JP6812551B2 - 前立腺特異的膜抗原結合タンパク質 - Google Patents
前立腺特異的膜抗原結合タンパク質 Download PDFInfo
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Landscapes
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| US201662426086P | 2016-11-23 | 2016-11-23 | |
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| PCT/US2017/063121 WO2018098354A1 (en) | 2016-11-23 | 2017-11-22 | Prostate specific membrane antigen binding protein |
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| JP2021061842A (ja) * | 2016-11-23 | 2021-04-22 | ハープーン セラピューティクス，インク． | 前立腺特異的膜抗原結合タンパク質 |
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| KR20190080992A (ko) | 2015-05-21 | 2019-07-08 | 하푼 테라퓨틱스, 인크. | 삼중특이성 결합 단백질 및 사용 방법 |
| EP3493844A4 (en) | 2016-05-20 | 2021-03-24 | Harpoon Therapeutics Inc. | SINGLE DOMAIN SERUM ALBUMIN BINDING PROTEIN |
| US11623958B2 (en) | 2016-05-20 | 2023-04-11 | Harpoon Therapeutics, Inc. | Single chain variable fragment CD3 binding proteins |
| PL3461261T3 (pl) | 2016-05-20 | 2025-11-12 | Harpoon Therapeutics, Inc. | Białka wiążące jednołańcuchowy fragment zmienny CD3 |
| MX2019006045A (es) | 2016-11-23 | 2019-11-11 | Harpoon Therapeutics Inc | Proteinas triespecificas dirigidas a psma y metodos de uso. |
| US11535668B2 (en) | 2017-02-28 | 2022-12-27 | Harpoon Therapeutics, Inc. | Inducible monovalent antigen binding protein |
| CA3063362A1 (en) | 2017-05-12 | 2018-11-15 | Harpoon Therapeutics, Inc. | Msln targeting trispecific proteins and methods of use |
| SG10202107880XA (en) | 2017-05-12 | 2021-09-29 | Harpoon Therapeutics Inc | Mesothelin binding proteins |
| PL3694529T3 (pl) | 2017-10-13 | 2024-12-16 | Harpoon Therapeutics, Inc. | Trójswoiste białka i sposoby zastosowania |
| IL315737A (en) | 2017-10-13 | 2024-11-01 | Harpoon Therapeutics Inc | B-cell maturation antigen-binding proteins |
| MX2020012217A (es) | 2018-05-14 | 2021-03-02 | Harpoon Therapeutics Inc | Porción de unión para activación condicional de moléculas de inmunoglobulina. |
| EP3802617A4 (en) * | 2018-06-07 | 2022-04-27 | Cullinan Oncology, Inc. | MULTISPECIFIC BINDING PROTEINS AND METHODS OF USE THEREOF |
| US12195544B2 (en) | 2018-09-21 | 2025-01-14 | Harpoon Therapeutics, Inc. | EGFR binding proteins and methods of use |
| CN113286817B (zh) | 2018-09-25 | 2025-01-28 | 哈普恩治疗公司 | Dll3结合蛋白及使用方法 |
| MX2021012205A (es) | 2019-04-05 | 2022-02-21 | Teneobio Inc | Anticuerpos de cadena pesada que se unen al psma. |
| KR20220144841A (ko) | 2020-02-21 | 2022-10-27 | 하푼 테라퓨틱스, 인크. | Flt3 결합 단백질 및 사용 방법 |
| WO2021202376A1 (en) | 2020-03-30 | 2021-10-07 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Method for blocking uptake of prostate-specific membrane antigen (psma)-targeted radionuclides by exocrine organs |
| JP2023532807A (ja) * | 2020-07-08 | 2023-07-31 | ラヴァ・セラピューティクス・エヌ・ヴイ | Ｐｓｍａ及びガンマ－デルタｔ細胞受容体に結合する抗体 |
| EP4355778A1 (en) | 2021-06-17 | 2024-04-24 | Boehringer Ingelheim International GmbH | Novel tri-specific binding molecules |
| AU2024233625A1 (en) | 2023-03-03 | 2025-09-18 | Arsenal Biosciences, Inc. | Systems targeting psma and ca9 |
| CN118629502A (zh) * | 2024-06-19 | 2024-09-10 | 中山百灵生物技术股份有限公司 | 基于数据处理的核苷酸序列实验预测优化系统 |
Family Cites Families (198)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| 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 |
