JP6860342B2 - アフコシル化された抗ｆｇｆｒ２ｉｉｉｂ抗体 - Google Patents
アフコシル化された抗ｆｇｆｒ２ｉｉｉｂ抗体 Download PDFInfo
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- JP6860342B2 JP6860342B2 JP2016531878A JP2016531878A JP6860342B2 JP 6860342 B2 JP6860342 B2 JP 6860342B2 JP 2016531878 A JP2016531878 A JP 2016531878A JP 2016531878 A JP2016531878 A JP 2016531878A JP 6860342 B2 JP6860342 B2 JP 6860342B2
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| CN114901687A (zh) * | 2019-12-24 | 2022-08-12 | 迪哲(江苏)医药股份有限公司 | 新颖抗fgfr2b抗体 |
| CN115768465A (zh) | 2020-03-06 | 2023-03-07 | Ona疗法有限公司 | 抗cd36抗体及其治疗癌症的用途 |
| AU2021366691B2 (en) * | 2020-10-22 | 2024-06-06 | Regeneron Pharmaceuticals, Inc. | Anti-FGFR2 antibodies and methods of use thereof |
| JP2024501565A (ja) * | 2020-12-29 | 2024-01-12 | 深▲せん▼福沃薬業有限公司 | 抗ｆｇｆｒ２抗体およびその使用 |
| JP2024529502A (ja) | 2021-07-30 | 2024-08-06 | オーエヌエー セラピューティクス エセ．エレ． | 抗ｃｄ３６抗体及び癌を治療するためのそれらの使用 |
| EP4414387A4 (en) * | 2021-10-08 | 2025-10-29 | Shenzhen Forward Pharmaceuticals Co Ltd | ANTI-FGFR2 ANTIBODY WITH IMPROVED ADCC AND ITS USE |
| TW202342527A (zh) | 2022-02-25 | 2023-11-01 | 美商安進公司 | 鱗狀非小細胞肺癌之治療 |
| WO2024067876A1 (en) * | 2022-09-30 | 2024-04-04 | 3H Pharmaceuticals Co., Ltd. | Anti-fgfr2b antibodies and uses thereof |
| CN117917435A (zh) * | 2022-10-21 | 2024-04-23 | 北京天广实生物技术股份有限公司 | 结合fgfr2b的抗体及其用途 |
| AU2023416563A1 (en) * | 2022-12-28 | 2025-07-17 | Suzhou Transcenta Therapeutics Co., Ltd. | Anti-fgfr2b antibody and uses thereof |
| WO2024222912A1 (zh) * | 2023-04-28 | 2024-10-31 | 武汉人福创新药物研发中心有限公司 | 抗FGFR2b单抗 |
| WO2025103358A1 (en) * | 2023-11-14 | 2025-05-22 | Suzhou Transcenta Therapeutics Co., Ltd. | Anti-fgfr2b immunoconjugates and their use in the treatment of cancer |
| WO2025130860A1 (zh) * | 2023-12-18 | 2025-06-26 | 山东先声生物制药有限公司 | 抗FGFR2b抗体及其应用 |
| WO2025232811A1 (zh) * | 2024-05-09 | 2025-11-13 | 正大天晴药业集团股份有限公司 | 靶向成纤维细胞生长因子受体2IIIb的抗体及其应用 |
Family Cites Families (107)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US5981216A (en) | 1985-04-01 | 1999-11-09 | Alusuisse Holdings A.G. | Transformed myeloma cell-line and a process for the expression of a gene coding for a eukaryotic polypeptide employing same |
| US6548640B1 (en) | 1986-03-27 | 2003-04-15 | Btg International Limited | Altered antibodies |
| IL85035A0 (en) | 1987-01-08 | 1988-06-30 | Int Genetic Eng | Polynucleotide molecule,a chimeric antibody with specificity for human b cell surface antigen,a process for the preparation and methods utilizing the same |
| GB8717430D0 (en) | 1987-07-23 | 1987-08-26 | Celltech Ltd | Recombinant dna product |
| ATE179862T1 (de) | 1989-07-06 | 1999-05-15 | Univ California | Rezeptoren für fibroblasten-wachstumsfaktoren |
| US5863888A (en) | 1990-07-06 | 1999-01-26 | Rhone-Poulenc Rorer Pharmaceuticals Inc. | Human Bek Fibroblast growth factor receptor |
| AU675916B2 (en) | 1991-06-14 | 1997-02-27 | Genentech Inc. | Method for making humanized antibodies |
| GB9603256D0 (en) | 1996-02-16 | 1996-04-17 | Wellcome Found | Antibodies |
| US6323316B1 (en) | 1996-06-18 | 2001-11-27 | The United States Of America As Represented By The Secretary Of The Department Of And Human Services | Fibroblast growth factor receptor activating gene 1 and related compositions and methods |
