JP2010527356A - 好酸球レベルを低下させる方法 - Google Patents
好酸球レベルを低下させる方法 Download PDFInfo
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| JP2016527325A (ja) * | 2013-08-12 | 2016-09-08 | メディミューン，エルエルシー | ベンラリツマブを使用して喘息患者の努力肺活量を増大させる方法 |
| JP2016527324A (ja) * | 2013-08-12 | 2016-09-08 | メディミューン，エルエルシー | ベンラリツマブを使用して喘息の増悪率を低減する方法 |
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Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1997010354A1 (fr) * | 1995-09-11 | 1997-03-20 | Kyowa Hakko Kogyo Co., Ltd. | Anticorps de la chaine alpha du recepteur de l'interleukine 5 humaine |
| WO2005035583A1 (ja) * | 2003-10-08 | 2005-04-21 | Kyowa Hakko Kogyo Co., Ltd. | Ｉｌ－５受容体に特異的に結合する抗体組成物 |
Family Cites Families (128)
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|---|---|---|---|---|
| US633187A (en) | 1898-12-20 | 1899-09-19 | Alba L Holmes | Meter-box. |
| US4444887A (en) | 1979-12-10 | 1984-04-24 | Sloan-Kettering Institute | Process for making human antibody producing B-lymphocytes |
| US4714681A (en) | 1981-07-01 | 1987-12-22 | The Board Of Reagents, The University Of Texas System Cancer Center | Quadroma cells and trioma cells and methods for the production of same |
| US4474893A (en) | 1981-07-01 | 1984-10-02 | The University of Texas System Cancer Center | Recombinant monoclonal antibodies |
| US4716111A (en) | 1982-08-11 | 1987-12-29 | Trustees Of Boston University | Process for producing human antibodies |
| GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US5807715A (en) | 1984-08-27 | 1998-09-15 | The Board Of Trustees Of The Leland Stanford Junior University | Methods and transformed mammalian lymphocyte cells for producing functional antigen-binding protein including chimeric immunoglobulin |
| JP2532858B2 (ja) | 1985-04-01 | 1996-09-11 | セルテツク リミテツド | 形質転換したミエロ―マ細胞系 |
| US4676980A (en) | 1985-09-23 | 1987-06-30 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Target specific cross-linked heteroantibodies |
| GB8601597D0 (en) | 1986-01-23 | 1986-02-26 | Wilson R H | Nucleotide sequences |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| GB8607679D0 (en) | 1986-03-27 | 1986-04-30 | Winter G P | Recombinant dna product |
| WO1988007089A1 (en) | 1987-03-18 | 1988-09-22 | Medical Research Council | Altered antibodies |
| GB8717430D0 (en) | 1987-07-23 | 1987-08-26 | Celltech Ltd | Recombinant dna product |
| US5336603A (en) | 1987-10-02 | 1994-08-09 | Genentech, Inc. | CD4 adheson variants |
| US4925648A (en) | 1988-07-29 | 1990-05-15 | Immunomedics, Inc. | Detection and treatment of infectious and inflammatory lesions |
| US5601819A (en) | 1988-08-11 | 1997-02-11 | The General Hospital Corporation | Bispecific antibodies for selective immune regulation and for selective immune cell binding |
| EP1892296A1 (en) | 1988-09-02 | 2008-02-27 | Dyax Corporation | Generation and selection of recombinant varied binding proteins |
| US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| KR900005995A (ko) | 1988-10-31 | 1990-05-07 | 우메모또 요시마사 | 변형 인터류킨-2 및 그의 제조방법 |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| EP0479909B1 (en) | 1989-06-29 | 1996-10-30 | Medarex, Inc. | Bispecific reagents for aids therapy |
| US5112946A (en) | 1989-07-06 | 1992-05-12 | Repligen Corporation | Modified pf4 compositions and methods of use |
| US5413923A (en) | 1989-07-25 | 1995-05-09 | Cell Genesys, Inc. | Homologous recombination for universal donor cells and chimeric mammalian hosts |
