ES2560871T3 - Proteínas de fusión de colectina de la superfamilia de TNF - Google Patents
Proteínas de fusión de colectina de la superfamilia de TNF Download PDFInfo
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- ES2560871T3 ES2560871T3 ES08773964.5T ES08773964T ES2560871T3 ES 2560871 T3 ES2560871 T3 ES 2560871T3 ES 08773964 T ES08773964 T ES 08773964T ES 2560871 T3 ES2560871 T3 ES 2560871T3
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Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP07013506 | 2007-07-10 | ||
| EP07013506 | 2007-07-10 | ||
| PCT/EP2008/005644 WO2009007120A2 (en) | 2007-07-10 | 2008-07-10 | Tnf superfamily collectin fusion proteins |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2560871T3 true ES2560871T3 (es) | 2016-02-23 |
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| Application Number | Title | Priority Date | Filing Date |
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| ES08773964.5T Active ES2560871T3 (es) | 2007-07-10 | 2008-07-10 | Proteínas de fusión de colectina de la superfamilia de TNF |
| ES16150412.1T Active ES2657801T3 (es) | 2007-07-10 | 2008-07-10 | Proteínas de fusión de colectina de la superfamilia de TNF |
| ES12166865.1T Active ES2567704T3 (es) | 2007-07-10 | 2008-07-10 | Proteínas de fusión de colectina de la superfamilia de TNF |
Family Applications After (2)
| Application Number | Title | Priority Date | Filing Date |
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| ES16150412.1T Active ES2657801T3 (es) | 2007-07-10 | 2008-07-10 | Proteínas de fusión de colectina de la superfamilia de TNF |
| ES12166865.1T Active ES2567704T3 (es) | 2007-07-10 | 2008-07-10 | Proteínas de fusión de colectina de la superfamilia de TNF |
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Families Citing this family (82)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP3097926B1 (en) * | 2007-11-01 | 2019-10-02 | The Board of Trustees of the University of Arkansas | Compositions and methods of enhancing immune responses to eimeria |
| ES2524553T3 (es) | 2008-06-17 | 2014-12-10 | Apogenix Gmbh | Receptores multiméricos de TNF |
| EP2806029B1 (en) | 2008-07-21 | 2016-05-25 | Apogenix AG | TNFSF single chain molecules |
| CA2744940A1 (en) | 2008-12-10 | 2010-06-17 | Paka Pulmonary Pharmaceuticals, Inc. | Methods and compositions for delivery of medicaments to the lungs |
| US8664366B2 (en) | 2009-01-09 | 2014-03-04 | Apogenix Gmbh | Fusion proteins forming trimers |
| CN101698852B (zh) * | 2009-10-23 | 2014-08-13 | 江苏先声药物研究有限公司 | 具有cd137l功能的蛋白或多肽及其基因和应用 |
| JP4918627B2 (ja) * | 2010-02-26 | 2012-04-18 | 積水メディカル株式会社 | 偽陽性反応を抑制する検体抽出液 |
| WO2012040101A1 (en) | 2010-09-21 | 2012-03-29 | University Of Miami | Compositions and methods for inducing migration by dendritic cells and an immune response |
| WO2012040266A2 (en) * | 2010-09-24 | 2012-03-29 | University Of Miami | Gene-based adjuvants and compositions thereof to increase antibody production in response to gene-based vaccines |
| SG189370A1 (en) * | 2010-12-03 | 2013-05-31 | Adamed Sp Zoo | Anticancer fusion protein |