| ES2244066T3 (es) | 1997-06-24 | 2005-12-01 | Genentech, Inc. | Procedimiento y composiciones de glicoproteinas galactosiladas. |
| DE69840412D1 (de) | 1997-10-31 | 2009-02-12 | Genentech Inc | Methoden und zusammensetzungen bestehend aus glykoprotein-glykoformen |
| ES2375931T3 (es) | 1997-12-05 | 2012-03-07 | The Scripps Research Institute | Humanización de anticuerpo murino. |
| US6194551B1 (en) | 1998-04-02 | 2001-02-27 | Genentech, Inc. | Polypeptide variants |
| AU3369999A (en) | 1998-04-02 | 1999-10-25 | Genentech Inc. | Antibody variants and fragments thereof |
| AU3657899A (en) | 1998-04-20 | 1999-11-08 | James E. Bailey | Glycosylation engineering of antibodies for improving antibody-dependent cellular cytotoxicity |
| WO2000025803A1 (en) | 1998-10-30 | 2000-05-11 | Takeda Chemical Industries, Ltd. | Betacellulin protein-containing preparations |
| US6737056B1 (en) | 1999-01-15 | 2004-05-18 | Genentech, Inc. | Polypeptide variants with altered effector function |
| EP2275540B1 (en) | 1999-04-09 | 2016-03-23 | Kyowa Hakko Kirin Co., Ltd. | Method for controlling the activity of immunologically functional molecule |
| EP1185559A2 (en) | 1999-04-28 | 2002-03-13 | Board Of Regents, The University Of Texas System | Compositions and methods for cancer treatment by selectively inhibiting vegf |
| AU7950400A (en) | 1999-10-19 | 2001-04-30 | Kyowa Hakko Kogyo Co. Ltd. | Process for producing polypeptide |
| JP2001302699A (ja) | 2000-04-17 | 2001-10-31 | Nichirei Corp | ヒトｋｇｆｒに対する抗体 |
| US7064191B2 (en) | 2000-10-06 | 2006-06-20 | Kyowa Hakko Kogyo Co., Ltd. | Process for purifying antibody |
| CA2424602C (en) | 2000-10-06 | 2012-09-18 | Kyowa Hakko Kogyo Co., Ltd. | Antibody composition-producing cell |
| US6946292B2 (en) | 2000-10-06 | 2005-09-20 | Kyowa Hakko Kogyo Co., Ltd. | Cells producing antibody compositions with increased antibody dependent cytotoxic activity |
| AU2002314495A1 (en) | 2001-06-20 | 2003-01-02 | Prochon Biotech Ltd. | Antibodies that block receptor protein tyrosine kinase activation, methods of screening for and uses thereof |
| EP2180044A1 (en) | 2001-08-03 | 2010-04-28 | GlycArt Biotechnology AG | Antibody glycosylation variants having increased anti-body-dependent cellular cytotoxicity |
| MXPA04003798A (es) | 2001-10-25 | 2004-07-30 | Genentech Inc | Composiciones de glicoproteina. |
| CN101357943A (zh) * | 2001-10-25 | 2009-02-04 | 杰南技术公司 | 糖蛋白组合物 |
| US20040093621A1 (en) | 2001-12-25 | 2004-05-13 | Kyowa Hakko Kogyo Co., Ltd | Antibody composition which specifically binds to CD20 |
| WO2003063893A2 (en) | 2002-01-31 | 2003-08-07 | MAX-PLANCK-Gesellschaft zur Förderung der Wissenschaften e.V. | Fgfr agonists |
| US7662925B2 (en) * | 2002-03-01 | 2010-02-16 | Xencor, Inc. | Optimized Fc variants and methods for their generation |
| US20040132101A1 (en) * | 2002-09-27 | 2004-07-08 | Xencor | Optimized Fc variants and methods for their generation |
| JPWO2003085118A1 (ja) | 2002-04-09 | 2005-08-11 | 協和醗酵工業株式会社 | 抗体組成物の製造方法 |
