JP6498601B2 - 多価ヘテロ多量体足場設計および構築物 - Google Patents
多価ヘテロ多量体足場設計および構築物 Download PDFInfo
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- C—CHEMISTRY; METALLURGY
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- C07K14/475—Growth factors; Growth regulators
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- C07K—PEPTIDES
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- C07K14/575—Hormones
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- C—CHEMISTRY; METALLURGY
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- C07K—PEPTIDES
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- C07K14/76—Albumins
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- C—CHEMISTRY; METALLURGY
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- C07K16/2803—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily
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- C—CHEMISTRY; METALLURGY
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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- C07K—PEPTIDES
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- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
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- C07K2319/31—Fusion polypeptide fusions, other than Fc, for prolonged plasma life, e.g. albumin
Landscapes
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- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
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| US201361845945P | 2013-07-12 | 2013-07-12 | |
| PCT/US2013/050408 WO2014012082A2 (en) | 2012-07-13 | 2013-07-12 | Multivalent heteromultimer scaffold design an constructs |
| US61/845,945 | 2013-07-12 |
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| AU2012222833B2 (en) | 2011-03-03 | 2017-03-16 | Zymeworks Inc. | Multivalent heteromultimer scaffold design and constructs |
| KR102052774B1 (ko) | 2011-11-04 | 2019-12-04 | 자임워크스 인코포레이티드 | Ｆｃ 도메인 내의 돌연변이를 갖는 안정한 이종이합체 항체 설계 |
| US9499634B2 (en) | 2012-06-25 | 2016-11-22 | Zymeworks Inc. | Process and methods for efficient manufacturing of highly pure asymmetric antibodies in mammalian cells |
| IN2015DN01115A (enExample) * | 2012-07-13 | 2015-06-26 | Zymeworks Inc | |
| US9914785B2 (en) | 2012-11-28 | 2018-03-13 | Zymeworks Inc. | Engineered immunoglobulin heavy chain-light chain pairs and uses thereof |
| WO2014209855A1 (en) * | 2013-06-24 | 2014-12-31 | Anthrogenesis Corporation | Methods of expanding t cells |
| RU2723940C2 (ru) * | 2014-03-21 | 2020-06-18 | Экс-Боди, Инк. | Биспецифические антигенсвязывающие полипептиды |
| EA201692476A1 (ru) | 2014-05-28 | 2017-07-31 | Займворкс Инк. | Модифицированные антигенсвязывающие полипептидные конструкции и их применение |
| CN106659779B (zh) * | 2014-12-22 | 2021-05-18 | 西雅图免疫公司 | 双特异性四价抗体及其制造和使用方法 |
| EP3322735A4 (en) | 2015-07-15 | 2019-03-13 | Zymeworks Inc. | ACTIVE CONJUGATED BIS-SPECIFIC ANTIGEN-BONDING CONSTRUCTS |
| US10946063B2 (en) * | 2016-10-11 | 2021-03-16 | Welltat Ophthalmics Corporation | Fusion protein between short form rod-derived cone viability factor and a hydrophilic peptide |
| JP7165717B2 (ja) | 2017-03-15 | 2022-11-04 | パンディオン・オペレーションズ・インコーポレイテッド | 標的免疫寛容 |
| JOP20190222A1 (ar) | 2017-04-11 | 2019-09-24 | Zymeworks Inc | الأجسام المضادة ثنائية النوعية المضادة لـ pd-l1 والمضادة لـ tim-3 |
| US11531030B2 (en) | 2017-04-21 | 2022-12-20 | Mayo Foundation For Medical Education And Research | Polypeptide-antibody complexes and uses thereof |