| 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 |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| 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 |
| 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 |
| US6534055B1 (en) | 1988-11-23 | 2003-03-18 | Genetics Institute, Inc. | Methods for selectively stimulating proliferation of 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 |
| GB8928874D0 (en) | 1989-12-21 | 1990-02-28 | Celltech Ltd | Humanised antibodies |
| US5859205A (en) | 1989-12-21 | 1999-01-12 | Celltech Limited | Humanised antibodies |
| US5061620A (en) | 1990-03-30 | 1991-10-29 | Systemix, Inc. | Human hematopoietic stem cell |
| DE69233482T2 (de) | 1991-05-17 | 2006-01-12 | Merck & Co., Inc. | Verfahren zur Verminderung der Immunogenität der variablen Antikörperdomänen |
| US5199942A (en) | 1991-06-07 | 1993-04-06 | Immunex Corporation | Method for improving autologous transplantation |
| EP0940468A1 (en) | 1991-06-14 | 1999-09-08 | Genentech, Inc. | Humanized antibody variable domain |
| 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 |
| ATE249840T1 (de) | 1991-12-13 | 2003-10-15 | Xoma Corp | Verfahren und materialien zur herstellung von modifizierten variablen antikörperdomänen und ihre therapeutische verwendung |
| DE69330523D1 (de) | 1992-08-21 | 2001-09-06 | Vrije Universiteit Brussel Bru | Immunoglobuline ohne leichte ketten |
| US6005079A (en) | 1992-08-21 | 1999-12-21 | Vrije Universiteit Brussels | Immunoglobulins devoid of light chains |
| 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 |
| BR9813276A (pt) | 1997-10-27 | 2000-08-22 | Unilever Nv | Proteìna multivalente de ligação de antìgeno, sequências de nucleotìdeos, vetor de expressão, célula hospedeira, processo para preparação de proteìna multivalente de ligação de antìgeno, e, uso da mesma |
| WO1999037681A2 (en) | 1998-01-26 | 1999-07-29 | Unilever Plc | Method for producing antibody fragments |
| 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 |
| WO2000043507A1 (en) | 1999-01-19 | 2000-07-27 | Unilever Plc | Method for producing antibody fragments |
| 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 |
| AU4328801A (en) | 2000-02-24 | 2001-09-03 | Xcyte Therapies Inc | Simultaneous stimulation and concentration of cells |
| US6867041B2 (en) | 2000-02-24 | 2005-03-15 | Xcyte Therapies, Inc. | Simultaneous stimulation and concentration of cells |
| US6797514B2 (en) | 2000-02-24 | 2004-09-28 | Xcyte Therapies, Inc. | Simultaneous stimulation and concentration of cells |
| US20030190598A1 (en) | 2000-05-26 | 2003-10-09 | Jasmid Tanha | 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 |
| WO2003025020A1 (en) | 2001-09-13 | 2003-03-27 | Institute For Antibodies Co., Ltd. | Method of constructing camel antibody library |
| US20050215472A1 (en) | 2001-10-23 | 2005-09-29 | Psma Development Company, Llc | PSMA formulations and uses thereof |
| EP2360169B1 (en) | 2001-10-23 | 2015-10-14 | Psma Development Company, L.L.C. | PSMA antibodies |
| JP2005289809A (ja) | 2001-10-24 | 2005-10-20 | Vlaams Interuniversitair Inst Voor Biotechnologie Vzw (Vib Vzw) | 突然変異重鎖抗体 |
| CA2474616A1 (en) | 2002-01-28 | 2003-08-07 | Medarex, Inc. | Human monoclonal antibodies to prostate specific membrane antigen (psma) |
| US9321832B2 (en) | 2002-06-28 | 2016-04-26 | Domantis Limited | Ligand |
