TW202208414A - April及baff抑制性免疫調節蛋白及其使用方法 - Google Patents
April及baff抑制性免疫調節蛋白及其使用方法 Download PDFInfo
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Families Citing this family (14)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA3077509A1 (en) | 2017-10-10 | 2019-04-18 | Alpine Immune Sciences, Inc. | Ctla-4 variant immunomodulatory proteins and uses thereof |
| AU2019205273B2 (en) | 2018-01-03 | 2024-04-04 | Alpine Immune Sciences, Inc. | Multi-domain immunomodulatory proteins and methods of use thereof |
| CN113573732A (zh) * | 2019-12-24 | 2021-10-29 | 荣昌生物制药(烟台)股份有限公司 | TACI-Fc融合蛋白及其用途 |
| PE20230494A1 (es) | 2020-05-08 | 2023-03-23 | Alpine Immune Sciences Inc | Proteinas inmunomoduladoras inhibidoras de april y baff y metodos de uso de las mismas |
| JP2024514077A (ja) * | 2021-03-31 | 2024-03-28 | 江▲蘇▼恒瑞医▲薬▼股▲フン▼有限公司 | 切断したtaciポリペプチド及びその融合タンパク質並びに使用 |
| CA3216795A1 (en) * | 2021-05-07 | 2022-11-10 | Alpine Immune Sciences, Inc. | Methods of dosing and treatment with a taci-fc fusion immunomodulatory protein |
| EP4384201A4 (en) * | 2021-08-11 | 2025-07-30 | Akso Biopharmaceutical Inc | METHODS FOR REDUCING THE PRODUCTION OF IGA, IGM AND/OR IGG IMMUNOGLOBULINS USING SBCMA VARIANTS AND THEIR FC FUSION PROTEINS |
| JP2024538452A (ja) * | 2021-11-17 | 2024-10-21 | オーリニア・ファーマシューティカルズ・インコーポレイテッド | B細胞活性化因子(baff)-増殖誘導リガンド(april)二重阻害剤 |
| JP2025501171A (ja) * | 2022-06-08 | 2025-01-17 | 榮昌生物制薬(烟台)股▲フン▼有限公司 | TACI-Fc融合タンパク質を用いた重症筋無力症の治療方法 |
| WO2024044721A1 (en) * | 2022-08-25 | 2024-02-29 | University Of Washington | Injectable recombinant protein-based hydrogels for therapeutic delivery |
| AU2023356958A1 (en) * | 2022-10-04 | 2025-04-03 | Alpine Immune Sciences, Inc. | Mutated taci-fc fusion proteins for use in the treatment of autoantibody-mediated diseases |
| AU2023391468A1 (en) * | 2022-12-05 | 2025-07-17 | Alexion Pharmaceuticals, Inc. | Taci-fc fusion proteins for multifunctional inhibition of baff, april, and neonatal fc receptor |
| WO2025007943A1 (zh) * | 2023-07-06 | 2025-01-09 | 荣昌生物制药(烟台)股份有限公司 | 用taci-fc融合蛋白治疗anca相关性血管炎的方法 |
| WO2025240392A1 (en) * | 2024-05-13 | 2025-11-20 | Paragon Therapeutics, Inc. | Fusion proteins |
Family Cites Families (173)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7045313B1 (en) | 1982-11-30 | 2006-05-16 | The United States Of America As Represented By The Department Of Health And Human Services | Recombinant vaccinia virus containing a chimeric gene having foreign DNA flanked by vaccinia regulatory DNA |
| US5168062A (en) | 1985-01-30 | 1992-12-01 | University Of Iowa Research Foundation | Transfer vectors and microorganisms containing human cytomegalovirus immediate-early promoter-regulatory DNA sequence |
| US4751180A (en) | 1985-03-28 | 1988-06-14 | Chiron Corporation | Expression using fused genes providing for protein product |
| US4935233A (en) | 1985-12-02 | 1990-06-19 | G. D. Searle And Company | Covalently linked polypeptide cell modulators |
| 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 |
| EP0307434B2 (en) | 1987-03-18 | 1998-07-29 | Scotgen Biopharmaceuticals, Inc. | Altered antibodies |
