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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- Rheumatology (AREA)
- Pain & Pain Management (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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Family Applications (1)
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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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| AT (1) | ATE342976T1 (enExample) |
| AU (1) | AU780031B2 (enExample) |
| BR (1) | BR9916209A (enExample) |
| CA (1) | CA2356779C (enExample) |
| CY (1) | CY1107657T1 (enExample) |
| DE (1) | DE69933696T2 (enExample) |
| DK (1) | DK1141286T3 (enExample) |
| ES (1) | ES2277460T3 (enExample) |
| MX (1) | MXPA01006006A (enExample) |
| NZ (1) | NZ512942A (enExample) |
| PT (1) | PT1141286E (enExample) |
| WO (1) | WO2000036103A1 (enExample) |
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| US7553487B2 (en) * | 1998-12-14 | 2009-06-30 | Genetics Institute, Llc | Method and compositions for treating asthma |
| ES2277460T3 (es) | 1998-12-14 | 2007-07-01 | Genetics Institute, Llc | Cadena del receptor de la citoquina. |
| EP2027867A1 (en) * | 2000-10-20 | 2009-02-25 | Genetics Institute, LLC | Method and composition for inhibition of tumor growth and enhancing an immune response |
| EP1587534A1 (en) * | 2003-01-17 | 2005-10-26 | Children's Hospital Medical Center | Use of tff2, or agents inducing tff2, in the therapy of allergies |
| CA2512808A1 (en) * | 2003-01-18 | 2004-08-12 | Marc Elliot Rothenberg | 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 |
| PL1711528T3 (pl) | 2003-12-23 | 2012-11-30 | Genentech Inc | Leczenie nowotworu nowymi przeciwciałami monoklonalnymi anty-IL13 |
| 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 |
| AR049390A1 (es) | 2004-06-09 | 2006-07-26 | Wyeth Corp | Anticuerpos contra la interleuquina-13 humana y usos de los mismos |
| US7501121B2 (en) * | 2004-06-17 | 2009-03-10 | Wyeth | IL-13 binding agents |
| US20090098142A1 (en) * | 2004-06-09 | 2009-04-16 | Kasaian Marion T | Methods and compositions for treating and monitoring treatment of IL-13-associated disorders |
| MX2007005866A (es) | 2004-11-17 | 2007-11-12 | Amgen Inc | Anticuerpos monoclonales totalmente humanos para il-13. |
| MY144906A (en) | 2005-10-21 | 2011-11-30 | Novartis Ag | Human antibodies against il13 and therapeutic uses |
| RU2009140134A (ru) * | 2007-04-23 | 2011-05-27 | Вайет (Us) | Способы и композиции для лечения и мониторинга лечения связанных с ил-13 нарушений |
| EP2162743A4 (en) * | 2007-05-29 | 2010-07-14 | Univ Cincinnati | METHOD FOR MODULATING IGNITION AND COMPOSITIONS THEREFOR |
| CR20160132A (es) | 2013-08-12 | 2016-08-25 | Genentech Inc | Composiciones y método para tratar condiciones asociadas con el complemento |
| BR112016004437A2 (pt) | 2013-09-13 | 2017-10-17 | Genentech Inc | métodos de imunoteste e de seleção de linhagem de células, anticorpos e kit |
| CN105722532A (zh) | 2013-09-13 | 2016-06-29 | 豪夫迈·罗氏有限公司 | 包含纯化的重组多肽的方法和组合物 |
| CA3059731A1 (en) | 2017-04-21 | 2018-10-25 | Kindred Biosciences, 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 |
| CZ283050B6 (cs) | 1989-12-20 | 1997-12-17 | Schering Corporation | Polypeptid, jeho subsekvence a jejich použití |
| 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 |
| ATE130869T1 (de) | 1991-03-29 | 1995-12-15 | Sanofi Sa | Protein mit der aktivität vom typ von cytokin, dafür kodierende rekombinante dns, transformierte zellen und mikroorganismen. |
| 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 |
| WO1994004680A1 (en) | 1992-08-21 | 1994-03-03 | 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 |
| EP0721346B1 (en) | 1993-09-02 | 1998-06-10 | Trustees of Dartmouth College | Methods for inducing antigen-specific t cell tolerance |