| EP2586793A1 (en) * | 2011-10-27 | 2013-05-01 | Centre National de la Recherche Scientifique | Chimeric molecule involving oligomerized FasL extracellular domain |
| US20150191506A1 (en) * | 2012-06-29 | 2015-07-09 | Asahi Kasei Medical Co., Ltd. | Adsorbent consisting of carrier which bound with polypeptide comprising b-domain mutant derived from protein a |
| NO2776305T3 (enExample) | 2014-04-23 | 2018-01-27 | ||
| WO2016079527A1 (en) | 2014-11-19 | 2016-05-26 | Tetralogic Birinapant Uk Ltd | Combination therapy |
| WO2016097773A1 (en) | 2014-12-19 | 2016-06-23 | Children's Cancer Institute | Therapeutic iap antagonists for treating proliferative disorders |
| MA41460A (fr) | 2015-02-03 | 2017-12-12 | Oncomed Pharm Inc | Agents de liaison à la tnfrsf et leurs utilisations |
| EP3352800B1 (en) * | 2015-09-24 | 2022-01-05 | The University of North Carolina at Chapel Hill | Methods and compositions for reducing metastases |
| JP6959229B2 (ja) * | 2015-10-23 | 2021-11-02 | アポジェニックス アーゲー | 一本鎖ｇｉｔｒ受容体アゴニストタンパク質 |
| CA3003511A1 (en) | 2015-10-28 | 2017-05-04 | Apogenix Ag | Single-chain tl1a receptor agonist proteins |
| TWI788307B (zh) | 2016-10-31 | 2023-01-01 | 美商艾歐凡斯生物治療公司 | 用於擴增腫瘤浸潤性淋巴細胞之工程化人造抗原呈現細胞 |
| CA3049165A1 (en) | 2017-01-06 | 2018-07-12 | Iovance Biotherapeutics, Inc. | Expansion of tumor infiltrating lymphocytes with potassium channel agonists and therapeutic uses thereof |
| JP7780248B2 (ja) | 2017-01-06 | 2025-12-04 | アイオバンス バイオセラピューティクス，インコーポレイテッド | 腫瘍壊死因子受容体スーパーファミリー（ｔｎｆｒｓｆ）アゴニストによる腫瘍浸潤リンパ球（ｔｉｌ）の拡大培養及びｔｉｌとｔｎｆｒｓｆアゴニストとの治療的併用 |
| EP3606949A1 (en) * | 2017-04-06 | 2020-02-12 | Universität Stuttgart | Tumor necrosis factor receptor (tnfr) binding protein complex with improved binding and bioactivity |
| TW201904578A (zh) | 2017-05-10 | 2019-02-01 | 美商艾歐凡斯生物治療公司 | 源自液體腫瘤之腫瘤浸潤性淋巴細胞的擴增和該經擴增腫瘤浸潤性淋巴細胞之治療用途 |
| AR112072A1 (es) | 2017-06-05 | 2019-09-18 | Iovance Biotherapeutics Inc | Métodos de uso de linfocitos infiltrantes de tumor en melanoma doble refractario |
| CA3081436A1 (en) | 2017-10-31 | 2019-05-09 | Western Oncolytics Ltd. | Platform oncolytic vector for systemic delivery |
| MX2020004967A (es) | 2017-11-17 | 2020-08-27 | Iovance Biotherapeutics Inc | Expansion de linfocitos infiltrantes del tumor (til) de aspirados con aguja fina y biopsias por puncion. |
| CA3083118A1 (en) | 2017-11-22 | 2019-05-31 | Iovance Biotherapeutics, Inc. | Expansion of peripheral blood lymphocytes (pbls) from peripheral blood |
| CA3085765A1 (en) | 2017-12-15 | 2019-06-20 | Iovance Biotherapeutics, Inc. | Systems and methods for determining the beneficial administration of tumor infiltrating lymphocytes, and methods of use thereof and beneficial administration of tumor infiltrating lymphocytes, and methods of use thereof |
| US11713446B2 (en) | 2018-01-08 | 2023-08-01 | Iovance Biotherapeutics, Inc. | Processes for generating TIL products enriched for tumor antigen-specific T-cells |
| WO2019136459A1 (en) | 2018-01-08 | 2019-07-11 | Iovance Biotherapeutics, Inc. | Processes for generating til products enriched for tumor antigen-specific t-cells |
| JP2021509586A (ja) | 2018-01-08 | 2021-04-01 | アイオバンス バイオセラピューティクス，インコーポレイテッド | 腫瘍抗原特異的ｔ細胞について濃縮されたｔｉｌ製品を生成するためのプロセス |
