NO321707B1 - Isolert DNA som koder for et TRAIL-polypeptid og et opploselig TRAIL-polypeptid, ekspresjonsvektor, fremgangsmate for fremstilling av et TRAIL-polypeptid, isolert DNA som koder for et fusjonsprotein, fremgangsmate for fremstilling av en TRAIL-oligomer, antistoff som binder et TRAIL-polypeptid, renset TRAIL-polypeptid og opploselig TRAIL-polypeptid, oligomer, farmasoytisk preparat, farmasoytisk preparat for bruk som et medikament, farmasoytisk preparat for anvendelse ved indusering av apoptose hos malceller samt anvendelse av et TRAIL-polypeptid ved fremstilling av et medikament. - Google Patents
Isolert DNA som koder for et TRAIL-polypeptid og et opploselig TRAIL-polypeptid, ekspresjonsvektor, fremgangsmate for fremstilling av et TRAIL-polypeptid, isolert DNA som koder for et fusjonsprotein, fremgangsmate for fremstilling av en TRAIL-oligomer, antistoff som binder et TRAIL-polypeptid, renset TRAIL-polypeptid og opploselig TRAIL-polypeptid, oligomer, farmasoytisk preparat, farmasoytisk preparat for bruk som et medikament, farmasoytisk preparat for anvendelse ved indusering av apoptose hos malceller samt anvendelse av et TRAIL-polypeptid ved fremstilling av et medikament. Download PDFInfo
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- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
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- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
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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
- C07H—SUGARS; DERIVATIVES THEREOF; NUCLEOSIDES; NUCLEOTIDES; NUCLEIC ACIDS
- C07H21/00—Compounds containing two or more mononucleotide units having separate phosphate or polyphosphate groups linked by saccharide radicals of nucleoside groups, e.g. nucleic acids
- C07H21/04—Compounds containing two or more mononucleotide units having separate phosphate or polyphosphate groups linked by saccharide radicals of nucleoside groups, e.g. nucleic acids with deoxyribosyl as saccharide radical
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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
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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
- C07K16/2875—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the NGF/TNF superfamily, e.g. CD70, CD95L, CD153, CD154
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
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- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
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- H—ELECTRICITY
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- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
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- C07K2319/00—Fusion polypeptide
Landscapes
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Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US49663295A | 1995-06-29 | 1995-06-29 | |
US54836895A | 1995-11-01 | 1995-11-01 | |
PCT/US1996/010895 WO1997001633A1 (en) | 1995-06-29 | 1996-06-25 | Cytokine that induces apoptosis |
Publications (3)
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NO976045D0 NO976045D0 (no) | 1997-12-22 |
NO976045L NO976045L (no) | 1998-03-02 |
NO321707B1 true NO321707B1 (no) | 2006-06-26 |
Family
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Application Number | Title | Priority Date | Filing Date |
