JP2003508028A - 腫瘍治療のための組成物と方法 - Google Patents
腫瘍治療のための組成物と方法Info
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- JP2003508028A JP2003508028A JP2001513995A JP2001513995A JP2003508028A JP 2003508028 A JP2003508028 A JP 2003508028A JP 2001513995 A JP2001513995 A JP 2001513995A JP 2001513995 A JP2001513995 A JP 2001513995A JP 2003508028 A JP2003508028 A JP 2003508028A
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- 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
- C07K16/2896—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against molecules with a "CD"-designation, not provided for elsewhere
-
- 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
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2799/00—Uses of viruses
- C12N2799/02—Uses of viruses as vector
- C12N2799/021—Uses of viruses as vector for the expression of a heterologous nucleic acid
- C12N2799/026—Uses of viruses as vector for the expression of a heterologous nucleic acid where the vector is derived from a baculovirus
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Immunology (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Zoology (AREA)
- Cell Biology (AREA)
- Veterinary Medicine (AREA)
- Toxicology (AREA)
- Public Health (AREA)
- Gastroenterology & Hepatology (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (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)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US14621799P | 1999-07-28 | 1999-07-28 | |
| US60/146,217 | 1999-07-28 | ||
| PCT/US2000/020731 WO2001009189A2 (en) | 1999-07-28 | 2000-07-27 | Compositions and methods for the treatment of tumors |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2011231764A Division JP5897300B2 (ja) | 1999-07-28 | 2011-10-21 | 腫瘍治療のための組成物と方法 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2003508028A true JP2003508028A (ja) | 2003-03-04 |
| JP2003508028A5 JP2003508028A5 (enExample) | 2007-10-04 |
Family
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| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2001513995A Withdrawn JP2003508028A (ja) | 1999-07-28 | 2000-07-27 | 腫瘍治療のための組成物と方法 |
| JP2011231764A Expired - Lifetime JP5897300B2 (ja) | 1999-07-28 | 2011-10-21 | 腫瘍治療のための組成物と方法 |
| JP2014040627A Pending JP2014144959A (ja) | 1999-07-28 | 2014-03-03 | 腫瘍治療のための組成物と方法 |
Family Applications After (2)
| Application Number | Title | Priority Date | Filing Date |
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| JP2011231764A Expired - Lifetime JP5897300B2 (ja) | 1999-07-28 | 2011-10-21 | 腫瘍治療のための組成物と方法 |
| JP2014040627A Pending JP2014144959A (ja) | 1999-07-28 | 2014-03-03 | 腫瘍治療のための組成物と方法 |
Country Status (9)
| Country | Link |
|---|---|
| US (2) | US7226596B2 (enExample) |
| EP (1) | EP1204682B1 (enExample) |
| JP (3) | JP2003508028A (enExample) |
| AT (1) | ATE488529T1 (enExample) |
| AU (1) | AU776600B2 (enExample) |
| CA (1) | CA2378182C (enExample) |
| DE (1) | DE60045247D1 (enExample) |
| ES (1) | ES2355055T3 (enExample) |
| WO (1) | WO2001009189A2 (enExample) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2008525041A (ja) * | 2004-12-22 | 2008-07-17 | ジェネンテック・インコーポレーテッド | 可溶性多膜貫通型タンパク質の産生方法 |
Families Citing this family (19)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE60045247D1 (de) * | 1999-07-28 | 2010-12-30 | Genentech Inc | Zusammensetzungen und verfahren zur behandlung von tumoren |
| WO2003070936A1 (fr) * | 2002-02-20 | 2003-08-28 | Yamanouchi Pharmaceutical Co., Ltd. | Nouveau polypeptide |
| CN1854313B (zh) * | 2002-09-30 | 2010-10-20 | 肿瘤疗法科学股份有限公司 | 非小细胞肺癌的诊断方法 |
| WO2005090991A1 (en) * | 2004-03-24 | 2005-09-29 | Oncotherapy Science, Inc. | Adam8 as tumor marker and therapeutic target for non-small cell lung cancer |
| US20080014594A1 (en) * | 2003-01-31 | 2008-01-17 | Kevin Hestir | Lung-Expressed Polypeptides |
| AU2005304486B2 (en) * | 2004-11-10 | 2011-08-11 | Novartis Vaccines And Diagnostics Inc. | Deamidated interferon-beta |
| FR2879462B1 (fr) * | 2004-12-21 | 2008-12-26 | Sod Conseils Rech Applic | Utilisation de toxine botulique pour une insensibilisation locale prolongee |
