KR20070009637A - 암 세포 증식을 억제하는 항α5β1 항체의 용도 - Google Patents
암 세포 증식을 억제하는 항α5β1 항체의 용도 Download PDFInfo
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- KR20070009637A KR20070009637A KR1020067021955A KR20067021955A KR20070009637A KR 20070009637 A KR20070009637 A KR 20070009637A KR 1020067021955 A KR1020067021955 A KR 1020067021955A KR 20067021955 A KR20067021955 A KR 20067021955A KR 20070009637 A KR20070009637 A KR 20070009637A
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- cancer
- antibody
- tumor
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- antiα5β1
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- Biomedical Technology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicinal Preparation (AREA)
Applications Claiming Priority (10)
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| US62504904P | 2004-11-03 | 2004-11-03 | |
| US60/625,049 | 2004-11-03 | ||
| US65109805P | 2005-02-07 | 2005-02-07 | |
| US60/651,098 | 2005-02-07 | ||
| US65751405P | 2005-02-28 | 2005-02-28 | |
| US60/657,514 | 2005-02-28 |
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| NO (1) | NO20064794L (enExample) |
| NZ (1) | NZ549893A (enExample) |
| WO (1) | WO2005092073A2 (enExample) |
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| CA3022097C (en) | 2006-03-15 | 2020-10-27 | Alexion Pharmaceuticals, Inc. | Treatment of paroxysmal nocturnal hemoglobinuria patients by an inhibitor of complement |
| KR101454491B1 (ko) * | 2006-03-21 | 2014-10-29 | 제넨테크, 인크. | 알파5베타1 길항제를 포함하는 조합 치료법 |
| WO2007114851A1 (en) * | 2006-04-04 | 2007-10-11 | The Board Of Trustees Of The University Of Illinois | Methods and compositions to induce cell death of invasive tumors |
| CA2652886A1 (en) * | 2006-05-24 | 2007-11-29 | Bayer Schering Pharma Aktiengesellschaft | High affinity human and humanized anti-.alpha.5.beta.1 integrin function blocking antibodies with reduced immunogenicity |
| WO2008061377A1 (en) * | 2006-11-22 | 2008-05-29 | Centre Hospitalier De L'universite De Montreal | Novel receptor for cd40l and uses thereof |
| WO2009018226A2 (en) * | 2007-07-27 | 2009-02-05 | Facet Biotech Corporation | Pharmaceutical combinations comprising a tyrosine kinase inhibitor and an antibody against integrin alpha 1 beta 5 (cd49e) |
| US7973138B2 (en) | 2007-09-26 | 2011-07-05 | Genentech, Inc. | Antibodies |
| NZ587440A (en) | 2008-02-05 | 2013-01-25 | Pfizer | Antibodies specific for human integrin alpha 5 - beta 1 and their uses for treating tumours |
| WO2010072740A2 (en) | 2008-12-23 | 2010-07-01 | Astrazeneca Ab | TARGETED BINDING AGENTS DIRECTED TO α5β1 AND USES THEREOF |
| CN102365297B (zh) * | 2009-03-25 | 2014-10-29 | 霍夫曼-拉罗奇有限公司 | 新型抗-α5β1抗体及其应用 |
| US20110319335A1 (en) | 2010-06-23 | 2011-12-29 | Xiaodong Feng | Combined administration of integrin receptor antagonists for anti-angiogenic therapy |
| IN2014CN03555A (enExample) | 2011-10-25 | 2015-07-03 | Onclave Therapeutics Ltd | |
| US8946159B2 (en) | 2011-12-22 | 2015-02-03 | California Northstate College Of Pharmacy, Llc | Administration of an antagonist of α5β1 for anti-angiogenesis and cancer treatment |
| NO2760138T3 (enExample) | 2012-10-01 | 2018-08-04 | ||
| CA3060581A1 (en) | 2017-05-02 | 2018-11-08 | Merck Sharp & Dohme Corp. | Formulations of anti-lag3 antibodies and co-formulations of anti-lag3 antibodies and anti-pd-1 antibodies |
| JOP20190260A1 (ar) | 2017-05-02 | 2019-10-31 | Merck Sharp & Dohme | صيغ ثابتة لأجسام مضادة لمستقبل الموت المبرمج 1 (pd-1) وطرق استخدامها |