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NO19976045A NO321707B1 (no) | 1995-06-29 | 1997-12-22 | Isolert DNA som koder for et TRAIL-polypeptid og et opploselig TRAIL-polypeptid, ekspresjonsvektor, fremgangsmate for fremstilling av et TRAIL-polypeptid, isolert DNA som koder for et fusjonsprotein, fremgangsmate for fremstilling av en TRAIL-oligomer, antistoff som binder et TRAIL-polypeptid, renset TRAIL-polypeptid og opploselig TRAIL-polypeptid, oligomer, farmasoytisk preparat, farmasoytisk preparat for bruk som et medikament, farmasoytisk preparat for anvendelse ved indusering av apoptose hos malceller samt anvendelse av et TRAIL-polypeptid ved fremstilling av et medikament. |
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US (1) | US5763223A (ko) |
EP (2) | EP0835305B1 (ko) |
JP (1) | JP4435304B2 (ko) |
KR (2) | KR100510234B1 (ko) |
AT (2) | ATE310813T1 (ko) |
AU (1) | AU708239B2 (ko) |
CA (1) | CA2225378C (ko) |
DE (2) | DE69635480T2 (ko) |
DK (2) | DK0835305T3 (ko) |
ES (2) | ES2253753T3 (ko) |
HK (2) | HK1010215A1 (ko) |
IL (6) | IL149261A0 (ko) |
NO (1) | NO321707B1 (ko) |
NZ (1) | NZ311982A (ko) |
PT (1) | PT1666591E (ko) |
WO (1) | WO1997001633A1 (ko) |
Families Citing this family (170)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US8715645B2 (en) * | 1994-05-27 | 2014-05-06 | The Regents Of The University Of Colorado | Viral vectors encoding apoptosis-inducing proteins and methods for making and using the same |
US20050089958A1 (en) * | 1996-01-09 | 2005-04-28 | Genentech, Inc. | Apo-2 ligand |
US6030945A (en) * | 1996-01-09 | 2000-02-29 | Genentech, Inc. | Apo-2 ligand |
US6998116B1 (en) * | 1996-01-09 | 2006-02-14 | Genentech, Inc. | Apo-2 ligand |
US6046048A (en) * | 1996-01-09 | 2000-04-04 | Genetech, Inc. | Apo-2 ligand |
US20040038347A1 (en) * | 1996-03-14 | 2004-02-26 | Human Genome Sciences, Inc. | Apoptosis inducing molecule I |
CA2256464A1 (en) * | 1996-06-07 | 1997-12-11 | Amgen Inc. | Tumor necrosis factor-related polypeptide |
JP2002509431A (ja) * | 1996-12-23 | 2002-03-26 | イミュネックス・コーポレーション | NF−κBのレセプター活性化因子−レセプターはTNFレセプタースーパーファミリーの一員である− |
US7452538B2 (en) | 1997-01-28 | 2008-11-18 | Human Genome Sciences, Inc. | Death domain containing receptor 4 antibodies and methods |
WO1998032856A1 (en) * | 1997-01-28 | 1998-07-30 | Human Genome Sciences, Inc. | Death domain containing receptor 4 (dr4: death receptor 4), member of the tnf-receptor superfamily and binding to trail (ap02-l) |
US6433147B1 (en) | 1997-01-28 | 2002-08-13 | Human Genome Sciences, Inc. | Death domain containing receptor-4 |
US8329179B2 (en) | 1997-01-28 | 2012-12-11 | Human Genome Sciences, Inc. | Death domain containing receptor 4 antibodies and methods |
US20020009467A1 (en) | 1997-01-29 | 2002-01-24 | Shozo Koyama | Antigenic substance inductor, vaccine precursor, vaccine, antibody, neutralizing antibody, antitoxin, idiotype antibody and/or anti-idiotype antibody which is induced by its idiotype antibody |
JP3813682B2 (ja) * | 1997-01-29 | 2006-08-23 | 小山 省三 | ワクチン前駆体およびワクチン |
WO1998035061A2 (en) * | 1997-02-12 | 1998-08-13 | Abbott Laboratories | Member of the tnf family useful for treatment and diagnosis of disease |
US7528239B1 (en) * | 1997-02-13 | 2009-05-05 | Immunex Corporation | Receptor that binds trail |
US6072047A (en) | 1997-02-13 | 2000-06-06 | Immunex Corporation | Receptor that binds trail |
US20010010924A1 (en) * | 1997-03-14 | 2001-08-02 | Keith Charles Deen | Tumor necrosis factor related receptor, tr6 polynecleotides |
CA2644454A1 (en) * | 1997-03-17 | 1998-09-24 | Human Genome Sciences, Inc. | Death domain containing receptor 5 |
US20050233958A1 (en) * | 1997-03-17 | 2005-10-20 | Human Genome Sciences, Inc. | Death domain containing receptor 5 |