| CA3090795A1 (en) | 2018-02-13 | 2019-08-22 | Iovance Biotherapeutics, Inc. | Expansion of tumor infiltrating lymphocytes (tils) with adenosine a2a receptor antagonists and therapeutic combinations of tils and adenosine a2a receptor antagonists |
| EA202092319A1 (ru) | 2018-03-29 | 2021-03-04 | Айовэнс Байотерапьютикс, Инк. | Способы получения опухоль-инфильтрирующих лимфоцитов и применения их в иммунотерапии |
| SG11202010319RA (en) | 2018-04-27 | 2020-11-27 | Iovance Biotherapeutics Inc | Closed process for expansion and gene editing of tumor infiltrating lymphocytes and uses of same in immunotherapy |
| US12473532B2 (en) | 2018-05-10 | 2025-11-18 | Iovance Biotherapeutics, Inc. | Processes for production of tumor infiltrating lymphocytes and uses of same in immunotherapy |
| CA3098498A1 (en) * | 2018-06-14 | 2019-12-19 | Nantbio, Inc. | Tnf-type receptor-ligand fusion proteins and methods |
| TW202031273A (zh) | 2018-08-31 | 2020-09-01 | 美商艾歐凡斯生物治療公司 | 抗ｐｄ－１抗體難治療性之非小細胞肺癌（ｎｓｃｌｃ）病患的治療 |
| JP7658896B2 (ja) | 2018-09-20 | 2025-04-08 | アイオバンス バイオセラピューティクス，インコーポレイテッド | 凍結保存腫瘍サンプルからのｔｉｌの拡大培養 |
| KR20210099573A (ko) | 2018-11-05 | 2021-08-12 | 이오반스 바이오테라퓨틱스, 인크. | 개선된 종양 반응성 t-세포의 선택 |
| CA3118634A1 (en) | 2018-11-05 | 2020-05-14 | Iovance Biotherapeutics, Inc. | Treatment of nsclc patients refractory for anti-pd-1 antibody |
| JP2022506508A (ja) | 2018-11-05 | 2022-01-17 | アイオバンス バイオセラピューティクス，インコーポレイテッド | Ａｋｔ経路阻害剤を利用したｔｉｌの拡大培養 |
| US12453697B2 (en) | 2018-11-05 | 2025-10-28 | Iovance Biotherapeutics, Inc. | Processes for production of tumor infiltrating lymphocytes and uses of the same in immunotherapy |
| EP3898949A1 (en) | 2018-12-19 | 2021-10-27 | Iovance Biotherapeutics, Inc. | Methods of expanding tumor infiltrating lymphocytes using engineered cytokine receptor pairs and uses thereof |
| US20220135649A1 (en) * | 2019-02-06 | 2022-05-05 | The Regents Of The University Of California | Dominant negative cd40l polypeptides |
| CN113677712A (zh) * | 2019-02-15 | 2021-11-19 | 爱披萨佛公司 | 染色质相关蛋白的定量作图 |
| US20220133795A1 (en) | 2019-03-01 | 2022-05-05 | Iovance Biotherapeutics, Inc. | Expansion of Tumor Infiltrating Lymphocytes From Liquid Tumors and Therapeutic Uses Thereof |
| WO2020180144A1 (ko) * | 2019-03-07 | 2020-09-10 | 경북대학교 산학협력단 | 트레일 트라이머와 암표적 펩타이드를 멀티디스플레이하는 페리틴 나노케이지 및 이의 항암제로서의 용도 |
| KR20220002336A (ko) | 2019-03-29 | 2022-01-06 | 미스트 쎄라퓨틱스, 엘엘씨 | T 세포 치료제를 제조하기 위한 생체외 방법 및 관련 조성물 및 방법 |
| US20220249559A1 (en) | 2019-05-13 | 2022-08-11 | Iovance Biotherapeutics, Inc. | Methods and compositions for selecting tumor infiltrating lymphocytes and uses of the same in immunotherapy |
| EP3986920B1 (en) | 2019-06-24 | 2025-04-16 | Universität Stuttgart | Tnfr2 agonists with improved stability |
| EP4048295A1 (en) | 2019-10-25 | 2022-08-31 | Iovance Biotherapeutics, Inc. | Gene editing of tumor infiltrating lymphocytes and uses of same in immunotherapy |
| EP4065229A1 (en) | 2019-11-27 | 2022-10-05 | Myst Therapeutics, LLC | Method of producing tumor-reactive t cell composition using modulatory agents |
| CA3161104A1 (en) | 2019-12-11 | 2021-06-17 | Cecile Chartier-Courtaud | Processes for the production of tumor infiltrating lymphocytes (tils) and methods of using the same |
