CA2927099A1 - Specific anti-cd38 antibodies for treating human cancers - Google Patents
Specific anti-cd38 antibodies for treating human cancers Download PDFInfo
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- CA2927099A1 CA2927099A1 CA2927099A CA2927099A CA2927099A1 CA 2927099 A1 CA2927099 A1 CA 2927099A1 CA 2927099 A CA2927099 A CA 2927099A CA 2927099 A CA2927099 A CA 2927099A CA 2927099 A1 CA2927099 A1 CA 2927099A1
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- A61K31/57—Compounds containing cyclopenta[a]hydrophenanthrene ring systems; Derivatives thereof, e.g. steroids substituted in position 17 beta by a chain of two carbon atoms, e.g. pregnane or progesterone
- A61K31/573—Compounds containing cyclopenta[a]hydrophenanthrene ring systems; Derivatives thereof, e.g. steroids substituted in position 17 beta by a chain of two carbon atoms, e.g. pregnane or progesterone substituted in position 21, e.g. cortisone, dexamethasone, prednisone or aldosterone
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- A61K39/39533—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals
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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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- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
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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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Landscapes
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| JOP20210044A1 (ar) | 2010-12-30 | 2017-06-16 | Takeda Pharmaceuticals Co | الأجسام المضادة لـ cd38 |
| US10342869B2 (en) * | 2012-12-07 | 2019-07-09 | The Regents Of The University Of California | Compositions comprising anti-CD38 antibodies and lenalidomide |
| IL241407B (en) * | 2013-03-13 | 2022-06-01 | Univ California | Compositions comprising anti-cd38 antibodies and carfilzomib |
| US9732154B2 (en) | 2014-02-28 | 2017-08-15 | Janssen Biotech, Inc. | Anti-CD38 antibodies for treatment of acute lymphoblastic leukemia |
| US9603927B2 (en) | 2014-02-28 | 2017-03-28 | Janssen Biotech, Inc. | Combination therapies with anti-CD38 antibodies |
| MX386886B (es) | 2014-09-09 | 2025-03-12 | Janssen Biotech Inc | Combinación de anticuerpos anti-cd38 y ácido todo-trans retinoico para usarse en terapias. |
| US10793630B2 (en) | 2014-12-04 | 2020-10-06 | Janssen Biotech, Inc. | Anti-CD38 antibodies for treatment of acute myeloid leukemia |
| PT3294769T (pt) * | 2015-05-13 | 2021-04-13 | Morphosys Ag | Tratamento para mieloma múltiplo (mm) |
| KR102602754B1 (ko) * | 2015-05-20 | 2023-11-14 | 얀센 바이오테크 인코포레이티드 | 경쇄 아밀로이드증 및 다른 cd38-양성 혈액학적 악성종양을 치료하기 위한 항-cd38 항체 |
| EP3303373B1 (en) | 2015-05-30 | 2020-04-08 | Molecular Templates, Inc. | De-immunized, shiga toxin a subunit scaffolds and cell-targeting molecules comprising the same |
| WO2016201337A1 (en) * | 2015-06-12 | 2016-12-15 | Immungene, Inc. | Engineered antibody-interferon fusion molecules for the treatment of glucose-regulated protein 94 (grp94) expressing cancers |
| PE20181323A1 (es) | 2015-06-22 | 2018-08-14 | Janssen Biotech Inc | Terapias de combinacion para enfermedades malignas hematologicas con anticuerpos anti-cd38 e inhibidores de survivina |
| US20170044265A1 (en) | 2015-06-24 | 2017-02-16 | Janssen Biotech, Inc. | Immune Modulation and Treatment of Solid Tumors with Antibodies that Specifically Bind CD38 |