| AU2003244817B2 (en) | 2002-06-28 | 2010-08-26 | Domantis Limited | Antigen-binding immunoglobulin single variable domains and dual-specific constructs |
| DE60320828D1 (de) | 2002-11-07 | 2008-06-19 | Univ Erasmus | Fret proben und verfahren zur erkennung aufeinander einwirkeneden moleküle |
| US9320792B2 (en) | 2002-11-08 | 2016-04-26 | Ablynx N.V. | Pulmonary administration of immunoglobulin single variable domains and constructs thereof |
| ATE517922T1 (de) | 2002-11-08 | 2011-08-15 | Ablynx Nv | Stabilisierte einzel-domänen-antikörper in einer pharmazeutischen zusammensetzung ausgestaltet für inhalation |
| AU2003286002B2 (en) | 2002-11-08 | 2011-06-16 | Ablynx N.V. | Single domain antibodies directed against tumour necrosis factor-alpha and uses therefor |
| JP2006519763A (ja) | 2002-11-08 | 2006-08-31 | アブリンクス エン．ヴェー． | 治療用ポリペプチドの投与法およびそのためのポリペプチド |
| GB0228210D0 (en) | 2002-12-03 | 2003-01-08 | Babraham Inst | Single chain antibodies |
| US8784821B1 (en) | 2003-05-31 | 2014-07-22 | Amgen Research (Munich) Gmbh | Human-anti-human cd3 binding molecules |
| EP1638510B1 (en) | 2003-07-01 | 2015-09-02 | Immunomedics, Inc. | Multivalent carriers of bi-specific antibodies |
| ES2458636T3 (es) | 2003-08-18 | 2014-05-06 | Medimmune, Llc | Humanización de anticuerpos |
| EP1660534A2 (en) | 2003-08-22 | 2006-05-31 | 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 |
| AU2005250216B2 (en) | 2004-06-01 | 2009-12-10 | Domantis Limited | Bispecific fusion antibodies with enhanced serum half-life |
| EP1786918A4 (en) | 2004-07-17 | 2009-02-11 | Imclone Systems Inc | NEW BISPECIFIC ANTIBODY TETRAVALENT |
| US20080069772A1 (en) | 2004-08-26 | 2008-03-20 | Eberhard-Karls-Universitaet Tuebingen Universitaetsklinikum | Treatment of transformed or infected biological cells |
| EP1634603A1 (de) | 2004-08-26 | 2006-03-15 | Eberhard-Karls-Universität Tübingen Universitätsklinikum | Behandlung von transformierten oder infizierten biologischen Zellen |
| FR2879605B1 (fr) | 2004-12-16 | 2008-10-17 | Centre Nat Rech Scient Cnrse | Production de formats d'anticorps et applications immunologiques de ces formats |
| PL1699826T3 (pl) | 2005-01-05 | 2009-08-31 | F Star Biotechnologische Forschungs Und Entw M B H | Syntetyczne domeny immunoglobulinowe o właściwościach wiążących modyfikowane w regionach cząsteczki różnych od regionów determinujących komplementarność |
| 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 |
| EP2949668B1 (en) | 2005-05-18 | 2019-08-14 | Ablynx N.V. | Improved nanobodies tm against tumor necrosis factor-alpha |
| BRPI0609797B8 (pt) | 2005-05-20 | 2021-05-25 | Ablynx Nv | nanocorpos melhorados para o tratamento de desordens mediadas por agregação |
| EP1726650A1 (en) | 2005-05-27 | 2006-11-29 | Universitätsklinikum Freiburg | Monoclonal antibodies and single chain antibody fragments against cell-surface prostate specific membrane antigen |
| EP2520588A1 (en) | 2005-08-19 | 2012-11-07 | Abbott Laboratories | Dual variable domain immunoglobulin and uses thereof |
| DK1940881T3 (en) | 2005-10-11 | 2017-02-20 | Amgen Res Munich Gmbh | COMPOSITIONS WITH ARTICLE CROSS-SPECIFIC ANTIBODIES AND APPLICATIONS THEREOF |
| EP1962961B1 (en) | 2005-11-29 | 2013-01-09 | The University Of Sydney | Demibodies: dimerisation-activated therapeutic agents |
