CA2442318A1 - Antibodies against cancer - Google Patents
Antibodies against cancer Download PDFInfo
- Publication number
- CA2442318A1 CA2442318A1 CA002442318A CA2442318A CA2442318A1 CA 2442318 A1 CA2442318 A1 CA 2442318A1 CA 002442318 A CA002442318 A CA 002442318A CA 2442318 A CA2442318 A CA 2442318A CA 2442318 A1 CA2442318 A1 CA 2442318A1
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- protein
- cancer
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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
- C07K16/30—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants from tumour cells
-
- 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
- C07K16/30—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants from tumour cells
- C07K16/3046—Stomach, Intestines
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- A61P35/02—Antineoplastic agents specific for leukemia
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- 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
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Immunology (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Cell Biology (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Pharmacology & Pharmacy (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Oncology (AREA)
- Hematology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicinal Preparation (AREA)
- Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| AUPR3958A AUPR395801A0 (en) | 2001-03-26 | 2001-03-26 | Antibodies against cancer |
| AUPR3958 | 2001-03-26 | ||
| PCT/AU2002/000362 WO2002077033A1 (en) | 2001-03-26 | 2002-03-26 | Antibodies against cancer |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2442318A1 true CA2442318A1 (en) | 2002-10-03 |
Family
ID=3827964
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002442318A Abandoned CA2442318A1 (en) | 2001-03-26 | 2002-03-26 | Antibodies against cancer |
Country Status (9)
| Country | Link |
|---|---|
| US (1) | US7318924B2 (enExample) |
| EP (1) | EP1383801A4 (enExample) |
| JP (2) | JP4854912B2 (enExample) |
| KR (1) | KR100909290B1 (enExample) |
| CN (2) | CN100457781C (enExample) |
| AU (3) | AUPR395801A0 (enExample) |
| CA (1) | CA2442318A1 (enExample) |
| NZ (1) | NZ528624A (enExample) |
| WO (1) | WO2002077033A1 (enExample) |
Families Citing this family (28)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB0020953D0 (en) | 2000-08-24 | 2000-10-11 | Smithkline Beecham Biolog | Vaccine |
| US7582299B2 (en) | 2001-04-26 | 2009-09-01 | Biogen Idec Ma Inc. | Cripto-specific antibodies |
| RS20110024A (sr) | 2001-04-26 | 2011-08-31 | Biogen Idec Ma Inc. | Antitela koja blokiraju cripto i njihova upotreba |
| AU2003301619A1 (en) * | 2002-10-23 | 2004-05-13 | Exelixis, Inc. | MBMs AS MODIFIERS OF BRANCHING MORPHOGENESIS AND METHODS OF USE |
| US7824872B2 (en) | 2003-04-03 | 2010-11-02 | Theravalues Corporation | Pharmaceutical agents |
| US20050163782A1 (en) * | 2003-06-27 | 2005-07-28 | Biogen Idec Ma Inc. | Modified binding molecules comprising connecting peptides |
| AU2004274433B2 (en) * | 2003-09-15 | 2010-08-12 | Research Development Foundation | Cripto antagonism of activin and TGF-beta signaling |
| WO2005037293A1 (en) | 2003-10-16 | 2005-04-28 | Univ Monash | Immunomodulating compositions and uses therefor |
| EP2311881A3 (en) * | 2005-01-05 | 2011-07-27 | Biogen Idec MA Inc. | Cripto binding molecules |
| US7939056B2 (en) * | 2005-11-14 | 2011-05-10 | The Brigham And Women's Hospital, Inc. | Interleukin-10 compositions for the treatment of adenocarcinomas |
| CA2688563A1 (en) * | 2007-06-01 | 2008-12-11 | Biogen Idec Ma Inc. | Cripto binding molecules |
| EP3156069B8 (en) | 2008-06-20 | 2020-10-21 | Duke University | Compositions, methods, and kits for eliciting an immune response |
| KR100973029B1 (ko) * | 2008-10-07 | 2010-08-11 | 박지운 | 알루미늄 합금 가로등 등주 |
| EP2350131B1 (en) * | 2008-11-07 | 2017-06-07 | Research Development Foundation | Compositions and methods for the inhibition of cripto/grp78 complex formation and signaling |
| WO2012105219A1 (ja) * | 2011-01-31 | 2012-08-09 | オリンパス株式会社 | 抗体療法の効果増強剤 |
| KR102023496B1 (ko) | 2011-04-21 | 2019-09-20 | 시애틀 지네틱스, 인크. | 신규 결합제-약물 콘주게이트 (adc) 및 그의 용도 |
| MX380273B (es) | 2013-12-23 | 2025-04-01 | Bayer Pharma AG | Conjugados de farmacos anticuerpo (adcs) con inhibidores de ksp. |
| US11198738B2 (en) * | 2015-04-20 | 2021-12-14 | Minomic International Ltd. | Therapeutic antibodies and uses thereof |
| SG10201908685QA (en) | 2015-06-22 | 2019-10-30 | Bayer Pharma AG | Antibody drug conjugates (adcs) and antibody prodrug conjugates (apdcs) with enzymatically cleavable groups |
