JP2000508522A - アポトーシス誘導分子ｉｉ - Google Patents
アポトーシス誘導分子ｉｉInfo
- Publication number
- JP2000508522A JP2000508522A JP9533436A JP53343697A JP2000508522A JP 2000508522 A JP2000508522 A JP 2000508522A JP 9533436 A JP9533436 A JP 9533436A JP 53343697 A JP53343697 A JP 53343697A JP 2000508522 A JP2000508522 A JP 2000508522A
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- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
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- 241000894007 species Species 0.000 description 1
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- 230000009885 systemic effect Effects 0.000 description 1
- 229910052713 technetium Inorganic materials 0.000 description 1
- GKLVYJBZJHMRIY-UHFFFAOYSA-N technetium atom Chemical compound [Tc] GKLVYJBZJHMRIY-UHFFFAOYSA-N 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 229940126585 therapeutic drug Drugs 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 230000005026 transcription initiation Effects 0.000 description 1
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- 238000012546 transfer Methods 0.000 description 1
- 230000010474 transient expression Effects 0.000 description 1
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- 108091005703 transmembrane proteins Proteins 0.000 description 1
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- 230000032258 transport Effects 0.000 description 1
- 239000013638 trimer Substances 0.000 description 1
- HRXKRNGNAMMEHJ-UHFFFAOYSA-K trisodium citrate Chemical compound [Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O HRXKRNGNAMMEHJ-UHFFFAOYSA-K 0.000 description 1
- 229940038773 trisodium citrate Drugs 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
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Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/70575—NGF/TNF-superfamily, e.g. CD70, CD95L, CD153, CD154
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/02—Drugs for skeletal disorders for joint disorders, e.g. arthritis, arthrosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/08—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease
- A61P19/10—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease for osteoporosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P33/00—Antiparasitic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P33/00—Antiparasitic agents
- A61P33/02—Antiprotozoals, e.g. for leishmaniasis, trichomoniasis, toxoplasmosis
- A61P33/06—Antimalarials
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
-
- 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
- C07K2319/00—Fusion polypeptide
-
- 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)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Veterinary Medicine (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Immunology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Physical Education & Sports Medicine (AREA)
- Rheumatology (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Tropical Medicine & Parasitology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Cell Biology (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Transplantation (AREA)
- Epidemiology (AREA)
- Pain & Pain Management (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US1392396P | 1996-03-22 | 1996-03-22 | |
| US60/013,923 | 1996-03-22 | ||