| US20110038854A1 (en) | 2006-03-30 | 2011-02-17 | University Of Medicine And Dentistry Of New Jersey | Strategy for homo- or hetero-dimerization of various proteins in solution and in cell |
| US20070269422A1 (en) | 2006-05-17 | 2007-11-22 | Ablynx N.V. | Serum albumin binding proteins with long half-lives |
| AU2007285695B2 (en) | 2006-08-18 | 2012-05-24 | Ablynx N.V. | Amino acid sequences directed against IL-6R and polypeptides comprising the same for the treatment of diseases and disorders associated with IL-6-mediated signalling |
| 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 |
| HUE040467T2 (hu) | 2007-04-03 | 2019-03-28 | Amgen Res Munich Gmbh | Keresztfaj-specifikus kötõdomén |
| MX2009012650A (es) | 2007-05-24 | 2010-02-18 | Ablynx Nv | Secuencias de aminoacido dirigidas contra rank-l y polipeptidos que comprenden lo mismo para el tratamiento de enfermedades y trastornos de huesos. |
| EP2014680A1 (en) | 2007-07-10 | 2009-01-14 | Friedrich-Alexander-Universität Erlangen-Nürnberg | Recombinant, single-chain, trivalent tri-specific or bi-specific antibody derivatives |
| CA3128656A1 (en) | 2007-08-22 | 2009-02-26 | The Regents Of The University Of California | Activatable binding polypeptides and methods of identification and use thereof |
| AU2007358569B2 (en) | 2007-09-07 | 2014-09-04 | 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 |
| LT2285408T (lt) | 2008-06-05 | 2019-01-25 | Ablynx N.V. | Aminorūgščių sekos, nukreiptos prieš viruso apvalkalo baltymus, ir tokias sekas turintys polipeptidai, skirti virusinių ligų gydymui |
| 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 |
| CA2729810A1 (en) | 2008-07-02 | 2010-01-07 | Emergent Product Development Seattle, Llc | Tgf-.beta. antagonist multi-target binding proteins |
| WO2010037836A2 (en) | 2008-10-01 | 2010-04-08 | Micromet Ag | Cross-species-specific psmaxcd3 bispecific single chain antibody |
| EP2352765B1 (en) | 2008-10-01 | 2018-01-03 | Amgen Research (Munich) GmbH | Cross-species-specific single domain bispecific single chain antibody |
| ES2582603T5 (es) | 2008-10-01 | 2022-12-02 | Amgen Res Munich Gmbh | Anticuerpos biespecíficos de cadena sencilla con especificidad por antígenos diana de alto peso molecular |
| CA2740561C (en) | 2008-10-14 | 2021-01-19 | National Research Council Of Canada | Bsa-specific antibodies |
| US20100189727A1 (en) | 2008-12-08 | 2010-07-29 | Tegopharm Corporation | Masking Ligands For Reversible Inhibition Of Multivalent Compounds |
| EP2210902A1 (en) | 2009-01-14 | 2010-07-28 | TcL Pharma | Recombinant monovalent antibodies |
| KR101579771B1 (ko) | 2009-03-05 | 2015-12-28 | 애브비 인코포레이티드 | Ｉｌ-17 결합 단백질 |
| 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 |
| CN102770456B (zh) | 2009-12-04 | 2018-04-06 | 弗·哈夫曼-拉罗切有限公司 | 多特异性抗体、抗体类似物、组合物和方法 |
| EP2332994A1 (en) | 2009-12-09 | 2011-06-15 | Friedrich-Alexander-Universität Erlangen-Nürnberg | Trispecific therapeutics against acute myeloid leukaemia |
| SI2519543T1 (sl) | 2009-12-29 | 2016-08-31 | Emergent Product Development Seattle, Llc | Beljakovine, ki se vežejo s heterodimeri in njihova uporaba |
| 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 |
| WO2011117423A1 (en) | 2010-03-26 | 2011-09-29 | Ablynx N.V. | Immunoglobulin single variable domains directed against 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 |
