JP2009519011A - インターロイキン1受容体1型に結合する非競合ドメイン抗体フォーマット - Google Patents
インターロイキン1受容体1型に結合する非競合ドメイン抗体フォーマット Download PDFInfo
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| EP2114443A4 (en) | 2006-12-29 | 2011-08-10 | Abbott Lab | IL-1A / IL-1B ANTIBODY WITH DOUBLE SPECIFICITY |
| GB0724331D0 (en) | 2007-12-13 | 2008-01-23 | Domantis Ltd | Compositions for pulmonary delivery |
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| CN102089325A (zh) | 2008-04-17 | 2011-06-08 | 埃博灵克斯股份有限公司 | 能够结合血清白蛋白的肽,以及包含其的化合物、构建体和多肽 |
| US8298533B2 (en) | 2008-11-07 | 2012-10-30 | Medimmune Limited | Antibodies to IL-1R1 |
| CN102224169A (zh) * | 2008-11-26 | 2011-10-19 | 葛兰素集团有限公司 | 多肽、抗体可变结构域和拮抗剂 |
| EA022925B1 (ru) * | 2009-02-19 | 2016-03-31 | Глаксо Груп Лимитед | Улучшенные полипептиды, вариабельные домены антител и антагонисты против tnfr1 |
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| US20110082055A1 (en) * | 2009-09-18 | 2011-04-07 | Codexis, Inc. | Reduced codon mutagenesis |
| DK2478137T3 (da) * | 2009-09-18 | 2017-11-27 | Codexis Inc | Reduceret kodonmutagenese |
| CA2788993A1 (en) | 2010-02-05 | 2011-08-11 | Ablynx N.V. | Peptides capable of binding to serum albumin and compounds, constructs and polypeptides comprising the same |
| US20130149312A1 (en) * | 2010-04-16 | 2013-06-13 | Mcmaster University | Compositions and methods for treating copd exacerbation |
| US20140112929A1 (en) * | 2011-06-17 | 2014-04-24 | Glaxo Group Limited | Tumour necrosis factor receptor 1 antagonists |
| DK2723769T4 (da) | 2011-06-23 | 2022-09-05 | Ablynx Nv | Teknikker til at forudsige, påvise og reducere uspecifik proteininterferens i assays, som involverer variable immunglobulin-enkeltdomæner |
| EP2974737B1 (en) | 2011-06-23 | 2025-10-22 | Ablynx N.V. | Techniques for predicting, detecting and reducing a specific protein interference in assays involving immunoglobulin single variable domains |
| EP4350345A3 (en) | 2011-06-23 | 2024-07-24 | Ablynx N.V. | Techniques for predicting, detecting and reducing aspecific protein interference in assays involving immunoglobin single variable domains |
| EA027160B1 (ru) * | 2011-08-17 | 2017-06-30 | Глаксо Груп Лимитед | Модифицированные белки и пептиды |
| CA2948945C (en) | 2014-05-16 | 2023-08-08 | Ablynx Nv | Methods for detecting and/or measuring anti-drug antibodies, in particular treatment-emergent anti-drug antibodies |
| IL295534B2 (en) | 2014-05-16 | 2025-03-01 | Ablynx Nv | Improved immunoglobulin variable sites |
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| US11142569B2 (en) | 2015-11-13 | 2021-10-12 | Ablynx N.V. | Serum albumin-binding immunoglobulin variable domains |
| EA038179B1 (ru) | 2015-11-18 | 2021-07-20 | Мерк Шарп И Доум Корп. | Ctla4-связывающие вещества |
| CA3005488A1 (en) | 2015-11-18 | 2017-05-26 | Ablynx Nv | Improved serum albumin binders |
| WO2017210749A1 (en) * | 2016-06-10 | 2017-12-14 | Adelaide Research & Innovation Pty Ltd | Methods and products for treating autoimmune diseases |