| US5443964A (en) | 1987-08-10 | 1995-08-22 | Duke University | Poxvirus insertion/expression vector |
| US5283173A (en) | 1990-01-24 | 1994-02-01 | The Research Foundation Of State University Of New York | System to detect protein-protein interactions |
| US6410010B1 (en) | 1992-10-13 | 2002-06-25 | Board Of Regents, The University Of Texas System | Recombinant P53 adenovirus compositions |
| DE69233186T2 (de) | 1991-05-06 | 2004-06-03 | The Government Of The United States Of America As Represented By The Secretary Of National Institute Of Health, Office Of Technology Transfer | Karcinoembryonale antigen expremierende rekombinante viren und methoden ihrer anwendung |
| CA2103059C (en) | 1991-06-14 | 2005-03-22 | Paul J. Carter | Method for making humanized antibodies |
| US5262522A (en) | 1991-11-22 | 1993-11-16 | Immunex Corporation | Receptor for oncostatin M and leukemia inhibitory factor |
| WO1994029351A2 (en) | 1993-06-16 | 1994-12-22 | Celltech Limited | Antibodies |
| US5457035A (en) | 1993-07-23 | 1995-10-10 | Immunex Corporation | Cytokine which is a ligand for OX40 |
| WO1996009380A1 (en) | 1994-09-23 | 1996-03-28 | The University Of British Columbia | Method of enhancing expression of mhc class i molecules bearing endogenous peptides |
| DE69519521T2 (de) | 1994-10-03 | 2001-06-28 | The Government Of The United States Of America, As Represented By The Secretary National Institute Of Health | Zusammensetzung enthaltend ein antigen exprimierendes rekombinantes virus und ein immunstimulierendes molekül exprimierendes rekombinantes virus |
| US5731168A (en) | 1995-03-01 | 1998-03-24 | Genentech, Inc. | Method for making heteromultimeric polypeptides |
| US5641870A (en) | 1995-04-20 | 1997-06-24 | Genentech, Inc. | Low pH hydrophobic interaction chromatography for antibody purification |
| CA2665133A1 (en) | 1996-10-25 | 1998-05-07 | Human Genome Sciences, Inc. | Neutrokine .alpha. |
| US5969102A (en) | 1997-03-03 | 1999-10-19 | St. Jude Children's Research Hospital | Lymphocyte surface receptor that binds CAML, nucleic acids encoding the same and methods of use thereof |
| DK0979281T3 (da) | 1997-05-02 | 2005-11-21 | Genentech Inc | Fremgangsmåde til fremstilling af multispecifikke antistoffer med heteromultimere og fælles bestanddele |
| GB9801930D0 (en) | 1998-01-29 | 1998-03-25 | Univ London | Mutant herpes simplex viruses and uses thereof |
| US6194551B1 (en) | 1998-04-02 | 2001-02-27 | Genentech, Inc. | Polypeptide variants |
| DK1068241T3 (da) | 1998-04-02 | 2008-02-04 | Genentech Inc | Antistofvarianter og fragmenter deraf |
| GB2337755B (en) | 1998-05-29 | 2003-10-29 | Secr Defence | Virus vaccine |
| WO2001060397A1 (en) | 2000-02-16 | 2001-08-23 | Genentech, Inc. | Uses of agonists and antagonists to modulate activity of tnf-related molecules |
| DK2272859T3 (en) | 1998-08-07 | 2015-01-19 | Univ Washington | Immunological herpes simplex virus antigens and methods for their use |
| US20060067933A1 (en) | 1999-01-07 | 2006-03-30 | Gross Jane A | Soluble receptor BR43x2 and methods of using |
| PT1642972E (pt) | 1999-01-07 | 2010-04-07 | Zymogenetics Inc | Utilizações terapêuticas de receptores solúveis br43x2 |
