annulaire |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| US6548640B1 (en) | 1986-03-27 | 2003-04-15 | Btg International Limited | Altered antibodies |
| GB8607679D0 (en) | 1986-03-27 | 1986-04-30 | Winter G P | Recombinant dna product |
| US5858358A (en) | 1992-04-07 | 1999-01-12 | The United States Of America As Represented By The Secretary Of The Navy | Methods for selectively stimulating proliferation of T cells |
| US6534055B1 (en) | 1988-11-23 | 2003-03-18 | Genetics Institute, Inc. | Methods for selectively stimulating proliferation of T cells |
| US6352694B1 (en) | 1994-06-03 | 2002-03-05 | Genetics Institute, Inc. | Methods for inducing a population of T cells to proliferate using agents which recognize TCR/CD3 and ligands which stimulate an accessory molecule on the surface of the T cells |
| US6905680B2 (en) | 1988-11-23 | 2005-06-14 | Genetics Institute, Inc. | Methods of treating HIV infected subjects |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US5703055A (en) | 1989-03-21 | 1997-12-30 | Wisconsin Alumni Research Foundation | Generation of antibodies through lipid mediated DNA delivery |
| US5399346A (en) | 1989-06-14 | 1995-03-21 | The United States Of America As Represented By The Department Of Health And Human Services | Gene therapy |
| US5585362A (en) | 1989-08-22 | 1996-12-17 | The Regents Of The University Of Michigan | Adenovirus vectors for gene therapy |
| US5859205A (en) | 1989-12-21 | 1999-01-12 | Celltech Limited | Humanised antibodies |
| GB8928874D0 (en) | 1989-12-21 | 1990-02-28 | Celltech Ltd | Humanised antibodies |
| US5061620A (en) | 1990-03-30 | 1991-10-29 | Systemix, Inc. | Human hematopoietic stem cell |
| EP0519596B1 (en) | 1991-05-17 | 2005-02-23 | Merck & Co. Inc. | A method for reducing the immunogenicity of antibody variable domains |
| US5199942A (en) | 1991-06-07 | 1993-04-06 | Immunex Corporation | Method for improving autologous transplantation |
| CA2103059C (en) | 1991-06-14 | 2005-03-22 | Paul J. Carter | Method for making humanized antibodies |
| US5565332A (en) | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| AU2764792A (en) | 1991-10-04 | 1993-05-03 | Iit Research Institute | Conversion of plastic waste to useful oils |
| GB9125768D0 (en) | 1991-12-04 | 1992-02-05 | Hale Geoffrey | Therapeutic method |
| WO1993011794A1 (en) | 1991-12-13 | 1993-06-24 | Xoma Corporation | Methods and materials for preparation of modified antibody variable domains and therapeutic uses thereof |
| US6005079A (en) | 1992-08-21 | 1999-12-21 | Vrije Universiteit Brussels | Immunoglobulins devoid of light chains |
| ATE427968T1 (de) | 1992-08-21 | 2009-04-15 | Univ Bruxelles | Immunoglobuline ohne leichtkette |
| US5350674A (en) | 1992-09-04 | 1994-09-27 | Becton, Dickinson And Company | Intrinsic factor - horse peroxidase conjugates and a method for increasing the stability thereof |
| US5639641A (en) | 1992-09-09 | 1997-06-17 | Immunogen Inc. | Resurfacing of rodent antibodies |
| US7175843B2 (en) | 1994-06-03 | 2007-02-13 | Genetics Institute, Llc | Methods for selectively stimulating proliferation of T cells |
| US5731168A (en) | 1995-03-01 | 1998-03-24 | Genentech, Inc. | Method for making heteromultimeric polypeptides |
