CA2278848A1 - Anti-alpha-v beta-3 recombinant humanized antibodies, nucleic acids encoding same and methods of use - Google Patents
Anti-alpha-v beta-3 recombinant humanized antibodies, nucleic acids encoding same and methods of use Download PDFInfo
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- CA2278848A1 CA2278848A1 CA002278848A CA2278848A CA2278848A1 CA 2278848 A1 CA2278848 A1 CA 2278848A1 CA 002278848 A CA002278848 A CA 002278848A CA 2278848 A CA2278848 A CA 2278848A CA 2278848 A1 CA2278848 A1 CA 2278848A1
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Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2839—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the integrin superfamily
- C07K16/2848—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the integrin superfamily against integrin beta3-subunit-containing molecules, e.g. CD41, CD51, CD61
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Immunology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- General Chemical & Material Sciences (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Cardiology (AREA)
- Heart & Thoracic Surgery (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)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US08/791,391 | 1997-01-30 | ||
| US08/791,391 US6590079B2 (en) | 1997-01-30 | 1997-01-30 | Anti-αvβ3 recombinant human antibodies, nucleic acids encoding same |
| PCT/US1998/001826 WO1998033919A2 (en) | 1997-01-30 | 1998-01-30 | Anti-alpha-v beta-3 recombinant humanized antibodies, nucleic acids encoding same and methods of use |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2278848A1 true CA2278848A1 (en) | 1998-08-06 |
Family
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Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002278848A Abandoned CA2278848A1 (en) | 1997-01-30 | 1998-01-30 | Anti-alpha-v beta-3 recombinant humanized antibodies, nucleic acids encoding same and methods of use |
Country Status (6)
| Country | Link |
|---|---|
| US (2) | US6590079B2 (enExample) |
| EP (1) | EP0970217A2 (enExample) |
| JP (1) | JP2001511149A (enExample) |
| AU (1) | AU737569B2 (enExample) |
| CA (1) | CA2278848A1 (enExample) |
| WO (1) | WO1998033919A2 (enExample) |
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| US6590079B2 (en) * | 1997-01-30 | 2003-07-08 | Ixsys, Incorporated | Anti-αvβ3 recombinant human antibodies, nucleic acids encoding same |
| US20010011125A1 (en) * | 1997-01-30 | 2001-08-02 | William D. Huse | Anti-alpha v beta 3 recombinant human antibodies, nucleic acids encoding same and methods of use |
| US6596850B1 (en) * | 1998-01-30 | 2003-07-22 | Ixsys, Incorporated | Anti-αv3β3 recombinant human antibodies, nucleic acids encoding same |
| EP1135688A2 (en) * | 1998-12-04 | 2001-09-26 | Novartis AG | Methods and compositions useful for targeting activated vitronectin receptor alpha(nu)-beta(3) |
| US6521593B1 (en) * | 1999-02-01 | 2003-02-18 | Childrens Hospital Los Angeles | Methods for inhibiting brain tumor growth |
| US6531580B1 (en) * | 1999-06-24 | 2003-03-11 | Ixsys, Inc. | Anti-αvβ3 recombinant human antibodies and nucleic acids encoding same |
| WO2001024827A2 (en) * | 1999-10-06 | 2001-04-12 | Basf Aktiengesellschaft | INHIBITORS OF THE ENDOTHELIN SIGNALLING PATHWAY AND αVβ3 INTEGRIN RECEPTOR ANTAGONISTS FOR COMBINATION THERAPY |
| US7229619B1 (en) | 2000-11-28 | 2007-06-12 | Medimmune, Inc. | Methods of administering/dosing anti-RSV antibodies for prophylaxis and treatment |
| AU2001238079A1 (en) * | 2000-02-09 | 2001-08-20 | Med Immune, Inc. | Antibody gene therapy with adeno-associated viral vectors |
| EP2341074A1 (en) * | 2000-03-01 | 2011-07-06 | MedImmune, LLC | Antibodies binding to the f protein of a respiratory syncytial virus (rsv) |