| AU2003236019A1 (en) | 2002-04-09 | 2003-10-20 | Kyowa Hakko Kirin Co., Ltd. | Drug containing antibody composition appropriate for patient suffering from Fc Gamma RIIIa polymorphism |
| PL373256A1 (en) | 2002-04-09 | 2005-08-22 | Kyowa Hakko Kogyo Co, Ltd. | Cells with modified genome |
| JPWO2003085119A1 (ja) | 2002-04-09 | 2005-08-11 | 協和醗酵工業株式会社 | 抗体組成物のＦｃγ受容体ＩＩＩａに対する結合活性を高める方法 |
| ATE503829T1 (de) | 2002-04-09 | 2011-04-15 | Kyowa Hakko Kirin Co Ltd | Zelle mit erniedrigter oder deletierter aktivität eines am gdp-fucosetransport beteiligten proteins |
| AU2003236017B2 (en) | 2002-04-09 | 2009-03-26 | Kyowa Kirin Co., Ltd. | Drug containing antibody composition |
| KR100493460B1 (ko) | 2002-08-29 | 2005-06-07 | 재단법인서울대학교산학협력재단 | 암 세포에서 발현되는 ｆｇｆｒ2 이성체 |
| US7217797B2 (en) | 2002-10-15 | 2007-05-15 | Pdl Biopharma, Inc. | Alteration of FcRn binding affinities or serum half-lives of antibodies by mutagenesis |
| TWI335821B (en) | 2002-12-16 | 2011-01-11 | Genentech Inc | Immunoglobulin variants and uses thereof |
| KR100973564B1 (ko) * | 2003-05-02 | 2010-08-03 | 젠코어 인코포레이티드 | 최적화된 Ｆｃ 변이체 및 그의 제조 방법 |
| JPWO2005035586A1 (ja) | 2003-10-08 | 2007-11-22 | 協和醗酵工業株式会社 | 融合蛋白質組成物 |
| EP1705251A4 (en) | 2003-10-09 | 2009-10-28 | Kyowa Hakko Kirin Co Ltd | PROCESS FOR PRODUCING ANTIBODY COMPOSITION BY RNA INHIBITION OF FUNCTION OF $ G (A) 1,6-FUCOSYLTRANSFERASE |
| SI1680140T1 (sl) * | 2003-10-16 | 2011-08-31 | Imclone Llc | Inhibitorji receptorja-1 za fibroblastni rastni faktor in metode za zdravljenje z le-temi |
| DK2330201T3 (en) | 2003-10-22 | 2017-07-24 | Keck Graduate Inst | PROCEDURES FOR SYNTHESIS OF HEATER-MULTIMATE POLYPEPTIDES WHEN USING A HAPLOID COUPLE STRATEGY |
| NO347530B1 (no) | 2003-11-05 | 2023-12-11 | Roche Glycart Ag | Et humanisert type II anti-CD20 antistoff og vertscelle som produserer et humanisert type II anti-CD20 antistoff samt en fremgangsmåte for fremstilling og en farmasøytisk sammensetning. |
| WO2005053742A1 (ja) | 2003-12-04 | 2005-06-16 | Kyowa Hakko Kogyo Co., Ltd. | 抗体組成物を含有する医薬 |
| EP1697420A2 (en) | 2003-12-19 | 2006-09-06 | Five Prime Therapeutics, Inc. | Fibroblast growth factor receptors 1, 2, 3, and 4 as targets for therapeutic intervention |
| RU2386638C2 (ru) | 2004-03-31 | 2010-04-20 | Дженентек, Инк. | Гуманизированные анти-тфр-бета-антитела |
| EP1773305A2 (en) | 2004-05-25 | 2007-04-18 | Yale University Corporation | Method for treating skeletal disorders resulting from fgfr malfunction |
| ATE454455T1 (de) | 2005-01-27 | 2010-01-15 | Five Prime Therapeutics Inc | Leitsequenzen zur anleitung von polypeptidsekretion und verfahren zur herstellung |
| SG170006A1 (en) * | 2005-02-18 | 2011-04-29 | Medarex Inc | Monoclonal antibodies against cd30 lacking fucosyl residues |
| US7923538B2 (en) | 2005-07-22 | 2011-04-12 | Kyowa Hakko Kirin Co., Ltd | Recombinant antibody composition |
| US7890267B2 (en) | 2006-03-31 | 2011-02-15 | Ordway Research Institute | Prognostic and diagnostic method for cancer therapy |
| WO2007134210A2 (en) | 2006-05-12 | 2007-11-22 | Genentech, Inc. | Methods and compositions for the diagnosis and treatment of cancer |
| CA2655246A1 (en) * | 2006-06-09 | 2007-12-21 | University Of Maryland, Baltimore | Glycosylation engineered antibody therapy |