| RU2013110876A (ru) | 2010-08-24 | 2014-09-27 | Рош Гликарт Аг | Активируемые биспецифические антитела |
| WO2012025530A1 (en) | 2010-08-24 | 2012-03-01 | F. Hoffmann-La Roche Ag | Bispecific antibodies comprising a disulfide stabilized - fv fragment |
| EP2621953B1 (en) | 2010-09-30 | 2017-04-05 | Ablynx N.V. | Biological materials related to c-met |
| US20130273055A1 (en) | 2010-11-16 | 2013-10-17 | Eric Borges | Agents and methods for treating diseases that correlate with bcma expression |
| WO2012131053A1 (en) | 2011-03-30 | 2012-10-04 | Ablynx Nv | Methods of treating immune disorders with single domain antibodies against tnf-alpha |
| ES2872077T3 (es) | 2011-04-08 | 2021-11-02 | Us Health | Receptor de antígenos quiméricos anti-variante III del receptor de factor de crecimiento epidérmico y uso de los mismos para el tratamiento de cáncer |
| CN107936121B (zh) * | 2011-05-16 | 2022-01-14 | 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 |
| US20150158934A1 (en) | 2011-09-09 | 2015-06-11 | Ucl Business Plc | 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 |
| MX359411B (es) | 2012-01-13 | 2018-09-27 | Univ Wuerzburg J Maximilians | Complementación funcional bipartita inducida por antígenos, dual. |
| EP2807189B1 (en) | 2012-01-23 | 2019-03-20 | Ablynx N.V. | Sequences directed against hepatocyte growth factor (hgf) and polypeptides comprising the same for the treatment of cancers and/or tumors |
| ES2812849T3 (es) | 2012-02-24 | 2021-03-18 | Abbvie Stemcentrx Llc | Anticuerpos anti-DLL3 y procedimientos de utilización de los mismos |
| GB201203442D0 (en) | 2012-02-28 | 2012-04-11 | Univ Birmingham | Immunotherapeutic molecules and uses |
| MX353382B (es) | 2012-03-01 | 2018-01-10 | Amgen Res Munich Gmbh | Moleculas de union polipeptido de larga duracion. |
| JP6283017B2 (ja) | 2012-03-30 | 2018-02-21 | バイエル・ヘルスケア・エルエルシーＢａｙｅｒ ＨｅａｌｔｈＣａｒｅ ＬＬＣ | プロテアーゼ制御抗体 |
| MX366813B (es) | 2012-04-20 | 2019-07-25 | Aptevo Res & Development Llc | Polipeptidos de enlace cd3. |
| US9856314B2 (en) | 2012-06-22 | 2018-01-02 | Cytomx Therapeutics, Inc. | Activatable antibodies having non-binding steric moieties and methods of using the same |
| US20140004121A1 (en) | 2012-06-27 | 2014-01-02 | Amgen Inc. | Anti-mesothelin binding proteins |
| CN112587658A (zh) | 2012-07-18 | 2021-04-02 | 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 |
| US9416190B2 (en) | 2012-09-27 | 2016-08-16 | 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 |
| EP2964675B1 (en) | 2013-03-05 | 2018-06-20 | Baylor College Of Medicine | Engager cells for immunotherapy |
| EP2971045B1 (en) | 2013-03-13 | 2019-06-19 | Health Research, Inc. | Compositions and methods for use of recombinant t cell receptors for direct recognition of tumor antigen |
| SI2970449T1 (sl) | 2013-03-15 | 2019-11-29 | Amgen Res Munich Gmbh | Enoverižne vezavne molekule, ki vsebujejo N-terminalni ABP |
| CA2903258C (en) | 2013-03-15 | 2019-11-26 | Amgen Inc. | Heterodimeric bispecific antibodies |
| US20140302037A1 (en) | 2013-03-15 | 2014-10-09 | Amgen Inc. | BISPECIFIC-Fc MOLECULES |
| HRP20220553T1 (hr) | 2013-07-25 | 2022-06-10 | Cytomx Therapeutics Inc. | Polispecifična protutijela, polispecifična protutijela koja se mogu aktivirati i postupci uporabe navedenih protutijela |
| BR112016006564B1 (pt) | 2013-09-24 | 2023-11-21 | University Of Washington Through Its Center For Commercialization | Polipeptídeo de fibra adb-2/3 recombinante e composição farmacêutica |
