MX2012011986A - RECEPTOR FGF HUMANO Y PROTEINAS ENLAZADAS A ß-KLOTHO. - