NZ582815A - Therapeutic use of anti- tweak receptor antibodies to treat cancer - Google Patents
Therapeutic use of anti- tweak receptor antibodies to treat cancerInfo
- Publication number
- NZ582815A NZ582815A NZ582815A NZ58281508A NZ582815A NZ 582815 A NZ582815 A NZ 582815A NZ 582815 A NZ582815 A NZ 582815A NZ 58281508 A NZ58281508 A NZ 58281508A NZ 582815 A NZ582815 A NZ 582815A
- Authority
- NZ
- New Zealand
- Prior art keywords
- antibody
- seq
- tweakr
- xaa
- cancer
- Prior art date
Links
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Classifications
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- 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
- C07K16/2878—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-receptor/TNF-receptor superfamily, e.g. CD27, CD30, CD40, CD95
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
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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
-
- 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
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- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
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- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/52—Constant or Fc region; Isotype
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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
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
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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
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
- C07K2317/732—Antibody-dependent cellular cytotoxicity [ADCC]
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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
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
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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
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/55—Fusion polypeptide containing a fusion with a toxin, e.g. diphteria toxin
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Immunology (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Animal Behavior & Ethology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Pharmacology & Pharmacy (AREA)
- General Chemical & Material Sciences (AREA)
- Cell Biology (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US95374507P | 2007-08-03 | 2007-08-03 | |
| US12362308P | 2008-04-09 | 2008-04-09 | |
| PCT/US2008/072146 WO2009020933A2 (en) | 2007-08-03 | 2008-08-04 | Therapeutic use of anti-tweak receptor antibodies |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| NZ582815A true NZ582815A (en) | 2012-07-27 |
Family
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Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NZ582815A NZ582815A (en) | 2007-08-03 | 2008-08-04 | Therapeutic use of anti- tweak receptor antibodies to treat cancer |
Country Status (12)
| Country | Link |
|---|---|
| US (1) | US9056908B2 (Direct) |
| EP (2) | EP2182982B1 (Direct) |
| JP (1) | JP5409628B2 (Direct) |
| KR (1) | KR20100053607A (Direct) |
| CN (1) | CN102006886A (Direct) |
| BR (1) | BRPI0814768A2 (Direct) |
| CA (1) | CA2694751C (Direct) |
| ES (1) | ES2411907T3 (Direct) |
| IL (1) | IL203038A (Direct) |
| MX (1) | MX2010001378A (Direct) |
| NZ (1) | NZ582815A (Direct) |
| WO (1) | WO2009020933A2 (Direct) |