US20080248046A1 (en) * | 1997-03-17 | 2008-10-09 | Human Genome Sciences, Inc. | Death domain containing receptor 5 |
US6872568B1 (en) | 1997-03-17 | 2005-03-29 | Human Genome Sciences, Inc. | Death domain containing receptor 5 antibodies |
US20040136951A1 (en) * | 1997-03-17 | 2004-07-15 | Human Genome Sciences, Inc. | Death domain containing receptor 5 |
US20020102706A1 (en) * | 1997-06-18 | 2002-08-01 | Genentech, Inc. | Apo-2DcR |
US6316408B1 (en) | 1997-04-16 | 2001-11-13 | Amgen Inc. | Methods of use for osetoprotegerin binding protein receptors |
EP1717315A3 (en) * | 1997-04-16 | 2007-06-20 | Amgen Inc. | Osteoprotegerin binding proteins and receptors |
DK1860187T3 (da) * | 1997-05-15 | 2011-10-31 | Genentech Inc | Apo-2-receptor |
US6342369B1 (en) * | 1997-05-15 | 2002-01-29 | Genentech, Inc. | Apo-2-receptor |
US20100152426A1 (en) * | 1997-05-15 | 2010-06-17 | Ashkenazi Avi J | Apo-2 receptor fusion proteins |
EP1032661A1 (en) * | 1997-06-18 | 2000-09-06 | Genentech, Inc. | Apo-2DcR |
US6171787B1 (en) * | 1997-06-26 | 2001-01-09 | Abbott Laboratories | Member of the TNF family useful for treatment and diagnosis of disease |
WO1999002653A1 (en) * | 1997-07-11 | 1999-01-21 | Trustees Of The University Of Pennsylvania | Nucleic acid encoding a novel chemotherapy-induced protein, and methods of use |
FR2766713B1 (fr) * | 1997-08-04 | 1999-09-24 | Bio Merieux | Facteur proteique associe a une maladie neuro-degenerative et/ou auto-immune et/ou inflammatoire |
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 |
AU5201399A (en) | 1997-09-30 | 1999-10-18 | Pharmacia & Upjohn Company | Tnf-related death ligand |
EP1032672B1 (en) * | 1997-11-18 | 2008-12-31 | Genentech, Inc. | Dna19355 polypeptide, a tumor necrosis factor homolog |
US7019119B2 (en) * | 1997-12-12 | 2006-03-28 | The Rockefeller University | Protein belonging to the TNF superfamily involved in signal transduction, nucleic acids encoding same, and methods of use thereof |
DE69939732D1 (de) | 1998-01-15 | 2008-11-27 | Genentech Inc | Apo-2 ligand |
US20040120947A1 (en) * | 1998-01-26 | 2004-06-24 | Genentech, Inc. | DR4 antibodies and uses thereof |
US20040180049A1 (en) * | 1998-01-26 | 2004-09-16 | Genentech, Inc. | DR4 antibodies and uses thereof |
EP2050762A3 (en) | 1998-03-10 | 2009-07-08 | Genentech, Inc. | Human cornichon-like protein and nucleic acids encoding it |
PT1064027E (pt) * | 1998-03-27 | 2008-09-29 | Genentech Inc | Sinergismo de ligando de apo-2 e anticorpo anti-her-2 |
EP1941905A1 (en) | 1998-03-27 | 2008-07-09 | Genentech, Inc. | APO-2 Ligand-anti-her-2 antibody synergism |
WO2001060397A1 (en) | 2000-02-16 | 2001-08-23 | Genentech, Inc. | Uses of agonists and antagonists to modulate activity of tnf-related molecules |
EP2058334B1 (en) * | 1998-06-12 | 2012-10-31 | Genentech, Inc. | Monoclonal antibodies, cross-reactive antibodies and method for producing the same |
AU2004202605B2 (en) | 1998-07-13 | 2007-10-25 | Board Of Regents, The University Of Texas System | Cancer treatment methods using antibodies to aminophospholipids |
WO2000026228A1 (en) * | 1998-11-02 | 2000-05-11 | Clontech Laboratories, Inc. | Gene and protein for regulation of cell death |
US20030009013A1 (en) * | 1998-12-30 | 2003-01-09 | Genentech, Inc. | Secreted and transmembrane polypeptides and nucleic acids encoding the same |
US20050281821A1 (en) * | 1999-01-06 | 2005-12-22 | Flavia Pernasetti | Method and composition for angiogenesis inhibition |
US7696325B2 (en) | 1999-03-10 | 2010-04-13 | Chugai Seiyaku Kabushiki Kaisha | Polypeptide inducing apoptosis |
JP4716578B2 (ja) | 1999-04-12 | 2011-07-06 | ジェネンテック, インコーポレイテッド | 腫瘍壊死因子相同体及びそれをコードする核酸 |