| FR2650598B1 (fr) | 1989-08-03 | 1994-06-03 | Rhone Poulenc Sante | Derives de l'albumine a fonction therapeutique |
| WO1991006570A1 (en) | 1989-10-25 | 1991-05-16 | The University Of Melbourne | HYBRID Fc RECEPTOR MOLECULES |
| GB8928874D0 (en) | 1989-12-21 | 1990-02-28 | Celltech Ltd | Humanised antibodies |
| AU7247191A (en) | 1990-01-11 | 1991-08-05 | Molecular Affinities Corporation | Production of antibodies using gene libraries |
| US5780225A (en) | 1990-01-12 | 1998-07-14 | Stratagene | Method for generating libaries of antibody genes comprising amplification of diverse antibody DNAs and methods for using these libraries for the production of diverse antigen combining molecules |
| JP3068180B2 (ja) | 1990-01-12 | 2000-07-24 | アブジェニックス インコーポレイテッド | 異種抗体の生成 |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| US5349053A (en) | 1990-06-01 | 1994-09-20 | Protein Design Labs, Inc. | Chimeric ligand/immunoglobulin molecules and their uses |
| GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| US5661016A (en) | 1990-08-29 | 1997-08-26 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US5814318A (en) | 1990-08-29 | 1998-09-29 | Genpharm International Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
| US5625126A (en) | 1990-08-29 | 1997-04-29 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| WO1992003918A1 (en) | 1990-08-29 | 1992-03-19 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5698426A (en) | 1990-09-28 | 1997-12-16 | Ixsys, Incorporated | Surface expression libraries of heteromeric receptors |
| DK0553244T4 (da) | 1990-10-05 | 2005-08-01 | Celldex Therapeutics Inc | Målrettet immunostimulering med bispecifikke reagenser |
| AU8727291A (en) | 1990-10-29 | 1992-06-11 | Cetus Oncology Corporation | Bispecific antibodies, method of production, and uses thereof |
| ES2113940T3 (es) | 1990-12-03 | 1998-05-16 | Genentech Inc | Metodo de enriquecimiento para variantes de proteinas con propiedades de union alteradas. |
| EP0732402A3 (en) | 1990-12-14 | 1997-05-21 | Cell Genesys Inc | Chimeric chains for transduction of receptor-linked signaling pathways |
| IE921169A1 (en) | 1991-04-10 | 1992-10-21 | Scripps Research Inst | Heterodimeric receptor libraries using phagemids |
| DE69214709T2 (de) | 1991-04-26 | 1997-02-20 | Surface Active Ltd | Neue Antikörper und Verfahren zu ihrer Verwendung |
| DE69233482T2 (de) | 1991-05-17 | 2006-01-12 | Merck & Co., Inc. | Verfahren zur Verminderung der Immunogenität der variablen Antikörperdomänen |
| WO1992022653A1 (en) | 1991-06-14 | 1992-12-23 | Genentech, Inc. | Method for making humanized antibodies |
| JPH07503124A (ja) | 1991-06-14 | 1995-04-06 | ゾーマ・コーポレーション | 微生物によって生産される抗体断片とそれらの複合体 |
| US5565332A (en) | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| DK1024191T3 (da) | 1991-12-02 | 2008-12-08 | Medical Res Council | Fremstilling af autoantistoffer fremvist på fag-overflader ud fra antistofsegmentbiblioteker |
| US5766886A (en) | 1991-12-13 | 1998-06-16 | Xoma Corporation | Modified antibody variable domains |
| US5622929A (en) | 1992-01-23 | 1997-04-22 | Bristol-Myers Squibb Company | Thioether conjugates |
| FR2686901A1 (fr) | 1992-01-31 | 1993-08-06 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides antithrombotiques, leur preparation et compositions pharmaceutiques les contenant. |