Families Citing this family (34)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20090124993A1 (en) | 2005-02-17 | 2009-05-14 | Burkly Linda C | Treating neurological disorders |
| WO2006138219A2 (en) | 2005-06-13 | 2006-12-28 | Biogen Idec Ma Inc. | Methods of diagnosis / prognosis of inflammatory conditions |
| AU2009246640A1 (en) * | 2008-05-15 | 2009-11-19 | Biogen Idec Ma Inc. | Anti-Fn14 antibodies and uses thereof |
| ES2363669B1 (es) * | 2009-06-10 | 2012-08-09 | Fundacio Privada Institut D'investigacio Biomedica De Bellvitge (Idibell) | Metodo para determinar el riesgo de desarrollar metastasis cerebral y un kit para llevar a cabo dicho procedimiento |
| CN102675460B (zh) * | 2011-02-28 | 2015-08-19 | 珠海市丽珠单抗生物技术有限公司 | 抗肿瘤坏死因子α的人源化抗体 |
| US8609818B2 (en) | 2011-03-10 | 2013-12-17 | Omeros Corporation | Generation of anti-FN14 monoclonal antibodies by ex-vivo accelerated antibody evolution |
| ES2748021T3 (es) | 2011-08-23 | 2020-03-12 | Univ La Trobe | Proteínas de unión a Fn14 y usos de las mismas |
| AU2014203658B2 (en) * | 2011-08-23 | 2016-04-28 | La Trobe University | FN14 binding proteins and uses thereof |
| WO2013166290A1 (en) | 2012-05-04 | 2013-11-07 | Abbvie Biotherapeutics Inc. | P21 biomarker assay |
| WO2013177386A1 (en) * | 2012-05-24 | 2013-11-28 | Abbvie Biotherapeutics Inc. | Biomarkers for predicting response to tweak receptor (tweakr) agonist therapy |
| KR20150034209A (ko) | 2012-06-26 | 2015-04-02 | 델 마 파마슈티컬스 인코포레이티드 | 디안하이드로갈락티톨, 디아세틸디안하이드로갈락티톨, 디브로모둘시톨, 또는 그의 유사체 또는 유도체를 이용하여 유전학적 다형성이 있는 환자에 있어서 티로신-키나아제-억제제 내성 악성종양, ahi1 조절곤란 또는 돌연변이를 치료하는 방법 |
| NO2760138T3 (Direct) | 2012-10-01 | 2018-08-04 | ||
| US11491154B2 (en) | 2013-04-08 | 2022-11-08 | Dennis M. Brown | Therapeutic benefit of suboptimally administered chemical compounds |
| KR20160019434A (ko) | 2013-06-14 | 2016-02-19 | 바이엘 파마 악티엔게젤샤프트 | 항-tweakr 항체 및 그의 용도 |
| US9797882B2 (en) | 2013-07-09 | 2017-10-24 | The Translational Genomics Research Institute | Method of screening for a compound for inhibitory activity of FN14-tweak interaction |
| EP3019874B1 (en) * | 2013-07-09 | 2019-08-21 | The Translational Genomics Research Institute | Compositions and methods of screening for compounds that modulate activity at a tweak binding site on a crd of fn14 |
| PE20160996A1 (es) | 2013-12-23 | 2016-11-09 | Bayer Pharma AG | Conjugados de farmacos anticuerpo (adcs) con inhibidores de ksp |
| EP3209697A4 (en) | 2014-10-23 | 2018-05-30 | La Trobe University | Fn14-binding proteins and uses thereof |
| EP3233127A1 (de) * | 2014-12-15 | 2017-10-25 | Bayer Pharma Aktiengesellschaft | Antikörper-wirkstoff-konjugate (adcs) von ksp-inhibitoren mit aglycosylierten anti-tweakrantikörpern |
| CN108025084B (zh) * | 2015-06-22 | 2024-08-09 | 拜耳医药股份有限公司 | 具有酶可裂解基团的抗体药物缀合物（adc）和抗体前药缀合物（apdc） |
| EP3313521A1 (de) | 2015-06-23 | 2018-05-02 | Bayer Pharma Aktiengesellschaft | Antikörper-wirkstoff-konjugate (adcs) von ksp-inhibitoren mit anti-tweakr-antikörpern |
| US11071788B2 (en) | 2015-06-23 | 2021-07-27 | Bayer Pharma Aktiengesellschaft | Antibody drug conjugates of kinesin spindel protein (KSP) inhibitors with antiB7H3-antibodies |
| AU2016282724A1 (en) * | 2015-06-23 | 2018-01-18 | Bayer Pharma Aktiengesellschaft | Targeted conjugates of KSP inhibitors |
| WO2017060322A2 (en) | 2015-10-10 | 2017-04-13 | Bayer Pharma Aktiengesellschaft | Ptefb-inhibitor-adc |
| CA3018630A1 (en) | 2016-03-24 | 2017-09-28 | Bayer Pharma Aktiengesellschaft | Prodrugs of cytotoxic active agents having enzymatically cleavable groups |
