ES2277460T3 - Cadena del receptor de la citoquina. - Google Patents
Cadena del receptor de la citoquina. Download PDFInfo
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- ES2277460T3 ES2277460T3 ES99966166T ES99966166T ES2277460T3 ES 2277460 T3 ES2277460 T3 ES 2277460T3 ES 99966166 T ES99966166 T ES 99966166T ES 99966166 T ES99966166 T ES 99966166T ES 2277460 T3 ES2277460 T3 ES 2277460T3
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- Pain & Pain Management (AREA)
- Urology & Nephrology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
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| US21133598A | 1998-12-14 | 1998-12-14 | |
| US211335 | 1998-12-14 |
Publications (1)
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| ES2277460T3 true ES2277460T3 (es) | 2007-07-01 |
Family
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| ES99966166T Expired - Lifetime ES2277460T3 (es) | 1998-12-14 | 1999-12-13 | Cadena del receptor de la citoquina. |
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| JP (3) | JP5519087B2 (https=) |
| CN (2) | CN104611339A (https=) |
| AT (1) | ATE342976T1 (https=) |
| AU (1) | AU780031B2 (https=) |
| BR (1) | BR9916209A (https=) |
| CA (1) | CA2356779C (https=) |
| CY (1) | CY1107657T1 (https=) |
| DE (1) | DE69933696T2 (https=) |
| DK (1) | DK1141286T3 (https=) |
| ES (1) | ES2277460T3 (https=) |
| MX (1) | MXPA01006006A (https=) |
| NZ (1) | NZ512942A (https=) |
| PT (1) | PT1141286E (https=) |
| WO (1) | WO2000036103A1 (https=) |
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| US7553487B2 (en) * | 1998-12-14 | 2009-06-30 | Genetics Institute, Llc | Method and compositions for treating asthma |
| PT1141286E (pt) | 1998-12-14 | 2007-01-31 | Genetics Inst Llc | Cadeia de receptores de citocina |
| WO2002055100A2 (en) * | 2000-10-20 | 2002-07-18 | Genetics Institute, Llc | Method and composition for inhibition of tumor growth and enhancing an immune response |
| US20040209806A1 (en) * | 2003-01-17 | 2004-10-21 | Children's Hospital Medical Center | Regulation of allergen induced gene |
| US20040198686A1 (en) * | 2003-01-18 | 2004-10-07 | Rothenberg Marc Elliot | Regulation of allergen induced gene |
| EP1444989A1 (en) | 2003-02-07 | 2004-08-11 | Giorgio Dr. Stassi | Sensitizing cells for apoptosis by selectively blocking cytokines |
| WO2004092404A2 (en) * | 2003-04-11 | 2004-10-28 | Wyeth | Inhibitors of acidic mammalian chitinase as asthma therapeutics |
| GB0407315D0 (en) | 2003-07-15 | 2004-05-05 | Cambridge Antibody Tech | Human antibody molecules |
| SG10201404273QA (en) | 2003-12-23 | 2014-10-30 | Genentech Inc | Novel anti-il 13 antibodies and uses thereof |
| US20070178520A1 (en) * | 2004-02-27 | 2007-08-02 | Barbara Wolff-Winiski | Screening assay for modulators of interaction between interleukin-12 and/or -23 with their receptors |
| US20090098142A1 (en) * | 2004-06-09 | 2009-04-16 | Kasaian Marion T | Methods and compositions for treating and monitoring treatment of IL-13-associated disorders |
| US7501121B2 (en) * | 2004-06-17 | 2009-03-10 | Wyeth | IL-13 binding agents |
| AR049390A1 (es) | 2004-06-09 | 2006-07-26 | Wyeth Corp | Anticuerpos contra la interleuquina-13 humana y usos de los mismos |
| JP2008520684A (ja) | 2004-11-17 | 2008-06-19 | アブジェニックス・インコーポレーテッド | Ｉｌ−１３に対する完全ヒトモノクローナル抗体 |
| RU2421464C2 (ru) | 2005-10-21 | 2011-06-20 | Новартис Аг | Человеческие антитела к il-13 и их терапевтическое применение |
| BRPI0810561A2 (pt) * | 2007-04-23 | 2019-09-24 | Wyeth Corp | métodos e composições para tratar e monitorar tratamento de desordens associadas à il-13. |
| WO2008153790A2 (en) * | 2007-05-29 | 2008-12-18 | University Of Cincinnati | Methods of modulating inflammation and compositions therefore |
| AU2014306867B2 (en) | 2013-08-12 | 2017-10-26 | Genentech, Inc. | Compositions and method for treating complement-associated conditions |