| US6692964B1 (en) | 1995-05-04 | 2004-02-17 | The United States Of America As Represented By The Secretary Of The Navy | Methods for transfecting T cells |
| US7067318B2 (en) | 1995-06-07 | 2006-06-27 | The Regents Of The University Of Michigan | Methods for transfecting T cells |
| US5773292A (en) | 1995-06-05 | 1998-06-30 | Cornell University | Antibodies binding portions, and probes recognizing an antigen of prostate epithelial cells but not antigens circulating in the blood |
| US6136311A (en) | 1996-05-06 | 2000-10-24 | Cornell Research Foundation, Inc. | Treatment and diagnosis of cancer |
| US6107090A (en) | 1996-05-06 | 2000-08-22 | Cornell Research Foundation, Inc. | Treatment and diagnosis of prostate cancer with antibodies to extracellur PSMA domains |
| EP1027439B1 (en) | 1997-10-27 | 2010-03-17 | Bac Ip B.V. | Multivalent antigen-binding proteins |
| BR9907241A (pt) | 1998-01-26 | 2000-10-17 | Unilever Nv | Biblioteca de expressão, processo para preparar a mesma, uso de uma fonte não imunizada de sequências de ácido nucleico, e, processos para preparar fragmentos de anticorpos e, para preparar um anticorpo |
| CZ121599A3 (cs) | 1998-04-09 | 1999-10-13 | Aventis Pharma Deutschland Gmbh | Jednořetězcová molekula vázající několik antigenů, způsob její přípravy a léčivo obsahující tuto molekulu |
| ATE276359T1 (de) | 1999-01-19 | 2004-10-15 | Unilever Nv | Verfahren zur herstellung von antikörperfragmenten |
| US6326193B1 (en) | 1999-11-05 | 2001-12-04 | Cambria Biosciences, Llc | Insect control agent |
| US20060228364A1 (en) | 1999-12-24 | 2006-10-12 | Genentech, Inc. | Serum albumin binding peptides for tumor targeting |
| US7572631B2 (en) | 2000-02-24 | 2009-08-11 | Invitrogen Corporation | Activation and expansion of T cells |
| US6797514B2 (en) | 2000-02-24 | 2004-09-28 | Xcyte Therapies, Inc. | Simultaneous stimulation and concentration of cells |
| HK1047770A1 (zh) | 2000-02-24 | 2003-03-07 | Xcyte Therapies, Inc. | 细胞的同时刺激与浓缩 |
| US6867041B2 (en) | 2000-02-24 | 2005-03-15 | Xcyte Therapies, Inc. | Simultaneous stimulation and concentration of cells |
| CA2380443C (en) | 2000-05-26 | 2013-03-12 | Ginette Dubuc | Single-domain antigen-binding antibody fragments derived from llama antibodies |
| WO2001096584A2 (en) | 2000-06-12 | 2001-12-20 | Akkadix Corporation | Materials and methods for the control of nematodes |
| CN1294148C (zh) | 2001-04-11 | 2007-01-10 | 中国科学院遗传与发育生物学研究所 | 环状单链三特异抗体 |
| GB0110029D0 (en) | 2001-04-24 | 2001-06-13 | Grosveld Frank | Transgenic animal |
| CN1195779C (zh) | 2001-05-24 | 2005-04-06 | 中国科学院遗传与发育生物学研究所 | 抗人卵巢癌抗人cd3双特异性抗体 |
| US7666414B2 (en) | 2001-06-01 | 2010-02-23 | Cornell Research Foundation, Inc. | Methods for treating prostate cancer using modified antibodies to prostate-specific membrane antigen |
| EP1433793A4 (en) | 2001-09-13 | 2006-01-25 | Inst Antibodies Co Ltd | METHOD FOR CREATING A CAMEL ANTIBODY LIBRARY |
| EP1448588A4 (en) | 2001-10-23 | 2006-10-25 | Psma Dev Company L L C | ANTIBODIES AND MULTIMERS OF PSMA PROTEINS |
| US20050215472A1 (en) | 2001-10-23 | 2005-09-29 | Psma Development Company, Llc | PSMA formulations and uses thereof |
| JP2005289809A (ja) | 2001-10-24 | 2005-10-20 | Vlaams Interuniversitair Inst Voor Biotechnologie Vzw (Vib Vzw) | 突然変異重鎖抗体 |