| BR112021008873A8 (pt) | 2018-11-07 | 2023-04-11 | Merck Sharp & Dohme | Formulação |
| WO2025106724A2 (en) * | 2023-11-15 | 2025-05-22 | Morphic Therapeutic, Inc. | USE OF ANTI-α5β1 ANTIBODIES IN THE TREATMENT OF PULMONARY HYPERTENSION AND HEART FAILURE |
| WO2025106725A2 (en) * | 2023-11-15 | 2025-05-22 | Morphic Therapeutic, Inc. | HUMAN ANTI-α5β1 ANTIBODIES AND USES THEREOF |
Family Cites Families (36)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4704366A (en) * | 1984-06-22 | 1987-11-03 | Bio-Rad Laboratories, Inc. | Process for binding IgG to protein A |
| JPS61134325A (ja) * | 1984-12-04 | 1986-06-21 | Teijin Ltd | ハイブリツド抗体遺伝子の発現方法 |
| US5618920A (en) * | 1985-11-01 | 1997-04-08 | Xoma Corporation | Modular assembly of antibody genes, antibodies prepared thereby and use |
| US4946778A (en) * | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| US4801687A (en) * | 1986-10-27 | 1989-01-31 | Bioprobe International, Inc. | Monoclonal antibody purification process using protein A |
| US5530101A (en) * | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| ATE247168T1 (de) * | 1991-03-06 | 2003-08-15 | Merck Patent Gmbh | Humanisierte monoklonale antikörper |
| AU669124B2 (en) * | 1991-09-18 | 1996-05-30 | Kyowa Hakko Kirin Co., Ltd. | Process for producing humanized chimera antibody |
| GB9125979D0 (en) * | 1991-12-06 | 1992-02-05 | Wellcome Found | Antibody |
| EP0627002B1 (en) * | 1992-02-19 | 1998-09-23 | Schering Corporation | Cloning and expression of humanized monoclonal antibodies against human interleukin-4 |
| US5639641A (en) * | 1992-09-09 | 1997-06-17 | Immunogen Inc. | Resurfacing of rodent antibodies |
| AU673865B2 (en) | 1992-10-29 | 1996-11-28 | Australian National University, The | Angiogenesis inhibitory antibodies |
| US5536814A (en) * | 1993-09-27 | 1996-07-16 | La Jolla Cancer Research Foundation | Integrin-binding peptides |
| US5981478A (en) | 1993-11-24 | 1999-11-09 | La Jolla Cancer Research Foundation | Integrin-binding peptides |
| WO1995022618A1 (en) | 1994-02-22 | 1995-08-24 | Dana-Farber Cancer Institute | Nucleic acid delivery system, method of synthesis and uses thereof |
| DE69516351T2 (de) * | 1994-09-21 | 2000-12-07 | Matsushita Electric Industrial Co., Ltd. | Sekundäre Lithium Feststoffbatterie |
| US5705154A (en) * | 1995-03-08 | 1998-01-06 | Schering Corporation | Humanized monoclonal antibodies against human interleukin-4 |
| AU2421797A (en) | 1996-03-15 | 1997-10-01 | Du Pont Pharmaceuticals Company | Spirocycle integrin inhibitors |
| US5922676A (en) * | 1996-09-20 | 1999-07-13 | The Burnham Institute | Methods of inhibiting cancer by using superfibronectin |
| US5846536A (en) | 1996-10-04 | 1998-12-08 | The Regents Of The University Of California | Restoration of normal phenotype in cancer cells |
| EP0896002A4 (en) | 1997-01-29 | 2005-02-02 | Toray Industries | CHIMERIC PROTEINS, THEIR HETERODIMER COMPLEXES AND BLOOD PLATE REPLACEMENT |
| US6171586B1 (en) * | 1997-06-13 | 2001-01-09 | Genentech, Inc. | Antibody formulation |
| WO1999037329A1 (en) * | 1998-01-22 | 1999-07-29 | Astrazeneca Ab | Pharmaceutical formulation comprising an antibody and a citrate buffer |
| US6495319B1 (en) | 1998-04-27 | 2002-12-17 | Sidney Kimmel Cancer Center | Reduced complexity nucleic acid targets and methods of using same |
| PT1075277E (pt) | 1998-05-08 | 2009-05-08 | Univ California | Métodos para detectar e inibir a angiogénese |