| MX2019013517A (es) | 2017-05-24 | 2020-08-17 | Pandion Operations Inc | Inmunotolerancia dirigida. |
| RU2019142330A (ru) | 2017-06-30 | 2021-07-30 | Займворкс, Инк. | Стабилизированные химерные fab |
| AR112603A1 (es) | 2017-07-10 | 2019-11-20 | Lilly Co Eli | Anticuerpos biespecíficos inhibidores de punto de control |
| US10174091B1 (en) | 2017-12-06 | 2019-01-08 | Pandion Therapeutics, Inc. | IL-2 muteins |
| USRE50550E1 (en) | 2017-12-06 | 2025-08-26 | Pandion Operations, Inc. | IL-2 muteins and uses thereof |
| US10946068B2 (en) | 2017-12-06 | 2021-03-16 | Pandion Operations, Inc. | IL-2 muteins and uses thereof |
| US20210023233A1 (en) * | 2018-02-06 | 2021-01-28 | Mayo Foundation For Medical Education And Research | Antibody-peptide complexes and uses thereof |
| IL277049B2 (en) | 2018-03-13 | 2024-02-01 | Zymeworks Bc Inc | Conjugates of biparatopic anti-HER2 antibody and drug and methods of use |
| AU2019282836B2 (en) * | 2018-06-07 | 2025-09-04 | Cullinan Oncology, Inc. | Multi-specific binding proteins and methods of use thereof |
| EP3930687A4 (en) | 2019-02-25 | 2023-06-07 | The University of Chicago | METHODS AND COMPOSITIONS FOR THE TREATMENT OF INFLAMMATORY AND AUTOIMMUNE CONDITIONS USING ECM AFFINITY PEPTIDES LINKED TO ANTI-INFLAMMATORY AGENTS |
| MA55504A (fr) | 2019-04-01 | 2022-02-09 | Novo Nordisk As | Anticorps dirigés contre le liraglutide et leur utilisation |
| KR102244760B1 (ko) * | 2019-04-29 | 2021-04-27 | 주식회사 다나그린 | 혈청유래 단백질을 포함하는 다공성 세포지지체 및 제조방법 |
| EP3972992A4 (en) | 2019-05-20 | 2023-07-19 | Pandion Operations, Inc. | MADCAM TARGETED IMMUNOTLERANCE |
| CN118852456A (zh) * | 2019-05-29 | 2024-10-29 | Cue生物制药股份有限公司 | 多聚体t细胞调节多肽及其使用方法 |
| IL293725A (en) | 2019-12-11 | 2022-08-01 | Cullinan Oncology Inc | Anti-cd19 antibodies and multispecific binding proteins |
| WO2021168079A1 (en) | 2020-02-21 | 2021-08-26 | Pandion Operations, Inc. | Tissue targeted immunotolerance with a cd39 effector |
| WO2022065913A1 (ko) | 2020-09-25 | 2022-03-31 | 주식회사 프로앱텍 | 요산산화효소-알부민 접합체, 그 제조방법 및 용도 |
| KR102723629B1 (ko) * | 2020-09-25 | 2024-10-30 | 주식회사 프로앱텍 | 기능성폴리펩티드 변이체의 컨쥬게이트 및 그 용도 |
| CN114736291B (zh) * | 2021-01-07 | 2023-08-11 | 中国科学院微生物研究所 | 特异性结合发热伴血小板减少综合征病毒的囊膜蛋白Gn的人源单克隆抗体及其用途 |
| CN113563474B (zh) * | 2021-06-11 | 2023-05-02 | 广州医科大学附属第三医院（广州重症孕产妇救治中心、广州柔济医院） | EpCAM-CD16-NKG2D三特异性抗体及其应用 |
| WO2023147042A2 (en) * | 2022-01-28 | 2023-08-03 | Sigilon Therapeutics, Inc. | Compositions, devices and methods for treating cns disorders |
| CN115057925B (zh) * | 2022-06-22 | 2024-03-26 | 中国检验检疫科学研究院 | 一种抗赤羽病病毒单克隆抗体及其应用 |
| CN117024578B (zh) * | 2023-07-19 | 2024-05-24 | 重庆明道捷测生物科技有限公司 | 一种用于捕获HBV核心颗粒的IgG抗体及应用 |
| CN116990504B (zh) * | 2023-09-27 | 2023-12-01 | 苏州旭光科星抗体生物科技有限公司 | 检测人可溶性cd4的双抗体夹心酶联免疫试剂盒 |
Family Cites Families (109)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4179337A (en) | 1973-07-20 | 1979-12-18 | Davis Frank F | Non-immunogenic polypeptides |
| EP0216846B2 (en) | 1985-04-01 | 1995-04-26 | Celltech Limited | Transformed myeloma cell-line and a process for the expression of a gene coding for a eukaryotic polypeptide employing same |
| GB8510219D0 (en) | 1985-04-22 | 1985-05-30 | Bass Plc | Isolation of fermentation products |
| US4980286A (en) | 1985-07-05 | 1990-12-25 | Whitehead Institute For Biomedical Research | In vivo introduction and expression of foreign genetic material in epithelial cells |