| AU2021226903A1 (en) | 2020-02-27 | 2022-10-20 | Turnstone Biologics Corp. | Methods for ex vivo enrichment and expansion of tumor reactive T cells and related compositions thereof |
| CA3176826A1 (en) | 2020-05-04 | 2021-11-11 | Iovance Biotherapeutics, Inc. | Processes for production of tumor infiltrating lymphocytes and uses of the same in immunotherapy |
| CA3177413A1 (en) | 2020-05-04 | 2021-11-11 | Michelle SIMPSON-ABELSON | Selection of improved tumor reactive t-cells |
| WO2022076606A1 (en) | 2020-10-06 | 2022-04-14 | Iovance Biotherapeutics, Inc. | Treatment of nsclc patients with tumor infiltrating lymphocyte therapies |
| EP4225330A1 (en) | 2020-10-06 | 2023-08-16 | Iovance Biotherapeutics, Inc. | Treatment of nsclc patients with tumor infiltrating lymphocyte therapies |
| WO2022079308A1 (en) * | 2020-10-16 | 2022-04-21 | Institut Pasteur | Chimeric constructs useful in vaccination and cancer therapy |
| AU2021385059A1 (en) | 2020-11-19 | 2023-06-08 | Kalivir Immunotherapeutics, Inc. | Oncolytic immunotherapy by tumor micro-environment remodeling |
| TW202241468A (zh) | 2020-12-11 | 2022-11-01 | 美商艾歐凡斯生物治療公司 | 用腫瘤浸潤性淋巴球療法與ｂｒａｆ抑制劑及／或ｍｅｋ抑制劑組合治療癌症患者 |
| AU2021401302A1 (en) | 2020-12-17 | 2023-07-06 | Iovance Biotherapeutics, Inc. | Treatment with tumor infiltrating lymphocyte therapies in combination with ctla-4 and pd-1 inhibitors |
| EP4262827A1 (en) | 2020-12-17 | 2023-10-25 | Iovance Biotherapeutics, Inc. | Treatment of cancers with tumor infiltrating lymphocytes |
| EP4288140A1 (en) | 2021-02-05 | 2023-12-13 | Iovance Biotherapeutics, Inc. | Adjuvant therapy for cancer |
| JP2024509184A (ja) | 2021-03-05 | 2024-02-29 | アイオバンス バイオセラピューティクス，インコーポレイテッド | 腫瘍保存及び細胞培養組成物 |
| EP4326287A2 (en) | 2021-04-19 | 2024-02-28 | Iovance Biotherapeutics, Inc. | Chimeric costimulatory receptors, chemokine receptors, and the use of same in cellular immunotherapies |
| IL316712B2 (en) | 2021-04-30 | 2025-12-01 | Kalivir Immunotherapeutics Inc | Oncolytic viruses for modified mhc expression |
| US20240269180A1 (en) | 2021-05-17 | 2024-08-15 | Iovance Biotherapeutics, Inc. | Pd-1 gene-edited tumor infiltrating lymphocytes and uses of same in immunotherapy |
| WO2022266163A2 (en) * | 2021-06-17 | 2022-12-22 | Kalivir Immunotherapeutics, Inc. | Tnfsf-l fusion proteins and uses thereof |
| JP2024527961A (ja) | 2021-07-28 | 2024-07-26 | アイオバンス バイオセラピューティクス，インコーポレイテッド | Ｋｒａｓ阻害剤と併用した腫瘍浸潤リンパ球療法によるがん患者の治療 |
| WO2023049862A1 (en) | 2021-09-24 | 2023-03-30 | Iovance Biotherapeutics, Inc. | Expansion processes and agents for tumor infiltrating lymphocytes |
| WO2023077015A2 (en) | 2021-10-27 | 2023-05-04 | Iovance Biotherapeutics, Inc. | Systems and methods for coordinating manufacturing of cells for patient-specific immunotherapy |
| CA3237410A1 (en) | 2021-11-10 | 2023-05-19 | Friedrich Graf Finck VON FINCKENSTEIN | Methods of expansion treatment utilizing cd8 tumor infiltrating lymphocytes |
| WO2023088889A1 (en) | 2021-11-16 | 2023-05-25 | Apogenix Ag | CD137 ligands |
| JP2025503987A (ja) | 2022-01-28 | 2025-02-06 | アイオバンス バイオセラピューティクス，インコーポレイテッド | ペイロードを発現するように操作された腫瘍浸潤リンパ球 |