AU3923000A (en) * | 1999-04-16 | 2000-11-02 | Amgen, Inc. | Agp-1 fusion protein compositions and methods |
EP1873244A3 (en) * | 1999-06-02 | 2008-04-02 | Genentech, Inc. | Methods and compositions for inhibiting neoplastic cell growth |
WO2001000832A1 (en) * | 1999-06-28 | 2001-01-04 | Genentech, Inc. | Methods for making apo-2 ligand using divalent metal ions |
US6444640B1 (en) * | 1999-09-30 | 2002-09-03 | Ludwig Institute For Cancer Research | Compositions of trail and DNA damaging drugs and uses thereof |
CA2386002A1 (en) * | 1999-09-30 | 2001-04-05 | The Trustees Of The University Of Pennsylvania | Trail: an inhibitor of autoimmune inflammation and cell cycle progression |
EP2298334A3 (en) | 1999-12-20 | 2012-04-04 | Immunex Corporation | Tweak receptor |
US7927602B2 (en) | 2002-07-23 | 2011-04-19 | University Of Louisville Research Foundation, Inc. | Fas ligand-avidin/streptavidin fusion proteins |
JP4898049B2 (ja) * | 2000-01-24 | 2012-03-14 | ユニバーシティ オブ ルイビル リサーチ ファウンデーション,インコーポレイティド | デスレセプター誘導アポトーシスによる免疫調節 |
US20030103978A1 (en) * | 2000-02-23 | 2003-06-05 | Amgen Inc. | Selective binding agents of osteoprotegerin binding protein |
DK2857516T3 (en) | 2000-04-11 | 2017-08-07 | Genentech Inc | Multivalent antibodies and uses thereof |
US6900185B1 (en) | 2000-04-12 | 2005-05-31 | University Of Iowa Research Foundation | Method of inducing tumor cell apoptosis using trail/Apo-2 ligand gene transfer |
US7238360B2 (en) * | 2000-06-30 | 2007-07-03 | Unversity Of Louisville Research Foundation, Inc. | Alteration of cell membrane with B7 |
JP2004509078A (ja) | 2000-07-27 | 2004-03-25 | ジェネンテック・インコーポレーテッド | Apo−2LレセプターアゴニストとCPT−11の相乗作用 |
DE10045591A1 (de) * | 2000-09-15 | 2002-04-04 | Klaus Pfizenmaier | Ortsspezifische, antikörpervermittelte Aktivierung proapoptotischer Zytokine - AMAIZe (Antibody-Mediated Apoptosis Inducing Zytokine) |
ATE391174T1 (de) | 2000-10-20 | 2008-04-15 | Chugai Pharmaceutical Co Ltd | Modifizierter tpo-agonisten antikörper |
WO2002079377A2 (en) * | 2000-11-08 | 2002-10-10 | Human Genome Sciences, Inc. | Antibodies that immunospecifically bind to trail receptors |
US20060062786A1 (en) * | 2000-11-08 | 2006-03-23 | Human Genome Sciences, Inc. | Antibodies that immunospecifically bind to TRAIL receptors |
US20030228309A1 (en) * | 2000-11-08 | 2003-12-11 | Theodora Salcedo | Antibodies that immunospecifically bind to TRAIL receptors |
US20020155109A1 (en) * | 2001-04-20 | 2002-10-24 | Lynch David H. | Bispecific antibodies that bind TRAIL-R1 and TRAIL-R2 |
US7361341B2 (en) * | 2001-05-25 | 2008-04-22 | Human Genome Sciences, Inc. | Methods of treating cancer using antibodies that immunospecifically bind to trail receptors |
WO2002097033A2 (en) * | 2001-05-25 | 2002-12-05 | Human Genome Sciences, Inc. | Antibodies that immunospecifically bind to trail receptors |
US7348003B2 (en) | 2001-05-25 | 2008-03-25 | Human Genome Sciences, Inc. | Methods of treating cancer using antibodies that immunospecifically bind to TRAIL receptors |
US20050129616A1 (en) * | 2001-05-25 | 2005-06-16 | Human Genome Sciences, Inc. | Antibodies that immunospecifically bind to TRAIL receptors |
US20090226429A1 (en) * | 2001-05-25 | 2009-09-10 | Human Genome Sciences, Inc. | Antibodies That Immunospecifically Bind to TRAIL Receptors |
US20050214209A1 (en) * | 2001-05-25 | 2005-09-29 | Human Genome Sciences, Inc. | Antibodies that immunospecifically bind to TRAIL receptors |
GB0113920D0 (en) * | 2001-06-07 | 2001-08-01 | Sterix Ltd | Composition |
TR201809008T4 (tr) | 2001-06-26 | 2018-07-23 | Amgen Fremont Inc | Opgl ye karşi antikorlar. |