| EP3919518A1 (en) | 2016-06-15 | 2021-12-08 | Bayer Pharma Aktiengesellschaft | Specific antibody-drug-conjugates (adcs) with ksp inhibitors and anti-cd123-antibodies |
| RU2761390C2 (ru) | 2016-12-21 | 2021-12-07 | Байер Фарма Акциенгезельшафт | Конъюгаты связующего и активного вещества (adc), имеющие ферментативно расщепляемые группы |
| JP7174704B2 (ja) | 2016-12-21 | 2022-11-17 | バイエル・アクチエンゲゼルシヤフト | 酵素開裂基を有する細胞毒性活性剤のプロドラッグ |
| CN110072556B (zh) | 2016-12-21 | 2023-05-02 | 拜耳制药股份公司 | 具有ksp抑制剂的特异性抗体药物缀合物(adc) |
| WO2019149637A1 (en) | 2018-01-31 | 2019-08-08 | Bayer Aktiengesellschaft | Antibody drug conjugates (adcs) with nampt inhibitors |
| US11629179B2 (en) | 2018-06-29 | 2023-04-18 | Stichting Het Nederlands Kanker Instituut—Antoni van Leeuwenhoek Ziekenhuis | TWEAK-receptor agonists for use in combination with immunotherapy of a cancer |
| MA54097A (fr) * | 2018-10-31 | 2022-02-09 | Astellas Pharma Inc | Anticorps anti-fn14 humain |
| WO2021013693A1 (en) | 2019-07-23 | 2021-01-28 | Bayer Pharma Aktiengesellschaft | Antibody drug conjugates (adcs) with nampt inhibitors |
| EP4619044A1 (en) | 2022-11-17 | 2025-09-24 | Hans-Georg Lerchen | Antibody-drug-conjugates cleavable in a tumor microenvironment |
Family Cites Families (35)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7001992B2 (en) * | 1997-05-30 | 2006-02-21 | Human Genome Sciences, Inc. | Antibodies to secreted protein HEMCM42 |
| PT1015477E (pt) | 1997-05-30 | 2010-12-28 | Human Genome Sciences Inc | 32 proteínas humanas segregadas |
| AU7549498A (en) | 1997-06-03 | 1998-12-21 | Protegene Inc. | Human proteins having transmembrane domains and dnas encoding these prot eins |
| EP1080194A2 (en) | 1998-05-29 | 2001-03-07 | Incyte Pharmaceuticals, Inc. | Human transmembrane proteins |
| CZ20012548A3 (cs) | 1999-01-15 | 2001-10-17 | Biogen, Inc. | Farmaceutické přípravky obsahující činidlo blokující protein TWEAK nebo receptor TWEAK |
| JP5148795B2 (ja) * | 1999-12-20 | 2013-02-20 | イミュネックス・コーポレーション | Ｔｗｅａｋ受容体 |
| US6727225B2 (en) * | 1999-12-20 | 2004-04-27 | Immunex Corporation | TWEAK receptor |
| US7495086B2 (en) | 1999-12-20 | 2009-02-24 | Immunex Corporation | TWEAK receptor |
| US20030165831A1 (en) | 2000-03-21 | 2003-09-04 | John Lee | Novel genes, compositions, kits, and methods for identification, assessment, prevention, and therapy of ovarian cancer |
| US6812339B1 (en) * | 2000-09-08 | 2004-11-02 | Applera Corporation | Polymorphisms in known genes associated with human disease, methods of detection and uses thereof |
| US7208151B2 (en) * | 2001-09-12 | 2007-04-24 | Biogen Idec Ma Inc. | Tweak receptor agonists as anti-angiogenic agents |
| EP1317283B1 (en) | 2000-09-14 | 2011-07-06 | Biogen Idec MA Inc. | Tweak receptor agonists as anti-angiogenic agents |
| JP4344519B2 (ja) | 2000-12-28 | 2009-10-14 | 旭化成ファーマ株式会社 | ＮＦ−κＢ活性化遺伝子 |
| US7227007B2 (en) * | 2000-12-28 | 2007-06-05 | Asahi Kasei Pharma Corporation | NF-κB activating gene |
| US20040214167A9 (en) * | 2000-12-28 | 2004-10-28 | Akio Matsuda | NF-kappa B activating gene |
| US20040142325A1 (en) * | 2001-09-14 | 2004-07-22 | Liat Mintz | Methods and systems for annotating biomolecular sequences |
| US20030228305A1 (en) | 2002-01-02 | 2003-12-11 | Genentech, Inc. | Compositions and methods for the diagnosis and treatment of tumor |
| WO2003077939A1 (en) | 2002-03-19 | 2003-09-25 | Genset Sa | Treatment of metabolic disorders with a tnf receptor family member (fradj and/or cryptic) agonists or antagonists |