| 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 |
| EP0907730B1 (en) * | 1995-10-23 | 2009-10-07 | Zenyth Operations Pty Ltd | Haemopoietin receptor and genetic sequences encoding same |
| FR2742156A1 (fr) | 1995-12-06 | 1997-06-13 | Sanofi Sa | Polypeptide recepteur de l'il-13 |
| DE69721548T2 (de) | 1996-02-09 | 2004-04-01 | Abbott Laboratories(Bermuda)Ltd. | HUMANE ANTIKÖRPER WELCHE AN HUMANEN TNFalpha BINDEN |
| US6664227B1 (en) | 1996-03-01 | 2003-12-16 | Genetics Institute, Llc | Treatment of fibrosis by antagonism of IL-13 and IL-13 receptor chains |
| US5710023A (en) * | 1996-03-01 | 1998-01-20 | Genetics Institute, Inc. | IL-13 cytokine receptor chain |
| WO1997033913A1 (en) * | 1996-03-13 | 1997-09-18 | 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 |
| AU6175696A (en) * | 1996-06-12 | 1998-01-07 | Human Genome Sciences, Inc. | Hr-1 receptor |
| WO1997047742A1 (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 |
| TR200001247T2 (tr) | 1997-01-10 | 2002-06-21 | Biogen Inc. | Anti-CD40L bileşikleri ile lupus nefritis tedavisi. |
| 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 |
| JP4460155B2 (ja) | 1997-12-05 | 2010-05-12 | ザ・スクリプス・リサーチ・インステイチユート | マウス抗体のヒト化 |
| ES2277460T3 (es) | 1998-12-14 | 2007-07-01 | Genetics Institute, Llc | Cadena del receptor de la citoquina. |
| 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 |
| EP1222212A4 (en) | 1999-10-06 | 2005-05-04 | Penn State Res Found | MUTANTS OF IL-13 |
| 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 ES ES99966166T patent/ES2277460T3/es not_active Expired - Lifetime
- 1999-12-13 CN CN99815591A patent/CN1352686A/zh active Pending
- 1999-12-13 JP JP2000588352A patent/JP5519087B2/ja not_active Expired - Fee Related
- 1999-12-13 MX MXPA01006006A patent/MXPA01006006A/es not_active IP Right Cessation
- 1999-12-13 CN CN201410767170.2A patent/CN104611339A/zh active Pending
- 1999-12-13 PT PT99966166T patent/PT1141286E/pt unknown
- 1999-12-13 BR BR9916209-1A patent/BR9916209A/pt not_active Application Discontinuation
- 1999-12-13 US US09/868,123 patent/US7507706B1/en not_active Expired - Fee Related
- 1999-12-13 AT AT99966166T patent/ATE342976T1/de active
- 1999-12-13 CA CA2356779A patent/CA2356779C/en not_active Expired - Fee Related
- 1999-12-13 WO PCT/US1999/029493 patent/WO2000036103A1/en not_active Ceased
- 1999-12-13 EP EP99966166A patent/EP1141286B1/en not_active Revoked
- 1999-12-13 DE DE69933696T patent/DE69933696T2/de not_active Revoked
- 1999-12-13 AU AU21775/00A patent/AU780031B2/en not_active Ceased
- 1999-12-13 DK DK99966166T patent/DK1141286T3/da active
- 1999-12-13 NZ NZ512942A patent/NZ512942A/xx not_active IP Right Cessation
-
2007
- 2007-01-17 CY CY20071100068T patent/CY1107657T1/el unknown
-
2010
- 2010-04-20 JP JP2010097430A patent/JP2010263889A/ja active Pending
-
2014
- 2014-02-13 JP JP2014025113A patent/JP2014113165A/ja not_active Withdrawn
Also Published As
| Publication number | Publication date |
|---|---|
| ATE342976T1 (de) | 2006-11-15 |
| CN1352686A (zh) | 2002-06-05 |
| PT1141286E (pt) | 2007-01-31 |
| US7507706B1 (en) | 2009-03-24 |
| CN104611339A (zh) | 2015-05-13 |
| DK1141286T3 (da) | 2007-02-19 |
| EP1141286A1 (en) | 2001-10-10 |
| EP1141286B1 (en) | 2006-10-18 |
| CA2356779A1 (en) | 2000-06-22 |
| AU2177500A (en) | 2000-07-03 |
| DE69933696T2 (de) | 2007-08-23 |
| CA2356779C (en) | 2012-03-13 |
| JP2014113165A (ja) | 2014-06-26 |
| AU780031B2 (en) | 2005-02-24 |
| DE69933696D1 (de) | 2006-11-30 |
| WO2000036103A1 (en) | 2000-06-22 |
| WO2000036103A9 (en) | 2002-04-11 |
| JP2010263889A (ja) | 2010-11-25 |
| CY1107657T1 (el) | 2013-04-18 |
| EP1141286A4 (en) | 2002-06-26 |
| JP2003511007A (ja) | 2003-03-25 |
| JP5519087B2 (ja) | 2014-06-11 |
| BR9916209A (pt) | 2001-12-26 |
| MXPA01006006A (es) | 2004-08-12 |
| NZ512942A (en) | 2004-01-30 |
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