| FR2686899B1 (fr) | 1992-01-31 | 1995-09-01 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides biologiquement actifs, leur preparation et compositions pharmaceutiques les contenant. |
| GB9203459D0 (en) | 1992-02-19 | 1992-04-08 | Scotgen Ltd | Antibodies with germ-line variable regions |
| PT627940E (pt) | 1992-03-05 | 2003-07-31 | Univ Texas | Utilizacao de imunoconjugados para o diagnostico e/ou terapia de tumores vascularizados |
| US5733743A (en) | 1992-03-24 | 1998-03-31 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| US5447851B1 (en) | 1992-04-02 | 1999-07-06 | Univ Texas System Board Of | Dna encoding a chimeric polypeptide comprising the extracellular domain of tnf receptor fused to igg vectors and host cells |
| US6005079A (en) | 1992-08-21 | 1999-12-21 | Vrije Universiteit Brussels | Immunoglobulins devoid of light chains |
| EP1498427B1 (en) | 1992-08-21 | 2009-12-16 | Vrije Universiteit Brussel | Immunoglobulins devoid of light chains |
| US5639641A (en) | 1992-09-09 | 1997-06-17 | Immunogen Inc. | Resurfacing of rodent antibodies |
| DE69427974T2 (de) | 1993-04-29 | 2001-12-06 | Unilever N.V., Rotterdam | Herstellung von antikörpern oder funktionstüchtig gemachten teilen davon, abgeleitet von schweren ketten von immunglobulinen von camelidae |
| EP0733070A1 (en) | 1993-12-08 | 1996-09-25 | Genzyme Corporation | Process for generating specific antibodies |
| PT1231268E (pt) | 1994-01-31 | 2005-11-30 | Univ Boston | Bancos de anticorpos policlonais |
| US5837458A (en) | 1994-02-17 | 1998-11-17 | Maxygen, Inc. | Methods and compositions for cellular and metabolic engineering |
| US5605793A (en) | 1994-02-17 | 1997-02-25 | Affymax Technologies N.V. | Methods for in vitro recombination |
| US5834252A (en) | 1995-04-18 | 1998-11-10 | Glaxo Group Limited | End-complementary polymerase reaction |
| US6465616B1 (en) | 1994-04-08 | 2002-10-15 | Bresagen Limited | Interleukin-5 antagonist |
| US5516637A (en) | 1994-06-10 | 1996-05-14 | Dade International Inc. | Method involving display of protein binding pairs on the surface of bacterial pili and bacteriophage |
| AU3382595A (en) | 1994-07-29 | 1996-03-04 | Smithkline Beecham Corporation | Novel compounds |
| AU5632296A (en) | 1995-04-27 | 1996-11-18 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| CA2219486A1 (en) | 1995-04-28 | 1996-10-31 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US5702892A (en) | 1995-05-09 | 1997-12-30 | The United States Of America As Represented By The Department Of Health And Human Services | Phage-display of immunoglobulin heavy chain libraries |
| US5677280A (en) | 1995-06-07 | 1997-10-14 | Glaxo Group Limited | Peptides and compounds that bind to the IL-5 receptor |
| US6410690B1 (en) | 1995-06-07 | 2002-06-25 | Medarex, Inc. | Therapeutic compounds comprised of anti-Fc receptor antibodies |
| GB9601081D0 (en) | 1995-10-06 | 1996-03-20 | Cambridge Antibody Tech | Specific binding members for human transforming growth factor beta;materials and methods |
| JP2978435B2 (ja) | 1996-01-24 | 1999-11-15 | チッソ株式会社 | アクリロキシプロピルシランの製造方法 |
| WO1997034631A1 (en) | 1996-03-18 | 1997-09-25 | Board Of Regents, The University Of Texas System | Immunoglobin-like domains with increased half lives |
| US5916771A (en) | 1996-10-11 | 1999-06-29 | Abgenix, Inc. | Production of a multimeric protein by cell fusion method |