| PCT/US1996/016966 WO1997034911A1 (en) | 1996-03-22 | 1996-10-31 | Apoptosis inducing molecule ii |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2000508522A true JP2000508522A (ja) | 2000-07-11 |
| JP2000508522A5 JP2000508522A5 (enExample) | 2004-10-28 |
Family
ID=21762534
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP9533436A Withdrawn JP2000508522A (ja) | 1996-03-22 | 1996-10-31 | アポトーシス誘導分子ｉｉ |
Country Status (6)
| Country | Link |
|---|---|
| EP (1) | EP0904278A4 (enExample) |
| JP (1) | JP2000508522A (enExample) |
| KR (2) | KR20030096450A (enExample) |
| CN (2) | CN1107072C (enExample) |
| CA (1) | CA2248868A1 (enExample) |
| WO (1) | WO1997034911A1 (enExample) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2001509373A (ja) * | 1997-07-07 | 2001-07-24 | ラ ホヤ インスティチュート フォー アラジー アンド イムノロジー | 単純ヘルペスウイルス侵入メディエーターのためのリガンドおよびその使用方法 |
Families Citing this family (161)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7597886B2 (en) | 1994-11-07 | 2009-10-06 | Human Genome Sciences, Inc. | Tumor necrosis factor-gamma |
| US7429646B1 (en) | 1995-06-05 | 2008-09-30 | Human Genome Sciences, Inc. | Antibodies to human tumor necrosis factor receptor-like 2 |
| US7888466B2 (en) | 1996-01-11 | 2011-02-15 | Human Genome Sciences, Inc. | Human G-protein chemokine receptor HSATU68 |
| US7357927B2 (en) | 1996-03-12 | 2008-04-15 | Human Genome Sciences, Inc. | Death domain containing receptors |
| US6713061B1 (en) | 1996-03-12 | 2004-03-30 | Human Genome Sciences, Inc. | Death domain containing receptors |
| WO1997033904A1 (en) | 1996-03-12 | 1997-09-18 | Human Genome Sciences, Inc. | Death domain containing receptors |
| US6479254B2 (en) | 1996-03-22 | 2002-11-12 | Human Genome Sciences, Inc. | Apoptosis inducing molecule II |
| US7964190B2 (en) | 1996-03-22 | 2011-06-21 | Human Genome Sciences, Inc. | Methods and compositions for decreasing T-cell activity |
| US6495520B2 (en) | 1996-03-22 | 2002-12-17 | Human Genome Sciences, Inc. | Apoptosis Inducing Molecule II and methods of use |
| US6635743B1 (en) | 1996-03-22 | 2003-10-21 | Human Genome Sciences, Inc. | Apoptosis inducing molecule II and methods of use |
| WO1997046686A2 (en) * | 1996-06-07 | 1997-12-11 | Amgen Inc. | Tumor necrosis factor-related polypeptide |
| CA2260767A1 (en) | 1996-07-19 | 1998-01-29 | Takeda Chemical Industries, Ltd. | Fas ligand-like protein, its production and use |
| US8212004B2 (en) | 1999-03-02 | 2012-07-03 | Human Genome Sciences, Inc. | Neutrokine-alpha fusion proteins |
| US6812327B1 (en) | 1996-10-25 | 2004-11-02 | Human Genome Sciences, Inc. | Neutrokine-alpha polypeptides |
| US6998108B1 (en) | 1997-07-07 | 2006-02-14 | La Jolla Institute For Allergy And Immunology | Antibodies to p30 polypeptides and methods making and using same |
| US7118742B2 (en) | 1997-07-07 | 2006-10-10 | La Jolla Institute For Allergy And Immunology | Ligand for herpes simplex virus entry mediator and methods of use |
| US6346388B1 (en) | 1997-08-13 | 2002-02-12 | Smithkline Beecham Corporation | Method of identifying agonist and antagonists for tumor necrosis related receptors TR1 and TR2 |
| JP2002504333A (ja) * | 1998-02-20 | 2002-02-12 | ヒューマン ジノーム サイエンシーズ， インコーポレイテッド | アポトーシス誘導分子ｉｉおよび使用方法 |
| AU3501700A (en) | 1999-02-26 | 2000-09-14 | Human Genome Sciences, Inc. | Human endokine alpha and methods of use |
| WO2000053223A1 (en) * | 1999-03-11 | 2000-09-14 | Human Genome Sciences, Inc. | Apoptosis inducing molecule ii and methods of use |