| CA3029133C (en) | 2016-06-23 | 2024-04-30 | Ablynx N.V. | Improved pharmacokinetic assays for immunoglobulin single variable domains |
| KR20240018673A (ko) | 2016-11-28 | 2024-02-13 | 추가이 세이야쿠 가부시키가이샤 | 항원 결합 도메인 및 운반 부분을 포함하는 폴리펩티드 |
| KR102533814B1 (ko) | 2016-11-28 | 2023-05-19 | 추가이 세이야쿠 가부시키가이샤 | 리간드 결합 활성을 조정 가능한 리간드 결합 분자 |
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| EP3571224B1 (en) | 2017-01-17 | 2024-08-07 | Ablynx NV | Improved serum albumin binders |
| SG11201906264YA (en) | 2017-01-17 | 2019-08-27 | Ablynx Nv | Improved serum albumin binders |
| EP3602056A1 (en) | 2017-03-31 | 2020-02-05 | Ablynx N.V. | Improved immunogenicity assays |
| TWI818934B (zh) | 2017-11-28 | 2023-10-21 | 日商中外製藥股份有限公司 | 可調整配體結合活性的配體結合分子 |
| JP7482630B2 (ja) | 2017-11-28 | 2024-05-14 | 中外製薬株式会社 | 抗原結合ドメインおよび運搬部分を含むポリペプチド |
| JP7414736B2 (ja) | 2018-05-30 | 2024-01-16 | 中外製薬株式会社 | アグリカン結合ドメインおよび運搬部分を含むポリペプチド |
| EP3802831A4 (en) * | 2018-05-30 | 2022-07-27 | Chugai Seiyaku Kabushiki Kaisha | Polypeptide comprising il-1r1 binding domain and carrying moiety |
| CN109336977A (zh) * | 2018-10-11 | 2019-02-15 | 暨南大学 | 肿瘤干细胞标志分子EpCAM的结合蛋白及其应用 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2004022718A2 (en) * | 2002-09-06 | 2004-03-18 | Amgen, Inc. | Therapeutic human anti-il-1r1 monoclonal antibody |
| WO2005035572A2 (en) * | 2003-10-08 | 2005-04-21 | Domantis Limited | Antibody compositions and methods |
Family Cites Families (78)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CU22545A1 (es) * | 1994-11-18 | 1999-03-31 | Centro Inmunologia Molecular | Obtención de un anticuerpo quimérico y humanizado contra el receptor del factor de crecimiento epidérmico para uso diagnóstico y terapéutico |
| US3907502A (en) * | 1973-12-11 | 1975-09-23 | Miless L Brink | Method for identifying Bence Jones proteins |
| GB2148299B (en) * | 1983-09-01 | 1988-01-06 | Hybritech Inc | Antibody compositions of therapeutic agents having an extended serum half-life |
| US5120712A (en) * | 1986-05-05 | 1992-06-09 | The General Hospital Corporation | Insulinotropic hormone |
| US6511665B1 (en) * | 1987-11-25 | 2003-01-28 | Immunex Corporation | Antibodies to interleukin-1 receptors |
| AU4128089A (en) * | 1988-09-15 | 1990-03-22 | Rorer International (Overseas) Inc. | Monoclonal antibodies specific to human epidermal growth factor receptor and therapeutic methods employing same |
| ATE102631T1 (de) * | 1988-11-11 | 1994-03-15 | Medical Res Council | Klonierung von immunglobulin sequenzen aus den variabelen domaenen. |
| US5116964A (en) * | 1989-02-23 | 1992-05-26 | Genentech, Inc. | Hybrid immunoglobulins |
| US6451983B2 (en) * | 1989-08-07 | 2002-09-17 | Peptech Limited | Tumor necrosis factor antibodies |
| US5459061A (en) * | 1990-01-26 | 1995-10-17 | W. Alton Jones Cell Science Center, Inc. | Hybridomas producing monoclonal antibodies which specifically bind to continuous epitope on the human EGF receptor and compete with EGF for binding to the EGF receptor |
| US5726152A (en) * | 1990-09-21 | 1998-03-10 | Merck & Co., Inc. | Vascular endothelial cell growth factor II |