EP2192130A1 (en) | 2001-07-03 | 2010-06-02 | Genentech, Inc. | Human DR4 antibodies and uses thereof |
JP2005502645A (ja) * | 2001-08-08 | 2005-01-27 | ザ ボード オブ リージェンツ,ザ ユニバーシティ オブ テキサス システム | 細胞特異的プロモーターからの発現を増幅するための方法 |
IL161051A0 (en) | 2001-10-02 | 2004-08-31 | Genentech Inc | Apo-2 ligand variants and uses thereof |
EP2332531B1 (en) * | 2001-11-13 | 2019-07-10 | Genentech, Inc. | Methods of purifying Apo2-Ligand/TRAIL |
US7741285B2 (en) * | 2001-11-13 | 2010-06-22 | Genentech, Inc. | APO-2 ligand/trail formulations |
AU2007200478A1 (en) * | 2001-11-13 | 2007-02-22 | Genentech, Inc. | APO2 ligand/trail formulations |
US7842668B1 (en) | 2001-11-13 | 2010-11-30 | Genentech, Inc. | Apo-2 ligand/trail formulations |
JP2005516958A (ja) * | 2001-12-20 | 2005-06-09 | 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 | Trailレセプターに免疫特異的に結合する抗体 |
ES2557741T3 (es) | 2002-03-27 | 2016-01-28 | Immunex Corporation | Procedimientos para incrementar la producción de polipéptidos |
EP1494714A4 (en) | 2002-04-05 | 2008-03-05 | Amgen Inc | HUMAN ANTI-OPGL NEUTRALIZING ANTIBODIES AS SELECTIVE OPGL PATH HEMMER |
CA2489348A1 (en) | 2002-06-24 | 2003-12-31 | Genentech, Inc. | Apo-2 ligand/trail variants and uses thereof |
NZ584715A (en) | 2002-07-15 | 2011-12-22 | Univ Texas | Peptides binding to phosphatidylethanolamine and their use in treating viral infections and cancer |
WO2004052292A2 (en) * | 2002-12-06 | 2004-06-24 | University Of South Florida | Histone deacetylase inhibitor enhancement of trail-induced apoptosis |
JP2004279086A (ja) | 2003-03-13 | 2004-10-07 | Konica Minolta Holdings Inc | 放射線画像変換パネル及び放射線画像変換パネルの製造方法 |
AU2004271730A1 (en) * | 2003-09-18 | 2005-03-24 | Novartis Ag | Combination of a histone deacetylase inhibitor with a death receptor ligand |
JP4688678B2 (ja) * | 2003-11-03 | 2011-05-25 | 北京沙東生物技術有限公司 | 抗癌作用を有する組換えタンパク質、それをコードする遺伝子、及びそれらの使用 |
WO2005056605A1 (ja) | 2003-12-12 | 2005-06-23 | Chugai Seiyaku Kabushiki Kaisha | 3量体以上の受容体を認識する改変抗体 |
ES2410587T3 (es) | 2004-01-22 | 2013-07-02 | University Of Miami | Formulaciones tópicas de coenzima Q10 y métodos de uso |
US20080242603A1 (en) * | 2004-02-20 | 2008-10-02 | Yan Wang | Novel Apo2L and IL-24 Polypeptides, Polynucleotides, and Methods of Their Use |
CN1954074B (zh) | 2004-03-11 | 2011-08-24 | 健泰科生物技术公司 | 多肽的制备方法 |
CN1980957A (zh) | 2004-03-23 | 2007-06-13 | 比奥根艾迪克Ma公司 | 受体偶联剂及其治疗用途 |
JP5237638B2 (ja) | 2004-08-06 | 2013-07-17 | ジェネンテック, インコーポレイテッド | バイオマーカーを用いたアッセイおよび方法 |
CN101061238B (zh) * | 2004-08-06 | 2013-11-20 | 健泰科生物技术公司 | 使用生物标志的测定法和方法 |
EP1791864A2 (en) * | 2004-09-08 | 2007-06-06 | Genentech, Inc. | Methods of using death receptor ligands and cd20 antibodies |
AU2005282397A1 (en) * | 2004-09-08 | 2006-03-16 | Genentech, Inc. | Methods of using death receptor ligands and CD20 antibodies |
EP1645875A1 (en) * | 2004-10-08 | 2006-04-12 | Deutsches Krebsforschungszentrum Stiftung des öffentlichen Rechts | Diagnosis and therapy of cell proliferative disorders characterized by resistance to TRAIL induced apoptosis |
JO3000B1 (ar) * | 2004-10-20 | 2016-09-05 | Genentech Inc | مركبات أجسام مضادة . |
US8029783B2 (en) | 2005-02-02 | 2011-10-04 | Genentech, Inc. | DR5 antibodies and articles of manufacture containing same |
US20060228352A1 (en) * | 2005-02-24 | 2006-10-12 | Schoenberger Stephen P | TRAIL and methods of modulating T cell activity and adaptive immune responses using TRAIL |
JP2006265155A (ja) * | 2005-03-23 | 2006-10-05 | Link Genomics Kk | 癌の免疫療法 |
EP1870458B1 (en) | 2005-03-31 | 2018-05-09 | Chugai Seiyaku Kabushiki Kaisha | sc(Fv)2 STRUCTURAL ISOMERS |
