HRP20040147A2 - Antagonistic anti-htnfsf13b human antibodies - Google Patents
Antagonistic anti-htnfsf13b human antibodies Download PDFInfo
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- HRP20040147A2 HRP20040147A2 HR20040147A HRP20040147A HRP20040147A2 HR P20040147 A2 HRP20040147 A2 HR P20040147A2 HR 20040147 A HR20040147 A HR 20040147A HR P20040147 A HRP20040147 A HR P20040147A HR P20040147 A2 HRP20040147 A2 HR P20040147A2
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Landscapes
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Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US31280801P | 2001-08-16 | 2001-08-16 | |
| PCT/US2002/021842 WO2003016468A2 (en) | 2001-08-16 | 2002-08-15 | Antagonistic anti-htnfsf13b human antibodies |
Publications (1)
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|---|---|
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| KR (1) | KR100961299B1 (xx) |
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| CA (1) | CA2452447C (xx) |
| CO (1) | CO5560617A2 (xx) |
| DK (2) | DK1432735T3 (xx) |
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| EC (1) | ECSP044978A (xx) |
| ES (2) | ES2389834T3 (xx) |
| HR (1) | HRP20040147A2 (xx) |
| HU (1) | HU230006B1 (xx) |
| IL (1) | IL160373A0 (xx) |
| MX (1) | MXPA04001344A (xx) |
| NO (1) | NO20040603L (xx) |
| NZ (1) | NZ530657A (xx) |
| PE (1) | PE20030334A1 (xx) |
| PL (1) | PL212404B1 (xx) |
| PT (2) | PT2348048E (xx) |
| UA (1) | UA89017C2 (xx) |
| WO (1) | WO2003016468A2 (xx) |
| ZA (1) | ZA200401154B (xx) |
Families Citing this family (39)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US8212004B2 (en) * | 1999-03-02 | 2012-07-03 | Human Genome Sciences, Inc. | Neutrokine-alpha fusion proteins |
| US6812327B1 (en) * | 1996-10-25 | 2004-11-02 | Human Genome Sciences, Inc. | Neutrokine-alpha polypeptides |
| US7879328B2 (en) | 2000-06-16 | 2011-02-01 | Human Genome Sciences, Inc. | Antibodies that immunospecifically bind to B lymphocyte stimulator |
| KR101287395B1 (ko) * | 2000-06-16 | 2014-11-04 | 휴먼 게놈 사이언시즈, 인코포레이티드 | 면역특이적으로 ＢＬｙＳ에 결합하는 항체 |
| US20030091565A1 (en) | 2000-08-18 | 2003-05-15 | Beltzer James P. | Binding polypeptides and methods based thereon |
| EP2292655B1 (en) | 2001-05-11 | 2012-03-14 | Amgen SF, LLC | Peptides and related molecules that bind to tall-1 |
| WO2006025345A1 (ja) * | 2004-08-31 | 2006-03-09 | Kowa Company, Ltd. | 抗ヒトｂａｆｆ抗体 |
| BRPI0610058A2 (pt) | 2005-05-16 | 2010-05-25 | Abbott Biotech Ltd | uso de inibidor de tnf para tratamento da poliartrite erosiva |
| US9168286B2 (en) * | 2005-10-13 | 2015-10-27 | Human Genome Sciences, Inc. | Methods and compositions for use in treatment of patients with autoantibody positive disease |
| KR20140077946A (ko) | 2005-10-13 | 2014-06-24 | 휴먼 게놈 사이언시즈, 인코포레이티드 | 자가항체 양성 질환 환자의 치료에 유용한 방법 및 조성물 |
| WO2007056288A2 (en) | 2005-11-08 | 2007-05-18 | Biogen Idec Ma Inc. | Methods of evaluating baff |
| WO2007123765A2 (en) | 2006-03-31 | 2007-11-01 | Human Genome Sciences Inc. | Neutrokine-alpha and neutrokine-alpha splice variant |