| US5843440A (en) * | 1990-10-03 | 1998-12-01 | Redcell Canada, Inc. | Cellular and serum protein anchors for modulating pharmacokinetics |
| WO1992015683A1 (en) * | 1991-03-06 | 1992-09-17 | MERCK Patent Gesellschaft mit beschränkter Haftung | Humanized and chimeric monoclonal antibodies |
| OA10149A (en) * | 1991-03-29 | 1996-12-18 | Genentech Inc | Vascular endothelial cell growth factor antagonists |
| EP0603194A4 (en) * | 1991-07-05 | 1994-12-07 | Seragen Inc | TO THE RECEPTOR OF THE EPIDERMAL GROWTH FACTOR TARGETED MOLECULES FOR TREATING INFLAMMABLE ARTHRITIS. |
| US5965132A (en) * | 1992-03-05 | 1999-10-12 | Board Of Regents, The University Of Texas System | Methods and compositions for targeting the vasculature of solid tumors |
| IL112372A (en) * | 1994-02-07 | 2001-08-26 | Res Dev Foundation | Non-viral vector for the delivery of genetic information to cells |
| GB9410533D0 (en) * | 1994-05-26 | 1994-07-13 | Lynxvale Ltd | In situ hybridisation and immuno-Chemical localisation of a growth factor |
| DK0706799T3 (da) * | 1994-09-16 | 2002-02-25 | Merck Patent Gmbh | Immunkonjugater II |
| US5928939A (en) * | 1995-03-01 | 1999-07-27 | Ludwig Institute For Cancer Research | Vascular endothelial growth factor-b and dna coding therefor |
| US5869046A (en) * | 1995-04-14 | 1999-02-09 | Genentech, Inc. | Altered polypeptides with increased half-life |
| US6410690B1 (en) * | 1995-06-07 | 2002-06-25 | Medarex, Inc. | Therapeutic compounds comprised of anti-Fc receptor antibodies |
| US7060808B1 (en) * | 1995-06-07 | 2006-06-13 | Imclone Systems Incorporated | Humanized anti-EGF receptor monoclonal antibody |
| US5770190A (en) * | 1995-07-14 | 1998-06-23 | Schering Corporation | Method of treatment of acute leukemia with inteleukin-10 |
| ES2176484T3 (es) | 1995-08-18 | 2002-12-01 | Morphosys Ag | Bancos de proteinas/(poli)peptidos. |
| US6020473A (en) * | 1995-08-25 | 2000-02-01 | Genentech, Inc. | Nucleic acids encoding variants of vascular endothelial cell growth factor |
| US5989830A (en) * | 1995-10-16 | 1999-11-23 | Unilever Patent Holdings Bv | Bifunctional or bivalent antibody fragment analogue |
| US5664034A (en) * | 1996-05-21 | 1997-09-02 | Lucent Technologies Inc. | Lightwave communication monitoring switch |
| US5922845A (en) * | 1996-07-11 | 1999-07-13 | Medarex, Inc. | Therapeutic multispecific compounds comprised of anti-Fcα receptor antibodies |
| US6013780A (en) * | 1996-09-06 | 2000-01-11 | Technion Research & Development Co. Ltd. | VEGF145 expression vectors |
| US6750044B1 (en) * | 1996-10-17 | 2004-06-15 | Genentech, Inc. | Variants of vascular endothelial cell growth factor having antagonistic properties, nucleic acids encoding the same and host cells comprising those nucleic acids |
| US20030165467A1 (en) * | 1997-01-21 | 2003-09-04 | Technion Research & Development Co., Ltd. | Angiogenic factor and use thereof in treating cardiovascular disease |
| US6294170B1 (en) * | 1997-08-08 | 2001-09-25 | Amgen Inc. | Composition and method for treating inflammatory diseases |
