KR20110021919A - 인터루킨-21 수용체의 결합 단백질을 사용하는 치료 방법 - Google Patents
인터루킨-21 수용체의 결합 단백질을 사용하는 치료 방법 Download PDFInfo
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- KR20110021919A KR20110021919A KR1020107028871A KR20107028871A KR20110021919A KR 20110021919 A KR20110021919 A KR 20110021919A KR 1020107028871 A KR1020107028871 A KR 1020107028871A KR 20107028871 A KR20107028871 A KR 20107028871A KR 20110021919 A KR20110021919 A KR 20110021919A
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Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2013012138A1 (ko) * | 2011-07-20 | 2013-01-24 | 주식회사 에이앤알쎄라퓨틱스 | 염증표적 수용체 및 염증 질환 치료용 약물 운반체 |
| KR20200058653A (ko) * | 2018-11-19 | 2020-05-28 | 한국생명공학연구원 | 신규한 il-15-il-21 융합 폴리펩티드 및 이의 용도 |
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| US6057128A (en) | 1998-03-17 | 2000-05-02 | Genetics Institute, Inc. | MU-1, member of the cytokine receptor family |
| JP5913103B2 (ja) | 2009-09-14 | 2016-04-27 | ザ リージェンツ オブ ザ ユニバーシティ オブ コロラド,ア ボディー コーポレイトTHE REGENTS OF THE UNIVERSITY OF COLORADO,a body corporate | 酵母ベースの免疫療法組成物を含む組合せ物及び被験者のスクリーニング方法 |
| CN102532320A (zh) * | 2012-03-06 | 2012-07-04 | 中国药科大学 | 全人源的抗人白介素21受体的单链抗体及其应用 |
| US9309318B2 (en) | 2012-10-17 | 2016-04-12 | Amgen, Inc. | Compositions relating to anti-IL-21 receptor antibodies |
| WO2019160978A1 (en) * | 2018-02-13 | 2019-08-22 | Cedars-Sinai Medical Center | Methods and systems for identification and treatment of pathological neurodegeneration and age-related cognitive decline |
| PH12022550211A1 (en) * | 2019-08-02 | 2022-12-12 | Cttq Akeso Shanghai Biomed Tech Co Ltd | Anti-pd-1 antibody and medical use thereof |
| US12012441B2 (en) | 2020-10-26 | 2024-06-18 | Neptune Biosciences Llc | Engineered human IL-21 cytokines and methods for using the same |
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| US7198789B2 (en) | 1998-03-17 | 2007-04-03 | Genetics Institute, Llc | Methods and compositions for modulating interleukin-21 receptor activity |
| US7189400B2 (en) | 1998-03-17 | 2007-03-13 | Genetics Institute, Llc | Methods of treatment with antagonists of MU-1 |
| US6576744B1 (en) | 1998-09-23 | 2003-06-10 | Zymogenetics, Inc. | Cytokine receptor zalpha11 |
| US6307024B1 (en) | 1999-03-09 | 2001-10-23 | Zymogenetics, Inc. | Cytokine zalpha11 Ligand |
| CN102406937A (zh) | 1999-03-09 | 2012-04-11 | 津莫吉尼蒂克斯公司 | 新的细胞因子zalpha11配体 |
| AU5142300A (en) | 1999-05-18 | 2000-12-05 | Millennium Pharmaceuticals, Inc. | Il-9/il-2 receptor-like molecules and uses thereof |
| AU2001253127A1 (en) | 2000-04-05 | 2001-10-23 | Zymogenetics Inc. | Soluble zalpha11 cytokine receptors |
| AU2001263088B2 (en) | 2000-05-11 | 2006-07-20 | Genetics Institute, Llc. | Mu-1, member of the cytokine receptor family |
| DE60233888D1 (de) | 2001-11-05 | 2009-11-12 | Zymogenetics Inc | Il-21-antagonisten |
| US20040016010A1 (en) | 2002-04-17 | 2004-01-22 | Marion Kasaian | IL-21 receptor knockout animal and methods of use thereof |
| PT1531850E (pt) | 2002-06-07 | 2012-05-07 | Zymogenetics Inc | Utilização de il-21 e anticorpo monoclonal para tratar cancros sólidos |
| KR20050037552A (ko) | 2002-07-15 | 2005-04-22 | 와이어쓰 | T 헬퍼(th) 세포 발생 및 기능을 조절하는 방법 및조성물 |