| CN105814082A (zh) | 2013-09-26 | 2016-07-27 | 埃博灵克斯股份有限公司 | 双特异性纳米抗体 |
| RU2016129959A (ru) | 2013-12-30 | 2018-02-02 | Эпимаб Биотерепьютикс Инк. | Иммуноглобулин с тандемным расположением fab-фрагментов и его применение |
| UA117289C2 (uk) | 2014-04-02 | 2018-07-10 | Ф. Хоффманн-Ля Рош Аг | Мультиспецифічне антитіло |
| TN2016000525A1 (en) | 2014-05-29 | 2018-04-04 | Macrogenics Inc | Tri-specific binding molecules and methods of use thereof |
| GB201412659D0 (en) | 2014-07-16 | 2014-08-27 | Ucb Biopharma Sprl | Molecules |
| AR101669A1 (es) | 2014-07-31 | 2017-01-04 | Amgen Res Munich Gmbh | Constructos de anticuerpos para cdh19 y cd3 |
| CA2952540C (en) | 2014-07-31 | 2022-06-21 | Amgen Research (Munich) Gmbh | Bispecific single chain antibody construct with enhanced tissue distribution |
| CN109842529B (zh) | 2014-09-05 | 2021-10-26 | 华为技术有限公司 | 用于配置业务的方法、装置和网络系统 |
| JO3568B1 (ar) | 2014-09-05 | 2020-07-05 | Janssen Pharmaceutica Nv | عوامل ربط cd123 واستخداماتها |
| JP2017529853A (ja) | 2014-09-25 | 2017-10-12 | アムジエン・インコーポレーテツド | プロテアーゼにより活性化可能な二重特異性タンパク質 |
| JP2017531430A (ja) | 2014-10-07 | 2017-10-26 | セレクティスＣｅｌｌｅｃｔｉｓ | Ｃａｒによって誘導される免疫細胞の活性を調節するための方法 |
| MX2017006918A (es) | 2014-11-26 | 2018-01-25 | Xencor Inc | Anticuerpos heterodimericos que se unen a cd3 y cd38. |
| EP3237449A2 (en) * | 2014-12-22 | 2017-11-01 | Xencor, Inc. | Trispecific antibodies |
| EP3253411A1 (en) | 2015-02-05 | 2017-12-13 | Janssen Vaccines & Prevention B.V. | Binding molecules directed against influenza hemagglutinin and uses thereof |
| CA2976360A1 (en) * | 2015-02-11 | 2016-08-18 | Aptevo Research And Development 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. |
| EP3778640A1 (en) | 2015-05-01 | 2021-02-17 | Genentech, Inc. | Masked anti-cd3 antibodies and methods of use |
| 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 |
| ES2881683T3 (es) | 2015-05-21 | 2021-11-30 | Full Spectrum Genetics Inc | Procedimiento para mejorar las características de las proteínas |
| KR20190080992A (ko) * | 2015-05-21 | 2019-07-08 | 하푼 테라퓨틱스, 인크. | 삼중특이성 결합 단백질 및 사용 방법 |
| CN114805503A (zh) | 2015-06-03 | 2022-07-29 | 农业生物群落股份有限公司 | 杀虫基因和使用方法 |
| WO2016210447A1 (en) | 2015-06-26 | 2016-12-29 | University Of Southern California | Masking chimeric antigen receptor t cells for tumor-specific activation |
| 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 |
| WO2017027392A1 (en) | 2015-08-07 | 2017-02-16 | 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 |
| ES2873846T5 (en) | 2015-11-19 | 2025-06-23 | Revitope Ltd | Functional antibody fragment complementation for a two-components system for redirected killing of unwanted cells |
| CN108884126B (zh) | 2016-02-03 | 2022-03-18 | 广州康睿生物医药科技股份有限公司 | 用于治疗眼睛病症或疾病的化合物 |
| KR20230041739A (ko) | 2016-03-08 | 2023-03-24 | 매버릭 테라퓨틱스, 인크. | 유도성 결합 단백질 및 사용 방법 |
| PL3461261T3 (pl) | 2016-05-20 | 2025-11-12 | Harpoon Therapeutics, Inc. | Białka wiążące jednołańcuchowy fragment zmienny CD3 |
| EP3493844A4 (en) | 2016-05-20 | 2021-03-24 | Harpoon Therapeutics Inc. | SINGLE DOMAIN SERUM ALBUMIN BINDING PROTEIN |
| US20190309092A1 (en) | 2016-07-21 | 2019-10-10 | Development Center For Biotechnology | Modified antigen-binding fab fragments and antigen-binding molecules comprising the same |