| US10781261B2 (en) | 2015-11-03 | 2020-09-22 | Janssen Biotech, Inc. | Subcutaneous formulations of anti-CD38 antibodies and their uses |
| BR112018008901A8 (pt) | 2015-11-03 | 2019-02-26 | Janssen Biotech Inc | formulações subcutâneas de anticorpos anti-cd 38 e seus usos |
| JP7362250B2 (ja) | 2016-03-04 | 2023-10-17 | モルフォシス・アーゲー | 多発性骨髄腫におけるｍタンパク質反応の臨床評価 |
| KR20230129583A (ko) | 2016-06-21 | 2023-09-08 | 테네오바이오, 인코포레이티드 | Cd3 결합 항체 |
| CA3030834A1 (en) | 2016-07-15 | 2018-01-18 | Takeda Pharmaceutical Company Limited | Methods and materials for assessing response to plasmablast- and plasma cell-depleting therapies |
| EP4050034B1 (en) | 2016-09-14 | 2024-05-08 | TeneoOne, Inc. | Cd3 binding antibodies |
| KR102633423B1 (ko) | 2016-12-21 | 2024-02-06 | 테네오바이오, 인코포레이티드 | 항-bcma 중쇄-단독 항체 |
| CA3067584A1 (en) | 2017-06-20 | 2018-12-27 | Teneobio, Inc. | Anti-bcma heavy chain-only antibodies |
| US11427642B2 (en) | 2017-06-20 | 2022-08-30 | Teneoone, Inc. | Anti-BCMA heavy chain-only antibodies |
| JPWO2019031444A1 (ja) * | 2017-08-07 | 2020-08-27 | 国立大学法人九州大学 | 細胞集団における特異的結合物質の占有率を測定する方法 |
| WO2019035938A1 (en) | 2017-08-16 | 2019-02-21 | Elstar Therapeutics, Inc. | MULTISPECIFIC MOLECULES BINDING TO BCMA AND USES THEREOF |
| JP2020533362A (ja) * | 2017-09-13 | 2020-11-19 | テネオバイオ， インコーポレイテッド | エクト酵素に結合する重鎖抗体 |
| WO2019089832A1 (en) | 2017-10-31 | 2019-05-09 | Janssen Biotech, Inc. | Methods of treating high risk multiple myeloma |
| KR20200076732A (ko) | 2017-11-03 | 2020-06-29 | 소렌토 쎄라퓨틱스, 인코포레이티드 | Cd38-지시된 키메라 항원 수용체 작제물 |
| BR112020014052A2 (pt) | 2018-01-12 | 2020-12-08 | Takeda Pharmaceutical Company Limited | Dosagem subcutânea de anticorpos anti-cd38 |
| KR20250117714A (ko) * | 2018-03-28 | 2025-08-05 | 다케다 야쿠힌 고교 가부시키가이샤 | 항-cd38 항체의 피하 투약 |
| AU2019301283B2 (en) * | 2018-07-10 | 2024-12-19 | Sanofi | Combination therapies against cancer targeting CD38 and TGF-beta |
| MX2021007047A (es) | 2018-12-14 | 2021-10-26 | Morphosys Ag | Formulaciones de anticuerpos. |
| CN113853204A (zh) * | 2019-03-21 | 2021-12-28 | 盖米达细胞有限公司 | 适用于移植组合疗法的扩增nk细胞组分的扩增及其用途 |
| KR20210149076A (ko) | 2019-04-05 | 2021-12-08 | 테네오바이오, 인코포레이티드 | Psma에 결합하는 중쇄 항체 |
| US11655302B2 (en) | 2019-06-10 | 2023-05-23 | Sanofi | Anti-CD38 antibodies and formulations |
| BR112021024956A2 (pt) | 2019-06-14 | 2022-01-25 | Teneobio Inc | Anticorpos multiespecíficos de cadeia pesada que se ligam a cd22 e cd3 |
| CN112876563B (zh) * | 2019-11-29 | 2022-08-16 | 康诺亚生物医药科技（成都）有限公司 | 药物组合物及其制备方法和应用 |
| EP4069743A1 (en) | 2019-12-05 | 2022-10-12 | Sanofi-Aventis U.S. LLC | Formulations of anti-cd38 antibodies for subcutaneous administration |
| MX2022006883A (es) * | 2019-12-06 | 2022-11-08 | Sanofi Aventis Us Llc | Uso de isatuximab para el tratamiento del mieloma multiple recidivante y/o refractario. |
| WO2021259227A1 (zh) * | 2020-06-23 | 2021-12-30 | 江苏康缘药业股份有限公司 | 抗cd38抗体及其用途 |
| US20240018248A1 (en) | 2020-12-02 | 2024-01-18 | Vib Vzw | An ltbr agonist in combination therapy against cancer |
| TW202432177A (zh) * | 2022-10-31 | 2024-08-16 | 丹麥商珍美寶股份有限公司 | Ｃｄ３８抗體及其用途 |
Family Cites Families (32)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4444887A (en) | 1979-12-10 | 1984-04-24 | Sloan-Kettering Institute | Process for making human antibody producing B-lymphocytes |
| US4716111A (en) | 1982-08-11 | 1987-12-29 | Trustees Of Boston University | Process for producing human antibodies |