| EP4507704A1 (en) | 2022-04-15 | 2025-02-19 | Iovance Biotherapeutics, Inc. | Til expansion processes using specific cytokine combinations and/or akti treatment |
| KR20250034101A (ko) | 2022-07-01 | 2025-03-10 | 트랜스진 | 계면활성제-단백질-d 및 tnfsf의 구성원을 포함하는 융합 단백질 |
| EP4565683A1 (en) | 2022-08-01 | 2025-06-11 | Iovance Biotherapeutics, Inc. | Chimeric costimulatory receptors, chemokine receptors, and the use of same in cellular immunotherapies |
| WO2024098024A1 (en) | 2022-11-04 | 2024-05-10 | Iovance Biotherapeutics, Inc. | Expansion of tumor infiltrating lymphocytes from liquid tumors and therapeutic uses thereof |
| WO2024151885A1 (en) | 2023-01-13 | 2024-07-18 | Iovance Biotherapeutics, Inc. | Use of til as maintenance therapy for nsclc patients who achieved pr/cr after prior therapy |
| WO2025101484A1 (en) | 2023-11-06 | 2025-05-15 | Iovance Biotherapeutics, Inc. | Treatment of endometrial cancers with tumor infiltrating lymphocyte therapies |
Family Cites Families (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB9409768D0 (en) * | 1994-05-16 | 1994-07-06 | Medical Res Council | Trimerising polypeptides |
| AU708239B2 (en) | 1995-06-29 | 1999-07-29 | Immunex Corporation | Cytokine that induces apoptosis |
| US7300774B1 (en) | 1999-12-09 | 2007-11-27 | The Regents Of The University Of California | Multimeric fusion proteins of the TNF superfamily ligands |
| DE19963859A1 (de) * | 1999-12-30 | 2001-07-12 | Apotech Res & Dev Ltd | Bi- oder Oligomer eines Di-, Tri-, Quattro- oder Pentamers von rekombinanten Fusionsproteinen |
| GB0015426D0 (en) * | 2000-06-24 | 2000-08-16 | Univ Southampton | Method for generating soluble highly multimeric proteins |
| AU2002232447A1 (en) * | 2000-11-02 | 2002-05-15 | Immunex Corporation | Method of enhancing lymphocyte-mediated immune responses |
| DE10122140A1 (de) * | 2001-05-08 | 2002-11-28 | Apotech Res & Dev Ltd | Rekombinante Fusionsproteine und deren Trimere |
| JP4660092B2 (ja) * | 2001-12-21 | 2011-03-30 | イミユネツクス・コーポレイシヨン | 組換えポリペプチド |
| EP1499351A4 (en) * | 2002-04-12 | 2006-04-05 | Human Genome Sciences Inc | ANTIBODIES BINDING SPECIFICALLY TO TR2 |
| ATE349538T1 (de) | 2002-09-10 | 2007-01-15 | Natlmmune As | Collectin-komplement aktivierende proteinchimären |
| GB0524316D0 (en) * | 2005-11-29 | 2006-01-04 | Medical Res Council | Tumour necrosis factor-related apoptosis-inducing ligands (TRAILs) |
| EP1979488A4 (en) * | 2006-01-09 | 2009-05-27 | Univ California | IMMUNOSTIMULATING COMBINATIONS OF TNFRSF, TLR, NLR, RHR, PURINERIC RECEPTOR, AND CYTOKIN RECEPTOR ANTONISTS FOR VACCINES AND TUMOR IMMUNOTHERAPY |
| WO2007102690A1 (en) | 2006-03-06 | 2007-09-13 | Postech Foundation | Vector including the codon-optimized dna cassette for producing secretory recombinant dodecamer trail |
| EP1894940A1 (en) | 2006-08-28 | 2008-03-05 | Apogenix GmbH | TNF superfamily fusion proteins |
| CA2673868C (en) * | 2006-12-28 | 2016-03-22 | Deutsches Krebsforschungszentrum Stiftung Des Oeffentlichen Rechts | Neutralization of cd95 activity blocks invasion of glioblastoma cells in vivo |
| US8664366B2 (en) | 2009-01-09 | 2014-03-04 | Apogenix Gmbh | Fusion proteins forming trimers |
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