| JPS6296086A (ja) | 1985-10-21 | 1987-05-02 | Agency Of Ind Science & Technol | 複合プラスミド |
| US5576195A (en) | 1985-11-01 | 1996-11-19 | Xoma Corporation | Vectors with pectate lyase signal sequence |
| GB8601597D0 (en) | 1986-01-23 | 1986-02-26 | Wilson R H | Nucleotide sequences |
| GB8615701D0 (en) | 1986-06-27 | 1986-08-06 | Delta Biotechnology Ltd | Stable gene integration vector |
| US4857467A (en) | 1986-07-23 | 1989-08-15 | Phillips Petroleum Company | Carbon and energy source markers for transformation of strains of the genes Pichia |
| GB8620926D0 (en) | 1986-08-29 | 1986-10-08 | Delta Biotechnology Ltd | Yeast promoter |
| US5869620A (en) | 1986-09-02 | 1999-02-09 | Enzon, Inc. | Multivalent antigen-binding proteins |
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| US5258498A (en) | 1987-05-21 | 1993-11-02 | Creative Biomolecules, Inc. | Polypeptide linkers for production of biosynthetic proteins |
| GB8725529D0 (en) | 1987-10-30 | 1987-12-02 | Delta Biotechnology Ltd | Polypeptides |
| DK159088C (da) | 1988-04-06 | 1991-01-28 | Oce Helioprint As | Skanner til aftastning af en original |
| GB8809129D0 (en) | 1988-04-18 | 1988-05-18 | Celltech Ltd | Recombinant dna methods vectors and host cells |
| DE68925893T2 (de) | 1988-07-23 | 1996-08-08 | Delta Biotechnology Ltd | Sekretorische leader-sequenzen |
| FR2649991B2 (fr) | 1988-08-05 | 1994-03-04 | Rhone Poulenc Sante | Utilisation de derives stables du plasmide pkd1 pour l'expression et la secretion de proteines heterologues dans les levures du genre kluyveromyces |
| DD275463A1 (de) | 1988-09-07 | 1990-01-24 | Forschungsstelle Fuer Medizini | Verfahren zur herstellung von serumeiweissen mit gesteigertem dipolmoment zu therapeutischen zwecken |
| EP0394827A1 (en) | 1989-04-26 | 1990-10-31 | F. Hoffmann-La Roche Ag | Chimaeric CD4-immunoglobulin polypeptides |
| US5073627A (en) | 1989-08-22 | 1991-12-17 | Immunex Corporation | Fusion proteins comprising GM-CSF and IL-3 |
| US5108910A (en) | 1989-08-22 | 1992-04-28 | Immunex Corporation | DNA sequences encoding fusion proteins comprising GM-CSF and IL-3 |
| GB8924021D0 (en) | 1989-10-25 | 1989-12-13 | Celltech Ltd | Recombinant dna method and vectors for the use therein |
| US5641670A (en) | 1991-11-05 | 1997-06-24 | Transkaryotic Therapies, Inc. | Protein production and protein delivery |
| US6270989B1 (en) | 1991-11-05 | 2001-08-07 | Transkaryotic Therapies, Inc. | Protein production and delivery |
| US5932448A (en) * | 1991-11-29 | 1999-08-03 | Protein Design Labs., Inc. | Bispecific antibody heterodimers |
| FR2686899B1 (fr) | 1992-01-31 | 1995-09-01 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides biologiquement actifs, leur preparation et compositions pharmaceutiques les contenant. |
| ATE419355T1 (de) | 1992-02-06 | 2009-01-15 | Novartis Vaccines & Diagnostic | Marker für krebs und biosynthetisches bindeprotein dafür |
| US6096289A (en) | 1992-05-06 | 2000-08-01 | Immunomedics, Inc. | Intraoperative, intravascular, and endoscopic tumor and lesion detection, biopsy and therapy |
| WO1994012520A1 (en) | 1992-11-20 | 1994-06-09 | Enzon, Inc. | Linker for linked fusion polypeptides |
| TW402639B (en) | 1992-12-03 | 2000-08-21 | Transkaryotic Therapies Inc | Protein production and protein delivery |
| GB9225453D0 (en) | 1992-12-04 | 1993-01-27 | Medical Res Council | Binding proteins |