| AU2003224604B2 (en) | 2002-01-28 | 2007-06-14 | Medarex, Inc. | Human monoclonal antibodies to prostate specific membrane antigen (PSMA) |
| DE60305919T2 (de) | 2002-06-28 | 2007-01-18 | Domantis Limited, Cambridge | Dual-specifische liganden mit erhöhter halbwertszeit |
| US9321832B2 (en) | 2002-06-28 | 2016-04-26 | Domantis Limited | Ligand |
| NZ540219A (en) | 2002-11-07 | 2008-08-29 | Univ Erasmus | Fret probes and methods for detecting interacting molecules |
| PT2316852E (pt) | 2002-11-08 | 2014-06-23 | Ablynx Nv | Anticorpos de domínio único estáveis |
| US9320792B2 (en) | 2002-11-08 | 2016-04-26 | Ablynx N.V. | Pulmonary administration of immunoglobulin single variable domains and constructs thereof |
| EP1558650A2 (en) | 2002-11-08 | 2005-08-03 | Ablynx N.V. | Camelidae antibodies against immunoglobulin e and use thereof for the treatment of allergic disorders |
| NZ540194A (en) | 2002-11-08 | 2008-07-31 | Ablynx Nv | Single domain antibodies directed against tumour necrosis factor-alpha and uses therefor |
| GB0228210D0 (en) | 2002-12-03 | 2003-01-08 | Babraham Inst | Single chain antibodies |
| CA2523716C (en) | 2003-05-31 | 2014-11-25 | Micromet Ag | Human anti-human cd3 binding molecules |
| CA2531118C (en) | 2003-07-01 | 2013-01-08 | Immunomedics, Inc. | Multivalent carriers of bi-specific antibodies |
| US20050048617A1 (en) | 2003-08-18 | 2005-03-03 | Medimmune, Inc. | Humanization of antibodies |
| US20050042664A1 (en) | 2003-08-22 | 2005-02-24 | Medimmune, Inc. | Humanization of antibodies |
| CN100376599C (zh) | 2004-04-01 | 2008-03-26 | 北京安波特基因工程技术有限公司 | 基因工程重组抗cea抗cd3抗cd28线性单链三特异抗体 |
| BRPI0511755A (pt) | 2004-06-01 | 2008-01-02 | Domantis Ltd | composições, fusões e conjugados de drogas e métodos de produção, tratamento e utilização |
| WO2006020258A2 (en) | 2004-07-17 | 2006-02-23 | Imclone Systems Incorporated | Novel tetravalent bispecific antibody |
| EP1634603A1 (de) | 2004-08-26 | 2006-03-15 | Eberhard-Karls-Universität Tübingen Universitätsklinikum | Behandlung von transformierten oder infizierten biologischen Zellen |
| US20080069772A1 (en) | 2004-08-26 | 2008-03-20 | Eberhard-Karls-Universitaet Tuebingen Universitaetsklinikum | Treatment of transformed or infected biological cells |
| FR2879605B1 (fr) | 2004-12-16 | 2008-10-17 | Centre Nat Rech Scient Cnrse | Production de formats d'anticorps et applications immunologiques de ces formats |
| ATE414718T1 (de) | 2005-01-05 | 2008-12-15 | F Star Biotech Forsch & Entw | Synthetische immunoglobulindomänen mit in regionen des moleküls, die sich von den die komplementarität bestimmenden bereichen unterscheiden, modifizierten bindeeigenschaften |
| US7833979B2 (en) | 2005-04-22 | 2010-11-16 | Amgen Inc. | Toxin peptide therapeutic agents |
| US20060252096A1 (en) | 2005-04-26 | 2006-11-09 | Glycofi, Inc. | Single chain antibody with cleavable linker |
| CN103254309B (zh) | 2005-05-18 | 2017-09-26 | 埃博灵克斯股份有限公司 | 针对肿瘤坏死因子α的改进的纳米体TM |
| PL2444424T3 (pl) | 2005-05-20 | 2019-01-31 | Ablynx N.V. | Ulepszone Nanociała TM do leczenia zaburzeń, w których pośredniczy agregacja |
| EP1726650A1 (en) * | 2005-05-27 | 2006-11-29 | Universitätsklinikum Freiburg | Monoclonal antibodies and single chain antibody fragments against cell-surface prostate specific membrane antigen |
| AU2006283532B2 (en) | 2005-08-19 | 2012-04-26 | Abbvie Inc. | Dual variable domain immunoglobin and uses thereof |