| WO1998023289A1 (en) | 1996-11-27 | 1998-06-04 | The General Hospital Corporation | MODULATION OF IgG BINDING TO FcRn |
| JP4215172B2 (ja) | 1996-12-03 | 2009-01-28 | アムジェン フレモント インク． | 複数のＶ▲下Ｈ▼およびＶ▲下κ▼領域を含むヒトＩｇ遺伝子座を有するトランスジェニック哺乳動物、ならびにそれから産生される抗体 |
| US6277375B1 (en) | 1997-03-03 | 2001-08-21 | Board Of Regents, The University Of Texas System | Immunoglobulin-like domains with increased half-lives |
| US7227002B1 (en) | 1997-04-14 | 2007-06-05 | Micromet Ag | Human antibodies that bind human 17-A1/EpCAM tumor antigen |
| US6235883B1 (en) | 1997-05-05 | 2001-05-22 | Abgenix, Inc. | Human monoclonal antibodies to epidermal growth factor receptor |
| ES2532910T3 (es) | 1998-04-02 | 2015-04-01 | Genentech, Inc. | Variantes de anticuerpos y fragmentos de los mismos |
| DK2180007T4 (da) | 1998-04-20 | 2017-11-27 | Roche Glycart Ag | Glycosyleringsteknik for antistoffer til forbedring af antistofafhængig cellecytotoxicitet |
| GB9809951D0 (en) | 1998-05-08 | 1998-07-08 | Univ Cambridge Tech | Binding molecules |
| ES2571230T3 (es) | 1999-04-09 | 2016-05-24 | Kyowa Hakko Kirin Co Ltd | Procedimiento para controlar la actividad de una molécula inmunofuncional |
| AU7950400A (en) | 1999-10-19 | 2001-04-30 | Kyowa Hakko Kogyo Co. Ltd. | Process for producing polypeptide |
| US7033840B1 (en) * | 1999-11-09 | 2006-04-25 | Sri International | Reaction calorimeter and differential scanning calorimeter for the high-throughput synthesis, screening and characterization of combinatorial libraries |
| DK1233987T3 (da) | 1999-11-29 | 2009-09-28 | Bac Ip B V | Immobiliserede enkelt-domæne antigenbindende molekyler |
| US7109299B1 (en) | 1999-12-16 | 2006-09-19 | Affymax, Inc. | Peptides and compounds that bind to the IL-5 receptor |
| WO2001060405A1 (en) | 2000-02-15 | 2001-08-23 | Kyowa Hakko Kogyo Co., Ltd. | Eosinophil-specific apoptosis inducer |
| JP2003530847A (ja) | 2000-04-12 | 2003-10-21 | ヒューマン ゲノム サイエンシズ インコーポレイテッド | アルブミン融合タンパク質 |
| EP1272526A4 (en) | 2000-04-13 | 2004-10-13 | Univ Rockefeller | REINFORCING ANTIBODY-IMMUNE RESPONSE |
| US20060257399A1 (en) | 2000-06-28 | 2006-11-16 | Glycofi, Inc. | Immunoglobulins comprising predominantly a Man5GIcNAc2 glycoform |
| KR100787073B1 (ko) | 2000-06-28 | 2007-12-21 | 글리코파이, 인크. | 변형된 당단백질의 제조방법 |
| US7632983B2 (en) | 2000-07-31 | 2009-12-15 | Biolex Therapeutics, Inc. | Expression of monoclonal antibodies in duckweed |
| WO2002030954A1 (en) | 2000-10-06 | 2002-04-18 | Kyowa Hakko Kogyo Co., Ltd. | Method of purifying antibody |
| AU9419801A (en) | 2000-10-06 | 2002-04-22 | Kyowa Hakko Kogyo Kk | Cells producing antibody compositions |
| US6946292B2 (en) | 2000-10-06 | 2005-09-20 | Kyowa Hakko Kogyo Co., Ltd. | Cells producing antibody compositions with increased antibody dependent cytotoxic activity |
| CA2442801A1 (en) | 2001-04-02 | 2002-10-10 | Idec Pharmaceutical Corporation | Recombinant antibodies coexpressed with gntiii |
| CN1555411A (zh) | 2001-08-03 | 2004-12-15 | ���迨�����＼���ɷݹ�˾ | 抗体-依赖性细胞毒性增大的抗体糖基化变体 |
| ES2326964T3 (es) | 2001-10-25 | 2009-10-22 | Genentech, Inc. | Composiciones de glicoproteina. |
| US7662925B2 (en) * | 2002-03-01 | 2010-02-16 | Xencor, Inc. | Optimized Fc variants and methods for their generation |
| US20040259150A1 (en) | 2002-04-09 | 2004-12-23 | Kyowa Hakko Kogyo Co., Ltd. | Method of enhancing of binding activity of antibody composition to Fcgamma receptor IIIa |