| WO2000071151A1 (en) * | 1999-05-21 | 2000-11-30 | Takeda Chemical Industries, Ltd. | Liver function controlling agents |
| WO2001079496A2 (en) * | 2000-03-13 | 2001-10-25 | La Jolla Institute For Allergy And Immunology | Ligand for herpes simplex virus entry mediator and methods of use |
| DE60143231D1 (de) * | 2000-04-12 | 2010-11-18 | Jolla Inst Allergy Immunolog | Ligand des zelleintritt-vermittelnden Proteins von Herpes Simplex und Methoden zu dessen Verwendungen |
| WO2001079444A2 (en) | 2000-04-12 | 2001-10-25 | Human Genome Sciences, Inc | Albumin fusion proteins |
| CA2413160A1 (en) | 2000-06-15 | 2001-12-20 | Human Genome Sciences, Inc. | Human tumor necrosis factor delta and epsilon |
| US7879328B2 (en) | 2000-06-16 | 2011-02-01 | Human Genome Sciences, Inc. | Antibodies that immunospecifically bind to B lymphocyte stimulator |
| ATE494304T1 (de) | 2000-06-16 | 2011-01-15 | Human Genome Sciences Inc | Immunspezifisch bindende antikörper gegen blys |
| US20030091565A1 (en) | 2000-08-18 | 2003-05-15 | Beltzer James P. | Binding polypeptides and methods based thereon |
| EP2027874B1 (en) | 2000-11-28 | 2013-10-16 | Medimmune, Inc. | Methods of administering/dosing anti-rsv antibodies for prophylaxis and treatment |
| AU2002248184C1 (en) | 2000-12-12 | 2018-01-04 | Board Of Regents, The University Of Texas System | Molecules with extended half-lives, compositions and uses thereof |
| WO2002066049A1 (fr) * | 2001-02-23 | 2002-08-29 | Takeda Chemical Industries, Ltd. | Agents pour changement plasmique |
| EP1364653A4 (en) * | 2001-02-23 | 2005-01-26 | Takeda Pharmaceutical | CASOASE-3 INHIBITORS |
| WO2002083704A1 (en) | 2001-04-13 | 2002-10-24 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| ES2437992T3 (es) | 2001-05-25 | 2014-01-15 | Human Genome Sciences, Inc. | Anticuerpos que se unen inmunoespecíficamente a los receptores de TRAIL |
| EP2277888A3 (en) | 2001-12-21 | 2011-04-27 | Human Genome Sciences, Inc. | Fusion proteins of albumin and erythropoietin |
| CA2481747A1 (en) | 2002-04-12 | 2003-10-23 | Medimmune, Inc. | Recombinant anti-interleukin-9 antibodies |
| US7132100B2 (en) | 2002-06-14 | 2006-11-07 | Medimmune, Inc. | Stabilized liquid anti-RSV antibody formulations |
| US7425618B2 (en) | 2002-06-14 | 2008-09-16 | Medimmune, Inc. | Stabilized anti-respiratory syncytial virus (RSV) antibody formulations |
| AU2003262650B2 (en) | 2002-08-14 | 2009-10-29 | Macrogenics, Inc. | FcgammaRIIB-specific antibodies and methods of use thereof |
| DE60336406D1 (de) | 2002-10-16 | 2011-04-28 | Purdue Pharma Lp | Antikörper, die an zellassoziiertes ca 125/0722p binden, und verfahren zu deren anwendung |
| JP2006524039A (ja) | 2003-01-09 | 2006-10-26 | マクロジェニクス，インコーポレーテッド | 変異型Ｆｃ領域を含む抗体の同定および作製ならびにその利用法 |
| EP1585815A4 (en) | 2003-01-21 | 2006-02-22 | Bristol Myers Squibb Co | A NEW ACYL-COENZYME A, MONOCLYLGLYCERIN ACYLTRANSFERASE-3 (MGAT3), CODING POLYNUCLEOTIDE, AND USES THEREOF |
| JP4764818B2 (ja) | 2003-04-11 | 2011-09-07 | メディミューン，エルエルシー | 組換えｉｌ−９抗体およびその使用 |
| CA2525929A1 (en) | 2003-05-13 | 2004-11-25 | Chiron Corporation | Methods of modulating metastasis and skeletal related events resulting from metastases |
| WO2005042743A2 (en) | 2003-08-18 | 2005-05-12 | Medimmune, Inc. | Humanization of antibodies |
| HRP20120376T1 (hr) | 2003-12-23 | 2012-05-31 | Genentech | Nova protutijela protiv il-13 i njihove upotrebe |
| PL1729795T3 (pl) | 2004-02-09 | 2016-08-31 | Human Genome Sciences Inc | Białka fuzyjne albuminy |