| WO2018071777A1 (en) | 2016-10-14 | 2018-04-19 | Harpoon Therapeutics, Inc. | Innate immune cell trispecific binding proteins and methods of use |
| MX2019006045A (es) | 2016-11-23 | 2019-11-11 | Harpoon Therapeutics Inc | Proteinas triespecificas dirigidas a psma y metodos de uso. |
| KR20210087108A (ko) * | 2016-11-23 | 2021-07-09 | 하푼 테라퓨틱스, 인크. | 전립선 특이 막 항원 결합 단백질 |
| WO2018136725A1 (en) | 2017-01-19 | 2018-07-26 | Harpoon Therapeutics, Inc. | Innate immune cell inducible binding proteins and methods of use |
| WO2018160671A1 (en) | 2017-02-28 | 2018-09-07 | Harpoon Therapeutics, Inc. | Targeted checkpoint inhibitors and methods of use |
| US11535668B2 (en) | 2017-02-28 | 2022-12-27 | Harpoon Therapeutics, Inc. | Inducible monovalent antigen binding protein |
| AU2018231127A1 (en) | 2017-03-09 | 2019-09-19 | Cytomx Therapeutics, Inc. | CD147 antibodies, activatable CD147 antibodies, and methods of making and use thereof |
| US20200115461A1 (en) | 2017-05-03 | 2020-04-16 | Harpoon Therapeutics, Inc. | Compositions and methods for adoptive cell therapies |
| CA3063362A1 (en) | 2017-05-12 | 2018-11-15 | Harpoon Therapeutics, Inc. | Msln targeting trispecific proteins and methods of use |
| SG10202107880XA (en) | 2017-05-12 | 2021-09-29 | Harpoon Therapeutics Inc | Mesothelin binding proteins |
| PL3694529T3 (pl) | 2017-10-13 | 2024-12-16 | Harpoon Therapeutics, Inc. | Trójswoiste białka i sposoby zastosowania |
| IL315737A (en) | 2017-10-13 | 2024-11-01 | Harpoon Therapeutics Inc | B-cell maturation antigen-binding proteins |
| US20210284728A1 (en) | 2018-05-14 | 2021-09-16 | Harpoon Therapeutics, Inc. | Dual binding moiety |
| US20210269530A1 (en) | 2018-05-14 | 2021-09-02 | Harpoon Therapeutics, Inc. | Conditionally activated binding protein comprising a sterically occluded target binding domain |
| MX2020012217A (es) | 2018-05-14 | 2021-03-02 | Harpoon Therapeutics Inc | Porción de unión para activación condicional de moléculas de inmunoglobulina. |
| US20210355219A1 (en) | 2018-09-21 | 2021-11-18 | Harpoon Therapeutics, Inc. | Conditionally activated target-binding molecules |
| US12195544B2 (en) | 2018-09-21 | 2025-01-14 | Harpoon Therapeutics, Inc. | EGFR binding proteins and methods of use |
| US20220054544A1 (en) | 2018-09-21 | 2022-02-24 | Harpoon Therapeutics, Inc. | Conditionally active receptors |
| CN113286817B (zh) | 2018-09-25 | 2025-01-28 | 哈普恩治疗公司 | Dll3结合蛋白及使用方法 |
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2021061842A (ja) * | 2016-11-23 | 2021-04-22 | ハープーン セラピューティクス，インク． | 前立腺特異的膜抗原結合タンパク質 |
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| IL266800A (en) | 2019-08-29 |
| KR20210087108A (ko) | 2021-07-09 |
| MX2019006043A (es) | 2019-09-26 |
| CN110198955A (zh) | 2019-09-03 |
| EP3544997A4 (en) | 2020-07-01 |
| US20180161428A1 (en) | 2018-06-14 |
| JP2021061842A (ja) | 2021-04-22 |
| WO2018098354A1 (en) | 2018-05-31 |
| US20210100902A1 (en) | 2021-04-08 |
| US10849973B2 (en) | 2020-12-01 |
| AU2017363300A1 (en) | 2019-06-20 |
| KR102275008B1 (ko) | 2021-07-13 |
| BR112019010604A2 (pt) | 2019-12-17 |
| JP2020501532A (ja) | 2020-01-23 |
| EP3544997A1 (en) | 2019-10-02 |
| CA3044659A1 (en) | 2018-05-31 |
| EA201991168A1 (ru) | 2019-12-30 |
| KR20190085542A (ko) | 2019-07-18 |
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