| GB8607679D0 (en) | 1986-03-27 | 1986-04-30 | Winter G P | Recombinant dna product |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| GB8928874D0 (en) | 1989-12-21 | 1990-02-28 | Celltech Ltd | Humanised antibodies |
| WO1991010741A1 (en) | 1990-01-12 | 1991-07-25 | Cell Genesys, Inc. | Generation of xenogeneic antibodies |
| US5814318A (en) | 1990-08-29 | 1998-09-29 | Genpharm International Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
| EP0519596B1 (en) | 1991-05-17 | 2005-02-23 | Merck & Co. Inc. | A method for reducing the immunogenicity of antibody variable domains |
| US5565332A (en) | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| US5639641A (en) | 1992-09-09 | 1997-06-17 | Immunogen Inc. | Resurfacing of rodent antibodies |
| DE69637481T2 (de) | 1995-04-27 | 2009-04-09 | Amgen Fremont Inc. | Aus immunisierten Xenomäusen stammende menschliche Antikörper gegen IL-8 |
| AU2466895A (en) | 1995-04-28 | 1996-11-18 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US5916771A (en) | 1996-10-11 | 1999-06-29 | Abgenix, Inc. | Production of a multimeric protein by cell fusion method |
| DE69738539T2 (de) | 1996-12-03 | 2009-03-26 | Amgen Fremont Inc. | Vollkommen humane Antikörper die EGFR binden |
| ES2172149T3 (es) | 1997-04-14 | 2002-09-16 | Micromet Ag | Nuevo metodo para la produccion de receptores de antigeno anti-humano y sus usos. |
| US6235883B1 (en) | 1997-05-05 | 2001-05-22 | Abgenix, Inc. | Human monoclonal antibodies to epidermal growth factor receptor |
| CN1976950B (zh) * | 2004-02-06 | 2012-08-29 | 莫佛塞斯公司 | 抗cd38人抗体及其用途 |
| IL316252A (en) | 2005-03-23 | 2024-12-01 | Genmab As | Antibodies against cd38 for treatment of multiple myeloma |
| EP2799451A1 (en) * | 2005-05-24 | 2014-11-05 | MorphoSys AG | Generation and profiling of fully human HuCAL GOLD®-derived therapeutic antibodies specific for human CD38 |
| EP2081595B1 (en) * | 2006-09-26 | 2019-04-10 | Genmab A/S | Anti-cd38 plus corticosteroids plus a non-corticosteroid chemotherapeutic for treating tumors |
| EP1914242A1 (en) * | 2006-10-19 | 2008-04-23 | Sanofi-Aventis | Novel anti-CD38 antibodies for the treatment of cancer |
| EP2050764A1 (en) | 2007-10-15 | 2009-04-22 | sanofi-aventis | Novel polyvalent bispecific antibody format and uses thereof |
| EP2191843A1 (en) | 2008-11-28 | 2010-06-02 | Sanofi-Aventis | Antitumor combinations containing antibodies recognizing specifically CD38 and cyclophosphamide |
| EP2191842A1 (en) | 2008-11-28 | 2010-06-02 | Sanofi-Aventis | Antitumor combinations containing antibodies recognizing specifically CD38 and cytarabine |
| EP2191841A1 (en) | 2008-11-28 | 2010-06-02 | Sanofi-Aventis | Antitumor combinations containing antibodies recognizing specifically CD38 and vincristine |
| EP2191840A1 (en) | 2008-11-28 | 2010-06-02 | Sanofi-Aventis | Antitumor combinations containing antibodies recognizing specifically CD38 and melphalan |
| UA112170C2 (uk) * | 2010-12-10 | 2016-08-10 | Санофі | Протипухлинна комбінація, що містить антитіло, яке специфічно розпізнає cd38, і бортезоміб |
| JOP20210044A1 (ar) * | 2010-12-30 | 2017-06-16 | Takeda Pharmaceuticals Co | الأجسام المضادة لـ cd38 |
| EA034989B1 (ru) * | 2011-10-28 | 2020-04-15 | Тева Фармасьютикал Австралия Пти Лтд | Полипептидная конструкция для применения при лечении рака, включающая аттенуированный альфа-интерферон |
| US10342869B2 (en) * | 2012-12-07 | 2019-07-09 | The Regents Of The University Of California | Compositions comprising anti-CD38 antibodies and lenalidomide |