| AU2005249360B2 (en) | 2004-04-12 | 2011-07-21 | Medimmune, Llc | Anti-IL-9 antibody formulations and uses thereof |
| AU2005286770A1 (en) | 2004-09-21 | 2006-03-30 | Medimmune, Llc | Antibodies against and methods for producing vaccines for respiratory syncytial virus |
| EP1809326A4 (en) | 2004-10-27 | 2009-11-04 | Medimmune Inc | MODULATION OF ANTIBODY SPECIFICITY BY MEASURING ADAPTATION OF ITS AFFINITY TO AN APPARENT ANTIGEN |
| WO2006102095A2 (en) | 2005-03-18 | 2006-09-28 | Medimmune, Inc. | Framework-shuffling of antibodies |
| ES2707152T3 (es) | 2005-04-15 | 2019-04-02 | Macrogenics Inc | Diacuerpos covalentes y usos de los mismos |
| WO2012018687A1 (en) | 2010-08-02 | 2012-02-09 | Macrogenics, Inc. | Covalent diabodies and uses thereof |
| JP2008546805A (ja) | 2005-06-23 | 2008-12-25 | メディミューン，エルエルシー | 最適な凝集および断片化プロフィールを有する抗体製剤 |
| SI1919503T1 (sl) | 2005-08-10 | 2015-02-27 | Macrogenics, Inc. | Identifikacija in inĺ˝eniring protiteles z variantnimi fc regijami in postopki za njih uporabo |
| NZ597082A (en) | 2005-10-13 | 2013-11-29 | Human Genome Sciences Inc | Methods and Compositions for Use in Treatment of Patients with Autoantibody Positive Diseases |
| US9168286B2 (en) | 2005-10-13 | 2015-10-27 | Human Genome Sciences, Inc. | Methods and compositions for use in treatment of patients with autoantibody positive disease |
| KR20130137716A (ko) | 2005-11-04 | 2013-12-17 | 제넨테크, 인크. | 안질환 치료를 위한 보체 경로 억제제의 용도 |
| US8211649B2 (en) | 2006-03-31 | 2012-07-03 | Human Genome Sciences, Inc. | Methods of diagnosing and prognosing hodgkin's lymphoma |
| AU2007260687B2 (en) | 2006-06-14 | 2013-12-12 | Provention Bio, Inc. | Methods for the treatment of autoimmune disorders using monoclonal antibodies with reduced toxicity |
| SI2029173T1 (sl) | 2006-06-26 | 2016-12-30 | Macrogenics, Inc. | Protitelesa, specifična za Fc RIIB, in postopki za njihovo uporabo |
| US7572618B2 (en) | 2006-06-30 | 2009-08-11 | Bristol-Myers Squibb Company | Polynucleotides encoding novel PCSK9 variants |
| EP2054437A2 (en) | 2006-08-07 | 2009-05-06 | Teva Biopharmaceuticals USA, Inc. | Albumin-insulin fusion proteins |
| SG170032A1 (en) | 2006-08-28 | 2011-04-29 | Kyowa Hakko Kirin Co Ltd | Antagonistic human light-specific human monoclonal antibodies |
| EP2407548A1 (en) | 2006-10-16 | 2012-01-18 | MedImmune, LLC | Molecules with reduced half-lives, compositions and uses thereof |
| EP2117571B1 (en) | 2006-12-08 | 2017-03-08 | Monopar Therapeutics Inc. | Urokinase-type plasminogen activator receptor epitope |
| AU2007333805B2 (en) | 2006-12-18 | 2013-07-25 | Genentech, Inc. | Antagonist anti-Notch3 antibodies and their use in the prevention and treatment of Notch3-related diseases |
| JP5466635B2 (ja) | 2007-03-30 | 2014-04-09 | メディミューン，エルエルシー | 脱アミド化プロフィールが低減した抗体 |
| CA2722754A1 (en) | 2007-04-27 | 2009-01-29 | The University Of Toledo | Modified plasminogen activator inhibitor type-1 molecule and methods based thereon |
| SG194368A1 (en) | 2007-05-04 | 2013-11-29 | Technophage Investigacao E Desenvolvimento Em Biotecnologia Sa | Engineered rabbit antibody variable domains and uses thereof |
| KR101599735B1 (ko) | 2007-06-21 | 2016-03-07 | 마크로제닉스, 인크. | 공유결합형 디아바디 및 이것의 사용 |
| KR20100058509A (ko) | 2007-07-31 | 2010-06-03 | 메디뮨 엘엘씨 | 다중특이적 에피토프 결합 단백질 및 이의 용도 |
| CN101842115B (zh) | 2007-08-29 | 2014-07-30 | 塞诺菲-安万特股份有限公司 | 人源化的抗-cxcr5抗体、其衍生物及它们的应用 |