| US7833529B1 (en) | 1999-01-07 | 2010-11-16 | Zymogenetics, Inc. | Methods for inhibiting B lymphocyte proliferation with soluble ztnf4 receptor |
| ES2694002T3 (es) | 1999-01-15 | 2018-12-17 | Genentech, Inc. | Polipéptido que comprende una región Fc de IgG1 humana variante |
| US6737056B1 (en) | 1999-01-15 | 2004-05-18 | Genentech, Inc. | Polypeptide variants with altered effector function |
| US20030095967A1 (en) | 1999-01-25 | 2003-05-22 | Mackay Fabienne | BAFF, inhibitors thereof and their use in the modulation of B-cell response and treatment of autoimmune disorders |
| US20030022233A1 (en) | 1999-04-30 | 2003-01-30 | Raymond G. Goodwin | Methods of use of the taci/taci-l interaction |
| ES2308989T3 (es) | 1999-08-09 | 2008-12-16 | Targeted Genetics Corporation | Aumento de la expresion de una secuencia nucleotidica heterologa a partir de vectores viricos recombinantes que contienen una secuencia que forman pares de bases intracatenarios. |
| US7329728B1 (en) | 1999-10-25 | 2008-02-12 | The Scripps Research Institute | Ligand activated transcriptional regulator proteins |
| DE60122337T2 (de) | 2000-04-27 | 2007-08-16 | Biogen Idec Ma Inc., Cambridge | Verwendung von taci als antitumormittel |
| EP1746106A3 (en) | 2000-04-27 | 2007-03-14 | Biogen Idec MA Inc. | Use of TACI as an anti-tumor agent |
| US20040013674A1 (en) | 2001-04-27 | 2004-01-22 | Christine Ambrose | Taci as an anti-tumor agent |
| WO2001087977A2 (en) | 2000-05-12 | 2001-11-22 | Amgen Inc. | Methods and compositions of matter concerning april/g70, bcma, blys/agp-3, and taci |
| EP1294949A4 (en) | 2000-06-15 | 2004-08-25 | Human Genome Sciences Inc | HUMAN TUMORNESCROSE FACTOR DELTA AND EPSILON |
| KR20060088905A (ko) | 2000-06-16 | 2006-08-07 | 휴먼 게놈 사이언시즈, 인코포레이티드 | 면역특이적으로 BLyS에 결합하는 항체 |
| US7879328B2 (en) | 2000-06-16 | 2011-02-01 | Human Genome Sciences, Inc. | Antibodies that immunospecifically bind to B lymphocyte stimulator |
| US7220840B2 (en) | 2000-06-16 | 2007-05-22 | Human Genome Sciences, Inc. | Antibodies that immunospecifically bind to B lymphocyte stimulator protein |
| AU2001272978A1 (en) | 2000-06-23 | 2002-01-08 | Maxygen, Inc. | Novel co-stimulatory molecules |
| EP2301971A1 (en) | 2001-02-20 | 2011-03-30 | ZymoGenetics, L.L.C. | Antibodies that bind both BCMA and TACI |
| PL403488A1 (pl) | 2001-05-24 | 2013-07-08 | Zymogenetics, Inc. | Zastosowanie bialka fuzyjnego TACI-immunoglobulina, bialko fuzyjne, czasteczka kwasu nukleinowego kodujaca bialko fuzyjne, kompozycja farmaceutyczna i sposób wytwarzania bialka fuzyjnego TACI-immunoglobulina |
| CA2446734A1 (en) | 2001-05-24 | 2002-11-28 | Human Genome Sciences, Inc. | Antibodies against tumor necrosis factor delta (april) |
| PL377119A1 (pl) | 2001-08-03 | 2006-01-23 | Genentech, Inc. | Peptydy TACIs i BR3 i ich zastosowanie |
| WO2003055979A2 (en) | 2001-11-16 | 2003-07-10 | Human Genome Sciences, Inc. | ANTIBODIES THAT IMMUNOSPECIFICALLY BIND TO BLyS |
| US7247615B2 (en) | 2001-11-30 | 2007-07-24 | United States Of America, Represented By The Secretary, Department Of Health And Human Services | Peptide agonists of prostate-specific antigen and uses therefor |