| US6855493B2 (en) | 2000-11-28 | 2005-02-15 | Medimmune, Inc. | Methods of administering/dosing anti-RSV antibodies for prophylaxis and treatment |
| US7179900B2 (en) | 2000-11-28 | 2007-02-20 | Medimmune, Inc. | Methods of administering/dosing anti-RSV antibodies for prophylaxis and treatment |
| PT1355919E (pt) | 2000-12-12 | 2011-03-02 | Medimmune Llc | Moléculas com semivida longa, composições que as contêm e suas utilizações |
| AU2002306651B2 (en) * | 2001-03-02 | 2007-12-13 | Medimmune, Llc | Methods of preventing or treating inflammatory or autoimmune disorders by administering integrin alphav Beta3 antagonists |
| AU2002316855B2 (en) * | 2001-04-24 | 2008-03-13 | Merck Patent Gmbh | Combination therapy using anti-angiogenic agents and TNFalpha |
| KR20050032507A (ko) * | 2001-10-10 | 2005-04-07 | 파마시아 이탈리아 에스.피.에이. | 스테로이드 화합물을 이용한 골소실의 예방 및 치료 방법 |
| US7365167B2 (en) | 2001-11-26 | 2008-04-29 | Cell Matrix, Inc. | Humanized collagen antibodies and related methods |
| US7390885B2 (en) * | 2001-11-26 | 2008-06-24 | Cell Matrix, Inc. | Humanized collagen antibodies and related methods |
| CA2478239A1 (en) * | 2002-03-04 | 2003-09-18 | Medimmune, Inc. | The prevention or treatment of cancer using integrin alphavbeta3 antagonists in combination with other agents |
| CA2478317A1 (en) * | 2002-03-04 | 2003-09-18 | Medimmune, Inc. | Methods of preventing or treating disorders by administering an integrin .alpha.v.beta.3 antagonist in combination with an hmg-coa reductase inhibitor or a bisphosphonate |
| CA2488441C (en) * | 2002-06-03 | 2015-01-27 | Genentech, Inc. | Synthetic antibody phage libraries |
| US7132100B2 (en) | 2002-06-14 | 2006-11-07 | Medimmune, Inc. | Stabilized liquid anti-RSV antibody formulations |
| CA2512174A1 (en) * | 2003-01-30 | 2004-08-12 | Christian B. Allan | Anti-integrin .alpha..nu..beta.3 antibody formulations and uses thereof |
| WO2004066956A2 (en) * | 2003-01-30 | 2004-08-12 | Medimmune, Inc. | Uses of integrin alphavbeta3 antagonists |
| US20040208869A1 (en) * | 2003-01-30 | 2004-10-21 | Medimmune, Inc. | Uses of anti-integrin alphanubeta3 antibody formulations |
| GB0302699D0 (en) * | 2003-02-06 | 2003-03-12 | Univ Bradford | Immunoglobulin |
| AU2004229501B2 (en) | 2003-04-11 | 2011-08-18 | Medimmune, Llc | Recombinant IL-9 antibodies and uses thereof |
| US7351739B2 (en) | 2004-04-30 | 2008-04-01 | Wellgen, Inc. | Bioactive compounds and methods of uses thereof |
| ATE461708T1 (de) * | 2004-05-07 | 2010-04-15 | Univ North Carolina | Verfahren zur verstärkung oder hemmung des insulinähnlichen wachstumsfaktors-i |
| US8187595B2 (en) * | 2004-05-07 | 2012-05-29 | The University Of North Carolina At Chapel Hill | Monoclonal antibodies for enhancing or inhibiting insulin-like growth factor-I |
| AU2005277567A1 (en) * | 2004-08-16 | 2006-03-02 | Medimmune, Llc | Integrin antagonists with enhanced antibody dependent cell-mediated cytotoxicity activity |
| US20060121042A1 (en) | 2004-10-27 | 2006-06-08 | Medimmune, Inc. | Modulation of antibody specificity by tailoring the affinity to cognate antigens |
| CA2585104A1 (en) | 2004-12-06 | 2006-06-15 | Kirin Beer Kabushiki Kaisha | Human monoclonal antibodies to influenza m2 protein and methods of making and using same |
| CA2611519A1 (en) | 2005-06-17 | 2006-12-28 | Tolerx, Inc. | Ilt3 binding molecules and uses therefor |
| WO2007002543A2 (en) | 2005-06-23 | 2007-01-04 | Medimmune, Inc. | Antibody formulations having optimized aggregation and fragmentation profiles |
| WO2008094176A2 (en) * | 2006-06-19 | 2008-08-07 | Tolerx, Inc. | Ilt3 binding molecules and uses therefor |
| AU2007272970C1 (en) | 2006-07-11 | 2013-01-10 | Roy C. Levitt | Rhinosinusitis prevention and therapy with proinflammatory cytokine inhibitors |
| CA2660519A1 (en) | 2006-08-10 | 2008-02-21 | Roy C. Levitt | Localized therapy of lower airways inflammatory disorders with proinflammatory cytokine inhibitors |