| EP3313523A2 (en) | 2015-06-23 | 2018-05-02 | Bayer Pharma Aktiengesellschaft | Targeted conjugates of ksp inhibitors |
| WO2017060322A2 (en) | 2015-10-10 | 2017-04-13 | Bayer Pharma Aktiengesellschaft | Ptefb-inhibitor-adc |
| JP7251981B2 (ja) | 2016-03-24 | 2023-04-04 | バイエル ファーマ アクチエンゲゼルシャフト | 酵素開裂基を有する細胞毒性活性剤のプロドラッグ |
| CA3027445A1 (en) | 2016-06-15 | 2017-12-21 | Bayer Pharma Aktiengesellschaft | Specific antibody-drug-conjugates (adcs) with ksp inhibitors and anti-cd123-antibodies |
| CA3047522A1 (en) | 2016-12-21 | 2018-06-28 | Bayer Pharma Aktiengesellschaft | Specific antibody drug conjugates (adcs) having ksp inhibitors |
| EP3558386A1 (de) | 2016-12-21 | 2019-10-30 | Bayer Aktiengesellschaft | Prodrugs von cytotoxischen wirkstoffen mit enzymatisch spaltbaren gruppen |
| JP7066714B2 (ja) | 2016-12-21 | 2022-05-13 | バイエル・ファルマ・アクティエンゲゼルシャフト | 酵素的に切断可能な基を有する抗体薬物コンジュゲート（ａｄｃ） |
| CN109744199A (zh) * | 2017-11-08 | 2019-05-14 | 南京艾莫瑞生物科技有限公司 | 一种肿瘤细胞异种移植斑马鱼模型、其构建方法及应用 |
| JP6761889B1 (ja) * | 2019-11-11 | 2020-09-30 | 株式会社Ｇｓｐエンタープライズ | 抗ヒトＣｒｉｐｔｏ−１抗体 |
Family Cites Families (14)
| 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 |
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| US5171665A (en) * | 1989-04-17 | 1992-12-15 | Oncogen | Monoclonal antibody to novel antigen associated with human tumors |
| US5256643A (en) * | 1990-05-29 | 1993-10-26 | The Government Of The United States | Human cripto protein |
| US5264557A (en) * | 1991-08-23 | 1993-11-23 | The United States Of America As Represented By The Department Of Health And Human Services | Polypeptide of a human cripto-related gene, CR-3 |
| US5981215A (en) * | 1995-06-06 | 1999-11-09 | Human Genome Sciences, Inc. | Human criptin growth factor |
| ES2312177T3 (es) * | 1996-05-22 | 2009-02-16 | Viventia Biotech Inc. | Fragmentos de union a antigenos que detectan especificamente celulas cancerosas, nucleotidos que codifican los fragmentos y el uso de los mismos para la profilaxis y deteccion de canceres. |
| IL125608A0 (en) * | 1998-07-30 | 1999-03-12 | Yeda Res & Dev | Tumor associated antigen peptides and use of same as anti-tumor vaccines |
| CA2358420C (en) * | 1999-03-11 | 2010-03-16 | Ardenia Investments Ltd. | New compounds for the treatment of cancer |
| US6333410B1 (en) * | 2000-08-18 | 2001-12-25 | Immunogen, Inc. | Process for the preparation and purification of thiol-containing maytansinoids |
| GB0020953D0 (en) * | 2000-08-24 | 2000-10-11 | Smithkline Beecham Biolog | Vaccine |
| AU2001292724B2 (en) * | 2000-09-18 | 2005-05-26 | Biogen Idec Ma Inc. | CRIPTO mutant and uses thereof |
| US7582299B2 (en) * | 2001-04-26 | 2009-09-01 | Biogen Idec Ma Inc. | Cripto-specific antibodies |
| RS20110024A (sr) | 2001-04-26 | 2011-08-31 | Biogen Idec Ma Inc. | Antitela koja blokiraju cripto i njihova upotreba |
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2001
- 2001-03-26 AU AUPR3958A patent/AUPR395801A0/en not_active Abandoned
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2002
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- 2002-03-26 CN CNB028073177A patent/CN100457781C/zh not_active Expired - Fee Related
- 2002-03-26 CA CA002442318A patent/CA2442318A1/en not_active Abandoned
- 2002-03-26 AU AU2002240719A patent/AU2002240719B2/en not_active Ceased
- 2002-03-26 NZ NZ528624A patent/NZ528624A/xx not_active IP Right Cessation
- 2002-03-26 WO PCT/AU2002/000362 patent/WO2002077033A1/en not_active Ceased
- 2002-03-26 CN CNA2008101103851A patent/CN101310770A/zh active Pending
- 2002-03-26 EP EP02706533A patent/EP1383801A4/en not_active Withdrawn
- 2002-03-26 US US10/470,013 patent/US7318924B2/en not_active Expired - Fee Related
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2003
- 2003-09-26 KR KR1020037012528A patent/KR100909290B1/ko not_active Expired - Fee Related
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- 2007-04-11 AU AU2007201587A patent/AU2007201587A1/en not_active Abandoned
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2008
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| KR20040010613A (ko) | 2004-01-31 |
| US7318924B2 (en) | 2008-01-15 |
| WO2002077033A1 (en) | 2002-10-03 |
| AU2007201587A1 (en) | 2007-05-03 |
| US20040176576A1 (en) | 2004-09-09 |
| EP1383801A1 (en) | 2004-01-28 |
| CN101310770A (zh) | 2008-11-26 |
| JP2004534741A (ja) | 2004-11-18 |
| AU2002240719B2 (en) | 2007-01-11 |
| EP1383801A4 (en) | 2005-06-01 |
| AUPR395801A0 (en) | 2001-04-26 |
| JP4854912B2 (ja) | 2012-01-18 |
| CN1639194A (zh) | 2005-07-13 |
| NZ528624A (en) | 2006-03-31 |
| JP2009024014A (ja) | 2009-02-05 |
| KR100909290B1 (ko) | 2009-07-24 |
| CN100457781C (zh) | 2009-02-04 |
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