| EP3770174A1 (en) | 2005-10-11 | 2021-01-27 | Amgen Research (Munich) GmbH | Compositions comprising cross-species-specific antibodies and uses thereof |
| WO2007062466A1 (en) | 2005-11-29 | 2007-06-07 | The University Of Sydney | Demibodies: dimerisation-activated therapeutic agents |
| WO2007115230A2 (en) | 2006-03-30 | 2007-10-11 | University Of Medicine And Dentistry Of New Jersey | A strategy for homo- or hetero-dimerization of various proteins in solutions and in cells |
| US20070269422A1 (en) | 2006-05-17 | 2007-11-22 | Ablynx N.V. | Serum albumin binding proteins with long half-lives |
| US8629244B2 (en) | 2006-08-18 | 2014-01-14 | Ablynx N.V. | Interleukin-6 receptor binding polypeptides |
| EP2069402A2 (en) | 2006-09-08 | 2009-06-17 | Ablynx N.V. | Serum albumin binding proteins with long half-lives |
| US20100166734A1 (en) | 2006-12-20 | 2010-07-01 | Edward Dolk | Oral delivery of polypeptides |
| PT2520590T (pt) | 2007-04-03 | 2018-11-14 | Amgen Res Munich Gmbh | Domínio de ligação específico de espécies cruzadas |
| NZ581097A (en) | 2007-05-24 | 2012-03-30 | Ablynx Nv | Amino acid sequences directed against rank-l and polypeptides comprising the same for the treatment of bone diseases and disorders |
| EP2014680A1 (en) | 2007-07-10 | 2009-01-14 | Friedrich-Alexander-Universität Erlangen-Nürnberg | Recombinant, single-chain, trivalent tri-specific or bi-specific antibody derivatives |
| JP6035009B2 (ja) | 2007-08-22 | 2016-11-30 | ザ リージェンツ オブ ザ ユニバーシティ オブ カリフォルニア | 活性化可能な結合ポリペプチドおよびその同定方法ならびに使用 |
| US20120039870A9 (en) | 2007-09-07 | 2012-02-16 | Ablynx N.V. | Binding molecules with multiple binding sites, compositions comprising the same and uses thereof |
| CA2700714C (en) | 2007-09-26 | 2018-09-11 | Ucb Pharma S.A. | Dual specificity antibody fusions |
| AU2009254501B2 (en) | 2008-06-05 | 2014-07-31 | Ablynx N.V. | Amino acid sequences directed against envelope proteins of a virus and polypeptides comprising the same for the treatment of viral diseases |
| US20100122358A1 (en) | 2008-06-06 | 2010-05-13 | Crescendo Biologics Limited | H-Chain-only antibodies |
| US8444976B2 (en) | 2008-07-02 | 2013-05-21 | Argen-X B.V. | Antigen binding polypeptides |
| US20110177070A1 (en) | 2008-07-02 | 2011-07-21 | Emergent Product Development Seatlle, LLC | TGF-Beta Antagonist Multi-Target Binding Proteins |
| EP2352765B1 (en) | 2008-10-01 | 2018-01-03 | Amgen Research (Munich) GmbH | Cross-species-specific single domain bispecific single chain antibody |
| CA2738566C (en) | 2008-10-01 | 2024-04-30 | Micromet Ag | Bispecific single chain antibodies with specificity for high molecular weight target antigens |
| DK2356153T3 (en) | 2008-10-01 | 2016-07-04 | Amgen Res Munich Gmbh | Bispecific single CHAIN PSMAXCD3 ANTIBODY THAT ARE SPECIFICALLY TO ALL SPECIES |
| US9327022B2 (en) | 2008-10-14 | 2016-05-03 | National Research Council Of Canada | BSA-specific antibodies |
| WO2010077643A1 (en) | 2008-12-08 | 2010-07-08 | Tegopharm Corporation | Masking ligands for reversible inhibition of multivalent compounds |
| EP2210902A1 (en) | 2009-01-14 | 2010-07-28 | TcL Pharma | Recombinant monovalent antibodies |
| TW201613969A (en) | 2009-03-05 | 2016-04-16 | Abbvie Inc | IL-17 binding proteins |