| US9605064B2 (en) | 2006-04-10 | 2017-03-28 | Abbvie Biotechnology Ltd | Methods and compositions for treatment of skin disorders |
| EP2010214A4 (en) | 2006-04-10 | 2010-06-16 | Abbott Biotech Ltd | USES AND COMPOSITIONS FOR THE TREATMENT OF RHEUMATOID ARTHRITIS |
| PE20110235A1 (es) | 2006-05-04 | 2011-04-14 | Boehringer Ingelheim Int | Combinaciones farmaceuticas que comprenden linagliptina y metmorfina |
| EP1852108A1 (en) | 2006-05-04 | 2007-11-07 | Boehringer Ingelheim Pharma GmbH & Co.KG | DPP IV inhibitor formulations |
| CA2810839A1 (en) | 2006-05-04 | 2007-11-15 | Boehringer Ingelheim International Gmbh | A polymorphic form of 1-[(4-methyl-quinazolin-2-yl)methyl]-3-methyl-7-(2-butyn-1-yl)-8-(3-(r)-amino-piperidin-1-yl)-xanthine |
| ES2439994T3 (es) | 2006-08-28 | 2014-01-27 | Kyowa Hakko Kirin Co., Ltd. | Anticuerpos antagonistas monoclonales humanos específicos de LIGHT humano |
| EP2109460B1 (en) | 2007-01-11 | 2016-05-18 | Novo Nordisk A/S | Anti-kir antibodies, formulations, and uses thereof |
| PE20091730A1 (es) | 2008-04-03 | 2009-12-10 | Boehringer Ingelheim Int | Formulaciones que comprenden un inhibidor de dpp4 |
| US20200155558A1 (en) | 2018-11-20 | 2020-05-21 | Boehringer Ingelheim International Gmbh | Treatment for diabetes in patients with insufficient glycemic control despite therapy with an oral antidiabetic drug |
| US20110014190A1 (en) * | 2009-02-12 | 2011-01-20 | Human Genome Sciences, Inc. | Use of b lymphocyte stimulator protein antagonists to promote transplantation tolerance |
| US9034883B2 (en) | 2010-11-15 | 2015-05-19 | Boehringer Ingelheim International Gmbh | Vasoprotective and cardioprotective antidiabetic therapy |
| WO2013059885A2 (en) | 2011-10-28 | 2013-05-02 | Cephalon Australia Pty Ltd | Polypeptide constructs and uses thereof |
| AR090626A1 (es) * | 2012-04-20 | 2014-11-26 | Lilly Co Eli | Anticuerpos anti-baff-anti-il-17 biespecificos |
| WO2014008404A1 (en) | 2012-07-03 | 2014-01-09 | Washington University | Antibodies to tau |
| JOP20140087B1 (ar) | 2013-03-13 | 2021-08-17 | Amgen Inc | بروتينات مخصصة ل baff و b7rp1 وإستخداماتها |
| US9458246B2 (en) | 2013-03-13 | 2016-10-04 | Amgen Inc. | Proteins specific for BAFF and B7RP1 |
| US9700485B2 (en) | 2013-04-24 | 2017-07-11 | Corning Incorporated | Delamination resistant pharmaceutical glass containers containing active pharmaceutical ingredients |
| EP3677591B1 (en) | 2013-04-29 | 2022-12-28 | Teva Pharmaceuticals Australia Pty Ltd | Anti-cd38 antibodies and fusions to attenuated interferon alpha-2b |
| US11117975B2 (en) | 2013-04-29 | 2021-09-14 | Teva Pharmaceuticals Australia Pty Ltd | Anti-CD38 antibodies and fusions to attenuated interferon alpha-2B |
| WO2015100246A1 (en) | 2013-12-24 | 2015-07-02 | Ossianix, Inc. | Baff selective binding compounds and related methods |
| KR20160113715A (ko) * | 2014-01-31 | 2016-09-30 | 베링거 인겔하임 인터내셔날 게엠베하 | 신규한 항-ｂａｆｆ 항체 |