| US8188231B2 (en) | 2002-09-27 | 2012-05-29 | Xencor, Inc. | Optimized FC variants |
| WO2004011611A2 (en) | 2002-07-25 | 2004-02-05 | Genentech, Inc. | Taci antibodies and uses thereof |
| JP2006502715A (ja) | 2002-10-11 | 2006-01-26 | ザイモジェネティクス,インコーポレイティド | ホモ3量体融合タンパク質の製造 |
| US7361740B2 (en) | 2002-10-15 | 2008-04-22 | Pdl Biopharma, Inc. | Alteration of FcRn binding affinities or serum half-lives of antibodies by mutagenesis |
| AR042485A1 (es) | 2002-12-16 | 2005-06-22 | Genentech Inc | Anticuerpo humanizado que se une al cd20 humano |
| MXPA05007019A (es) | 2002-12-30 | 2005-08-18 | Amgen Inc | Terapia de combinacion con factores co-estimuladores. |
| NZ543712A (en) | 2003-06-05 | 2008-06-30 | Genentech Inc | Combination therapy for B cell disorders |
| US20050163775A1 (en) | 2003-06-05 | 2005-07-28 | Genentech, Inc. | Combination therapy for B cell disorders |
| CN1897966A (zh) | 2003-10-20 | 2007-01-17 | 比奥根艾迪克Ma公司 | 使用baff拮抗剂的治疗方法 |
| EP2275448A3 (en) | 2003-12-19 | 2013-02-06 | Genentech, Inc. | Monovalent antibody fragments useful as therapeutics |
| CA2885854C (en) | 2004-04-13 | 2017-02-21 | F. Hoffmann-La Roche Ag | Anti-p-selectin antibodies |
| DK2471813T3 (en) | 2004-07-15 | 2015-03-02 | Xencor Inc | Optimized Fc variants |
| TWI309240B (en) | 2004-09-17 | 2009-05-01 | Hoffmann La Roche | Anti-ox40l antibodies |
| EP1810979B1 (en) | 2004-09-22 | 2012-06-20 | Kyowa Hakko Kirin Co., Ltd. | STABILIZED HUMAN IgG4 ANTIBODIES |
| CA2585927A1 (en) | 2004-11-04 | 2006-05-18 | Genentech, Inc. | Polypeptides that bind baff and/or april |
| US20090208924A1 (en) | 2004-12-01 | 2009-08-20 | Bayer Schering Pharma Aktiengesellschaft | Generation of Replication Competent Viruses for Therapeutic Use |
| US20080181888A1 (en) | 2004-12-31 | 2008-07-31 | Ambrose Christine M | Polypeptides That Bind Br3 and Uses Thereof |
| CN101198698B (zh) | 2005-03-31 | 2014-03-19 | 中外制药株式会社 | 通过调节多肽缔合制备多肽的方法 |
| KR101888321B1 (ko) | 2005-07-01 | 2018-08-13 | 이. 알. 스퀴부 앤드 선즈, 엘.엘.씨. | 예정 사멸 리간드 1 (피디-엘1)에 대한 인간 모노클로날 항체 |
| CN101262876A (zh) | 2005-08-09 | 2008-09-10 | 酶遗传学股份有限公司 | 用taci-ig融合分子治疗b细胞恶性肿瘤的方法 |
| WO2007019573A2 (en) | 2005-08-09 | 2007-02-15 | Zymogenetics, Inc. | Methods for the treatment and prevention of abnormal cell proliferation using taci-fusion molecules |
| AU2006281978A1 (en) | 2005-08-12 | 2007-02-22 | Garvan Institute Of Medical Research | Phrophylactic and/or therapeutic method for treatment of autoimmune disease |
| JP2007103345A (ja) | 2005-09-07 | 2007-04-19 | Toyota Motor Corp | チューブ状固体高分子型燃料電池、及びチューブ状固体高分子型燃料電池の製造方法 |
| EP1960525B1 (en) | 2005-09-09 | 2013-04-24 | Zymogenetics, Inc. | Method for preparing trimeric proteins |
| US9168286B2 (en) | 2005-10-13 | 2015-10-27 | Human Genome Sciences, Inc. | Methods and compositions for use in treatment of patients with autoantibody positive disease |
| CA2626082C (en) | 2005-10-13 | 2017-04-11 | Human Genome Sciences, Inc. | Methods and compositions for use in treatment of patients with autoantibody positive disease |
| US8202698B2 (en) | 2005-11-08 | 2012-06-19 | Biogen Idec Ma Inc. | Methods of evaluating BAFF |