| UY32917A (es) | 2009-10-02 | 2011-04-29 | Boehringer Ingelheim Int | Moléculas de unión a dll-4 |
| WO2011051327A2 (en) | 2009-10-30 | 2011-05-05 | Novartis Ag | Small antibody-like single chain proteins |
| US10584181B2 (en) | 2009-12-04 | 2020-03-10 | Genentech, Inc. | Methods of making and using multispecific antibody panels and antibody analog panels |
| EP2332994A1 (en) | 2009-12-09 | 2011-06-15 | Friedrich-Alexander-Universität Erlangen-Nürnberg | Trispecific therapeutics against acute myeloid leukaemia |
| PT2519543T (pt) | 2009-12-29 | 2016-10-07 | Emergent Product Dev Seattle | Proteínas de ligação de heterodímero e suas utilizações |
| GB2476681B (en) | 2010-01-04 | 2012-04-04 | Argen X Bv | Humanized camelid VH, VK and VL immunoglobulin domains |
| EP2550529B1 (en) * | 2010-03-23 | 2021-11-17 | Iogenetics, LLC. | Bioinformatic processes for determination of peptide binding |
| US8937164B2 (en) | 2010-03-26 | 2015-01-20 | Ablynx N.V. | Biological materials related to CXCR7 |
| US9556273B2 (en) | 2010-03-29 | 2017-01-31 | Vib Vzw | Anti-macrophage mannose receptor single variable domains for targeting and in vivo imaging of tumor-associated macrophages |
| JP5753903B2 (ja) | 2010-08-24 | 2015-07-22 | ロシュ グリクアート アーゲー | 活性化可能な二重特異性抗体 |
| CN103068846B9 (zh) | 2010-08-24 | 2016-09-28 | 弗·哈夫曼-拉罗切有限公司 | 包含二硫键稳定性Fv片段的双特异性抗体 |
| EP2621953B1 (en) | 2010-09-30 | 2017-04-05 | Ablynx N.V. | Biological materials related to c-met |
| JP2014500879A (ja) | 2010-11-16 | 2014-01-16 | ベーリンガー インゲルハイム インターナショナル ゲゼルシャフト ミット ベシュレンクテル ハフツング | Ｂｃｍａ発現に相関性を有する疾患を治療する因子及び方法 |
| WO2012131053A1 (en) | 2011-03-30 | 2012-10-04 | Ablynx Nv | Methods of treating immune disorders with single domain antibodies against tnf-alpha |
| CA2832540C (en) | 2011-04-08 | 2020-09-15 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Anti-epidermal growth factor receptor variant iii chimeric antigen receptors and use of same for the treatment of cancer |
| CN107903325B (zh) | 2011-05-16 | 2021-10-29 | 埃泰美德(香港)有限公司 | 多特异性fab融合蛋白及其使用方法 |
| UA117901C2 (uk) | 2011-07-06 | 2018-10-25 | Ґенмаб Б.В. | Спосіб посилення ефекторної функції вихідного поліпептиду, його варіанти та їх застосування |
| WO2013036130A1 (en) | 2011-09-09 | 2013-03-14 | Universiteit Utrecht Holding B.V. | Broadly neutralizing vhh against hiv-1 |
| US20140220017A1 (en) | 2011-09-23 | 2014-08-07 | Universitat Stuttgart | Serum half-life extension using igbd |
| TWI679212B (zh) | 2011-11-15 | 2019-12-11 | 美商安進股份有限公司 | 針對ｂｃｍａ之e3以及ｃｄ３的結合分子 |
| CN108034006A (zh) | 2012-01-13 | 2018-05-15 | 乌利班-马克西姆利安大学 | 双抗原诱导的双功能互补作用 |
| WO2013110531A1 (en) | 2012-01-23 | 2013-08-01 | Ablynx Nv | Sequences directed against hepatocyte growth factor (hgf) and polypeptides comprising the same for the treatment of cancers and/or tumors |
| SMT201700467T1 (it) | 2012-02-24 | 2017-11-15 | Abbvie Stemcentrx Llc | Modulatori di dll3 e metodi di uso |
| GB201203442D0 (en) | 2012-02-28 | 2012-04-11 | Univ Birmingham | Immunotherapeutic molecules and uses |
| EP2820047B1 (en) | 2012-03-01 | 2018-04-25 | Amgen Research (Munich) GmbH | Long life polypeptide binding molecules |
| US9975962B2 (en) | 2012-03-30 | 2018-05-22 | Bayer Healthcare Llc | Thrombin/plasmin-regulated antibodies that bind TFPI |