CN101262885B (zh) | 2005-06-10 | 2015-04-01 | 中外制药株式会社 | 含有sc(Fv)2的药物组合物 |
CA2610987C (en) | 2005-06-10 | 2013-09-10 | Chugai Seiyaku Kabushiki Kaisha | Stabilizer for protein preparation comprising meglumine and use thereof |
ATE533058T1 (de) * | 2005-08-16 | 2011-11-15 | Genentech Inc | Apoptosesensitivität gegenüber apo2l/trail mittels testen auf galnac-t14-expression in zellen/gewebe |
WO2007024921A2 (en) * | 2005-08-24 | 2007-03-01 | Cell Matrix | Combination therapies for inhibiting integrin-extracellular matrix interactions |
PE20071101A1 (es) * | 2005-08-31 | 2007-12-21 | Amgen Inc | Polipeptidos y anticuerpos |
JP6088723B2 (ja) | 2005-11-23 | 2017-03-01 | ジェネンテック, インコーポレイテッド | B細胞アッセイに関する組成物及び方法。 |
GB0524316D0 (en) * | 2005-11-29 | 2006-01-04 | Medical Res Council | Tumour necrosis factor-related apoptosis-inducing ligands (TRAILs) |
US20100047783A1 (en) * | 2006-06-20 | 2010-02-25 | El-Diery Wafik S | Small molecule modulators of p53 family signaling |
US8008261B2 (en) * | 2006-08-04 | 2011-08-30 | Mayo Foundation For Medical Education And Research | Methods of reducing trail-induced apoptosis by trail isoforms |
EP2136831B1 (en) | 2007-03-02 | 2012-09-12 | The Cleveland Clinic Foundation | Anti-angiogenic peptides |
AU2013203061B2 (en) * | 2007-07-10 | 2016-07-28 | Apogenix Ag | TNF superfamily collectin fusion proteins |
EP2176288B1 (en) | 2007-07-10 | 2015-11-04 | Apogenix GmbH | Tnf superfamily collectin fusion proteins |
WO2009025743A2 (en) * | 2007-08-17 | 2009-02-26 | University Of Massachusetts Medical School | Use of trail compositions as antiviral agents |
CN101157729B (zh) * | 2007-10-23 | 2011-01-12 | 南京大学 | 一种肿瘤坏死因子相关凋亡配体变体及其应用 |
KR20100102110A (ko) | 2007-11-09 | 2010-09-20 | 페레그린 파마수티컬즈, 인크 | 항-vegf 항체 조성물 및 방법 |
CA2744043A1 (en) | 2008-11-25 | 2010-06-03 | Biogen Idec Ma Inc. | Use of dr6 and p75 antagonists to promote survival of cells of the nervous system |
US8664366B2 (en) | 2009-01-09 | 2014-03-04 | Apogenix Gmbh | Fusion proteins forming trimers |
US20100316639A1 (en) | 2009-06-16 | 2010-12-16 | Genentech, Inc. | Biomarkers for igf-1r inhibitor therapy |
ES2356880B8 (es) | 2009-08-21 | 2012-10-30 | Universidad De Zaragoza | Liposomas recubiertos con el dominio extracelular de la proteína apo2l/trail. |
CA2777162A1 (en) * | 2009-10-09 | 2011-04-14 | Anaphore, Inc. | Polypeptides that bind il-23r |
KR101380840B1 (ko) * | 2010-04-01 | 2014-04-04 | 한국생명공학연구원 | Trail 센서타이저 타겟 유전자인 tip41의 발현 또는 활성 억제제를 함유하는 trail 감수성 증진용 조성물 |
PL391627A1 (pl) * | 2010-06-25 | 2012-01-02 | Adamed Spółka Z Ograniczoną Odpowiedzialnością | Przeciwnowotworowe białko fuzyjne |
EP2601287B1 (en) | 2010-08-05 | 2015-01-07 | Amgen Inc. | Dipeptides to enhance yield and viability from cell cultures |
EP2646464B1 (en) | 2010-12-03 | 2015-06-03 | Adamed sp. z o.o. | Anticancer fusion protein |
PL219845B1 (pl) | 2011-01-05 | 2015-07-31 | Adamed Spółka Z Ograniczoną Odpowiedzialnością | Przeciwnowotworowe białko fuzyjne |
PL394618A1 (pl) | 2011-04-19 | 2012-10-22 | Adamed Spólka Z Ograniczona Odpowiedzialnoscia | Przeciwnowotworowe bialko fuzyjne |
US9133493B2 (en) | 2011-04-21 | 2015-09-15 | Amgen Inc. | Method for culturing mammalian cells to improve recombinant protein production |
WO2012151317A1 (en) | 2011-05-03 | 2012-11-08 | Genentech, Inc. | Vascular disruption agents and uses thereof |
LT2837680T (lt) | 2011-07-01 | 2020-07-10 | Amgen Inc. | Žinduolių ląstelių kultūra |
CN102908612A (zh) * | 2011-08-02 | 2013-02-06 | 北京诺赛基因组研究中心有限公司 | TRAIL截短型变异体活化NF-κB和在炎症反应中的应用 |