| EP2050764A1 (en) | 2007-10-15 | 2009-04-22 | sanofi-aventis | Novel polyvalent bispecific antibody format and uses thereof |
| CA2710680C (en) | 2007-12-26 | 2018-10-16 | Vaccinex, Inc. | Anti-c35 antibody combination therapies and methods |
| JP2011509675A (ja) | 2008-01-18 | 2011-03-31 | メディミューン，エルエルシー | 部位特異的コンジュゲーションのためのシステイン操作抗体 |
| US20110020368A1 (en) | 2008-03-25 | 2011-01-27 | Nancy Hynes | Treating cancer by down-regulating frizzled-4 and/or frizzled-1 |
| KR101432474B1 (ko) | 2008-09-07 | 2014-08-21 | 글라이코넥스 인코포레이티드 | 항-연장된 ⅰ형 글라이코스핑고지질 항체, 이의 유도체 및 용도 |
| US8642280B2 (en) | 2008-11-07 | 2014-02-04 | Novartis Forschungsstiftung Zweigniederlassung Friedrich Miescher Institute For Biomedical Research | Teneurin and cancer |
| EP3482769B1 (en) | 2008-12-19 | 2024-05-29 | MacroGenics, Inc. | Covalent diabodies and uses thereof |
| WO2010087927A2 (en) | 2009-02-02 | 2010-08-05 | Medimmune, Llc | Antibodies against and methods for producing vaccines for respiratory syncytial virus |
| EP2396035A4 (en) | 2009-02-12 | 2012-09-12 | Human Genome Sciences Inc | USE OF ANTAGONISTS OF PROTEIN STIMULATING LYMPHOCYTES B TO PROMOTE GRAFT TOLERANCE |
| US20110311521A1 (en) | 2009-03-06 | 2011-12-22 | Pico Caroni | Novel therapy for anxiety |
| WO2010120511A2 (en) | 2009-03-31 | 2010-10-21 | Altair Therapeutics, Inc. | Method of treating respiratory disorders |
| EP2241323A1 (en) | 2009-04-14 | 2010-10-20 | Novartis Forschungsstiftung, Zweigniederlassung Friedrich Miescher Institute For Biomedical Research | Tenascin-W and brain cancers |
| BRPI1015234A2 (pt) | 2009-06-22 | 2018-02-20 | Medimmune Llc | regiões fc projetadas para conjugação sítio específica. |
| SMT201700293T1 (it) | 2009-07-20 | 2017-07-18 | Bristol Myers Squibb Co | Combinazione di un anticorpo anti-ctla-4 con etoposide per il trattamento sinergico di malattie proliferative |
| EP2292266A1 (en) | 2009-08-27 | 2011-03-09 | Novartis Forschungsstiftung, Zweigniederlassung | Treating cancer by modulating copine III |
| WO2011036118A1 (en) | 2009-09-22 | 2011-03-31 | Novartis Forschungsstiftung, Zweigniederlassung Friedrich Miescher Institute For Biomedical Research | Treating cancer by modulating mex-3 |
| PT2486141T (pt) | 2009-10-07 | 2018-05-09 | Macrogenics Inc | Polipéptidos contendo uma região fc que apresenta uma função efectora melhorada, devido a modificações do grau de fucosilação, e métodos para a sua utilização |
| WO2011045352A2 (en) | 2009-10-15 | 2011-04-21 | Novartis Forschungsstiftung | Spleen tyrosine kinase and brain cancers |
| US20120213801A1 (en) | 2009-10-30 | 2012-08-23 | Ekaterina Gresko | Phosphorylated Twist1 and cancer |
| US20130004519A1 (en) | 2010-03-05 | 2013-01-03 | Ruth Chiquet-Ehrismann | Smoci, tenascin-c and brain cancers |
| EP2561076A1 (en) | 2010-04-19 | 2013-02-27 | Novartis Forschungsstiftung, Zweigniederlassung Friedrich Miescher Institute For Biomedical Research | Modulating xrn1 |
| US20130089538A1 (en) | 2010-06-10 | 2013-04-11 | Novartis Forschungsstiftung, Zweigniederlassung Friedrich Miescher Institute forBiomedical Researh | Treating cancer by modulating mammalian sterile 20-like kinase 3 |
| WO2012019061A2 (en) | 2010-08-05 | 2012-02-09 | Stem Centrx, Inc. | Novel effectors and methods of use |
| AU2011293127B2 (en) | 2010-08-27 | 2016-05-12 | Abbvie Stemcentrx Llc | Notum protein modulators and methods of use |