| CA2870545A1 (en) | 2012-04-20 | 2013-10-24 | Emergent Product Development Seattle, Llc | Cd3 binding polypeptides |
| WO2013192546A1 (en) | 2012-06-22 | 2013-12-27 | Cytomx Therapeutics, Inc. | Activatable antibodies having non-binding steric moieties and mehtods of using the same |
| US20140004121A1 (en) | 2012-06-27 | 2014-01-02 | Amgen Inc. | Anti-mesothelin binding proteins |
| CN103566377A (zh) | 2012-07-18 | 2014-02-12 | 上海博笛生物科技有限公司 | 癌症的靶向免疫治疗 |
| CN104583236A (zh) | 2012-08-31 | 2015-04-29 | 阿尔金-X有限公司 | 高度多样的组合抗体文库 |
| KR101963231B1 (ko) | 2012-09-11 | 2019-03-28 | 삼성전자주식회사 | 이중특이 항체의 제작을 위한 단백질 복합체 및 이를 이용한 이중특이 항체 제조 방법 |
| JOP20200236A1 (ar) | 2012-09-21 | 2017-06-16 | Regeneron Pharma | الأجسام المضادة لمضاد cd3 وجزيئات ربط الأنتيجين ثنائية التحديد التي تربط cd3 وcd20 واستخداماتها |
| WO2014052064A1 (en) | 2012-09-27 | 2014-04-03 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Mesothelin antibodies and methods for eliciting potent antitumor activity |
| JO3519B1 (ar) | 2013-01-25 | 2020-07-05 | Amgen Inc | تركيبات أجسام مضادة لأجل cdh19 و cd3 |
| US20160015749A1 (en) | 2013-03-05 | 2016-01-21 | Baylor College Of Medicine | Engager cells for immunotherapy |
| ES2746240T3 (es) | 2013-03-13 | 2020-03-05 | Health Research Inc | Composiciones y procedimientos para la utilización de receptores de células T recombinantes para el reconocimiento directo de un antígeno tumoral |
| EP2970484B2 (en) | 2013-03-15 | 2022-09-21 | Amgen Inc. | Heterodimeric bispecific antibodies |
| UY35484A (es) | 2013-03-15 | 2014-10-31 | Amgen Res Munich Gmbh | Molécula de unión de cadena simple que comprenden ABP de extremo N |
| US20140302037A1 (en) | 2013-03-15 | 2014-10-09 | Amgen Inc. | BISPECIFIC-Fc MOLECULES |
| BR112016001611B1 (pt) | 2013-07-25 | 2024-01-09 | Cytomx Therapeutics, Inc | Anticorpo ativável multiespecífico, uso terapêutico do mesmo, molécula de ácido nucleico isolada, vetor e método para produzir um anticorpo ativável multiespecífico |
| US9688727B2 (en) | 2013-09-24 | 2017-06-27 | University Of Washington | Desmoglein 2 (DSG2) binding proteins and uses therefor |
| WO2015044386A1 (en) | 2013-09-26 | 2015-04-02 | Ablynx Nv | Bispecific nanobodies |
| DK3089994T3 (da) | 2013-12-30 | 2022-07-04 | Epimab Biotherapeutics Inc | Fabs-in-tandem-immunglobulin og anvendelser deraf |
| UA117289C2 (uk) | 2014-04-02 | 2018-07-10 | Ф. Хоффманн-Ля Рош Аг | Мультиспецифічне антитіло |
| SG10201913324PA (en) | 2014-05-29 | 2020-03-30 | Macrogenics Inc | Tri-specific binding molecules and methods of use thereof |
| GB201412659D0 (en) | 2014-07-16 | 2014-08-27 | Ucb Biopharma Sprl | Molecules |
| MX384418B (es) | 2014-07-31 | 2025-03-14 | Amgen Res Munich Gmbh | Constructo de anticuerpo de cadena individual biespecífico con distribución mejorada de tejido. |
| UY36245A (es) | 2014-07-31 | 2016-01-29 | Amgen Res Munich Gmbh | Constructos de anticuerpos para cdh19 y cd3 |
| CN105471609B (zh) | 2014-09-05 | 2019-04-05 | 华为技术有限公司 | 一种用于配置业务的方法和装置 |
| SG11201701599UA (en) | 2014-09-05 | 2017-03-30 | Janssen Pharmaceutica Nv | Cd123 binding agents and uses thereof |
| AU2015323313B2 (en) | 2014-09-25 | 2021-04-01 | Amgen Inc. | Protease-activatable bispecific proteins |
| CN107109368A (zh) | 2014-10-07 | 2017-08-29 | 塞勒克提斯公司 | 用于调节car诱导的免疫细胞活性的方法 |