| MX2008014365A (es) | 2006-05-15 | 2008-11-27 | Ares Trading Sa | Metodos para tratar enfermedades autoinmunitarias utilizando una molecula de fusion del activador de transmembrana-inmunoglobulina. |
| WO2008011636A2 (en) | 2006-07-21 | 2008-01-24 | California Institute Of Technology | Targeted gene delivery for dendritic cell vaccination |
| JP2010501622A (ja) | 2006-08-28 | 2010-01-21 | アレス トレーディング ソシエテ アノニム | Fc−融合タンパク質の精製法 |
| EP2061802A1 (en) | 2006-08-28 | 2009-05-27 | Ares Trading S.A. | Process for the purification of fc-fusion proteins |
| JP2010501623A (ja) | 2006-08-28 | 2010-01-21 | アレス トレーディング ソシエテ アノニム | Fc含有タンパク質の精製法 |
| WO2008092117A2 (en) | 2007-01-25 | 2008-07-31 | Xencor, Inc. | Immunoglobulins with modifications in the fcr binding region |
| ES2366593T3 (es) | 2007-01-26 | 2011-10-21 | Merck Serono S.A. | Purificación de proteínas de fusión taci-fc empleando la tecnología de cuerpos grasos. |
| ES2422479T3 (es) | 2007-03-27 | 2013-09-11 | Zymogenetics Inc | Combinación de inhibición de BLyS y micofenolato de mofetilo para tratamiento de enfermedades autoinmunitarias |
| PL2167038T3 (pl) | 2007-06-13 | 2018-10-31 | Zymogenetics, Inc. | Zastosowanie białka fuzyjnego TACI-lg, takiego jak atacicept, do wytwarzania leku do leczenia tocznia rumieniowatego |
| CN101323643B (zh) | 2007-06-15 | 2010-12-01 | 烟台荣昌生物工程有限公司 | 优化的TACI-Fc融合蛋白 |
| ES2362386T3 (es) | 2007-06-21 | 2011-07-04 | Technische Universität München | Proteínas activas biológicas que tienen estabilidad aumentada in vivo y/o in vitro. |
| JP2010533649A (ja) | 2007-07-13 | 2010-10-28 | ザ ジョンズ ホプキンス ユニバーシティー | B7−dc改変体 |
| EP2200631A1 (en) | 2007-10-16 | 2010-06-30 | Zymogenetics, Inc. | Combination of blys inhibition and anti-cd 20 agents for treatment of autoimmune disease |
| JP2011500757A (ja) | 2007-10-22 | 2011-01-06 | メルク セローノ ソシエテ アノニム | Fc含有タンパク質の精製方法 |
| JP2011503035A (ja) | 2007-11-12 | 2011-01-27 | アレス トレーディング ソシエテ アノニム | 視神経炎治療のためのtaci−免疫グロブリン融合タンパク質 |
| JP2011503036A (ja) | 2007-11-12 | 2011-01-27 | アレス トレーディング ソシエテ アノニム | 再発性多発性硬化症治療のためのtaci−免疫グロブリン融合タンパク質 |
| US8637021B2 (en) | 2007-11-12 | 2014-01-28 | Ares Trading S.A. | Formulations for TACI-immunoglobulin fusion proteins |
| TR201802323T4 (tr) | 2007-12-11 | 2018-03-21 | Univ North Carolina Chapel Hill | Polipürin yolu modifiye edilmiş retroviral vektörler. |
| WO2009132058A2 (en) | 2008-04-25 | 2009-10-29 | Zymogenetics, Inc. | Levels of bcma protein expression on b cells and use in diagnostic methods |
| US8003335B2 (en) | 2008-04-30 | 2011-08-23 | Universite Paris-SUD11 | Levels of APRIL in serum and use in diagnostic methods |
| HUE028784T2 (en) | 2008-05-01 | 2017-01-30 | Zymogenetics Inc | Serum levels and use of BLYS / APRIL heterotrimers in diagnostic procedures |
| WO2010003766A2 (en) | 2008-06-17 | 2010-01-14 | Apogenix Gmbh | Multimeric tnf receptors |
| MX2011002250A (es) | 2008-08-25 | 2011-08-17 | Amplimmune Inc | Antagonistas de muerte celular programada-1 y métodos de uso de los mismos. |
| US8217149B2 (en) | 2008-12-09 | 2012-07-10 | Genentech, Inc. | Anti-PD-L1 antibodies, compositions and articles of manufacture |
| EP2396035A4 (en) | 2009-02-12 | 2012-09-12 | Human Genome Sciences Inc | USE OF ANTAGONISTS OF PROTEIN STIMULATING LYMPHOCYTES B TO PROMOTE GRAFT TOLERANCE |