| AU2011295715B9 (en) | 2010-09-03 | 2017-02-23 | Abbvie Stemcentrx Llc | Novel modulators and methods of use |
| US20130171159A1 (en) | 2010-09-10 | 2013-07-04 | Brian Arthur Hemmings | Phosphorylated twist1 and metastasis |
| AU2011325833C1 (en) | 2010-11-05 | 2017-07-13 | Zymeworks Bc Inc. | Stable heterodimeric antibody design with mutations in the Fc domain |
| WO2012065937A1 (en) | 2010-11-15 | 2012-05-24 | Novartis Forschungsstiftung, Zweigniederlassung, Friedrich Miescher Institute For Biomedical Research | Anti-fungal agents |
| RU2592672C9 (ru) | 2010-12-08 | 2016-11-27 | СтемСентРкс, Инк. | Новые модуляторы и способы их применения |
| US20120189633A1 (en) | 2011-01-26 | 2012-07-26 | Kolltan Pharmaceuticals, Inc. | Anti-kit antibodies and uses thereof |
| SA112330278B1 (ar) | 2011-02-18 | 2015-10-09 | ستيم سينتركس، انك. | مواد ضابطة جديدة وطرق للاستخدام |
| AR085911A1 (es) | 2011-03-16 | 2013-11-06 | Sanofi Sa | Dosis terapeutica segura de una proteina similar a un anticuerpo con region v dual |
| CN104080804B (zh) | 2011-05-21 | 2017-06-09 | 宏观基因有限公司 | 去免疫化的血清结合结构域及其延长血清半衰期的用途 |
| EP2717911A1 (en) | 2011-06-06 | 2014-04-16 | Novartis Forschungsstiftung, Zweigniederlassung | Protein tyrosine phosphatase, non-receptor type 11 (ptpn11) and triple-negative breast cancer |
| US9561274B2 (en) | 2011-06-07 | 2017-02-07 | University Of Hawaii | Treatment and prevention of cancer with HMGB1 antagonists |
| US9244074B2 (en) | 2011-06-07 | 2016-01-26 | University Of Hawaii | Biomarker of asbestos exposure and mesothelioma |
| US20130058947A1 (en) | 2011-09-02 | 2013-03-07 | Stem Centrx, Inc | Novel Modulators and Methods of Use |
| EP2758422A1 (en) | 2011-09-23 | 2014-07-30 | Technophage, Investigação E Desenvolvimento Em Biotecnologia, SA | Modified albumin-binding domains and uses thereof to improve pharmacokinetics |
| PL2773671T3 (pl) | 2011-11-04 | 2022-01-24 | Zymeworks Inc. | Projekt stabilnego przeciwciała heterodimerycznego z mutacjami w domenie fc |
| US20140314787A1 (en) | 2011-11-08 | 2014-10-23 | Novartis Forschungsstiftung, Zweigniederlassung, Friedrich Miescher Institute | Treatment for neurodegenerative diseases |
| EP2776838A1 (en) | 2011-11-08 | 2014-09-17 | Novartis Forschungsstiftung, Zweigniederlassung Friedrich Miescher Institute For Biomedical Research | Early diagnostic of neurodegenerative diseases |
| JP2015502397A (ja) | 2011-12-23 | 2015-01-22 | ファイザー・インク | 部位特異的コンジュゲーションのための操作された抗体定常領域、ならびにそのための方法および使用 |
| US20140363448A1 (en) | 2012-01-02 | 2014-12-11 | Novartis Ag | Cdcp1 and breast cancer |
| HUE037021T2 (hu) | 2012-02-24 | 2018-08-28 | Abbvie Stemcentrx Llc | DLL3- modulátorok és eljárások alkalmazásukra |
| US9592289B2 (en) | 2012-03-26 | 2017-03-14 | Sanofi | Stable IgG4 based binding agent formulations |
| EP2831112A1 (en) | 2012-03-29 | 2015-02-04 | Friedrich Miescher Institute for Biomedical Research | Inhibition of interleukin- 8 and/or its receptor cxcrl in the treatment her2/her3 -overexpressing breast cancer |
| EP2866831A1 (en) | 2012-06-29 | 2015-05-06 | Novartis Forschungsstiftung, Zweigniederlassung Friedrich Miescher Institute For Biomedical Research | Treating diseases by modulating a specific isoform of mkl1 |
| WO2014006114A1 (en) | 2012-07-05 | 2014-01-09 | Novartis Forschungsstiftung, Zweigniederlassung Friedrich Miescher Institute For Biomedical Research | New treatment for neurodegenerative diseases |