| AU2015353416C1 (en) | 2014-11-26 | 2022-01-27 | Xencor, Inc. | Heterodimeric antibodies that bind CD3 and CD38 |
| EP3237449A2 (en) * | 2014-12-22 | 2017-11-01 | Xencor, Inc. | Trispecific antibodies |
| EA038407B1 (ru) | 2015-02-05 | 2021-08-24 | Янссен Вэксинс Энд Превеншн Б.В. | Связывающие молекулы, направленные против гемагглютинина вируса гриппа, и пути их применения |
| WO2016130819A2 (en) | 2015-02-11 | 2016-08-18 | Emergent Product Development Seattle Llc | Compositions and methods for combination therapy with prostate-specific membrane antigen binding proteins |
| MX382212B (es) * | 2015-04-22 | 2025-03-13 | Agbiome Inc | Genes pesticidas y metodos de uso. |
| CN107709363A (zh) | 2015-05-01 | 2018-02-16 | 基因泰克公司 | 掩蔽抗cd3抗体和使用方法 |
| CN107847594B (zh) * | 2015-05-06 | 2022-04-15 | 詹森生物科技公司 | 前列腺特异性膜抗原(psma)双特异性结合剂及其用途 |
| JP6867302B2 (ja) | 2015-05-21 | 2021-04-28 | フル スペクトラム ジェネティクス， インコーポレイテッド | タンパク質の特徴を改善する方法 |
| CN107849148B (zh) | 2015-05-21 | 2023-09-19 | 哈普恩治疗公司 | 三特异性结合蛋白质及使用方法 |
| CN108271390A (zh) | 2015-06-03 | 2018-07-10 | 农业生物群落股份有限公司 | 杀虫基因和使用方法 |
| DK3313874T3 (da) | 2015-06-26 | 2021-05-03 | Univ Southern California | Maskering af kimære antigen-receptor t-celler til tumorspecifik aktivering |
| TWI796283B (zh) | 2015-07-31 | 2023-03-21 | 德商安美基研究（慕尼黑）公司 | Ｍｓｌｎ及ｃｄ３抗體構築體 |
| EP3331913A1 (en) | 2015-08-07 | 2018-06-13 | Novartis AG | Treatment of cancer using chimeric cd3 receptor proteins |
| WO2017025698A1 (en) | 2015-08-11 | 2017-02-16 | Queen Mary University Of London | Bispecific, cleavable antibodies |
| CN106519037B (zh) | 2015-09-11 | 2019-07-23 | 科济生物医药（上海）有限公司 | 可活化的嵌合受体 |
| AU2016349482A1 (en) | 2015-11-05 | 2018-05-24 | City Of Hope | Methods for preparing cells for adoptive T cell therapy |
| WO2017087789A1 (en) | 2015-11-19 | 2017-05-26 | Revitope Limited | Functional antibody fragment complementation for a two-components system for redirected killing of unwanted cells |
| US10093694B2 (en) | 2016-02-03 | 2018-10-09 | Guangzhou Kangrui Biological Pharmaceutical Technology Co, Ltd. | Compounds for treating eye disorders or diseases |
| MX2018010824A (es) | 2016-03-08 | 2019-05-15 | Maverick Therapeutics Inc | Proteinas de union inducibles y metodos de uso. |
| LT3461261T (lt) | 2016-05-20 | 2025-08-25 | Harpoon Therapeutics, Inc. | Vienos grandinės kintamo fragmento cd3 surišantys baltymai |
| US10100106B2 (en) | 2016-05-20 | 2018-10-16 | Harpoon Therapeutics, Inc. | Single domain serum albumin binding protein |
| TW201815825A (zh) | 2016-07-21 | 2018-05-01 | 財團法人生物技術開發中心 | 經修飾之抗原結合fab片段及包含其之抗原結合分子 |
| WO2018071777A1 (en) | 2016-10-14 | 2018-04-19 | Harpoon Therapeutics, Inc. | Innate immune cell trispecific binding proteins and methods of use |
| WO2018098354A1 (en) | 2016-11-23 | 2018-05-31 | Harpoon Therapeutics, Inc. | Prostate specific membrane antigen binding protein |
| CA3044729A1 (en) | 2016-11-23 | 2018-05-31 | Harpoon Therapeutics, Inc. | Psma targeting trispecific proteins and methods of use |
| WO2018136725A1 (en) | 2017-01-19 | 2018-07-26 | Harpoon Therapeutics, Inc. | Innate immune cell inducible binding proteins and methods of use |
| EP3589662A4 (en) | 2017-02-28 | 2020-12-30 | Harpoon Therapeutics, Inc. | INDUCTIBLE MONOVALENT ANTIGEN BINDING PROTEIN |