| WO2008048545A2 (en) | 2006-10-16 | 2008-04-24 | Medimmune, Llc. | Molecules with reduced half-lives, compositions and uses thereof |
| US20100197896A1 (en) * | 2007-05-16 | 2010-08-05 | Leung Shui-On | Functional humanization of complementarity determining regions (cdrs) |
| EP1997830A1 (en) | 2007-06-01 | 2008-12-03 | AIMM Therapeutics B.V. | RSV specific binding molecules and means for producing them |
| US8633139B2 (en) | 2007-12-21 | 2014-01-21 | Abbvie Biotherapeutics Inc. | Methods of screening complex protein libraries to identify altered properties |
| NZ589795A (en) | 2008-06-16 | 2013-02-22 | Patrys Ltd | Use of LM-1 antibody which binds to NONO/nmt55 protein to prevent metastasis |
| US20120134984A1 (en) | 2009-06-01 | 2012-05-31 | Olga Lubman | Molecules with extended half-lives and uses thereof |
| US8568726B2 (en) | 2009-10-06 | 2013-10-29 | Medimmune Limited | RSV specific binding molecule |
| AU2013206788B2 (en) | 2011-12-28 | 2017-11-30 | Immunoqure Ag | Method of providing monoclonal auto-antibodies with desired specificity |
| EP2890716A4 (en) | 2012-08-31 | 2016-06-08 | Univ North Carolina | MONOCLONAL ANTIBODIES FOR THE REINFORCEMENT OR INHIBITION OF INSULINARY FACTOR 1 (IGF-1) |
| EP4056591A1 (en) | 2013-07-03 | 2022-09-14 | ImmunoQure AG | Human anti-ifn-alpha antibodies |
| AU2018243670B2 (en) | 2017-03-31 | 2025-05-01 | The Regents Of The University Of California | Compositions and methods for targeting and killing ALPHA-V BETA-3-positive cancer stem cells (CSCs) and treating drug resistant cancers |
| KR102098462B1 (ko) * | 2018-03-14 | 2020-04-08 | 가톨릭대학교 산학협력단 | αvβ3 인테그린 표적 단일 도메인 항체 |
| US20230092787A1 (en) * | 2020-02-17 | 2023-03-23 | University Of Virginia Patent Foundation | Car t cells targeting the integrin alphav beta3 exhibit robust anti-tumor responses against gliomas and other solid tumor malignancies |
Family Cites Families (11)
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| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| IL162181A (en) | 1988-12-28 | 2006-04-10 | Pdl Biopharma Inc | A method of producing humanized immunoglubulin, and polynucleotides encoding the same |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US5264563A (en) | 1990-08-24 | 1993-11-23 | Ixsys Inc. | Process for synthesizing oligonucleotides with random codons |
| US5667988A (en) | 1992-01-27 | 1997-09-16 | The Scripps Research Institute | Methods for producing antibody libraries using universal or randomized immunoglobulin light chains |
| DE69322860T2 (de) * | 1992-04-03 | 1999-07-01 | Genentech, Inc., South San Francisco, Calif. | Antikörper gegen alpha v beta 3 integrin |
| IT1268004B1 (it) * | 1994-02-02 | 1997-02-20 | Giuseppe Lambertini | Dispositivo per il bloccaggio di un pezzo su un piano d'appoggio, quale una tavola di macchina operatrice. |
| US5753230A (en) | 1994-03-18 | 1998-05-19 | The Scripps Research Institute | Methods and compositions useful for inhibition of angiogenesis |
| CA2223885A1 (en) | 1995-06-07 | 1996-12-19 | Centocor, Inc. | Platelet-specific chimeric immunoglobulin and methods of use therefor |
| US6590079B2 (en) | 1997-01-30 | 2003-07-08 | Ixsys, Incorporated | Anti-αvβ3 recombinant human antibodies, nucleic acids encoding same |
| US6531580B1 (en) | 1999-06-24 | 2003-03-11 | Ixsys, Inc. | Anti-αvβ3 recombinant human antibodies and nucleic acids encoding same |
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| JP2001511149A (ja) | 2001-08-07 |
| WO1998033919A3 (en) | 1998-12-17 |
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| AU6139198A (en) | 1998-08-25 |
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| EP0970217A2 (en) | 2000-01-12 |
| US20030208048A1 (en) | 2003-11-06 |
| US6590079B2 (en) | 2003-07-08 |
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