BR112014004591A2 (pt) | 2011-09-02 | 2017-03-28 | Amgen Inc | produto farmacêutico de análise da exposição à luz de um produto farmacêutico |
CN103534273B (zh) * | 2011-09-16 | 2020-05-12 | 北京沙东生物技术有限公司 | 环化变构trail/apo2l及其编码基因与应用 |
PL397167A1 (pl) | 2011-11-28 | 2013-06-10 | Adamed Spólka Z Ograniczona Odpowiedzialnoscia | Przeciwnowotworowe bialko fuzyjne |
AR089231A1 (es) | 2011-12-15 | 2014-08-06 | Amgen Inc | Metodo de floculacion |
PL223487B1 (pl) | 2011-12-28 | 2016-10-31 | Adamed Spółka Z Ograniczoną Odpowiedzialnością | Przeciwnowotworowe białko fuzyjne |
EP2931287B1 (de) * | 2012-12-11 | 2017-10-04 | Sapiotec GmbH | Delphinidin zur bekämpfung von melanomzellen |
WO2014109858A1 (en) | 2013-01-14 | 2014-07-17 | Amgen Inc. | Methods of using cell-cycle inhibitors to modulate one or more properties of a cell culture |
US10023608B1 (en) | 2013-03-13 | 2018-07-17 | Amgen Inc. | Protein purification methods to remove impurities |
EP2970473B1 (en) | 2013-03-14 | 2017-08-16 | Bristol-Myers Squibb Company | Combination of dr5 agonist and anti-pd-1 antagonist and methods of use |
JP6457479B2 (ja) | 2013-03-14 | 2019-01-23 | アムジエン・インコーポレーテツド | 漏出したアフィニティ精製リガンドの除去 |
TWI625390B (zh) | 2013-03-14 | 2018-06-01 | 安美基公司 | 用於增加重組蛋白質之甘露糖含量之方法 |
US9481901B2 (en) | 2013-05-30 | 2016-11-01 | Amgen Inc. | Methods for increasing mannose content of recombinant proteins |
JP6785653B2 (ja) | 2013-06-25 | 2020-11-18 | ザ・ウォルター・アンド・エリザ・ホール・インスティテュート・オブ・メディカル・リサーチ | 細胞内感染の処置方法 |
CN103555729B (zh) * | 2013-10-14 | 2016-08-24 | 成都华创生物技术有限公司 | 一种改造的trail基因序列、表达方法及应用 |
MX2016005572A (es) | 2013-10-31 | 2016-12-09 | Amgen Inc | Uso de monensina para regular la glicosilacion de proteinas recombinantes. |
BR122020004385B1 (pt) | 2014-01-13 | 2022-10-04 | Amgen Inc | Método para aumentar o teor de glicoforma de alta manose de uma glicoproteína recombinante e método de produção de uma glicoproteína recombinante |
US10106829B2 (en) | 2014-01-29 | 2018-10-23 | Amgen Inc. | Overexpression of N-glycosylation pathway regulators to modulate glycosylation of recombinant proteins |
CN113774084B (zh) | 2014-01-29 | 2024-04-16 | 美国安进公司 | 过表达n-糖基化途径调节基因以调节重组蛋白的糖基化 |
WO2015138638A1 (en) | 2014-03-11 | 2015-09-17 | Theraly Pharmaceuticals, Inc. | Long acting trail receptor agonists for treatment of autoimmune diseases |
US11384378B2 (en) | 2014-06-04 | 2022-07-12 | Amgen Inc. | Methods for harvesting mammalian cell cultures |
US11275090B2 (en) | 2014-11-19 | 2022-03-15 | Amgen Inc. | Quantitation of glycan moiety in recombinant glycoproteins |
SG11201704351WA (en) | 2014-12-01 | 2017-06-29 | Amgen Inc | Process for manipulating the level of glycan content of a glycoprotein |
US11279768B1 (en) | 2015-04-03 | 2022-03-22 | Precision Biologics, Inc. | Anti-cancer antibodies, combination therapies, and uses thereof |
AU2016371021B2 (en) | 2015-12-17 | 2020-04-09 | The Johns Hopkins University | Ameliorating systemic sclerosis with death receptor agonists |
IL299759A (en) | 2015-12-30 | 2023-03-01 | Genentech Inc | Formulations with reduced polysorbate dissolution |
CN116064677A (zh) * | 2016-02-05 | 2023-05-05 | 斯比根公司 | 表达trail和cd的间充质干细胞及其用途 |
KR102508650B1 (ko) | 2016-04-07 | 2023-03-13 | 더 존스 홉킨스 유니버시티 | 사멸 수용체 작용제로써 췌장암 및 통증을 치료하기 위한 조성물 및 방법 |
KR101739703B1 (ko) * | 2016-09-13 | 2017-05-24 | (주) 어드밴스드 엔티 | Trail 기반 뇌염 감별진단 방법 및 장치 |
MX2020011614A (es) | 2018-05-01 | 2020-12-09 | Amgen Inc | Anticuerpos con perfiles de glicanos modulados. |
US11519007B2 (en) | 2019-02-22 | 2022-12-06 | Arizona Board Of Regents On Behalf Of Arizona State University | Tumor-navigating, self-eradicating, trail-armed salmonella for precision cancer therapy |