| US20150224190A1 (en) | 2012-07-06 | 2015-08-13 | Mohamed Bentires-Alj | Combination of a phosphoinositide 3-kinase inhibitor and an inhibitor of the IL-8/CXCR interaction |
| DK3381943T3 (da) | 2012-07-25 | 2022-05-16 | Celldex Therapeutics Inc | Anti-kit-antistoffer og anvendelser deraf |
| CA2887129A1 (en) | 2012-10-09 | 2014-04-17 | Igenica, Inc. | Anti-c16orf54 antibodies and methods of use thereof |
| CA3206122A1 (en) | 2012-11-28 | 2014-06-05 | Zymeworks Bc Inc. | Engineered immunoglobulin heavy chain-light chain pairs and uses thereof |
| ME03394B (me) | 2013-02-22 | 2020-01-20 | Medimmune Ltd | Antidllз-antitelo-pbd konjugati i nihovа upotreba |
| US10100123B2 (en) | 2013-06-06 | 2018-10-16 | Pierre Fabre Medicament | Anti-C10orf54 antibodies and uses thereof |
| US20160178610A1 (en) | 2013-08-07 | 2016-06-23 | Friedrich Miescher Institute For Biomedical Research | New screening method for the treatment Friedreich's ataxia |
| KR20160044042A (ko) | 2013-08-28 | 2016-04-22 | 스템센트알엑스 인코포레이티드 | 부위-특이적 항체 접합 방법 및 조성물 |
| BR112016004245A2 (pt) | 2013-08-28 | 2017-10-17 | Stemcentrx Inc | moduladores de sez6 e métodos de uso |
| LT3097122T (lt) | 2014-01-24 | 2020-07-27 | Ngm Biopharmaceuticals, Inc. | Antikūnai, surišantys beta kloto domeną 2, ir jų panaudojimo būdai |
| EA201691683A1 (ru) | 2014-02-21 | 2017-04-28 | ЭББВИ СТЕМСЕНТРКС ЭлЭлСи | Антитела против dll3 и конъюгаты антитело-лекарственное средство для применения при меланоме |
| GB201403775D0 (en) | 2014-03-04 | 2014-04-16 | Kymab Ltd | Antibodies, uses & methods |
| GB201406767D0 (en) | 2014-04-15 | 2014-05-28 | Cancer Rec Tech Ltd | Humanized anti-Tn-MUC1 antibodies anf their conjugates |
| WO2015175375A1 (en) | 2014-05-13 | 2015-11-19 | Short Jay M | Conditionally active biological proteins |
| WO2015175874A2 (en) | 2014-05-16 | 2015-11-19 | Medimmune, Llc | Molecules with altered neonate fc receptor binding having enhanced therapeutic and diagnostic properties |
| AU2015265457B2 (en) | 2014-05-28 | 2021-02-18 | Zymeworks Bc Inc. | Modified antigen binding polypeptide constructs and uses thereof |
| EP3154579A1 (en) | 2014-06-13 | 2017-04-19 | Friedrich Miescher Institute for Biomedical Research | New treatment against influenza virus |
| WO2015198202A1 (en) | 2014-06-23 | 2015-12-30 | Friedrich Miescher Institute For Biomedical Research | Methods for triggering de novo formation of heterochromatin and or epigenetic silencing with small rnas |
| WO2016001830A1 (en) | 2014-07-01 | 2016-01-07 | Friedrich Miescher Institute For Biomedical Research | Combination of a brafv600e inhibitor and mertk inhibitor to treat melanoma |
| WO2016046768A1 (en) | 2014-09-24 | 2016-03-31 | Friedrich Miescher Institute For Biomedical Research | Lats and breast cancer |
| CN114230664B (zh) | 2014-12-11 | 2025-01-03 | 皮埃尔法布雷医药公司 | 抗c10orf54抗体及其用途 |
| EP3262217A4 (en) | 2015-02-24 | 2018-07-18 | BioAtla LLC | Conditionally active biological proteins |
| DE112016001013T5 (de) | 2015-03-03 | 2017-12-21 | Kymab Limited | Antikörper, verwendungen und verfahren |
| GB201506389D0 (en) | 2015-04-15 | 2015-05-27 | Berkel Patricius H C Van And Howard Philip W | Site-specific antibody-drug conjugates |
| GB201506402D0 (en) | 2015-04-15 | 2015-05-27 | Berkel Patricius H C Van And Howard Philip W | Site-specific antibody-drug conjugates |
| KR20180069839A (ko) | 2015-10-08 | 2018-06-25 | 자임워크스 인코포레이티드 | 카파 및 람다 경사슬을 포함하는 항원-결합 폴리펩티드 구조체 및 이의 용도 |