| US5780594A (en) | 1993-03-01 | 1998-07-14 | The United States Of America As Represented By The Administrator Of The National Aeronautics And Space Administration | Biologically active protein fragments containing specific binding regions of serum albumin or related proteins |
| US6001606A (en) | 1994-03-08 | 1999-12-14 | Human Genome Sciences, Inc. | Polynucleotides encoding myeloid progenitor inhibitory factor-1 (MPIF-1) and polypeptides encoded thereby |
| GB9404270D0 (en) | 1994-03-05 | 1994-04-20 | Delta Biotechnology Ltd | Yeast strains and modified albumins |
| US6077692A (en) | 1995-02-14 | 2000-06-20 | Human Genome Sciences, Inc. | Keratinocyte growth factor-2 |
| US5731168A (en) | 1995-03-01 | 1998-03-24 | Genentech, Inc. | Method for making heteromultimeric polypeptides |
| WO1996034891A1 (en) | 1995-05-05 | 1996-11-07 | Human Genome Sciences, Inc. | Human chemokine beta-8, chemokine beta-1 and macrophage inflammatory protein-4 |
| US6291207B1 (en) | 1995-07-28 | 2001-09-18 | Northwestern University | Herpes virus entry receptor protein |
| GB9526733D0 (en) | 1995-12-30 | 1996-02-28 | Delta Biotechnology Ltd | Fusion proteins |
| US7357927B2 (en) | 1996-03-12 | 2008-04-15 | Human Genome Sciences, Inc. | Death domain containing receptors |
| WO2001021658A1 (en) | 1999-09-24 | 2001-03-29 | Human Genome Sciences, Inc. | 32 human secreted proteins |
| EP0979281B1 (en) * | 1997-05-02 | 2005-07-20 | Genentech, Inc. | A method for making multispecific antibodies having heteromultimeric and common components |
| US7951917B1 (en) | 1997-05-02 | 2011-05-31 | Genentech, Inc. | Method for making multispecific antibodies having heteromultimeric and common components |
| US20020062010A1 (en) | 1997-05-02 | 2002-05-23 | Genentech, Inc. | Method for making multispecific antibodies having heteromultimeric and common components |
| US6350430B1 (en) | 1997-10-27 | 2002-02-26 | Lion Bioscience Science Ag | Melanocortin receptor ligands and methods of using same |
| WO1999058662A1 (fr) | 1998-05-14 | 1999-11-18 | Merck Patent Gmbh | Proteine fusionnee |
| WO2001007608A1 (en) | 1999-07-21 | 2001-02-01 | Human Genome Sciences, Inc. | Keratinocyte derived interferon |
| US7183387B1 (en) | 1999-01-15 | 2007-02-27 | Genentech, Inc. | Polypeptide variants with altered effector function |
| CA2361615A1 (en) | 1999-02-08 | 2000-08-10 | Human Genome Sciences, Inc. | The use of vascular endothelial growth factor 2 antagonist in the treatment of an injury to or disorder of an eye |
| EP1206541A4 (en) | 1999-08-05 | 2002-09-18 | Human Genome Sciences Inc | SECRETIED LYMPHOCYTE ACTIVATION MOLECUE, ENRICHED BY DENDRITIC CELLS |
| DE19963859A1 (de) | 1999-12-30 | 2001-07-12 | Apotech Res & Dev Ltd | Bi- oder Oligomer eines Di-, Tri-, Quattro- oder Pentamers von rekombinanten Fusionsproteinen |
| US6946134B1 (en) | 2000-04-12 | 2005-09-20 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| US20050100991A1 (en) | 2001-04-12 | 2005-05-12 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| CA2405550A1 (en) | 2000-04-12 | 2001-10-25 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| DK1355942T3 (da) | 2000-12-07 | 2008-11-17 | Lilly Co Eli | GLP-1-fusionsproteiner |
| US7507413B2 (en) | 2001-04-12 | 2009-03-24 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| US6833441B2 (en) | 2001-08-01 | 2004-12-21 | Abmaxis, Inc. | Compositions and methods for generating chimeric heteromultimers |