| EP2046384A4 (en) | 2006-06-15 | 2009-12-02 | Fibron Ltd | ANTIBODIES BLOCKING FIBROBLAST GROWTH FACTOR RECEPTOR ACTIVATION AND METHODS OF USING THE SAME |
| AR062223A1 (es) | 2006-08-09 | 2008-10-22 | Glycart Biotechnology Ag | Moleculas de adhesion al antigeno que se adhieren a egfr, vectores que los codifican, y sus usos de estas |
| EP2066694B1 (en) | 2006-09-29 | 2015-11-04 | Oncomed Pharmaceuticals, Inc. | Compositions and methods for diagnosing and treating cancer |
| US8394927B2 (en) | 2006-11-03 | 2013-03-12 | U3 Pharma Gmbh | FGFR4 antibodies |
| CL2007003411A1 (es) | 2006-11-28 | 2008-07-04 | Centelion | Proteina fusion que consiste en una region fc de una inmunoglobulina con un fragmento o dominio soluble de un receptor para fgf; polinucleotido que la codifica y vector y celula que lo comprenden; composicion farmaceutica que comprende la proteina fu |
| US20090068110A1 (en) | 2006-12-22 | 2009-03-12 | Genentech, Inc. | Antibodies to insulin-like growth factor receptor |
| US20080226635A1 (en) | 2006-12-22 | 2008-09-18 | Hans Koll | Antibodies against insulin-like growth factor I receptor and uses thereof |
| JP5071942B2 (ja) | 2007-01-24 | 2012-11-14 | 協和発酵キリン株式会社 | エフェクター活性が増強された遺伝子組換え抗体組成物 |
| BRPI0809137A2 (pt) | 2007-03-23 | 2016-07-26 | Translational Genomics Res Inst | métodos de diagnosticar, câncer endometrial e pré-câncer classificar e tratar |
| WO2008121876A2 (en) * | 2007-03-28 | 2008-10-09 | Biogen Idec Inc. | Non-fucosylated antibodies |
| WO2009052830A1 (en) | 2007-10-22 | 2009-04-30 | Genmab A/S | Novel antibody therapies |
| US9260525B2 (en) | 2008-02-04 | 2016-02-16 | Xiao-Jia Chang | Antibody molecules to oncogenic isoforms of fibroblast growth factor receptor-2 and uses thereof |
| US20110059091A1 (en) | 2008-02-04 | 2011-03-10 | Xiao-Jia Chang | Inhibitors of oncogenic isoforms and uses thereof |
| US8688158B2 (en) | 2008-03-26 | 2014-04-01 | Nec Corporation | Radio resource control method, radio station apparatus, recording medium storing radio station control program, and radio communication system |
| CA2727247A1 (en) * | 2008-06-10 | 2009-12-17 | University Of Southern California | Thymidylate synthase haplotype is associated with tumor recurrence in stage ii and stage iii colon cancer patients |
| EP2177615A1 (en) | 2008-10-10 | 2010-04-21 | Fraunhofer-Gesellschaft zur Förderung der angewandten Forschung e.V. | Method for a genome wide identification of expression regulatory sequences and use of genes and molecules derived thereof for the diagnosis and therapy of metabolic and/or tumorous diseases |
| LT2842573T (lt) | 2008-11-07 | 2017-12-11 | Galaxy Biotech, Llc | Monokloniniai antikūnai prieš fibroblastų augimo faktoriaus receptorių-2 |
| WO2011025814A1 (en) | 2009-08-25 | 2011-03-03 | National Jewish Health | Methods and compositions for treatment of lung injury |
| CN102666874B (zh) * | 2009-10-07 | 2016-06-01 | 宏观基因有限公司 | 由于岩藻糖基化程度的改变而表现出改善的效应子功能的含Fc区的多肽及其使用方法 |
| EP2488554B1 (en) * | 2009-10-14 | 2019-07-24 | Humanigen, Inc. | Antibodies to epha3 |
| CN102762221A (zh) | 2010-01-14 | 2012-10-31 | 耶鲁大学 | 受体酪氨酸激酶(rtk)的抑制剂及其使用方法 |