| CA2763439A1 (en) | 2009-05-28 | 2010-12-02 | Glaxo Group Limited | Antigen-binding proteins |
| WO2011109280A1 (en) | 2010-03-05 | 2011-09-09 | Lerner Research Institute | Methods and compositions to treat immune-mediated disorders |
| CN101851278B (zh) | 2010-05-26 | 2013-03-13 | 石药集团中奇制药技术(石家庄)有限公司 | B细胞激活因子拮抗剂及其制备方法与用途 |
| WO2011160086A2 (en) | 2010-06-18 | 2011-12-22 | Human Genome Sciences, Inc. | Use of b lymphocyte stimulator protein antagonists to treat asthma and other allergic and inflammatory conditions of the respiratory system |
| JP6267512B2 (ja) | 2010-09-10 | 2018-01-24 | ティゲニクス、エセ、ア、ウTiGenix,S.A.U. | 幹細胞培養培地および方法 |
| CN102085368B (zh) | 2011-01-19 | 2013-06-12 | 烟台荣昌生物工程有限公司 | 优化的TACI-Fc融合蛋白用于制备治疗系统性红斑狼疮药物的应用 |
| JP5972915B2 (ja) | 2011-03-16 | 2016-08-17 | アムジエン・インコーポレーテツド | Fc変異体 |
| EP3632463A1 (en) | 2011-04-08 | 2020-04-08 | Immune Design Corp. | Immunogenic compositions and methods of using the compositions for inducing humoral and cellular immune responses |
| US9469676B2 (en) | 2011-04-13 | 2016-10-18 | Bristol-Myers Squibb Company | Fc fusion proteins comprising novel linkers or arrangements |
| WO2012149364A1 (en) | 2011-04-28 | 2012-11-01 | Diamond Don J | Tumor associated vaccines and compositions for disrupting tumor-derived immunosuppression for use in combination cancer immunotherapy |
| WO2013041029A1 (en) * | 2011-09-23 | 2013-03-28 | Igenimed Pharmaceuticals Inc. | Novel soluble ctla4 variants |
| TWI476001B (zh) | 2011-12-26 | 2015-03-11 | Ind Tech Res Inst | 三倍體Fc融合蛋白及其用途 |
| CA3179537A1 (en) | 2012-02-27 | 2013-09-06 | Amunix Pharmaceuticals, Inc. | Xten conjugate compositions and methods of making same |
| CN102585016B (zh) * | 2012-03-06 | 2014-06-04 | 江苏健德生物药业有限公司 | 一种可同时抑制t、b淋巴细胞功能的免疫融合蛋白、其制备方法及其应用 |
| ES2707288T3 (es) | 2012-03-30 | 2019-04-03 | Immune Design Corp | Partículas de vectores lentivíricos que tienen eficiencia de transducción mejorada para células que expresan DC-SIGN |
| KR20150018604A (ko) | 2012-06-06 | 2015-02-23 | 온코메드 파마슈티칼스, 인크. | 히포 경로를 조절하는 결합제 및 그의 용도 |
| CN103232542B (zh) * | 2013-02-01 | 2015-05-13 | 殷勇 | 一种双靶标嵌合蛋白 |
| US10065987B2 (en) | 2013-02-12 | 2018-09-04 | Bristol-Myers Squibb Company | High pH protein refolding methods |
| WO2014126871A1 (en) | 2013-02-12 | 2014-08-21 | Bristol-Myers Squibb Company | Tangential flow filtration based protein refolding methods |
| HK1219740A1 (zh) | 2013-03-15 | 2017-04-13 | Biogen Ma Inc. | 使用抗αVβ5抗体治疗和预防急性肾损伤 |
| EP3835318B1 (en) | 2014-01-15 | 2025-10-29 | F. Hoffmann-La Roche AG | Fc-region variants with modified fcrn- and maintained protein a-binding properties |
| WO2015172305A1 (zh) | 2014-05-12 | 2015-11-19 | 上海康岱生物医药技术股份有限公司 | 抑制taci-baff复合物形成的融合蛋白及其制法和用途 |
| CA2947687C (en) | 2014-05-30 | 2021-07-06 | Ventana Medical Systems, Inc. | Multiplex assay for improved scoring of tumor tissues stained for pd-l1 |
| CA2955015A1 (en) | 2014-07-15 | 2016-01-21 | Immune Design Corp. | Prime-boost regimens with a tlr4 agonist adjuvant and a lentiviral vector |
| WO2016023001A1 (en) | 2014-08-08 | 2016-02-11 | The Board Of Trustees Of The Leland Stanford Junior University | Multispecific high affinity pd-1 agents and methods of use |