| ES2561985T3 (es) | 2001-10-10 | 2016-03-01 | Ratiopharm Gmbh | Remodelación y glicoconjugación de anticuerpos |
| AU2002364586A1 (en) | 2001-12-21 | 2003-07-30 | Delta Biotechnology Limited | Albumin fusion proteins |
| CA2484556A1 (en) | 2001-12-21 | 2003-07-24 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| US7332580B2 (en) | 2002-04-05 | 2008-02-19 | The Regents Of The University Of California | Bispecific single chain Fv antibody molecules and methods of use thereof |
| CA2499816C (en) | 2002-09-27 | 2013-07-30 | Xencor, Inc. | Optimized fc variants and methods for their generation |
| CA2513213C (en) | 2003-01-22 | 2013-07-30 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| WO2004082640A2 (en) | 2003-03-19 | 2004-09-30 | New Century Pharmaceuticals, Inc. | Human serum albumin conjugates with therapeutic compounds |
| SI1729795T1 (sl) | 2004-02-09 | 2016-04-29 | Human Genome Sciences, Inc. | Albuminski fuzijski proteini |
| JP5620626B2 (ja) | 2005-03-31 | 2014-11-05 | 中外製薬株式会社 | 会合制御によるポリペプチド製造方法 |
| CA2628253A1 (en) | 2005-11-03 | 2007-08-30 | Genentech, Inc. | Therapeutic anti-her2 antibody fusion polypeptides |
| US8441210B2 (en) | 2006-01-20 | 2013-05-14 | Point Somee Limited Liability Company | Adaptive current regulation for solid state lighting |
| ES2549128T3 (es) | 2006-05-19 | 2015-10-23 | Technion Research And Development Foundation Ltd. | Proteínas de fusión, usos de las mismas y procesos para producir las mismas |
| EP2799449A1 (en) | 2006-05-25 | 2014-11-05 | Bayer Intellectual Property GmbH | Dimeric molecular complexes |
| EP2032607B2 (en) | 2006-06-14 | 2017-02-22 | CSL Behring GmbH | Proteolytically cleavable fusion protein comprising a blood coagulation factor |
| WO2008140493A2 (en) | 2006-11-21 | 2008-11-20 | The Regents Of The University Of Californina | Anti-egfr family antibodies, bispecific anti-egfr family antibodies and methods of use thereof |
| US20080260738A1 (en) | 2007-04-18 | 2008-10-23 | Moore Margaret D | Single chain fc, methods of making and methods of treatment |
| WO2009012784A2 (en) | 2007-07-20 | 2009-01-29 | Nya Hamlet Pharma Ab | Methods for preparing cytotoxic complexes of emulsifier and fatty acid |
| US8197196B2 (en) | 2007-08-31 | 2012-06-12 | General Electric Company | Bushing and clock spring assembly for moveable turbine vane |
| PT2235064E (pt) | 2008-01-07 | 2016-03-01 | Amgen Inc | Método de preparação de moléculas heterodiméricas de fc de anticorpos utilizando efeitos de indução eletrostática |
| CA2711826C (en) | 2008-01-25 | 2018-02-27 | Amgen Inc. | Ferroportin antibodies and methods of use |
| CA2717015A1 (en) * | 2008-03-05 | 2009-09-11 | Ablynx Nv | Novel antigen binding dimer-complexes, methods of making and uses thereof |
| EP2285969B1 (en) | 2008-05-15 | 2013-01-16 | National Research Council Of Canada | Use of protein kinase b and valproic acid to increase heterologous gene expression in mammalian cells |
| WO2010027903A2 (en) | 2008-09-08 | 2010-03-11 | Fred Hutchinson Cancer Research Center | Lung cancer diagnosis |
| CN102282168A (zh) | 2008-11-18 | 2011-12-14 | 梅里麦克制药股份有限公司 | 人血清白蛋白接头以及其结合物 |
| KR101722961B1 (ko) * | 2009-02-11 | 2017-04-04 | 알부메딕스 에이/에스 | 알부민 변이체 및 접합체 |
| WO2010118169A2 (en) * | 2009-04-08 | 2010-10-14 | The Regents Of The University Of California | Human protein scaffold with controlled serum pharmacokinetics |