| US6485942B1 (en) * | 1997-02-14 | 2002-11-26 | Genentech, Inc. | Variants of vascular endothelial cell growth factor having altered pharmacological properties, and recombinant methods of production |
| US20020032315A1 (en) * | 1997-08-06 | 2002-03-14 | Manuel Baca | Anti-vegf antibodies |
| US20020173629A1 (en) * | 1997-05-05 | 2002-11-21 | Aya Jakobovits | Human monoclonal antibodies to epidermal growth factor receptor |
| US6777534B1 (en) * | 1997-12-09 | 2004-08-17 | Children's Medical Center Corporation | Peptide antagonists of vascular endothelial growth factor |
| US20020192211A1 (en) * | 1998-03-17 | 2002-12-19 | Hudziak Robert M. | Method of treating tumor cells by inhibiting growth factor receptor function |
| US20030224001A1 (en) * | 1998-03-19 | 2003-12-04 | Goldstein Neil I. | Antibody and antibody fragments for inhibiting the growth of tumors |
| ZA200007412B (en) * | 1998-05-15 | 2002-03-12 | Imclone Systems Inc | Treatment of human tumors with radiation and inhibitors of growth factor receptor tyrosine kinases. |
| US20030175271A1 (en) * | 1998-05-20 | 2003-09-18 | Kyowa Hakko Kogyo Co., Ltd. | VEGF activity inhibitor |
| US7264801B2 (en) * | 1998-08-11 | 2007-09-04 | Genentech, Inc. | EG-VEGF nucleic acids and polypeptides and method of use |
| US20020172678A1 (en) * | 2000-06-23 | 2002-11-21 | Napoleone Ferrara | EG-VEGF nucleic acids and polypeptides and methods of use |
| US7488590B2 (en) * | 1998-10-23 | 2009-02-10 | Amgen Inc. | Modified peptides as therapeutic agents |
| DE69926536T3 (de) * | 1998-12-22 | 2013-09-12 | Genentech, Inc. | Antagonisten von vaskular-endothelialen zellwachstumsfaktoren und ihre anwendung |
| US6703020B1 (en) * | 1999-04-28 | 2004-03-09 | Board Of Regents, The University Of Texas System | Antibody conjugate methods for selectively inhibiting VEGF |
| WO2000064946A2 (en) * | 1999-04-28 | 2000-11-02 | Board Of Regents, The University Of Texas System | Compositions and methods for cancer treatment by selectively inhibiting vegf |
| SK16522001A3 (sk) * | 1999-05-14 | 2002-10-08 | Imclone Systems Incorporated | Liečivo na inhibíciu rastu refraktérnych nádorov |
| US7049410B2 (en) * | 1999-05-14 | 2006-05-23 | Majumdar Adhip P N | Antibodies to a novel EGF-receptor related protein (ERRP) |
| EP1183352A1 (en) * | 1999-05-20 | 2002-03-06 | Scios Inc. | Vascular endothelial growth factor variants |
| JP4981229B2 (ja) * | 2000-02-25 | 2012-07-18 | ルードヴィッヒ インスティテュート フォー キャンサー リサーチ | ハイブリッド血管内皮成長因子DNAsおよびタンパク質に関与する物質および方法 |
| JP2003528632A (ja) * | 2000-03-31 | 2003-09-30 | インスティティ・パスツール | 血管内皮成長因子(vegf)−媒介性脈管形成を阻害するペプチド、該ペプチドをエンコードするポリヌクレオチド及びその使用方法 |
| MXPA02010011A (es) * | 2000-04-11 | 2003-04-25 | Genentech Inc | Anticuerpos multivalentes y usos para los mismos. |
| WO2001089549A2 (en) * | 2000-05-22 | 2001-11-29 | Hyseq, Inc. | Therapeutic uses of il-1 receptor antagonist |
| WO2001090192A2 (en) * | 2000-05-24 | 2001-11-29 | Imclone Systems Incorporated | Bispecific immunoglobulin-like antigen binding proteins and method of production |