| US6852318B1 (en) | 1998-05-08 | 2005-02-08 | The Regents Of The University Of California | Methods for detecting and inhibiting angiogenesis |
| EP1204764A2 (en) | 1999-08-11 | 2002-05-15 | EOS Biotechnology, Inc. | Methods of screening for angiogenesis modulators |
| AU780364B2 (en) | 2000-01-20 | 2005-03-17 | Merck Sharp & Dohme Corp. | Alpha V integrin receptor antagonists |
| EP1254116A4 (en) | 2000-01-24 | 2003-04-23 | Merck & Co Inc | ALPHA V INTEGRIN RECEPTOR ANTAGONISTS |
| US7740841B1 (en) * | 2000-01-28 | 2010-06-22 | Sunnybrook Health Science Center | Therapeutic method for reducing angiogenesis |
| US20040259152A1 (en) * | 2000-02-22 | 2004-12-23 | Richard Murray | Novel methods of diagnosing and screening for modulators of tissue remodeling and treating related diseases |
| CA2438030A1 (en) | 2001-02-14 | 2002-10-10 | Protein Design Labs | Methods of diagnosis of angiogenesis, compositions and methods of screening for angiogenesis modulators |
| AU2003298783B2 (en) | 2002-11-26 | 2010-11-04 | Abbvie Biotherapeutics Inc. | Chimeric and humanized antibodies to alpha5beta1 integrin that modulate angiogenesis |
| US7276589B2 (en) * | 2002-11-26 | 2007-10-02 | Pdl Biopharma, Inc. | Chimeric and humanized antibodies to α5β1 integrin that modulate angiogenesis |
| EP1625165A2 (en) * | 2003-04-03 | 2006-02-15 | Protein Design Labs, Inc. | Inhibitors of integrin alpha5beta1 and their use for the control of tissue granulation |
| CN1816356A (zh) | 2003-05-14 | 2006-08-09 | 免疫原公司 | 药物缀合物组合物 |
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2005
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- 2005-03-24 BR BRPI0509177-2A patent/BRPI0509177A/pt not_active IP Right Cessation
- 2005-03-24 EP EP05744016A patent/EP1755659B1/en not_active Expired - Lifetime
- 2005-03-24 AT AT05744016T patent/ATE531388T1/de active
- 2005-03-24 AU AU2005226736A patent/AU2005226736B2/en not_active Ceased
- 2005-03-24 DK DK05744016.6T patent/DK1755659T3/da active
- 2005-03-24 JP JP2007505204A patent/JP4857259B2/ja not_active Expired - Fee Related
- 2005-03-24 CA CA002560508A patent/CA2560508A1/en not_active Abandoned
- 2005-03-24 ES ES05744016T patent/ES2376556T3/es not_active Expired - Lifetime
- 2005-03-24 NZ NZ549893A patent/NZ549893A/en not_active IP Right Cessation
- 2005-03-24 KR KR1020067021955A patent/KR20070009637A/ko not_active Ceased
- 2005-03-24 US US11/090,331 patent/US7662384B2/en not_active Expired - Fee Related
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2006
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2009
- 2009-12-18 US US12/642,687 patent/US20100291111A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| JP4857259B2 (ja) | 2012-01-18 |
| US20050260210A1 (en) | 2005-11-24 |
| BRPI0509177A (pt) | 2007-09-18 |
| EP1755659A2 (en) | 2007-02-28 |
| JP2007530584A (ja) | 2007-11-01 |
| EP1755659A4 (en) | 2008-08-20 |
| DK1755659T3 (da) | 2012-02-27 |
| ES2376556T3 (es) | 2012-03-14 |
| HK1101348A1 (en) | 2007-10-18 |
| CA2560508A1 (en) | 2005-10-06 |
| US7662384B2 (en) | 2010-02-16 |
| AU2005226736A1 (en) | 2005-10-06 |
| IL178042A (en) | 2011-05-31 |
| WO2005092073A3 (en) | 2006-08-10 |
| US20100291111A1 (en) | 2010-11-18 |
| AU2005226736B2 (en) | 2009-11-26 |
| NZ549893A (en) | 2010-05-28 |
| NO20064794L (no) | 2006-10-23 |
| ATE531388T1 (de) | 2011-11-15 |
| WO2005092073A2 (en) | 2005-10-06 |
| EP1755659B1 (en) | 2011-11-02 |
| IL178042A0 (en) | 2006-12-31 |
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