| IL241407B (en) * | 2013-03-13 | 2022-06-01 | Univ California | Compositions comprising anti-cd38 antibodies and carfilzomib |
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2014
- 2014-10-31 TW TW103137932A patent/TW201522378A/zh unknown
- 2014-10-31 BR BR112016009403A patent/BR112016009403A2/pt not_active Application Discontinuation
- 2014-10-31 CA CA2927099A patent/CA2927099A1/en not_active Abandoned
- 2014-10-31 AU AU2014342103A patent/AU2014342103B2/en active Active
- 2014-10-31 MA MA44560A patent/MA44560B2/fr unknown
- 2014-10-31 SG SG11201603088RA patent/SG11201603088RA/en unknown
- 2014-10-31 MX MX2016005666A patent/MX373301B/es active IP Right Grant
- 2014-10-31 PT PT147990899T patent/PT3063173T/pt unknown
- 2014-10-31 MA MA39070A patent/MA39070A1/fr unknown
- 2014-10-31 EA EA201690905A patent/EA035098B1/ru not_active IP Right Cessation
- 2014-10-31 CN CN201480071448.0A patent/CN106103481A/zh active Pending
- 2014-10-31 EP EP14799089.9A patent/EP3063173B1/en active Active
- 2014-10-31 WO PCT/US2014/063380 patent/WO2015066450A1/en not_active Ceased
- 2014-10-31 PL PL14799089T patent/PL3063173T3/pl unknown
- 2014-10-31 US US14/529,719 patent/US20150118251A1/en not_active Abandoned
- 2014-10-31 JP JP2016527374A patent/JP2016536314A/ja active Pending
- 2014-10-31 NZ NZ719784A patent/NZ719784A/en unknown
- 2014-10-31 TN TN2016000142A patent/TN2016000142A1/en unknown
- 2014-10-31 SG SG10201803288RA patent/SG10201803288RA/en unknown
- 2014-10-31 EP EP20188077.0A patent/EP3805266A1/en not_active Withdrawn
- 2014-10-31 KR KR1020167013974A patent/KR20160077155A/ko not_active Ceased
-
2016
- 2016-04-19 IL IL245196A patent/IL245196B/en active IP Right Grant
- 2016-04-21 CR CR20160186A patent/CR20160186A/es unknown
-
2017
- 2017-04-05 US US15/479,500 patent/US20180022814A1/en not_active Abandoned
-
2023
- 2023-05-24 JP JP2023085105A patent/JP2023109927A/ja active Pending
-
2025
- 2025-05-07 JP JP2025077126A patent/JP2025139586A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| US20180022814A1 (en) | 2018-01-25 |
| WO2015066450A1 (en) | 2015-05-07 |
| JP2025139586A (ja) | 2025-09-26 |
| MA44560B1 (fr) | 2020-06-30 |
| SG11201603088RA (en) | 2016-05-30 |
| CR20160186A (es) | 2016-06-13 |
| MX2016005666A (es) | 2016-07-14 |
| EP3805266A1 (en) | 2021-04-14 |
| NZ719784A (en) | 2022-02-25 |
| EA201690905A1 (ru) | 2016-08-31 |
| TW201522378A (zh) | 2015-06-16 |
| US20150118251A1 (en) | 2015-04-30 |
| MA39070A1 (fr) | 2017-11-30 |
| IL245196A0 (en) | 2016-06-30 |
| KR20160077155A (ko) | 2016-07-01 |
| PT3063173T (pt) | 2020-10-20 |
| AU2014342103B2 (en) | 2020-06-04 |
| PL3063173T3 (pl) | 2021-01-11 |
| AU2014342103A1 (en) | 2016-05-26 |
| IL245196B (en) | 2021-04-29 |
| EP3063173B1 (en) | 2020-07-29 |
| EP3063173A1 (en) | 2016-09-07 |
| JP2016536314A (ja) | 2016-11-24 |
| MA44560B2 (fr) | 2021-01-29 |
| MA44560A1 (fr) | 2019-09-30 |
| MX373301B (es) | 2020-04-24 |
| EA035098B1 (ru) | 2020-04-27 |
| TN2016000142A1 (en) | 2017-10-06 |
| CN106103481A (zh) | 2016-11-09 |
| BR112016009403A2 (pt) | 2017-09-19 |
| JP2023109927A (ja) | 2023-08-08 |
| SG10201803288RA (en) | 2018-05-30 |
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Legal Events
| Date | Code | Title | Description |
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| EEER | Examination request |
Effective date: 20191030 |
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| FZDE | Discontinued |
Effective date: 20220301 |