| AU2003236015A1 (en) | 2002-04-09 | 2003-10-20 | Kyowa Hakko Kirin Co., Ltd. | Process for producing antibody composition |
| EA200401325A1 (ru) | 2002-04-09 | 2005-04-28 | Киова Хакко Когио Ко., Лтд. | Клетки с модифицированным геномом |
| WO2003085102A1 (en) | 2002-04-09 | 2003-10-16 | Kyowa Hakko Kogyo Co., Ltd. | Cell with depression or deletion of the activity of protein participating in gdp-fucose transport |
| CA2495251C (en) | 2002-08-14 | 2018-03-06 | Macrogenics, Inc. | Fc.gamma.riib-specific antibodies and methods of use thereof |
| DK2364996T3 (en) | 2002-09-27 | 2017-02-06 | Xencor Inc | Optimized Fc variants and methods for their formation |
| US20060147523A1 (en) * | 2002-10-16 | 2006-07-06 | Alan Fergusson | Composition for the regulation of the human immune system and the prevention and treatment of diseases thereof |
| US7355008B2 (en) | 2003-01-09 | 2008-04-08 | Macrogenics, Inc. | Identification and engineering of antibodies with variant Fc regions and methods of using same |
| US20050226867A1 (en) | 2003-10-08 | 2005-10-13 | Kyowa Hakko Kogyo Co., Ltd. | IL-5R-specific antibody composition |
| US20050095602A1 (en) * | 2003-11-04 | 2005-05-05 | West Jason A. | Microfluidic integrated microarrays for biological detection |
| EP2380911B1 (en) | 2003-11-05 | 2018-05-09 | Roche Glycart AG | Antigen binding molecules with increased Fc receptor binding affinity and effector function |
| ES2641831T3 (es) | 2003-12-10 | 2017-11-14 | E. R. Squibb & Sons, L.L.C. | Anticuerpos contra interferón alfa y sus usos |
| US20060014680A1 (en) * | 2004-07-13 | 2006-01-19 | Caiding Xu | Peptides and compounds that bind to the IL-5 receptor |
| PL2471813T3 (pl) * | 2004-07-15 | 2015-09-30 | Xencor Inc | Zoptymalizowane warianty Fc |
| WO2006023420A2 (en) | 2004-08-16 | 2006-03-02 | Medimmune, Inc. | Integrin antagonists with enhanced antibody dependent cell-mediated cytotoxicity activity |
| AU2005285347A1 (en) | 2004-08-19 | 2006-03-23 | Genentech, Inc. | Polypeptide variants with altered effector function |
| AU2005322617A1 (en) | 2004-12-23 | 2006-07-06 | Glycofi, Inc. | Immunoglobulins comprising predominantly a Ga1G1cNAcMan5GlcNAc2 glycoform |
| WO2006071856A2 (en) | 2004-12-23 | 2006-07-06 | Glycofi, Inc. | Immunoglobulins comprising predominantly a man5glcnac2 glycoform |
| WO2007041635A2 (en) * | 2005-10-03 | 2007-04-12 | Xencor, Inc. | Fc variants with optimized fc receptor binding properties |
| PL1945665T3 (pl) | 2005-10-21 | 2012-02-29 | Genzyme Corp | Leki oparte na przeciwciałach z ulepszoną aktywnością adcc |
| NO3072525T3 (OSRAM) * | 2007-05-14 | 2018-06-30 |
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1997010354A1 (fr) * | 1995-09-11 | 1997-03-20 | Kyowa Hakko Kogyo Co., Ltd. | Anticorps de la chaine alpha du recepteur de l'interleukine 5 humaine |
| WO2005035583A1 (ja) * | 2003-10-08 | 2005-04-21 | Kyowa Hakko Kogyo Co., Ltd. | Ｉｌ－５受容体に特異的に結合する抗体組成物 |
Non-Patent Citations (3)
| Title |
|---|
| "協和発酵、喘息治療向け抗体医薬品を臨床試験、０６年米子会社で", 化学工業日報, JPN6013014973, 2 November 2005 (2005-11-02), pages 6, ISSN: 0002493957 * |
| INT ARCH ALLERGY IMMUNOL., vol. 135, no. 1, JPN6013014974, 29 July 2004 (2004-07-29), pages 54 - 61, ISSN: 0002493958 * |
| PNAS, vol. 103, no. 11, JPN6013014976, 14 March 2006 (2006-03-14), pages 4005 - 4010, ISSN: 0002493959 * |
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