| CA2500687A1 (en) * | 2002-10-02 | 2004-04-15 | Genentech, Inc. | Compositions and methods for the diagnosis and treatment of tumor |
| WO2004112829A2 (en) | 2003-05-23 | 2004-12-29 | Genentech, Inc. | Compositions and methods for the diagnosis and treatment of tumors of glial origin |
| DE602004006871T2 (de) | 2003-07-24 | 2008-02-07 | Amgen Inc., Thousand Oaks | Zusammensetzungen und verfahren, die multimere und oligomere lösliche fragmente des tweak-rezeptors betreffen |
| US7507580B2 (en) * | 2003-10-16 | 2009-03-24 | Zymogenetics, Inc. | Ztnfr14, a tumor necrosis factor receptor |
| US20070298037A1 (en) * | 2003-10-16 | 2007-12-27 | Fox Brian A | ZTNFR14, A Tumor Necrosis Factor Receptor |
| WO2005037865A2 (en) | 2003-10-16 | 2005-04-28 | Zymogenetics, Inc. | Ztnfr14, A TUMOR NECROSIS FACTOR RECEPTOR |
| EP1566636A1 (en) | 2004-02-23 | 2005-08-24 | AXARON Bioscience AG | Use of Tweak modulators and inhibitors for the treatment of neurological conditions |
| WO2005092383A1 (ja) | 2004-03-26 | 2005-10-06 | Takeda Pharmaceutical Company Limited | 呼吸器疾患の予防・治療剤 |
| BRPI0608012A2 (pt) * | 2005-03-07 | 2009-11-03 | Genentech Inc | método de tratamento de cáncer, método de aumento de atividade de célula nk, método de aumento de resposta ou atividade th1 inata, método de tratamento de uma disfunção mediada por th2, método de tratamento de uma doença imune, usos de uma molécula antagonista e uso de uma molécula agonista |
| WO2006122187A2 (en) | 2005-05-10 | 2006-11-16 | Biogen Idec Ma Inc. | Treating and evaluating inflammatory disorders |
| WO2006125632A2 (en) | 2005-05-24 | 2006-11-30 | Rechtsanwalt Dr. Martin Prager Als Insolvenzverwalter Über Das Vermögen Der Xantos Biomedicine Ag, Pluta Rechtsanwalts Gmbh | Agonistic antibodies that bind to the tweak receptor fn14 and thereby modulate adiposity-associated phenotypes as well as their use in therapy |
| WO2006130429A2 (en) * | 2005-05-27 | 2006-12-07 | Biogen Idec Ma Inc. | Treatment of cancer |
| WO2006138219A2 (en) | 2005-06-13 | 2006-12-28 | Biogen Idec Ma Inc. | Methods of diagnosis / prognosis of inflammatory conditions |
| EP1876448A1 (en) | 2005-09-30 | 2008-01-09 | DIGILAB BioVisioN GmbH | Method and analytical reagents for identifying therapeutics using biomarkers responsive to thiazolidinediones. |
| WO2008140565A2 (en) | 2006-11-08 | 2008-11-20 | Zymogenetics, Inc. | Use of tumor necrosis factor receptor 14 antagonists for treating psoriasis |
| EP2240601B1 (en) | 2007-12-27 | 2016-10-12 | Compugen Ltd. | Biomarkers for the prediction of renal injury |
| EP2080812A1 (en) | 2008-01-18 | 2009-07-22 | Transmedi SA | Compositions and methods of detecting post-stop peptides |
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| WO2009020933A2 (en) | 2009-02-12 |
| AU2008284025A2 (en) | 2010-04-01 |
| CN102006886A (zh) | 2011-04-06 |
| WO2009020933A9 (en) | 2009-07-09 |
| EP2545938A1 (en) | 2013-01-16 |
| CA2694751C (en) | 2015-07-14 |
| EP2182982B1 (en) | 2013-03-27 |
| KR20100053607A (ko) | 2010-05-20 |
| US9056908B2 (en) | 2015-06-16 |
| EP2182982A2 (en) | 2010-05-12 |
| US20090074762A1 (en) | 2009-03-19 |
| BRPI0814768A2 (pt) | 2015-03-03 |
| MX2010001378A (es) | 2010-06-02 |
| WO2009020933A3 (en) | 2009-03-26 |
| JP2010535713A (ja) | 2010-11-25 |
| IL203038A (en) | 2014-03-31 |
| ES2411907T8 (es) | 2013-08-30 |
| CA2694751A1 (en) | 2009-02-12 |
| JP5409628B2 (ja) | 2014-02-05 |
| ES2411907T3 (es) | 2013-07-09 |
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