| ES2915378T3 (es) | 2013-09-13 | 2022-06-22 | Hoffmann La Roche | Procedimientos para detectar y cuantificar una proteína de célula huésped en líneas celulares |
| EP4331605A3 (en) | 2013-09-13 | 2024-05-22 | F. Hoffmann-La Roche AG | Methods and compositions comprising purified recombinant polypeptides |
| US11970526B2 (en) | 2017-04-21 | 2024-04-30 | Elanco Us Inc. | IL4/IL13 receptor molecule for veterinary use |
Family Cites Families (41)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| WO1989004838A1 (en) | 1987-11-25 | 1989-06-01 | Immunex Corporation | Interleukin-1 receptors |
| US5359037A (en) | 1988-09-12 | 1994-10-25 | Yeda Research And Development Co. Ltd. | Antibodies to TNF binding protein I |
| WO1990005183A1 (en) | 1988-10-31 | 1990-05-17 | Immunex Corporation | Interleukin-4 receptors |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US5011778A (en) | 1989-05-23 | 1991-04-30 | Otsuka Pharmaceutical Co., Ltd. | Monoclonal antibodies directed to IL-1 activated endothelial cells and medicaments employing the monoclonal antibodies |
| ES2085983T3 (es) | 1989-12-20 | 1996-06-16 | Schering Corp | Antagonistas de anticuerpos de la interleuquina-4 humana. |
| US5859205A (en) | 1989-12-21 | 1999-01-12 | Celltech Limited | Humanised antibodies |
| US5246701A (en) | 1990-10-05 | 1993-09-21 | Ludwig Institute For Cancer Research | Method for inhibiting production of IgE by using IL-9 inhibitors |
| HU217099B (hu) | 1991-03-29 | 1999-11-29 | Elf Sanofi Sa. | Eljárás citokin típusú aktivitással rendelkező fehérje, azt kódoló rekombináns DNS-szekvencia és a megfelelő transzformált sejtek és mikroorganizmusok előállítására |
| AU3658093A (en) | 1992-02-10 | 1993-09-03 | Seragen, Inc. | Desensitization to specific allergens |
| US5397703A (en) | 1992-07-09 | 1995-03-14 | Cetus Oncology Corporation | Method for generation of antibodies to cell surface molecules |
| US5596072A (en) | 1992-08-21 | 1997-01-21 | Schering Corporation | Method of refolding human IL-13 |
| EP0656947A1 (en) | 1992-08-21 | 1995-06-14 | Schering Corporation | Human interleukin-13 |
| EP0604693A1 (en) | 1992-12-29 | 1994-07-06 | Schering-Plough | Monoclonal antibodies against the human interleukin-4 receptor and hybridomas producing the same |
| DK0721469T3 (da) | 1993-09-02 | 2000-05-01 | Dartmouth College | Anti-gp39-antistoffer og anvendelse deraf |
| EP0659766A1 (en) | 1993-11-23 | 1995-06-28 | Schering-Plough | Human monoclonal antibodies against human cytokines and methods of making and using such antibodies |
| GB9415379D0 (en) | 1994-07-29 | 1994-09-21 | Smithkline Beecham Plc | Novel compounds |
| US5696234A (en) | 1994-08-01 | 1997-12-09 | Schering Corporation | Muteins of mammalian cytokine interleukin-13 |
| US5705154A (en) | 1995-03-08 | 1998-01-06 | Schering Corporation | Humanized monoclonal antibodies against human interleukin-4 |
| WO1997015663A1 (en) | 1995-10-23 | 1997-05-01 | Amrad Operations Pty. Ltd. | A novel haemopoietin receptor and genetic sequences encoding same |
| FR2742156A1 (fr) | 1995-12-06 | 1997-06-13 | Sanofi Sa | Polypeptide recepteur de l'il-13 |
| DK0929578T3 (da) | 1996-02-09 | 2003-08-25 | Abbott Lab Bermuda Ltd | Humane antistoffer, der binder human TNFalfa |
| US5710023A (en) * | 1996-03-01 | 1998-01-20 | Genetics Institute, Inc. | IL-13 cytokine receptor chain |
| US6664227B1 (en) | 1996-03-01 | 2003-12-16 | Genetics Institute, Llc | Treatment of fibrosis by antagonism of IL-13 and IL-13 receptor chains |
| AU2326097A (en) * | 1996-03-13 | 1997-10-01 | Zymogenetics Inc. | Cytokine-receptor expressed in testis cells |
| EP0812913A3 (en) * | 1996-06-12 | 1999-08-04 | Smithkline Beecham Corporation | HR-1 receptor, a receptor of the cytokine receptors family |
| WO1997047742A1 (en) | 1996-06-12 | 1997-12-18 | Smithkline Beecham Corporation | Hr-1 receptor |
| WO1997047741A1 (en) | 1996-06-12 | 1997-12-18 | Smithkline Beecham Corporation | Hr-1 receptor |
| WO1998010638A1 (en) * | 1996-09-10 | 1998-03-19 | Amrad Operations Pty. Ltd. | Therapeutic molecules |
