JP5406027B2 - ＥｐｈＢ３特異的抗体およびその使用 - Google Patents
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- JP5406027B2 JP5406027B2 JP2009523073A JP2009523073A JP5406027B2 JP 5406027 B2 JP5406027 B2 JP 5406027B2 JP 2009523073 A JP2009523073 A JP 2009523073A JP 2009523073 A JP2009523073 A JP 2009523073A JP 5406027 B2 JP5406027 B2 JP 5406027B2
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Classifications
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- C07K—PEPTIDES
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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
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- A—HUMAN NECESSITIES
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- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
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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
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- 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
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
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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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- 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
- C07K16/2866—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against receptors for cytokines, lymphokines, interferons
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
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- 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
- C07K2317/75—Agonist effect on antigen
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- 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
- C07K2317/77—Internalization into the cell
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
Landscapes
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- Investigating Or Analysing Biological Materials (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)
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| US8586716B2 (en) * | 2006-08-04 | 2013-11-19 | Novartis Ag | EPHB3-specific antibody and uses thereof |
| US20110046489A1 (en) * | 2009-08-18 | 2011-02-24 | University Of Calcutta | Systems and methods employing giant stokes shift |
| US9354170B2 (en) | 2011-02-15 | 2016-05-31 | University Of Calcutta | NIR fluorescence of heavy water |
| BR112014015323B1 (pt) | 2011-12-20 | 2022-09-27 | Janssen Biotech, Inc | Anticorpos anti-phf-tau, seu método de produção, polinucleotídeo isolado que codifica uma vh de anticorpo, e vetor |
| SG10202005460RA (en) * | 2015-06-30 | 2020-07-29 | Seattle Genetics Inc | Anti-ntb-a antibodies and related compositions and methods |
| JOP20180021A1 (ar) | 2017-03-16 | 2019-01-30 | Janssen Biotech Inc | الأجسام المضادة لتكتلات خيوط بروتين تاو (tau) الحلزونية المزدوجة واستخداماتها |
| KR102055350B1 (ko) * | 2017-09-28 | 2019-12-13 | 고려대학교 산학협력단 | 대장암의 항암제 내성 진단용 바이오마커 및 이의 용도 |
| TW201946654A (zh) | 2018-03-05 | 2019-12-16 | 比利時商健生藥品公司 | 抗ＰＨＦ－Ｔａｕ抗體及其用途 |
| EP3786174A1 (en) * | 2019-08-27 | 2021-03-03 | Ichnos Sciences SA | Methods for antibody purification |
| JP7704740B2 (ja) | 2019-09-16 | 2025-07-08 | アムジエン・インコーポレーテツド | 薬物送達デバイスの外部滅菌の方法 |
| CN119735674A (zh) * | 2024-12-06 | 2025-04-01 | 合肥综合性国家科学中心大健康研究院 | 抗vmat2的抗体或其抗原结合片段及其组合物和应用 |
Family Cites Families (109)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US30985A (en) | 1860-12-18 | Thomas l | ||
| US3773919A (en) * | 1969-10-23 | 1973-11-20 | Du Pont | Polylactide-drug mixtures |
| US4179337A (en) * | 1973-07-20 | 1979-12-18 | Davis Frank F | Non-immunogenic polypeptides |
| JPS6023084B2 (ja) * | 1979-07-11 | 1985-06-05 | 味の素株式会社 | 代用血液 |
| WO1981001145A1 (en) | 1979-10-18 | 1981-04-30 | Univ Illinois | Hydrolytic enzyme-activatible pro-drugs |