| EP3368566A1 (en) | 2015-10-28 | 2018-09-05 | Friedrich Miescher Institute for Biomedical Research | Tenascin-w and biliary tract cancers |
| KR102803158B1 (ko) | 2015-12-02 | 2025-05-08 | 주식회사 에스티큐브앤컴퍼니 | Btn1a1에 면역특이적으로 결합하는 항체와 분자 및 그의 치료 용도 |
| JP7227007B2 (ja) | 2015-12-02 | 2023-02-21 | ストサイエンシス， インコーポレイテッド | グリコシル化ｂｔｌａ（ｂ－及びｔ－リンパ球減弱因子）に特異的な抗体 |
| EP3534947A1 (en) | 2016-11-03 | 2019-09-11 | Kymab Limited | Antibodies, combinations comprising antibodies, biomarkers, uses & methods |
| AU2018277838C1 (en) | 2017-05-31 | 2025-08-07 | Stcube & Co., Inc. | Antibodies and molecules that immunospecifically bind to BTN1A1 and the therapeutic uses thereof |
| WO2018222685A1 (en) | 2017-05-31 | 2018-12-06 | Stcube & Co., Inc. | Methods of treating cancer using antibodies and molecules that immunospecifically bind to btn1a1 |
| WO2018226671A1 (en) | 2017-06-06 | 2018-12-13 | Stcube & Co., Inc. | Methods of treating cancer using antibodies and molecules that bind to btn1a1 or btn1a1-ligands |
| CN110831978A (zh) | 2017-06-30 | 2020-02-21 | 酵活有限公司 | 稳定的嵌合fab |
| EP3717069A1 (en) | 2017-11-27 | 2020-10-07 | Purdue Pharma L.P. | Humanized antibodies targeting human tissue factor |
| WO2020016459A1 (en) | 2018-07-20 | 2020-01-23 | Pierre Fabre Medicament | Receptor for vista |
| CN113874392B (zh) | 2019-03-28 | 2025-10-21 | 丹尼斯科美国公司 | 工程化抗体 |
| US11827671B2 (en) | 2019-05-24 | 2023-11-28 | Sanofi | Methods for treating systemic sclerosis |
| US20230203191A1 (en) | 2020-03-30 | 2023-06-29 | Danisco Us Inc | Engineered antibodies |
| WO2024015953A1 (en) | 2022-07-15 | 2024-01-18 | Danisco Us Inc. | Methods for producing monoclonal antibodies |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA2260767A1 (en) * | 1996-07-19 | 1998-01-29 | Takeda Chemical Industries, Ltd. | Fas ligand-like protein, its production and use |
| US6346388B1 (en) * | 1997-08-13 | 2002-02-12 | Smithkline Beecham Corporation | Method of identifying agonist and antagonists for tumor necrosis related receptors TR1 and TR2 |
| WO1999011662A1 (en) * | 1997-09-05 | 1999-03-11 | Millennium Biotherapeutics, Inc. | Novel molecules of the tnfr-ligand-related protein family and uses thereof |
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1996
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- 1996-10-31 CN CN96180284A patent/CN1107072C/zh not_active Expired - Fee Related
- 1996-10-31 EP EP96941944A patent/EP0904278A4/en not_active Ceased
- 1996-10-31 CA CA002248868A patent/CA2248868A1/en not_active Abandoned
- 1996-10-31 JP JP9533436A patent/JP2000508522A/ja not_active Withdrawn
- 1996-10-31 KR KR10-1998-0707496A patent/KR100497017B1/ko not_active Expired - Fee Related
- 1996-10-31 WO PCT/US1996/016966 patent/WO1997034911A1/en not_active Ceased
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2002
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2001509373A (ja) * | 1997-07-07 | 2001-07-24 | ラ ホヤ インスティチュート フォー アラジー アンド イムノロジー | 単純ヘルペスウイルス侵入メディエーターのためのリガンドおよびその使用方法 |
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| CN1428426A (zh) | 2003-07-09 |
| CA2248868A1 (en) | 1997-09-25 |
| CN1107072C (zh) | 2003-04-30 |
| WO1997034911A1 (en) | 1997-09-25 |
| EP0904278A4 (en) | 1999-09-15 |
| EP0904278A1 (en) | 1999-03-31 |
| KR100497017B1 (ko) | 2005-11-29 |
| KR20000064745A (ko) | 2000-11-06 |
| KR20030096450A (ko) | 2003-12-31 |
| CN1216994A (zh) | 1999-05-19 |
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