| DE10038624C2 (de) * | 2000-08-03 | 2002-11-21 | Broekelmann Aluminium F W | Wärmeübertragungsrohr mit gedrallten Innenrippen |
| US6699473B2 (en) * | 2000-10-13 | 2004-03-02 | Uab Research Foundation | Human anti-epidermal growth factor receptor single-chain antibodies |
| US20030133939A1 (en) * | 2001-01-17 | 2003-07-17 | Genecraft, Inc. | Binding domain-immunoglobulin fusion proteins |
| US7667004B2 (en) * | 2001-04-17 | 2010-02-23 | Abmaxis, Inc. | Humanized antibodies against vascular endothelial growth factor |
| RU2003134180A (ru) * | 2001-05-08 | 2005-02-10 | Мерк Патент ГмбХ (DE) | Комбинированная терапия, использующая антитела к egfr и антигормональные средства |
| BRPI0210405B8 (pt) * | 2001-06-13 | 2021-05-25 | Genmab As | anticorpo monoclonal humano, molécula biespecífica, método in vitro para inibir o crescimento de uma célula expressando egfr, para induzir a citólise de uma célula expressando egfr, e para detectar a presença de antígeno egfr ou uma célula expressando egfr em uma amostra, e, vetor de expressão |
| WO2003002609A2 (en) * | 2001-06-28 | 2003-01-09 | Domantis Limited | Dual-specific ligand and its use |
| WO2003014159A1 (en) * | 2001-08-03 | 2003-02-20 | Commonwealth Scientific And Industrial Research Organisation | Methods of screening based on the egf receptor crystal structure |
| JP2005507659A (ja) * | 2001-10-15 | 2005-03-24 | イミューノメディクス、インコーポレイテッド | 直接ターゲッティング結合タンパク質 |
| DE10163459A1 (de) * | 2001-12-21 | 2003-07-03 | Merck Patent Gmbh | Lyophilisierte Zubereitung enthaltend Antikörper gegen EGF-Rezeptor |
| AU2003209446B2 (en) * | 2002-03-01 | 2008-09-25 | Immunomedics, Inc. | Bispecific antibody point mutations for enhancing rate of clearance |
| AU2003244817B2 (en) * | 2002-06-28 | 2010-08-26 | Domantis Limited | Antigen-binding immunoglobulin single variable domains and dual-specific constructs |
| TW200501960A (en) * | 2002-10-02 | 2005-01-16 | Bristol Myers Squibb Co | Synergistic kits and compositions for treating cancer |
| AU2003290330A1 (en) * | 2002-12-27 | 2004-07-22 | Domantis Limited | Dual specific single domain antibodies specific for a ligand and for the receptor of the ligand |
| US20050043233A1 (en) * | 2003-04-29 | 2005-02-24 | Boehringer Ingelheim International Gmbh | Combinations for the treatment of diseases involving cell proliferation, migration or apoptosis of myeloma cells or angiogenesis |
| RS20050885A (sr) * | 2003-05-30 | 2008-04-04 | Genentech | Lečenje sa anti-vegf antitelima |
| CN104059147A (zh) * | 2003-06-27 | 2014-09-24 | 艾默根佛蒙特有限公司 | 针对表皮生长因子受体的缺失突变体的抗体及其使用 |
| UA84024C2 (ru) * | 2003-07-24 | 2008-09-10 | Мериал Лимитед | Новые вакцинные композиции, которые содержат эмульсию типа "масло в воде" |
| AR046510A1 (es) * | 2003-07-25 | 2005-12-14 | Regeneron Pharma | Composicion de un antagonista de vegf y un agente anti-proliferativo |
| US20050196340A1 (en) * | 2003-08-06 | 2005-09-08 | Jocelyn Holash | Use of a VEGF antagonist in combination with radiation therapy |