| UA119352C2 (uk) | 2014-05-01 | 2019-06-10 | Тева Фармасьютикалз Острейліа Пті Лтд | Комбінація леналідоміду або помалідоміду і конструкції анти-cd38 антитіло-атенуйований інтерферон альфа-2b та спосіб лікування суб'єкта, який має cd38-експресуючу пухлину |
| TWI694836B (zh) * | 2014-05-16 | 2020-06-01 | 英商葛蘭素史克智慧財產管理有限公司 | 抗體調配物 |
| EP3151857A4 (en) * | 2014-06-03 | 2018-04-18 | Merck Sharp & Dohme Corp. | Anti-blys antibodies |
| TW202136296A (zh) | 2014-06-27 | 2021-10-01 | 美商Ｃ２Ｎ醫療診斷有限責任公司 | 人類化抗-tau抗體 |
| MX2017005481A (es) | 2014-10-29 | 2017-10-26 | Teva Pharmaceuticals Australia Pty Ltd | Variantes de interferon a2b. |
| AR104368A1 (es) * | 2015-04-03 | 2017-07-19 | Lilly Co Eli | Anticuerpos biespecíficos anti-cd20- / anti-baff |
Family Cites Families (20)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5874299A (en) | 1990-08-29 | 1999-02-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5625126A (en) | 1990-08-29 | 1997-04-29 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| DK0546073T3 (da) | 1990-08-29 | 1998-02-02 | Genpharm Int | Frembringelse og anvendelse af transgene, ikke-humane dyr, der er i stand til at danne heterologe antistoffer |
| US5877397A (en) | 1990-08-29 | 1999-03-02 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US5789650A (en) | 1990-08-29 | 1998-08-04 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5661016A (en) | 1990-08-29 | 1997-08-26 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
| US5770429A (en) | 1990-08-29 | 1998-06-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5814318A (en) | 1990-08-29 | 1998-09-29 | Genpharm International Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US6096878A (en) | 1993-05-10 | 2000-08-01 | Japan Tobacco Inc. | Human immunoglobulin VH gene segments and DNA fragments containing the same |
| US6812327B1 (en) | 1996-10-25 | 2004-11-02 | Human Genome Sciences, Inc. | Neutrokine-alpha polypeptides |
| PT939804E (pt) | 1996-10-25 | 2005-11-30 | Human Genome Sciences Inc | Neutroquina alfa |
| AU5705898A (en) | 1996-12-17 | 1998-07-15 | Schering Corporation | Mammalian cell surface antigens; related reagents |
| WO1999012964A2 (en) | 1997-09-12 | 1999-03-18 | Biogen, Inc. | Kay - a novel immune system protein |
| US6297367B1 (en) | 1997-12-30 | 2001-10-02 | Chiron Corporation | Polynucleotide encoding TNFL1 |
| US6787638B1 (en) | 1998-12-02 | 2004-09-07 | Applied Molecular Evolution, Inc. | Tumor specific human monoclonal antibodies and methods of use |
| HUP0105283A3 (en) | 1999-01-25 | 2004-08-30 | Biogen Idec Ma Inc Cambridge | Baff, inhibitors thereof and their use in the modulation of b-cell response |
| NZ513290A (en) | 1999-02-23 | 2004-05-28 | Human Genome Sciences Inc | Neutrokine-alpha and neutrokine-alpha splice variant |
| KR101287395B1 (ko) | 2000-06-16 | 2014-11-04 | 휴먼 게놈 사이언시즈, 인코포레이티드 | 면역특이적으로 ＢＬｙＳ에 결합하는 항체 |
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- 2002-08-15 EP EP10184675.6A patent/EP2348048B1/en not_active Expired - Lifetime
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