| WO2018160671A1 (en) | 2017-02-28 | 2018-09-07 | Harpoon Therapeutics, Inc. | Targeted checkpoint inhibitors and methods of use |
| JP2020511130A (ja) | 2017-03-09 | 2020-04-16 | サイトメックス セラピューティクス インコーポレイテッド | Ｃｄ１４７抗体、活性化可能ｃｄ１４７抗体、ならびにその作製および使用の方法 |
| US20200115461A1 (en) | 2017-05-03 | 2020-04-16 | Harpoon Therapeutics, Inc. | Compositions and methods for adoptive cell therapies |
| EP3621648A4 (en) | 2017-05-12 | 2021-01-20 | Harpoon Therapeutics, Inc. | TRISPECIFIC PROTEINS MSLN AND METHOD OF USE |
| CN113896792B (zh) | 2017-05-12 | 2025-08-22 | 哈普恩治疗公司 | 间皮素结合蛋白质 |
| IL315737A (en) | 2017-10-13 | 2024-11-01 | Harpoon Therapeutics Inc | B-cell maturation antigen-binding proteins |
| KR102425983B1 (ko) | 2017-10-13 | 2022-07-29 | 하푼 테라퓨틱스, 인크. | 삼중특이적 단백질 및 사용 방법 |
| US20210269530A1 (en) | 2018-05-14 | 2021-09-02 | Harpoon Therapeutics, Inc. | Conditionally activated binding protein comprising a sterically occluded target binding domain |
| EP3794044A4 (en) | 2018-05-14 | 2022-02-16 | Harpoon Therapeutics, Inc. | DOUBLE BINDING UNIT |
| KR20210020903A (ko) | 2018-05-14 | 2021-02-24 | 하푼 테라퓨틱스, 인크. | 면역글로불린 분자의 조건부 활성화를 위한 결합 모이어티 |
| US12195544B2 (en) | 2018-09-21 | 2025-01-14 | Harpoon Therapeutics, Inc. | EGFR binding proteins and methods of use |
| WO2020061526A1 (en) | 2018-09-21 | 2020-03-26 | Harpoon Therapeutics, Inc. | Conditionally activated target-binding molecules |
| US20220054544A1 (en) | 2018-09-21 | 2022-02-24 | Harpoon Therapeutics, Inc. | Conditionally active receptors |
| IL281683B2 (en) | 2018-09-25 | 2023-04-01 | Harpoon Therapeutics Inc | dll3 binding proteins and methods of use |
-
2017
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- 2017-11-22 KR KR1020217020580A patent/KR20210087108A/ko not_active Ceased
- 2017-11-22 KR KR1020197017995A patent/KR102275008B1/ko not_active Expired - Fee Related
- 2017-11-22 EP EP17873939.7A patent/EP3544997A4/en not_active Withdrawn
- 2017-11-22 EA EA201991168A patent/EA201991168A1/ru unknown
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- 2017-11-22 MX MX2019006043A patent/MX2019006043A/es unknown
- 2017-11-22 CN CN201780084346.6A patent/CN110198955A/zh active Pending
- 2017-11-22 AU AU2017363300A patent/AU2017363300A1/en not_active Abandoned
- 2017-11-22 BR BR112019010604A patent/BR112019010604A2/pt not_active IP Right Cessation
- 2017-11-22 JP JP2019527508A patent/JP6812551B2/ja not_active Expired - Fee Related
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2019
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2020
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- 2020-12-15 JP JP2020207686A patent/JP2021061842A/ja active Pending
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| EP3544997A4 (en) | 2020-07-01 |
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| AU2017363300A1 (en) | 2019-06-20 |
| EP3544997A1 (en) | 2019-10-02 |
| US20180161428A1 (en) | 2018-06-14 |
| KR20210087108A (ko) | 2021-07-09 |
| JP6812551B2 (ja) | 2021-01-13 |
| US10849973B2 (en) | 2020-12-01 |
| KR102275008B1 (ko) | 2021-07-13 |
| JP2021061842A (ja) | 2021-04-22 |
| MX2019006043A (es) | 2019-09-26 |
| EA201991168A1 (ru) | 2019-12-30 |
| KR20190085542A (ko) | 2019-07-18 |
| CN110198955A (zh) | 2019-09-03 |
| WO2018098354A1 (en) | 2018-05-31 |
| IL266800A (en) | 2019-08-29 |
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