| US4419446A (en) * | 1980-12-31 | 1983-12-06 | The United States Of America As Represented By The Department Of Health And Human Services | Recombinant DNA process utilizing a papilloma virus DNA as a vector |
| US4485045A (en) * | 1981-07-06 | 1984-11-27 | Research Corporation | Synthetic phosphatidyl cholines useful in forming liposomes |
| NZ201705A (en) | 1981-08-31 | 1986-03-14 | Genentech Inc | Recombinant dna method for production of hepatitis b surface antigen in yeast |
| US4640835A (en) * | 1981-10-30 | 1987-02-03 | Nippon Chemiphar Company, Ltd. | Plasminogen activator derivatives |
| JPS5896026A (ja) * | 1981-10-30 | 1983-06-07 | Nippon Chemiphar Co Ltd | 新規ウロキナ−ゼ誘導体およびその製造法ならびにそれを含有する血栓溶解剤 |
| US4609546A (en) * | 1982-06-24 | 1986-09-02 | Japan Chemical Research Co., Ltd. | Long-acting composition |
| US4601978A (en) * | 1982-11-24 | 1986-07-22 | The Regents Of The University Of California | Mammalian metallothionein promoter system |
| US4560655A (en) * | 1982-12-16 | 1985-12-24 | Immunex Corporation | Serum-free cell culture medium and process for making same |
| US4657866A (en) * | 1982-12-21 | 1987-04-14 | Sudhir Kumar | Serum-free, synthetic, completely chemically defined tissue culture media |
| GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US4816567A (en) * | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US4675187A (en) * | 1983-05-16 | 1987-06-23 | Bristol-Myers Company | BBM-1675, a new antibiotic complex |
| US4544545A (en) * | 1983-06-20 | 1985-10-01 | Trustees University Of Massachusetts | Liposomes containing modified cholesterol for organ targeting |
| US4496285A (en) * | 1983-08-30 | 1985-01-29 | Baker Prolift, Inc. | Reciprocating drive and velocity control for long stroke well pumping unit |
| US4767704A (en) * | 1983-10-07 | 1988-08-30 | Columbia University In The City Of New York | Protein-free culture medium |
| US4496689A (en) * | 1983-12-27 | 1985-01-29 | Miles Laboratories, Inc. | Covalently attached complex of alpha-1-proteinase inhibitor with a water soluble polymer |
| US4965199A (en) * | 1984-04-20 | 1990-10-23 | Genentech, Inc. | Preparation of functional human factor VIII in mammalian cells using methotrexate based selection |
| JPS6147500A (ja) | 1984-08-15 | 1986-03-07 | Res Dev Corp Of Japan | キメラモノクロ−ナル抗体及びその製造法 |
| EP0173494A3 (en) | 1984-08-27 | 1987-11-25 | The Board Of Trustees Of The Leland Stanford Junior University | Chimeric receptors by dna splicing and expression |
| GB8422238D0 (en) | 1984-09-03 | 1984-10-10 | Neuberger M S | Chimeric proteins |
| EP0206448B1 (en) * | 1985-06-19 | 1990-11-14 | Ajinomoto Co., Inc. | Hemoglobin combined with a poly(alkylene oxide) |
| US4766106A (en) * | 1985-06-26 | 1988-08-23 | Cetus Corporation | Solubilization of proteins for pharmaceutical compositions using polymer conjugation |
| GB8516415D0 (en) | 1985-06-28 | 1985-07-31 | Celltech Ltd | Culture of animal cells |
| US4676980A (en) * | 1985-09-23 | 1987-06-30 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Target specific cross-linked heteroantibodies |
| US5057313A (en) * | 1986-02-25 | 1991-10-15 | The Center For Molecular Medicine And Immunology | Diagnostic and therapeutic antibody conjugates |
| EP0272253A4 (en) | 1986-03-07 | 1990-02-05 | Massachusetts Inst Technology | METHOD FOR IMPROVING GLYCOPROTE INSTABILITY. |
| US4927762A (en) * | 1986-04-01 | 1990-05-22 | Cell Enterprises, Inc. | Cell culture medium with antioxidant |
| US4791192A (en) * | 1986-06-26 | 1988-12-13 | Takeda Chemical Industries, Ltd. | Chemically modified protein with polyethyleneglycol |
| GB2193625B (en) * | 1986-07-04 | 1990-11-28 | Uni Charm Corp | Disposable diaper |
| US5567610A (en) * | 1986-09-04 | 1996-10-22 | Bioinvent International Ab | Method of producing human monoclonal antibodies and kit therefor |
