JP2009524422A - 結合分子３ - Google Patents
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Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2014530009A (ja) * | 2011-09-29 | 2014-11-17 | エーピーオー‐ティー ビー．ヴイ． | 異常細胞を標的とする多重特異性結合分子 |
| JP2015519055A (ja) * | 2012-05-17 | 2015-07-09 | カイマブ・リミテッド | 二重特異性免疫グロブリンまたは超変異重鎖のみの免疫グロブリンのｉｎｖｉｖｏでの生成のためのトランスジェニック非ヒト脊椎動物 |
| JP2020537506A (ja) * | 2017-10-04 | 2020-12-24 | アムジエン・インコーポレーテツド | トランスサイレチン免疫グロブリン融合物 |
| US10946104B2 (en) | 2012-01-13 | 2021-03-16 | Apo-Tb.V. | Aberrant cell-restricted immunoglobulins provided with a toxic moiety |
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| ES2667729T3 (es) | 2007-09-26 | 2018-05-14 | Ucb Biopharma Sprl | Fusiones de anticuerpos con doble especificidad |
| WO2010035012A1 (en) | 2008-09-26 | 2010-04-01 | Ucb Pharma S.A. | Biological products |
| DK2417156T3 (en) | 2009-04-07 | 2015-03-02 | Roche Glycart Ag | Trivalent, bispecific antibodies |
| US9676845B2 (en) | 2009-06-16 | 2017-06-13 | Hoffmann-La Roche, Inc. | Bispecific antigen binding proteins |
| US9445581B2 (en) | 2012-03-28 | 2016-09-20 | Kymab Limited | Animal models and therapeutic molecules |
| EP3028565B1 (en) | 2009-07-08 | 2017-09-27 | Kymab Limited | Animal models and therapeutic molecules |
| CA2781519A1 (en) | 2009-09-16 | 2011-03-24 | Genentech, Inc. | Coiled coil and/or tether containing protein complexes and uses thereof |
| CA2807278A1 (en) | 2010-08-24 | 2012-03-01 | F. Hoffmann - La Roche Ag | Bispecific antibodies comprising a disulfide stabilized - fv fragment |
| JP5764677B2 (ja) | 2011-02-28 | 2015-08-19 | エフ・ホフマン−ラ・ロシュ・アクチェンゲゼルシャフト | 抗原結合タンパク質 |
| CN103403025B (zh) | 2011-02-28 | 2016-10-12 | 弗·哈夫曼-拉罗切有限公司 | 单价抗原结合蛋白 |
| EP2757875B2 (en) | 2011-09-19 | 2023-03-22 | Kymab Limited | Manipulation of immunoglobulin gene diversity and multi-antibody therapeutics |
| WO2013045916A1 (en) | 2011-09-26 | 2013-04-04 | Kymab Limited | Chimaeric surrogate light chains (slc) comprising human vpreb |
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| GB201409558D0 (en) | 2014-05-29 | 2014-07-16 | Ucb Biopharma Sprl | Method |
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| US20230203198A1 (en) | 2020-06-04 | 2023-06-29 | Amgen Inc. | Bispecific binding constructs |
| CA3203468A1 (en) | 2020-12-03 | 2022-06-09 | Amgen Inc. | Immunoglobuline constructs with multiple binding domains |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2002002781A1 (en) * | 2000-06-30 | 2002-01-10 | Vlaams Interuniversitair Instituut Voor Biotechnologie Vzw | Heterodimeric fusion proteins |
| WO2006008548A2 (en) * | 2004-07-22 | 2006-01-26 | Erasmus University Medical Centre Rotterdam | Binding molecules |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CZ121599A3 (cs) * | 1998-04-09 | 1999-10-13 | Aventis Pharma Deutschland Gmbh | Jednořetězcová molekula vázající několik antigenů, způsob její přípravy a léčivo obsahující tuto molekulu |