| JP4914209B2 (ja) | 2003-03-14 | 2012-04-11 | ワイス | ヒトil−21受容体に対する抗体および該抗体の使用 |
| MXPA05010035A (es) * | 2003-03-21 | 2005-11-17 | Wyeth Corp | Tratamiento de desordenes inmunologicos usando agonistas de interleucina-21/receptor de interleucina-21. |
| US7276478B2 (en) | 2003-09-25 | 2007-10-02 | Zymogenetics, Inc. | Methods of treating autoimmune diseases using IL-21 |
| BRPI0510996A (pt) | 2004-05-19 | 2007-12-04 | Wyeth Corp | métodos para melhorar um sintoma de um distúrbio atópico, e para tratar ou prevenir um distúrbio atópico em um paciente, métodos para modular a produção de igg e ige em uma célula, e nìveis relativos de ige e igg, composição farmacêutica, recipiente, métodos para avaliar um paciente tendo ou suspeito de ter um distúrbio atópico, e para avaliar um paciente quanto ao risco de um distúrbio atópico |
| US20060039902A1 (en) * | 2004-08-05 | 2006-02-23 | Young Deborah A | Antagonizing interleukin-21 receptor activity |
| GT200600148A (es) | 2005-04-14 | 2006-11-22 | Metodos para el tratamiento y la prevencion de fibrosis | |
| WO2008081198A1 (en) | 2007-01-05 | 2008-07-10 | Imperial Innovations Ltd | Blood assays for predicting inflammatory responses |
-
2009
- 2009-05-26 AR ARP090101871A patent/AR072136A1/es unknown
- 2009-05-26 EP EP09751754A patent/EP2296689A1/en not_active Withdrawn
- 2009-05-26 WO PCT/US2009/045188 patent/WO2009143526A1/en not_active Ceased
- 2009-05-26 AU AU2009248812A patent/AU2009248812A1/en not_active Abandoned
- 2009-05-26 BR BRPI0912998A patent/BRPI0912998A2/pt not_active IP Right Cessation
- 2009-05-26 US US12/472,237 patent/US8178097B2/en not_active Expired - Fee Related
- 2009-05-26 RU RU2010152689/15A patent/RU2010152689A/ru not_active Application Discontinuation
- 2009-05-26 KR KR1020107028871A patent/KR20110021919A/ko not_active Withdrawn
- 2009-05-26 CA CA2725154A patent/CA2725154A1/en not_active Abandoned
- 2009-05-26 JP JP2011510745A patent/JP2011520989A/ja active Pending
- 2009-05-26 CN CN2009801289410A patent/CN102149403A/zh active Pending
- 2009-05-26 MX MX2010012812A patent/MX2010012812A/es active IP Right Grant
-
2010
- 2010-11-18 IL IL209455A patent/IL209455A0/en unknown
-
2012
- 2012-05-14 US US13/470,500 patent/US20120276102A1/en not_active Abandoned
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2013012138A1 (ko) * | 2011-07-20 | 2013-01-24 | 주식회사 에이앤알쎄라퓨틱스 | 염증표적 수용체 및 염증 질환 치료용 약물 운반체 |
| KR20200058653A (ko) * | 2018-11-19 | 2020-05-28 | 한국생명공학연구원 | 신규한 il-15-il-21 융합 폴리펩티드 및 이의 용도 |
Also Published As
| Publication number | Publication date |
|---|---|
| JP2011520989A (ja) | 2011-07-21 |
| IL209455A0 (en) | 2011-01-31 |
| CN102149403A (zh) | 2011-08-10 |
| US20120276102A1 (en) | 2012-11-01 |
| WO2009143526A1 (en) | 2009-11-26 |
| EP2296689A1 (en) | 2011-03-23 |
| MX2010012812A (es) | 2011-01-21 |
| BRPI0912998A2 (pt) | 2015-10-13 |
| CA2725154A1 (en) | 2009-11-26 |
| US20090298081A1 (en) | 2009-12-03 |
| RU2010152689A (ru) | 2012-06-27 |
| AR072136A1 (es) | 2010-08-11 |
| US8178097B2 (en) | 2012-05-15 |
| AU2009248812A1 (en) | 2009-11-26 |
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