| US9140689B2 (en) | 2010-03-14 | 2015-09-22 | Translational Genomics Research Institute | Methods of determining susceptibility of tumors to tyrosine kinase inhibitors |
| BR112012028764A2 (pt) | 2010-05-11 | 2017-03-14 | Aveo Pharmaceuticals Inc | anticor-pos antifgfr2 |
| US8907053B2 (en) | 2010-06-25 | 2014-12-09 | Aurigene Discovery Technologies Limited | Immunosuppression modulating compounds |
| EP2603521A4 (en) | 2010-08-12 | 2014-10-01 | Attogen Inc | ANTIBODY MOLECULARS FOR ONGOGEN FIBROBLAST GROWTH RECEPTOR 2 ISOFORMS AND ITS USES |
| US20120258496A1 (en) * | 2010-09-27 | 2012-10-11 | Boehringer Ingelheim International Gmbh | Production of low fucose antibodies in h4-ii-e rat cells |
| EP3828205A1 (en) * | 2010-10-01 | 2021-06-02 | Oxford BioTherapeutics Ltd | Anti-ror1 antibodies |
| CN103857699B (zh) | 2011-05-24 | 2016-08-31 | 泽恩格尼亚股份有限公司 | 多价和单价多特异性复合物及其用途 |
| AR088941A1 (es) | 2011-11-23 | 2014-07-16 | Bayer Ip Gmbh | Anticuerpos anti-fgfr2 y sus usos |
| US20150023989A1 (en) | 2011-12-14 | 2015-01-22 | Seattle Genetics, Inc. | New antibody drug conjugates (adcs) and the use thereof |
| DK2831110T3 (en) * | 2012-03-30 | 2018-08-06 | Univ California | Anti-EMP2 therapy to reduce cancer stem cells |
| JP6188681B2 (ja) | 2012-04-09 | 2017-08-30 | 第一三共株式会社 | 抗ｆｇｆｒ２抗体 |
| US9254288B2 (en) | 2012-05-07 | 2016-02-09 | The Translational Genomics Research Institute | Susceptibility of tumors to tyrosine kinase inhibitors and treatment thereof |
| KR102418979B1 (ko) | 2012-05-15 | 2022-07-11 | 브리스톨-마이어스 스큅 컴퍼니 | Pd-1/pd-l1 신호전달을 방해하는 것에 의한 암 면역요법 |
| CN104619840A (zh) | 2012-07-05 | 2015-05-13 | 日本国立癌症研究中心 | Fgfr2融合基因 |
| WO2014089193A1 (en) | 2012-12-04 | 2014-06-12 | Aveo Pharmaceuticals, Inc. | Anti-fgfr2 antibodies |
| AU2014207342C1 (en) | 2013-01-18 | 2019-04-04 | Foundation Medicine, Inc. | Methods of treating cholangiocarcinoma |
| US9415118B2 (en) | 2013-03-13 | 2016-08-16 | Novartis Ag | Antibody drug conjugates |
| US9498532B2 (en) | 2013-03-13 | 2016-11-22 | Novartis Ag | Antibody drug conjugates |
| HK1213817A1 (zh) | 2013-05-01 | 2016-07-15 | 戊瑞治疗有限公司 | 治療癌症的方法 |
| EP3800266A1 (en) | 2013-06-13 | 2021-04-07 | University Of South Australia | Methods for detecting prostate cancer |
| CA2915665C (en) | 2013-08-01 | 2020-07-28 | Five Prime Therapeutics, Inc. | Afucosylated anti-fgfr2iiib antibodies |
| JOP20200094A1 (ar) | 2014-01-24 | 2017-06-16 | Dana Farber Cancer Inst Inc | جزيئات جسم مضاد لـ pd-1 واستخداماتها |
| US20170175197A1 (en) | 2014-01-29 | 2017-06-22 | Caris Mpi, Inc. | Molecular profiling of immune modulators |
| KR20170080675A (ko) | 2014-11-05 | 2017-07-10 | 제넨테크, 인크. | 항-fgfr2/3 항체 및 이의 이용 방법 |
| WO2016100882A1 (en) | 2014-12-19 | 2016-06-23 | Novartis Ag | Combination therapies |
| US10478494B2 (en) | 2015-04-03 | 2019-11-19 | Astex Therapeutics Ltd | FGFR/PD-1 combination therapy for the treatment of cancer |
| WO2017091580A1 (en) | 2015-11-23 | 2017-06-01 | Five Prime Therapeutics, Inc. | Predicting response to cancer treatment with fgfr2 inhibitors |
| LT3624837T (lt) | 2017-05-16 | 2025-10-10 | Anti-fgfr2 antikūnai derinyje su chemoterapijos agentais vėžio gydymui |
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