| NL2014108B1 (en) | 2015-01-09 | 2016-09-30 | Aduro Biotech Holdings Europe B V | Altered april binding antibodies. |
| CN115058395B (zh) | 2015-06-25 | 2025-07-18 | 美商生物细胞基因治疗有限公司 | 嵌合抗原受体(car)、组合物及其使用方法 |
| WO2017222593A1 (en) | 2016-06-24 | 2017-12-28 | Icell Gene Therapeutics Llc | Chimeric antigen receptors (cars), compositions and methods thereof |
| MA42895A (fr) | 2015-07-15 | 2018-05-23 | Juno Therapeutics Inc | Cellules modifiées pour thérapie cellulaire adoptive |
| SI3328419T1 (sl) | 2015-07-30 | 2021-11-30 | Macrogenics, Inc. | PD-1-vezavne molekule in postopki uporabe le-teh |
| PL3380522T3 (pl) | 2015-11-25 | 2024-03-25 | Visterra, Inc. | Cząsteczki przeciwciał wobec april i ich zastosowania |
| AU2016370376B2 (en) * | 2015-12-14 | 2023-12-14 | Macrogenics, Inc. | Bispecific molecules having immunoreactivity with PD-1 and CTLA-4, and methods of use thereof |
| ES2898329T3 (es) | 2016-01-12 | 2022-03-07 | Oncotracker Inc | Métodos mejorados para supervisar el estado inmunitario de un sujeto |
| AU2017250358B2 (en) | 2016-04-15 | 2023-06-01 | Alpine Immune Sciences, Inc. | ICOS ligand variant immunomodulatory proteins and uses thereof |
| IL262366B2 (en) | 2016-04-15 | 2024-07-01 | Alpine Immune Sciences Inc | Immunomodulatory proteins and CD80 variants and their uses |
| EP3452101A2 (en) | 2016-05-04 | 2019-03-13 | CureVac AG | Rna encoding a therapeutic protein |
| EP3458853B1 (en) | 2016-05-16 | 2022-09-07 | Onco Tracker, Inc. | Improved methods for monitoring immune status of a subject |
| WO2018022945A1 (en) | 2016-07-28 | 2018-02-01 | Alpine Immune Sciences, Inc. | Cd112 variant immunomodulatory proteins and uses thereof |
| EP3491013A1 (en) | 2016-07-28 | 2019-06-05 | Alpine Immune Sciences, Inc. | Cd155 variant immunomodulatory proteins and uses thereof |
| SG11201903407XA (en) | 2016-10-20 | 2019-05-30 | Alpine Immune Sciences Inc | Secretable variant immunomodulatory proteins and engineered cell therapy |
| US11732022B2 (en) | 2017-03-16 | 2023-08-22 | Alpine Immune Sciences, Inc. | PD-L2 variant immunomodulatory proteins and uses thereof |
| KR20250083578A (ko) | 2017-03-16 | 2025-06-10 | 알파인 이뮨 사이언시즈, 인코포레이티드 | Cd80 변이체 면역조절 단백질 및 그의 용도 |
| HUE064136T2 (hu) | 2017-03-16 | 2024-02-28 | Alpine Immune Sciences Inc | PD-L1 variáns immunmódosító fehérjék és alkalmazásuk |
| WO2018236995A2 (en) | 2017-06-20 | 2018-12-27 | Dana-Farber Cancer Institute, Inc. | Methods for modulating regulatory t cells, regulatory b cells, and immune responses using modulators of the april-taci interaction |
| AU2018326805B2 (en) | 2017-09-01 | 2023-11-30 | Dana-Farber Cancer Institute, Inc. | Immunogenic peptides specific to BCMA and TACI antigens for treatment of cancer |
| CA3077509A1 (en) | 2017-10-10 | 2019-04-18 | Alpine Immune Sciences, Inc. | Ctla-4 variant immunomodulatory proteins and uses thereof |
| IL320945A (en) | 2017-10-18 | 2025-07-01 | Alpine Immune Sciences Inc | Immunomodulatory proteins, ligands for ICOs, and compositions and methods related thereto |