| GB9625899D0 (en) | 1996-12-13 | 1997-01-29 | Glaxo Group Ltd | Substances and their uses |
| KR20000070034A (ko) | 1997-01-10 | 2000-11-25 | 아스트루 마이클 제이 | 항 ｃｄ40ｌ 화합물로 신염성 루푸스를 치료하는 방법 |
| US6387615B2 (en) * | 1997-04-11 | 2002-05-14 | Isis Innovation Limited | Methods and materials for the diagnosis or prognosis of asthma |
| GB9723553D0 (en) | 1997-11-07 | 1998-01-07 | Duff Gordon W | Prediction of the risk of chronic obstructive airway disease |
| ES2375931T3 (es) | 1997-12-05 | 2012-03-07 | The Scripps Research Institute | Humanización de anticuerpo murino. |
| PT1141286E (pt) | 1998-12-14 | 2007-01-31 | Genetics Inst Llc | Cadeia de receptores de citocina |
| AU5756100A (en) | 1999-06-21 | 2001-01-09 | Genetics Institute Inc. | Treatment of fibrosis by antagonism of il-13 and il-13 receptor chains |
| AU2000278349A1 (en) | 1999-09-28 | 2001-04-30 | Genaissance Pharmaceuticals, Inc. | Drug target isogenes: polymorphisms in the interleukin 13 gene |
| AU7863900A (en) | 1999-10-06 | 2001-05-10 | Penn State Research Foundation, The | Il13 mutants |
| US6846486B1 (en) | 2000-02-24 | 2005-01-25 | Advanced Biotherapy Concepts, Inc. | Method of treating allergy by administering an anti-histamine antibody |
| EP2990420B1 (en) | 2000-05-26 | 2016-12-21 | Immunex Corporation | Use of interleukin-4 receptor antibodies and compositions thereof |
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1999
- 1999-12-13 PT PT99966166T patent/PT1141286E/pt unknown
- 1999-12-13 EP EP99966166A patent/EP1141286B1/en not_active Revoked
- 1999-12-13 BR BR9916209-1A patent/BR9916209A/pt not_active Application Discontinuation
- 1999-12-13 MX MXPA01006006A patent/MXPA01006006A/es not_active IP Right Cessation
- 1999-12-13 ES ES99966166T patent/ES2277460T3/es not_active Expired - Lifetime
- 1999-12-13 JP JP2000588352A patent/JP5519087B2/ja not_active Expired - Fee Related
- 1999-12-13 US US09/868,123 patent/US7507706B1/en not_active Expired - Fee Related
- 1999-12-13 CA CA2356779A patent/CA2356779C/en not_active Expired - Fee Related
- 1999-12-13 CN CN201410767170.2A patent/CN104611339A/zh active Pending
- 1999-12-13 AT AT99966166T patent/ATE342976T1/de active
- 1999-12-13 NZ NZ512942A patent/NZ512942A/xx not_active IP Right Cessation
- 1999-12-13 DE DE69933696T patent/DE69933696T2/de not_active Revoked
- 1999-12-13 WO PCT/US1999/029493 patent/WO2000036103A1/en not_active Ceased
- 1999-12-13 CN CN99815591A patent/CN1352686A/zh active Pending
- 1999-12-13 DK DK99966166T patent/DK1141286T3/da active
- 1999-12-13 AU AU21775/00A patent/AU780031B2/en not_active Ceased
-
2007
- 2007-01-17 CY CY20071100068T patent/CY1107657T1/el unknown
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2010
- 2010-04-20 JP JP2010097430A patent/JP2010263889A/ja active Pending
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2014
- 2014-02-13 JP JP2014025113A patent/JP2014113165A/ja not_active Withdrawn
Also Published As
| Publication number | Publication date |
|---|---|
| WO2000036103A1 (en) | 2000-06-22 |
| ATE342976T1 (de) | 2006-11-15 |
| MXPA01006006A (es) | 2004-08-12 |
| JP2003511007A (ja) | 2003-03-25 |
| JP2010263889A (ja) | 2010-11-25 |
| EP1141286A1 (en) | 2001-10-10 |
| CA2356779A1 (en) | 2000-06-22 |
| AU2177500A (en) | 2000-07-03 |
| NZ512942A (en) | 2004-01-30 |
| DE69933696D1 (de) | 2006-11-30 |
| CA2356779C (en) | 2012-03-13 |
| EP1141286B1 (en) | 2006-10-18 |
| CN1352686A (zh) | 2002-06-05 |
| EP1141286A4 (en) | 2002-06-26 |
| WO2000036103A9 (en) | 2002-04-11 |
| PT1141286E (pt) | 2007-01-31 |
| DK1141286T3 (da) | 2007-02-19 |
| DE69933696T2 (de) | 2007-08-23 |
| JP5519087B2 (ja) | 2014-06-11 |
| AU780031B2 (en) | 2005-02-24 |
| US7507706B1 (en) | 2009-03-24 |
| CY1107657T1 (el) | 2013-04-18 |
| CN104611339A (zh) | 2015-05-13 |
| BR9916209A (pt) | 2001-12-26 |
| JP2014113165A (ja) | 2014-06-26 |
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