| AU2005206536B2 (en) * | 2004-01-16 | 2010-09-02 | Regeneron Pharmaceuticals, Inc. | Fusion polypeptides capable of activating receptors |
| US7767792B2 (en) * | 2004-02-20 | 2010-08-03 | Ludwig Institute For Cancer Research Ltd. | Antibodies to EGF receptor epitope peptides |
| CA2588892A1 (en) * | 2004-12-02 | 2006-06-08 | Dormantis Limited | Anti-il-1r1 single domain antibodies and therapeutic uses |
-
2006
- 2006-11-30 JP JP2008542829A patent/JP2009519011A/ja active Pending
- 2006-11-30 CN CNA2006800518832A patent/CN101454344A/zh active Pending
- 2006-11-30 BR BRPI0619225A patent/BRPI0619225A2/pt not_active IP Right Cessation
- 2006-11-30 TW TW095144416A patent/TW200730539A/zh unknown
- 2006-11-30 US US12/085,920 patent/US20090155283A1/en not_active Abandoned
- 2006-11-30 EP EP06820376A patent/EP1957536A2/en not_active Withdrawn
- 2006-11-30 KR KR1020087015994A patent/KR20080077238A/ko not_active Withdrawn
- 2006-11-30 AU AU2006321364A patent/AU2006321364B2/en not_active Expired - Fee Related
- 2006-11-30 WO PCT/GB2006/004471 patent/WO2007063308A2/en not_active Ceased
- 2006-11-30 EA EA200801170A patent/EA200801170A1/ru unknown
- 2006-11-30 CA CA002632866A patent/CA2632866A1/en not_active Abandoned
-
2008
- 2008-05-15 NO NO20082215A patent/NO20082215L/no not_active Application Discontinuation
- 2008-05-27 CR CR10022A patent/CR10022A/es not_active Application Discontinuation
- 2008-06-02 MA MA30984A patent/MA30300B1/fr unknown
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2004022718A2 (en) * | 2002-09-06 | 2004-03-18 | Amgen, Inc. | Therapeutic human anti-il-1r1 monoclonal antibody |
| WO2005035572A2 (en) * | 2003-10-08 | 2005-04-21 | Domantis Limited | Antibody compositions and methods |
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR20190134617A (ko) * | 2017-03-31 | 2019-12-04 | 스위디쉬 오르펀 바이오비트럼 에이비 (피유비엘) | Il-1r-i 결합 폴리펩티드 |
| JP2020515252A (ja) * | 2017-03-31 | 2020-05-28 | スウェーディッシュ オーファン バイオヴィトルム エービー(ピーユービーエル) | Il−1r−i結合ポリペプチド |
| JP2023071776A (ja) * | 2017-03-31 | 2023-05-23 | スウェディッシュ オーファン バイオビトラム アクティエボラーグ (ペーウーベーエル) | Il-1r-i結合ポリペプチド |
| KR102717131B1 (ko) | 2017-03-31 | 2024-10-15 | 스위디쉬 오르펀 바이오비트럼 에이비 (피유비엘) | Il-1r-i 결합 폴리펩티드 |
| US12116397B2 (en) | 2017-03-31 | 2024-10-15 | Swedish Orphan Biovitrum Ab (Publ) | IL-IR-I binding polypeptide |
| JP7657021B2 (ja) | 2017-03-31 | 2025-04-04 | スウェディッシュ オーファン バイオビトラム アクティエボラーグ (ペーウーベーエル) | Il-1r-i結合ポリペプチド |
Also Published As
| Publication number | Publication date |
|---|---|
| WO2007063308A3 (en) | 2007-09-20 |
| CA2632866A1 (en) | 2007-06-07 |
| TW200730539A (en) | 2007-08-16 |
| AU2006321364A1 (en) | 2007-06-07 |
| NO20082215L (no) | 2008-08-14 |
| WO2007063308A2 (en) | 2007-06-07 |
| MA30300B1 (fr) | 2009-04-01 |
| CR10022A (es) | 2008-09-22 |
| KR20080077238A (ko) | 2008-08-21 |
| AU2006321364B2 (en) | 2011-11-10 |
| CN101454344A (zh) | 2009-06-10 |
| EA200801170A1 (ru) | 2008-12-30 |
| BRPI0619225A2 (pt) | 2017-11-07 |
| EP1957536A2 (en) | 2008-08-20 |
| US20090155283A1 (en) | 2009-06-18 |
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