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 (83)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2009059298A2 (en) * | 2007-11-01 | 2009-05-07 | Board Of Trustees Of The University Of Arkansas | Compositions and methods of enhancinc immune responses to eimeria |
| EP2310409A2 (en) | 2008-06-17 | 2011-04-20 | Apogenix GmbH | Multimeric tnf receptors |
| PL2604693T3 (pl) | 2008-07-21 | 2016-09-30 | Jednołańcuchowe cząsteczki TNFSF | |
| AU2009324637B2 (en) | 2008-12-10 | 2016-09-08 | Paka Pulmonary Pharmaceuticals, Inc. | Methods and compositions for delivery of medicaments to the lungs |
| WO2010078966A1 (en) * | 2009-01-09 | 2010-07-15 | 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 |
| US8932575B2 (en) | 2010-09-21 | 2015-01-13 | 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 |
| HRP20150664T1 (hr) * | 2010-12-03 | 2015-07-31 | Adamed Sp. Z O.O. | Antikancerogeni fuzijski 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 |
| US11219694B2 (en) | 2015-09-24 | 2022-01-11 | The University Of North Carolina At Chapel Hill | Methods and compositions for reducing metastases |
| CN108473549A (zh) | 2015-10-23 | 2018-08-31 | 阿珀吉科吉尼科斯股份公司 | 单链gitr受体激动剂蛋白 |
| EP3368558A1 (en) | 2015-10-28 | 2018-09-05 | 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 |
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| WO2018185247A1 (en) * | 2017-04-06 | 2018-10-11 | Universität Stuttgart | Tumor necrosis factor receptor (tnfr) binding protein complex with improved binding and bioactivity |
| WO2018209115A1 (en) | 2017-05-10 | 2018-11-15 | Iovance Biotherapeutics, Inc. | Expansion of tumor infiltrating lymphocytes from liquid tumors and therapeutic uses thereof |
| TW201919662A (zh) | 2017-06-05 | 2019-06-01 | 美商艾歐凡斯生物治療公司 | 對雙重難治性黑色素瘤使用腫瘤浸潤性淋巴細胞之方法 |
| WO2019089755A1 (en) | 2017-10-31 | 2019-05-09 | Western Oncolytics Ltd. | Platform oncolytic vector for systemic delivery |
| JP7557367B2 (ja) | 2017-11-17 | 2024-09-27 | 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 | 細針吸引及び小生検からのｔｉｌ拡大培養 |
| JP2021503885A (ja) | 2017-11-22 | 2021-02-15 | 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 | 末梢血からの末梢血リンパ球（ｐｂｌ）の拡大培養 |
| EP3724885A2 (en) | 2017-12-15 | 2020-10-21 | 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 |
| EP3737743A1 (en) | 2018-01-08 | 2020-11-18 | Iovance Biotherapeutics, Inc. | Processes for generating til products enriched for tumor antigen-specific t-cells |
| 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 |
| 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 |
| WO2019210131A1 (en) | 2018-04-27 | 2019-10-31 | Iovance Biotherapeutics, Inc. | Closed process for expansion and gene editing of tumor infiltrating lymphocytes and uses of same in immunotherapy |
| WO2019217753A1 (en) | 2018-05-10 | 2019-11-14 | Iovance Biotherapeutics, Inc. | Processes for production of tumor infiltrating lymphocytes and uses of same in immunotherapy |
| EP3807307A1 (en) * | 2018-06-14 | 2021-04-21 | 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 |
| SG11202101787XA (en) | 2018-09-20 | 2021-04-29 | Iovance Biotherapeutics Inc | Expansion of tils from cryopreserved tumor samples |
| CA3118493A1 (en) | 2018-11-05 | 2020-05-14 | Iovance Biotherapeutics, Inc. | Expansion of tils utilizing akt pathway inhibitors |
| IL282775B1 (en) | 2018-11-05 | 2026-05-01 | Iovance Biotherapeutics Inc | Selection of enhanced carrier-reactive T cells |
| 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 |
| BR112021008549A2 (pt) | 2018-11-05 | 2022-01-04 | Iovance Biotherapeutics Inc | Método de tratamento de carcinoma pulmonar de células não pequenas com uma população de linfócitos infiltrantes de tumor |
| WO2020131547A1 (en) | 2018-12-19 | 2020-06-25 | Iovance Biotherapeutics, Inc. | Methods of expanding tumor infiltrating lymphocytes using engineered cytokine receptor pairs and uses thereof |
| WO2020163534A1 (en) * | 2019-02-06 | 2020-08-13 | 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 |
| SG11202109331QA (en) | 2019-03-01 | 2021-09-29 | 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 |
| CN114269370A (zh) | 2019-03-29 | 2022-04-01 | 迈斯特治疗公司 | 离体产生t细胞治疗剂的方法以及相关的组合物和方法 |
| WO2020232029A1 (en) | 2019-05-13 | 2020-11-19 | Iovance Biotherapeutics, Inc. | Methods and compositions for selecting tumor infiltrating lymphocytes and uses of the same in immunotherapy |
| ES3031566T3 (en) | 2019-06-24 | 2025-07-09 | Univ 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 |
| IL293350A (en) | 2019-11-27 | 2022-07-01 | Myst Therapeutics Llc | Method of producing tumor-reactive t cell composition using modulatory agents |