| FR2612700B1 (fr) | 1987-03-17 | 1989-05-19 | Michaud Norbert | Dispositif pour la commande de l'alimentation d'appareils en energie electrique assurant trois fonctions : marche, marche programmee, arret |
| AU600575B2 (en) * | 1987-03-18 | 1990-08-16 | Sb2, Inc. | Altered antibodies |
| US4975278A (en) * | 1988-02-26 | 1990-12-04 | Bristol-Myers Company | Antibody-enzyme conjugates in combination with prodrugs for the delivery of cytotoxic agents to tumor cells |
| EP0315456B1 (en) | 1987-11-05 | 1994-06-01 | Hybritech Incorporated | Polysaccharide-modified immunoglobulins having reduced immunogenic potential or improved pharmacokinetics |
| US5283187A (en) * | 1987-11-17 | 1994-02-01 | Brown University Research Foundation | Cell culture-containing tubular capsule produced by co-extrusion |
| GB8823869D0 (en) * | 1988-10-12 | 1988-11-16 | Medical Res Council | Production of antibodies |
| US5175384A (en) * | 1988-12-05 | 1992-12-29 | Genpharm International | Transgenic mice depleted in mature t-cells and methods for making transgenic mice |
| 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 |
| FR2646437B1 (fr) | 1989-04-28 | 1991-08-30 | Transgene Sa | Nouvelles sequences d'adn, leur application en tant que sequence codant pour un peptide signal pour la secretion de proteines matures par des levures recombinantes, cassettes d'expression, levures transformees et procede de preparation de proteines correspondant |
| DE3920358A1 (de) | 1989-06-22 | 1991-01-17 | Behringwerke Ag | Bispezifische und oligospezifische, mono- und oligovalente antikoerperkonstrukte, ihre herstellung und verwendung |
| US5013556A (en) * | 1989-10-20 | 1991-05-07 | Liposome Technology, Inc. | Liposomes with enhanced circulation time |
| GB8928874D0 (en) | 1989-12-21 | 1990-02-28 | Celltech Ltd | Humanised antibodies |
| DE69133566T2 (de) | 1990-01-12 | 2007-12-06 | Amgen Fremont Inc. | Bildung von xenogenen Antikörpern |
| GB9001917D0 (en) | 1990-01-27 | 1990-03-28 | Smith & Nephew | Hygienic absorbent products |
| US5229275A (en) * | 1990-04-26 | 1993-07-20 | Akzo N.V. | In-vitro method for producing antigen-specific human monoclonal antibodies |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| GB9014932D0 (en) * | 1990-07-05 | 1990-08-22 | Celltech Ltd | Recombinant dna product and method |
| GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| US5770429A (en) * | 1990-08-29 | 1998-06-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5122469A (en) * | 1990-10-03 | 1992-06-16 | Genentech, Inc. | Method for culturing Chinese hamster ovary cells to improve production of recombinant proteins |
| US5565332A (en) * | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| DE69233204T2 (de) | 1991-12-13 | 2004-07-15 | Xoma Corp., Berkeley | Verfahren und materialien zur herstellung von modifizierten variablen antikörperdomänen und ihre therapeutische verwendung |
| EP0626012B1 (en) * | 1992-02-11 | 2003-07-09 | Cell Genesys, Inc. | Homogenotization of gene-targeting events |
| WO1993019172A1 (en) | 1992-03-24 | 1993-09-30 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| US5573905A (en) * | 1992-03-30 | 1996-11-12 | The Scripps Research Institute | Encoded combinatorial chemical libraries |
| AU4528493A (en) | 1992-06-04 | 1994-01-04 | Regents Of The University Of California, The | In vivo gene therapy with intron-free sequence of interest |
| WO1994002602A1 (en) | 1992-07-24 | 1994-02-03 | Cell Genesys, Inc. | Generation of xenogeneic antibodies |
| ES2091684T3 (es) | 1992-11-13 | 1996-11-01 | Idec Pharma Corp | Aplicacion terapeutica de anticuerpos quimericos y radiomarcados contra el antigeno de diferenciacion restringida de los linfocitos b humanos para el tratamiento del linfoma de las celulas b. |