| EP1558647B1 (en) * | 2002-11-08 | 2015-06-10 | Ablynx N.V. | Single domain antibodies directed against tumour necrosis factor-alpha and uses therefor |
| US7612181B2 (en) * | 2005-08-19 | 2009-11-03 | Abbott Laboratories | Dual variable domain immunoglobulin and uses thereof |
-
2006
- 2006-01-25 GB GBGB0601513.5A patent/GB0601513D0/en not_active Ceased
-
2007
- 2007-01-25 US US12/161,986 patent/US20090169548A1/en not_active Abandoned
- 2007-01-25 RU RU2008134519/13A patent/RU2008134519A/ru not_active Application Discontinuation
- 2007-01-25 KR KR1020087020710A patent/KR20080106201A/ko not_active Withdrawn
- 2007-01-25 TW TW096102902A patent/TW200808824A/zh unknown
- 2007-01-25 CN CNA200780010769XA patent/CN101472946A/zh active Pending
- 2007-01-25 ZA ZA200806492A patent/ZA200806492B/xx unknown
- 2007-01-25 EP EP07705029A patent/EP1989229A1/en not_active Withdrawn
- 2007-01-25 JP JP2008551872A patent/JP2009524422A/ja active Pending
- 2007-01-25 WO PCT/GB2007/000258 patent/WO2007085837A1/en not_active Ceased
- 2007-01-25 CA CA002637945A patent/CA2637945A1/en not_active Abandoned
- 2007-01-25 AU AU2007209130A patent/AU2007209130A1/en not_active Abandoned
- 2007-01-25 BR BRPI0706737-2A patent/BRPI0706737A2/pt not_active IP Right Cessation
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2002002781A1 (en) * | 2000-06-30 | 2002-01-10 | Vlaams Interuniversitair Instituut Voor Biotechnologie Vzw | Heterodimeric fusion proteins |
| WO2006008548A2 (en) * | 2004-07-22 | 2006-01-26 | Erasmus University Medical Centre Rotterdam | Binding molecules |
Non-Patent Citations (2)
| Title |
|---|
| JPN6012024431; Ｊ Ｂｉｏｌ Ｃｈｅｍ Ｖｏｌ．２７８， Ｎｏ．４８, 2003, ｐ．４７８１２-４７８１９ * |
| JPN6012024432; Ｊ Ｂｉｏｌ Ｃｈｅｍ Ｖｏｌ．２７６， Ｎｏ．１０, 2001, ｐ．７３４６-７３５０ * |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2014530009A (ja) * | 2011-09-29 | 2014-11-17 | エーピーオー‐ティー ビー．ヴイ． | 異常細胞を標的とする多重特異性結合分子 |
| US11098115B2 (en) | 2011-09-29 | 2021-08-24 | Apo-T B.V. | Multi-specific binding molecules targeting aberrant cells |
| US10946104B2 (en) | 2012-01-13 | 2021-03-16 | Apo-Tb.V. | Aberrant cell-restricted immunoglobulins provided with a toxic moiety |
| JP2015519055A (ja) * | 2012-05-17 | 2015-07-09 | カイマブ・リミテッド | 二重特異性免疫グロブリンまたは超変異重鎖のみの免疫グロブリンのｉｎｖｉｖｏでの生成のためのトランスジェニック非ヒト脊椎動物 |
| JP2020537506A (ja) * | 2017-10-04 | 2020-12-24 | アムジエン・インコーポレーテツド | トランスサイレチン免疫グロブリン融合物 |
Also Published As
| Publication number | Publication date |
|---|---|
| KR20080106201A (ko) | 2008-12-04 |
| GB0601513D0 (en) | 2006-03-08 |
| ZA200806492B (en) | 2009-12-30 |
| CN101472946A (zh) | 2009-07-01 |
| US20090169548A1 (en) | 2009-07-02 |
| EP1989229A1 (en) | 2008-11-12 |
| TW200808824A (en) | 2008-02-16 |
| CA2637945A1 (en) | 2007-08-02 |
| RU2008134519A (ru) | 2010-02-27 |
| AU2007209130A1 (en) | 2007-08-02 |
| BRPI0706737A2 (pt) | 2011-04-05 |
| WO2007085837A1 (en) | 2007-08-02 |
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