| GB201720426D0 (en) | 2017-12-07 | 2018-01-24 | Hummingbird Bioscience Pte Ltd | CD47 and BCMA antigen-binding molecules |
| AU2019205273B2 (en) | 2018-01-03 | 2024-04-04 | Alpine Immune Sciences, Inc. | Multi-domain immunomodulatory proteins and methods of use thereof |
| IL276831B2 (en) | 2018-03-02 | 2025-04-01 | Allogene Therapeutics Inc | Chimeric inducible cytokine receptors |
| US20210238295A1 (en) | 2018-04-26 | 2021-08-05 | University Of Virginia Patent Foundation | Compositions and methods for treating abdominal aortic aneurysm |
| CN110522908A (zh) | 2018-05-25 | 2019-12-03 | 荣昌生物制药(烟台)有限公司 | TACI-Fc融合蛋白用于制备治疗视神经脊髓炎谱系疾病和多发性硬化之药物中的应用 |
| US12065476B2 (en) | 2018-06-15 | 2024-08-20 | Alpine Immune Sciences, Inc. | PD-1 variant immunomodulatory proteins and uses thereof |
| WO2020028572A2 (en) | 2018-08-01 | 2020-02-06 | Unum Therapeutics Inc. | ANTIBODY-COUPLED T CELL RECEPTORS (ACTRs) IN COMBINATION WITH TRANS CO-STIMULATORY MOLECULES AND THERAPEUTIC USES THEREOF |
| WO2020047329A1 (en) | 2018-08-29 | 2020-03-05 | Shattuck Labs, Inc. | Chimeric proteins comprising extracellular domains and uses thereof |
| JP2022501361A (ja) | 2018-09-19 | 2022-01-06 | アルパイン イミューン サイエンシズ インコーポレイテッド | バリアントcd80融合タンパク質および関連構築物の方法および使用 |
| AU2019377854A1 (en) | 2018-11-08 | 2021-05-27 | Juno Therapeutics, Inc. | Methods and combinations for treatment and T cell modulation |
| AU2019389151B2 (en) | 2018-11-30 | 2025-07-24 | Alpine Immune Sciences, Inc. | CD86 variant immunomodulatory proteins and uses thereof |
| WO2020214867A1 (en) | 2019-04-17 | 2020-10-22 | Alpine Immune Sciences, Inc. | Methods and uses of variant icos ligand (icosl) fusion proteins |
| AU2020292421A1 (en) | 2019-06-14 | 2022-01-27 | Cugene, Inc. | Novel interleukin-2 variants and bifunctional fusion molecules thereof |
| WO2021049606A1 (ja) | 2019-09-13 | 2021-03-18 | 協和キリン株式会社 | DcR3改変体 |
| WO2021115321A1 (zh) | 2019-12-10 | 2021-06-17 | 荣昌生物制药(烟台)股份有限公司 | TACI-Fc融合蛋白药物制剂 |
| CN113573732A (zh) | 2019-12-24 | 2021-10-29 | 荣昌生物制药(烟台)股份有限公司 | TACI-Fc融合蛋白及其用途 |
| PE20230494A1 (es) | 2020-05-08 | 2023-03-23 | Alpine Immune Sciences Inc | Proteinas inmunomoduladoras inhibidoras de april y baff y metodos de uso de las mismas |
| JP2023528875A (ja) | 2020-06-02 | 2023-07-06 | アレス トレーディング ソシエテ アノニム | IgA腎症の処置に関する方法 |
| CA3216795A1 (en) | 2021-05-07 | 2022-11-10 | Alpine Immune Sciences, Inc. | Methods of dosing and treatment with a taci-fc fusion immunomodulatory protein |
| BR112023018745A2 (pt) | 2021-08-10 | 2024-03-12 | Remegen Co Ltd | Método para tratar nefropatia por iga com proteína de fusão de taci-fc |
| US20240018212A1 (en) | 2021-09-30 | 2024-01-18 | RemeGen Co., Ltd | Method for treating sjogren's syndrome using taci-fc fusion protein |
| JP2025501171A (ja) | 2022-06-08 | 2025-01-17 | 榮昌生物制薬(烟台)股▲フン▼有限公司 | TACI-Fc融合タンパク質を用いた重症筋無力症の治療方法 |
| AU2023356958A1 (en) | 2022-10-04 | 2025-04-03 | Alpine Immune Sciences, Inc. | Mutated taci-fc fusion proteins for use in the treatment of autoantibody-mediated diseases |
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| TWI882569B (zh) * | 2022-12-07 | 2025-05-01 | 大陸商榮昌生物製藥(煙臺)股份有限公司 | TACI-Fc融合蛋白液體藥物製劑 |
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