| US5807549A (en) * | 1993-05-21 | 1998-09-15 | Research Corporation Technologies, Inc. | Lymphocyte chemoattractant factor and uses thereof |
| WO1995015388A1 (en) | 1993-12-03 | 1995-06-08 | Medical Research Council | Recombinant binding proteins and peptides |
| US5443953A (en) * | 1993-12-08 | 1995-08-22 | Immunomedics, Inc. | Preparation and use of immunoconjugates |
| US6054287A (en) * | 1994-05-27 | 2000-04-25 | Methodist Hospital Of Indiana, Inc. | Cell-type-specific methods and devices for the low temperature preservation of the cells of an animal species |
| US5731168A (en) | 1995-03-01 | 1998-03-24 | Genentech, Inc. | Method for making heteromultimeric polypeptides |
| US6130364A (en) | 1995-03-29 | 2000-10-10 | Abgenix, Inc. | Production of antibodies using Cre-mediated site-specific recombination |
| US6096871A (en) | 1995-04-14 | 2000-08-01 | Genentech, Inc. | Polypeptides altered to contain an epitope from the Fc region of an IgG molecule for increased half-life |
| JP4312259B2 (ja) | 1995-04-27 | 2009-08-12 | アムジェン フレモント インク． | 免疫したゼノマウス（ＸｅｎｏＭｏｕｓｅ）に由来するヒト抗体 |
| EP0823941A4 (en) | 1995-04-28 | 2001-09-19 | Abgenix Inc | HUMAN ANTIBODIES DERIVED FROM IMMUNIZED XENO MOUSES |
| US6489145B1 (en) * | 1996-07-09 | 2002-12-03 | Diversa Corporation | Method of DNA shuffling |
| US6537776B1 (en) * | 1999-06-14 | 2003-03-25 | Diversa Corporation | Synthetic ligation reassembly in directed evolution |
| WO1997034631A1 (en) | 1996-03-18 | 1997-09-25 | Board Of Regents, The University Of Texas System | Immunoglobin-like domains with increased half lives |
| GB9712818D0 (en) * | 1996-07-08 | 1997-08-20 | Cambridge Antibody Tech | Labelling and selection of specific binding molecules |
| DE69738539T2 (de) | 1996-12-03 | 2009-03-26 | Amgen Fremont Inc. | Vollkommen humane Antikörper die EGFR binden |
| US6306393B1 (en) * | 1997-03-24 | 2001-10-23 | Immunomedics, Inc. | Immunotherapy of B-cell malignancies using anti-CD22 antibodies |
| US6057098A (en) * | 1997-04-04 | 2000-05-02 | Biosite Diagnostics, Inc. | Polyvalent display libraries |
| US20020032315A1 (en) * | 1997-08-06 | 2002-03-14 | Manuel Baca | Anti-vegf antibodies |
| US6194551B1 (en) * | 1998-04-02 | 2001-02-27 | Genentech, Inc. | Polypeptide variants |
| US20020029391A1 (en) * | 1998-04-15 | 2002-03-07 | Claude Geoffrey Davis | Epitope-driven human antibody production and gene expression profiling |
| GB9809951D0 (en) | 1998-05-08 | 1998-07-08 | Univ Cambridge Tech | Binding molecules |
| US6818749B1 (en) * | 1998-10-31 | 2004-11-16 | The United States Of America As Represented By The Department Of Health And Human Services | Variants of humanized anti carcinoma monoclonal antibody cc49 |
| ATE293989T1 (de) | 1998-11-20 | 2005-05-15 | Genentech Inc | Verwendung von eph-rezeptor-antagonisten und agonisten zur behandlung von vaskulären krankheiten |
| ATE477273T1 (de) * | 1998-12-01 | 2010-08-15 | Facet Biotech Corp | Humanisierte antikoerper gegen gamma-interferon |
| US6737056B1 (en) * | 1999-01-15 | 2004-05-18 | Genentech, Inc. | Polypeptide variants with altered effector function |
| US7560534B2 (en) * | 2000-05-08 | 2009-07-14 | Celldex Research Corporation | Molecular conjugates comprising human monoclonal antibodies to dendritic cells |
| DK1354034T3 (da) * | 2000-11-30 | 2008-03-25 | Medarex Inc | Transgene transchromosomale gnavere til fremstilling af humane antistoffer |
| US7829084B2 (en) * | 2001-01-17 | 2010-11-09 | Trubion Pharmaceuticals, Inc. | Binding constructs and methods for use thereof |
| US7754208B2 (en) * | 2001-01-17 | 2010-07-13 | Trubion Pharmaceuticals, Inc. | Binding domain-immunoglobulin fusion proteins |