WO2023129974A1 (en) | 2021-12-29 | 2023-07-06 | Bristol-Myers Squibb Company | Generation of landing pad cell lines |
Family Cites Families (27)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
ZA811368B (en) | 1980-03-24 | 1982-04-28 | Genentech Inc | Bacterial polypedtide expression employing tryptophan promoter-operator |
US4411993A (en) | 1981-04-29 | 1983-10-25 | Steven Gillis | Hybridoma antibody which inhibits interleukin 2 activity |
US4737462A (en) | 1982-10-19 | 1988-04-12 | Cetus Corporation | Structural genes, plasmids and transformed cells for producing cysteine depleted muteins of interferon-β |
US4518584A (en) | 1983-04-15 | 1985-05-21 | Cetus Corporation | Human recombinant interleukin-2 muteins |
US4703004A (en) | 1984-01-24 | 1987-10-27 | Immunex Corporation | Synthesis of protein with an identification peptide |
US5391485A (en) | 1985-08-06 | 1995-02-21 | Immunex Corporation | DNAs encoding analog GM-CSF molecules displaying resistance to proteases which cleave at adjacent dibasic residues |
US5071972A (en) | 1986-01-31 | 1991-12-10 | Genetics Institute, Inc. | DNA sequences encoding novel thrombolytic proteins |
US5011912A (en) | 1986-12-19 | 1991-04-30 | Immunex Corporation | Hybridoma and monoclonal antibody for use in an immunoaffinity purification system |
EP0276846A3 (en) | 1987-01-29 | 1989-07-26 | Zymogenetics, Inc. | Colony-stimulating factor derivatives |
US4965195A (en) | 1987-10-26 | 1990-10-23 | Immunex Corp. | Interleukin-7 |
US4968607A (en) | 1987-11-25 | 1990-11-06 | Immunex Corporation | Interleukin-1 receptors |
WO1990005183A1 (en) | 1988-10-31 | 1990-05-17 | Immunex Corporation | Interleukin-4 receptors |
ES2055907T3 (es) | 1989-03-07 | 1994-09-01 | Genentech Inc | Conjugados covalentes de lipidos y oligonucleotidos. |
JPH04505261A (ja) | 1989-05-10 | 1992-09-17 | スローン―ケツテリング・インステイテユート・フオー・キヤンサー・リサーチ | ポルiiiプロモーターの制御下の転写可能な外来dnaを含む安定的に形質転換された真核細胞 |
US5073627A (en) | 1989-08-22 | 1991-12-17 | Immunex Corporation | Fusion proteins comprising GM-CSF and IL-3 |
WO1991004753A1 (en) | 1989-10-02 | 1991-04-18 | Cetus Corporation | Conjugates of antisense oligonucleotides and therapeutic uses thereof |
EP0498843B1 (en) | 1989-10-24 | 1996-06-12 | Gilead Sciences, Inc. | Oligonucleotide analogs with novel linkages |
AU651596B2 (en) | 1990-06-05 | 1994-07-28 | Immunex Corporation | Type II interleukin-1 receptors |
US5716805A (en) | 1991-10-25 | 1998-02-10 | Immunex Corporation | Methods of preparing soluble, oligomeric proteins |
US5262522A (en) | 1991-11-22 | 1993-11-16 | Immunex Corporation | Receptor for oncostatin M and leukemia inhibitory factor |
NZ257942A (en) | 1992-10-23 | 1996-04-26 | Immunex Corp | Preparing a mammalian protein by expression of a fusion protein containing a leucine zipper domain |
US5512435A (en) * | 1993-02-05 | 1996-04-30 | Renschler; Markus F. | Receptor-binding antiproliferative peptides |
US5457035A (en) | 1993-07-23 | 1995-10-10 | Immunex Corporation | Cytokine which is a ligand for OX40 |
NZ275711A (en) | 1993-10-14 | 1998-03-25 | Immunex Corp | Monoclonal antibodies and binding proteins which bind to human fas antigen (nerve growth factor/tumour necrosis factor receptor type) |
US6030945A (en) * | 1996-01-09 | 2000-02-29 | Genentech, Inc. | Apo-2 ligand |
AU5711196A (en) * | 1996-03-14 | 1997-10-01 | Human Genome Sciences, Inc. | Apoptosis inducing molecule i |
CA2256464A1 (en) * | 1996-06-07 | 1997-12-11 | Amgen Inc. | Tumor necrosis factor-related polypeptide |
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