| US12516291B2 (en) | 2019-12-11 | 2026-01-06 | Iovance Biotherapeutics, Inc. | Processes for the production of tumor infiltrating lymphocytes (TILs) and methods of using the same |
| EP4110799B1 (en) | 2020-02-27 | 2024-11-06 | Turnstone Biologics Corp. | Methods for ex vivo enrichment and expansion of tumor reactive t cells and related compositions thereof |
| EP4146793A1 (en) | 2020-05-04 | 2023-03-15 | Iovance Biotherapeutics, Inc. | Selection of improved tumor reactive t-cells |
| WO2021226061A1 (en) | 2020-05-04 | 2021-11-11 | Iovance Biotherapeutics, Inc. | Processes for production of tumor infiltrating lymphocytes and uses of the same in immunotherapy |
| CA3195019A1 (en) | 2020-10-06 | 2022-04-14 | Maria Fardis | Treatment of nsclc patients with tumor infiltrating lymphocyte therapies |
| WO2022076606A1 (en) | 2020-10-06 | 2022-04-14 | 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 |
| JP2023552289A (ja) | 2020-11-19 | 2023-12-15 | カリヴィル イムノセラピューティクス， インコーポレイテッド | 腫瘍微小環境リモデリングによる腫瘍溶解性免疫療法 |
| JP2024501452A (ja) | 2020-12-11 | 2024-01-12 | 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 | Ｂｒａｆ阻害剤及び／またはｍｅｋ阻害剤と併用した腫瘍浸潤リンパ球治療によるがん患者の治療 |
| JP2023554395A (ja) | 2020-12-17 | 2023-12-27 | 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 | Ｃｔｌａ－４及びｐｄ－１阻害剤と併用した腫瘍浸潤リンパ球療法による治療 |
| US20240123067A1 (en) | 2020-12-17 | 2024-04-18 | Iovance Biotherapeutics, Inc. | Treatment of cancers with tumor infiltrating lymphocyte therapies |
| US20240299540A1 (en) | 2021-02-05 | 2024-09-12 | 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 |
| EP4314253A2 (en) | 2021-03-25 | 2024-02-07 | Iovance Biotherapeutics, Inc. | Methods and compositions for t-cell coculture potency assays and use with cell therapy products |
| AU2022263418A1 (en) | 2021-04-19 | 2023-10-26 | Iovance Biotherapeutics, Inc. | Chimeric costimulatory receptors, chemokine receptors, and the use of same in cellular immunotherapies |
| EP4329786A4 (en) | 2021-04-30 | 2024-12-11 | 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 |
| EP4355789A4 (en) * | 2021-06-17 | 2025-11-19 | Kalivir Immunotherapeutics Inc | TNFSF-L Fusion Proteins and Their Uses |
| CA3226942A1 (en) | 2021-07-28 | 2023-02-02 | Iovance Biotherapeutics, Inc. | Treatment of cancer patients with tumor infiltrating lymphocyte therapies in combination with kras inhibitors |
| US20250000903A1 (en) | 2021-09-24 | 2025-01-02 | Iovance Biotherapeutics, Inc. | Expansion processes and agents for tumor infiltrating lymphocytes |
| US20230187042A1 (en) | 2021-10-27 | 2023-06-15 | Iovance Biotherapeutics, Inc. | Systems and methods for coordinating manufacturing of cells for patient-specific immunotherapy |
| AU2022388729A1 (en) | 2021-11-10 | 2024-05-16 | Iovance Biotherapeutics, Inc. | 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 |
| CN119654339A (zh) | 2022-07-01 | 2025-03-18 | 特兰斯吉恩股份有限公司 | 包含表面活性蛋白-d和tnfsf成员的融合蛋白 |
| EP4565683A1 (en) | 2022-08-01 | 2025-06-11 | Iovance Biotherapeutics, Inc. | Chimeric costimulatory receptors, chemokine receptors, and the use of same in cellular immunotherapies |
| US20260124242A1 (en) | 2022-11-04 | 2026-05-07 | 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 |
| IL328125A (en) | 2023-11-06 | 2026-06-01 | 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 |
| CA2225378C (en) * | 1995-06-29 | 2012-04-17 | 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 |
| WO2002036141A2 (en) * | 2000-11-02 | 2002-05-10 | 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 |
| AU2002359780B2 (en) | 2001-12-21 | 2009-08-13 | Immunex Corporation | Recombinant polypeptides |
| CA2482938A1 (en) | 2002-04-12 | 2003-10-23 | Human Genome Sciences, Inc. | Antibodies that specifically bind to tr2 |
| ES2279981T3 (es) | 2002-09-10 | 2007-09-01 | Natlmmune A/S | Proteinas quimericas activantes de colectina-complemento. |
| GB0524316D0 (en) * | 2005-11-29 | 2006-01-04 | Medical Res Council | Tumour necrosis factor-related apoptosis-inducing ligands (TRAILs) |
| WO2007120368A2 (en) * | 2006-01-09 | 2007-10-25 | The Regents Of The University Of California | Immunostimulatory combinations for vaccine adjuvants |
| 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 |
| US9309320B2 (en) * | 2006-12-28 | 2016-04-12 | Deutsches Krebsforschungszentrum Stiftung Des Oeffentlichen Rechts | Neutralization of CD95 activity blocks invasion of glioblastoma cells in vivo |
| WO2010078966A1 (en) | 2009-01-09 | 2010-07-15 | Apogenix Gmbh | Fusion proteins forming trimers |
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