| US20030133939A1 (en) * | 2001-01-17 | 2003-07-17 | Genecraft, Inc. | Binding domain-immunoglobulin fusion proteins |
| JP2004532038A (ja) | 2001-05-17 | 2004-10-21 | ディヴァーサ コーポレイション | 新規抗原結合分子の治療、診断、予防、酵素、産業ならびに農業各分野への応用とそのための新規抗原結合分子の作製とスクリーニングの方法 |
| WO2003004057A1 (en) * | 2001-07-03 | 2003-01-16 | The Hospital For Sick Children | Ephrin and eph receptor mediated immune modulation |
| US7074175B2 (en) * | 2001-07-25 | 2006-07-11 | Erik Schroeder Handy | Thermotherapy via targeted delivery of nanoscale magnetic particles |
| US6997863B2 (en) | 2001-07-25 | 2006-02-14 | Triton Biosystems, Inc. | Thermotherapy via targeted delivery of nanoscale magnetic particles |
| JP4213586B2 (ja) * | 2001-09-13 | 2009-01-21 | 株式会社抗体研究所 | ラクダ抗体ライブラリーの作製方法 |
| SI1478667T1 (sl) * | 2002-02-26 | 2010-12-31 | Sigma Tau Ind Farmaceuti | Monoklonski protitelesni anti-äśloveĺ ki tenascin |
| US20040132101A1 (en) * | 2002-09-27 | 2004-07-08 | Xencor | Optimized Fc variants and methods for their generation |
| MXPA04009418A (es) * | 2002-03-29 | 2005-06-08 | Schering Corp | Anticuerpos monoclonales humanos par interleucina-5, y metodos y composiciones que comprenden los mismos. |
| GB0208089D0 (en) * | 2002-04-09 | 2002-05-22 | Oxford Glycosciences Uk Ltd | Protein |
| EP1380644A1 (en) * | 2002-07-08 | 2004-01-14 | Kylix B.V. | The use of specified TCF target genes to identify drugs for the treatment of cancer, in particular colorectal cancer, in which TCF/beta-catenin/WNT signalling plays a central role |
| US20040058392A1 (en) * | 2002-09-17 | 2004-03-25 | Kylix B.V. | Use of novel stem cell markers for isolation of intestinal stem cells, and use of the intestinal stem cells thus obtained for the preparation of a therapeutical composition |
| WO2005031002A2 (en) | 2003-09-22 | 2005-04-07 | Rosetta Inpharmatics Llc | Synthetic lethal screen using rna interference |
| US20060121042A1 (en) * | 2004-10-27 | 2006-06-08 | Medimmune, Inc. | Modulation of antibody specificity by tailoring the affinity to cognate antigens |
| AU2006255536A1 (en) * | 2005-06-03 | 2006-12-14 | Novartis Vaccines And Diagnostics Inc. | Methods of treating, diagnosing or detecting cancer using an EphB3 modulator |
| US8586716B2 (en) * | 2006-08-04 | 2013-11-19 | Novartis Ag | EPHB3-specific antibody and uses thereof |
| KR20140119831A (ko) * | 2006-12-07 | 2014-10-10 | 노파르티스 아게 | Ｅｐｈｂ３에 대한 길항제 항체 |
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- 2007-08-03 RU RU2009107707/10A patent/RU2009107707A/ru unknown
- 2007-08-03 EP EP07840695.6A patent/EP2057193B1/en not_active Not-in-force
- 2007-08-03 EP EP20110173812 patent/EP2420252A1/en not_active Withdrawn
- 2007-08-03 ES ES07840695.6T patent/ES2452067T3/es active Active
- 2007-08-03 CA CA002659820A patent/CA2659820A1/en not_active Abandoned
- 2007-08-03 KR KR1020147004072A patent/KR20140033236A/ko not_active Ceased
- 2007-08-03 WO PCT/US2007/075215 patent/WO2008019326A2/en not_active Ceased
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| EP2420252A1 (en) | 2012-02-22 |
| CA2659820A1 (en) | 2008-02-14 |
| US9006398B2 (en) | 2015-04-14 |
| BRPI0715332A2 (pt) | 2013-10-08 |
| KR20140033236A (ko) | 2014-03-17 |
| KR20090039799A (ko) | 2009-04-22 |
| EP2057193A2 (en) | 2009-05-13 |
| ES2452067T3 (es) | 2014-03-31 |
| JP2013153769A (ja) | 2013-08-15 |
| AU2007281717A1 (en) | 2008-02-14 |
| JP2010500006A (ja) | 2010-01-07 |
| WO2008019326A2 (en) | 2008-02-14 |
| US20090142261A1 (en) | 2009-06-04 |
| MX2009001341A (es) | 2009-05-28 |
| EP2057193B1 (en) | 2013-12-18 |
| US8586716B2 (en) | 2013-11-19 |
| WO2008019326A3 (en) | 2008-05-02 |
| CN101626783A (zh) | 2010-01-13 |
| RU2009107707A (ru) | 2010-09-10 |
| US20140148584A1 (en) | 2014-05-29 |
| KR101437188B1 (ko) | 2014-10-02 |
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