| US20060242012A1 (en) * | 2005-04-22 | 2006-10-26 | Sumit Agarwal | Determining or scoring properties to solicit to join ad network using advertiser or aggregated advertiser interest |
| EP2514767A1 (en) * | 2006-12-19 | 2012-10-24 | Ablynx N.V. | Amino acid sequences directed against a metalloproteinase from the ADAM family and polypeptides comprising the same for the treatment of ADAM-related diseases and disorders |
| EP3492488A1 (en) | 2007-08-22 | 2019-06-05 | The Regents of The University of California | Activatable binding polypeptides and methods of identification and use thereof |
| GB2453589A (en) | 2007-10-12 | 2009-04-15 | King S College London | Protease inhibition |
| WO2009070392A1 (en) * | 2007-11-27 | 2009-06-04 | Veridex, Llc | Automated enumeration and characterization of circulating melanoma cells in blood |
| WO2010081173A2 (en) | 2009-01-12 | 2010-07-15 | Cytomx Therapeutics, Llc | Modified antibody compositions, methods of making and using thereof |
| AU2010215761B2 (en) * | 2009-02-23 | 2017-04-06 | Cytomx Therapeutics, Inc | Proproteins and methods of use thereof |
| CA2912542A1 (en) * | 2013-05-13 | 2014-11-20 | Tufts University | Methods and compositions for prognosis, diagnosis and treatment of adam8-expressing cancer |
| TW201613622A (en) * | 2014-10-14 | 2016-04-16 | Bionet Corp | Composition for skincare and pharmaceutical composition and preparation method thereof |
| TW201613621A (en) * | 2014-10-14 | 2016-04-16 | Bionet Corp | Composition for promoting growth of dermal papilla cells, pharmaceutical composition, and preparation method thereof |
| JP2018130113A (ja) * | 2017-02-15 | 2018-08-23 | 国立大学法人 東京大学 | 慢性骨髄性白血病（ｃｍｌ）の検査方法及び検査用キット、チロシンキナーゼ阻害剤（ｔｋｉ）耐性ｃｍｌの単離方法、並びにｃｍｌにおけるｔｋｉ耐性の低減剤及びそのスクリーニング方法 |
| CA3142238A1 (en) * | 2019-05-31 | 2020-12-03 | Trustees Of Tufts College | Anti-adam8 antibodies and uses of the same |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH04187084A (ja) * | 1990-11-22 | 1992-07-03 | Otsuka Pharmaceut Co Ltd | 単球表面に発現する抗原及び該抗原に対するモノクローナル抗体 |
| WO1998051706A1 (en) * | 1997-05-13 | 1998-11-19 | Incyte Pharmaceuticals, Inc. | Tumor-associated antigen |
| WO1998057665A2 (en) * | 1997-03-18 | 1998-12-23 | Oxford Biomedica (Uk) Limited | The use of mononuclear phagocytes in in vivo imaging of hypoxic/ischaemic tissue |
Family Cites Families (24)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| BR9506535A (pt) * | 1994-01-20 | 1997-09-16 | British Biotech Pharm | Inibidores de metaloproteinases |
| GB9608130D0 (en) | 1996-04-19 | 1996-06-26 | Univ Sheffield | Adam proteins and uses thereof |
| BR9806793A (pt) * | 1997-01-22 | 2000-05-16 | Univ Texas | Processos e composições de fator tissular para coagulação e tratamento de tumores. |
| CA2330929A1 (en) * | 1998-06-06 | 1999-12-16 | Genostic Pharma Limited | Probes used for genetic profiling |
| WO2000040749A2 (en) * | 1999-01-06 | 2000-07-13 | Genenews Inc. | Method for the detection of gene transcripts in blood and uses thereof |
| US20010034023A1 (en) * | 1999-04-26 | 2001-10-25 | Stanton Vincent P. | Gene sequence variations with utility in determining the treatment of disease, in genes relating to drug processing |
| DE60045247D1 (de) * | 1999-07-28 | 2010-12-30 | Genentech Inc | Zusammensetzungen und verfahren zur behandlung von tumoren |
| US7074408B2 (en) * | 2000-02-25 | 2006-07-11 | Immunex Corporation | Use of integrin antagonists to inhibit angiogenesis |
| CA2402534C (en) * | 2000-03-24 | 2011-05-24 | Micromet Ag | Mrna amplification |
| US6458552B1 (en) * | 2000-06-06 | 2002-10-01 | Ortho-Mcneil Pharmaceutical, Inc. | Metalloprotease peptide substrates and methods |
| WO2002029107A2 (en) * | 2000-10-02 | 2002-04-11 | Board Of Regents, The University Of Texas System | Method of detection and interpretation of mutations through expression or function tests of haploid genes |
| WO2002048310A2 (en) * | 2000-12-15 | 2002-06-20 | Genetics Institute, Llc | Methods and compositions for diagnosing and treating rheumatoid arthritis |