| US9493578B2 (en) | 2009-09-02 | 2016-11-15 | Xencor, Inc. | Compositions and methods for simultaneous bivalent and monovalent co-engagement of antigens |
| CA2777242A1 (en) | 2009-10-14 | 2011-04-21 | Merrimack Pharmaceuticals, Inc. | Bispecific binding agents targeting igf-1r and erbb3 signalling and uses thereof |
| MX2012004793A (es) | 2009-10-30 | 2012-07-20 | Novozymes Biopharma Dk As | Variantes de albumina. |
| JP5960598B2 (ja) * | 2009-11-04 | 2016-08-02 | アフィボディ・アーベー | Ｈｅｒ３結合ポリペプチド |
| WO2011069090A1 (en) | 2009-12-04 | 2011-06-09 | Alavita Pharmaceuticals, Inc. | Inhibition of the activation of coagulation factor xii by ligands of phosphatidylserine |
| RU2012145183A (ru) | 2010-03-29 | 2014-05-10 | Займворкс, Инк. | Антитела с повышенной или пониженной эффекторной функцией |
| DK2560683T4 (da) * | 2010-04-23 | 2022-08-29 | Hoffmann La Roche | Fremstilling af heteromultimeriske proteiner |
| EP2569337A1 (en) | 2010-05-14 | 2013-03-20 | Rinat Neuroscience Corp. | Heterodimeric proteins and methods for producing and purifying them |
| EP2575880B1 (en) | 2010-05-27 | 2019-01-16 | Genmab A/S | Monoclonal antibodies against her2 epitope |
| WO2012006635A1 (en) | 2010-07-09 | 2012-01-12 | Biogen Idec Hemophilia Inc. | Processable single chain molecules and polypeptides made using same |
| RU2604490C2 (ru) | 2010-11-05 | 2016-12-10 | Займворкс Инк. | ДИЗАЙН УСТОЙЧИВОГО ГЕТЕРОДИМЕРНОГО АНТИТЕЛА С МУТАЦИЯМИ В Fc ДОМЕНЕ |
| AU2012222833B2 (en) * | 2011-03-03 | 2017-03-16 | Zymeworks Inc. | Multivalent heteromultimer scaffold design and constructs |
| PT2748201T (pt) | 2011-08-23 | 2018-02-08 | Roche Glycart Ag | Moléculas de ligação ao antigénio biespecíficas que ativam as células t |
| KR102052774B1 (ko) | 2011-11-04 | 2019-12-04 | 자임워크스 인코포레이티드 | Ｆｃ 도메인 내의 돌연변이를 갖는 안정한 이종이합체 항체 설계 |
| JP6849868B2 (ja) | 2012-05-10 | 2021-03-31 | ザイムワークス，インコーポレイテッド | シングルアーム一価抗体構築物およびその用途 |
| CA2872540A1 (en) | 2012-05-10 | 2013-11-14 | Zymeworks Inc. | Heteromultimer constructs of immunoglobulin heavy chains with mutations in the fc domain |
| US9499634B2 (en) | 2012-06-25 | 2016-11-22 | Zymeworks Inc. | Process and methods for efficient manufacturing of highly pure asymmetric antibodies in mammalian cells |
| IN2015DN01115A (enExample) * | 2012-07-13 | 2015-06-26 | Zymeworks Inc | |
| CA2878843A1 (en) * | 2012-07-13 | 2014-01-16 | Zymeworks Inc. | Bispecific asymmetric heterodimers comprising anti-cd3 constructs |
| AU2013293092A1 (en) | 2012-07-23 | 2015-02-26 | Zymeworks Inc. | Immunoglobulin constructs comprising selective pairing of the light and heavy chains |
| US9914785B2 (en) | 2012-11-28 | 2018-03-13 | Zymeworks Inc. | Engineered immunoglobulin heavy chain-light chain pairs and uses thereof |
| KR102545617B1 (ko) | 2012-11-28 | 2023-06-20 | 자임워크스 비씨 인코포레이티드 | 가공된 면역글로불린 중쇄-경쇄 쌍 및 이들의 용도 |
| WO2014182970A1 (en) | 2013-05-08 | 2014-11-13 | Zymeworks Inc. | Bispecific her2 and her3 antigen binding constructs |
| MX2016000272A (es) | 2013-07-12 | 2016-08-03 | Zymeworks Inc | Construcciones de unión a los antígenos cd19 y cd3 biespecificos. |
| US9870656B2 (en) | 2015-12-08 | 2018-01-16 | Smartcar, Inc. | System and method for processing vehicle requests |
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| AU2013289881A1 (en) | 2015-02-26 |
| CN104768571B (zh) | 2018-11-09 |
| JP2015524799A (ja) | 2015-08-27 |
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