| US20030087259A1 (en) * | 2001-04-18 | 2003-05-08 | Clancy Brian M. | Methods and compositions for regulating bone and cartilage formation |
| US20030138792A1 (en) * | 2001-05-31 | 2003-07-24 | Millennium Pharmaceuticals, Inc. | Compositions, kits, and methods for identification, assessment, prevention and therapy of cervical cancer |
| WO2003012061A2 (en) * | 2001-08-01 | 2003-02-13 | Coley Pharmaceutical Gmbh | Methods and compositions relating to plasmacytoid dendritic cells |
| US20030148334A1 (en) * | 2001-10-12 | 2003-08-07 | Zairen Sun | Differentially-expressed genes and polypeptides in angiogenesis |
| AU2003213633A1 (en) * | 2002-03-01 | 2003-09-16 | Children's Hospital Medical Center | Treatment for asthma or allergies |
| US20040018522A1 (en) * | 2002-05-09 | 2004-01-29 | Brigham And Women's Hospital, Inc. | Identification of dysregulated genes in patients with multiple sclerosis |
| US20050003390A1 (en) * | 2002-05-17 | 2005-01-06 | Axenovich Sergey A. | Targets for controlling cellular growth and for diagnostic methods |
| JP2004041121A (ja) * | 2002-07-12 | 2004-02-12 | Hitachi Ltd | アレルギー解析方法及びシステム |
| EP2474630B1 (en) * | 2002-12-20 | 2016-04-27 | Celera Corporation | Genetic polymorphisms associated with myocardial infarction, methods of detection and uses thereof |
| US8088737B2 (en) * | 2003-04-04 | 2012-01-03 | Incyte Corporation | Compositions, methods and kits relating to Her-2 cleavage |
| US20050009067A1 (en) * | 2003-05-19 | 2005-01-13 | Craig Logsdon | Expression profile of pancreatic cancer |
| WO2005026325A2 (en) * | 2003-09-10 | 2005-03-24 | Surromed, Inc, | Bivalent targeting of cell surfaces |
-
2000
- 2000-07-27 DE DE60045247T patent/DE60045247D1/de not_active Expired - Lifetime
- 2000-07-27 AT AT00950879T patent/ATE488529T1/de active
- 2000-07-27 JP JP2001513995A patent/JP2003508028A/ja not_active Withdrawn
- 2000-07-27 EP EP00950879A patent/EP1204682B1/en not_active Expired - Lifetime
- 2000-07-27 AU AU63913/00A patent/AU776600B2/en not_active Expired
- 2000-07-27 WO PCT/US2000/020731 patent/WO2001009189A2/en not_active Ceased
- 2000-07-27 CA CA2378182A patent/CA2378182C/en not_active Expired - Lifetime
- 2000-07-27 ES ES00950879T patent/ES2355055T3/es not_active Expired - Lifetime
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2002
- 2002-08-22 US US10/226,844 patent/US7226596B2/en not_active Expired - Lifetime
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2007
- 2007-05-25 US US11/754,196 patent/US20080175842A1/en not_active Abandoned
-
2011
- 2011-10-21 JP JP2011231764A patent/JP5897300B2/ja not_active Expired - Lifetime
-
2014
- 2014-03-03 JP JP2014040627A patent/JP2014144959A/ja active Pending
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH04187084A (ja) * | 1990-11-22 | 1992-07-03 | Otsuka Pharmaceut Co Ltd | 単球表面に発現する抗原及び該抗原に対するモノクローナル抗体 |
| WO1998057665A2 (en) * | 1997-03-18 | 1998-12-23 | Oxford Biomedica (Uk) Limited | The use of mononuclear phagocytes in in vivo imaging of hypoxic/ischaemic tissue |
| WO1998051706A1 (en) * | 1997-05-13 | 1998-11-19 | Incyte Pharmaceuticals, Inc. | Tumor-associated antigen |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2008525041A (ja) * | 2004-12-22 | 2008-07-17 | ジェネンテック・インコーポレーテッド | 可溶性多膜貫通型タンパク質の産生方法 |
| US8323902B2 (en) | 2004-12-22 | 2012-12-04 | Genentech, Inc. | Methods for producing soluble membrane-spanning proteins |
Also Published As
| Publication number | Publication date |
|---|---|
| AU776600B2 (en) | 2004-09-16 |
| DE60045247D1 (de) | 2010-12-30 |
| US20080175842A1 (en) | 2008-07-24 |
| WO2001009189A3 (en) | 2001-06-14 |
| WO2001009189A2 (en) | 2001-02-08 |
| CA2378182C (en) | 2014-09-23 |
| AU6391300A (en) | 2001-02-19 |
| JP2012068254A (ja) | 2012-04-05 |
| US20030113764A1 (en) | 2003-06-19 |
| CA2378182A1 (en) | 2001-02-08 |
| EP1204682B1 (en) | 2010-11-17 |
| US7226596B2 (en) | 2007-06-05 |
| ES2355055T3 (es) | 2011-03-22 |
| JP2014144959A (ja) | 2014-08-14 |
| EP1204682A2 (en) | 2002-05-15 |
| ATE488529T1 (de) | 2010-12-15 |
| JP5897300B2 (ja) | 2016-03-30 |
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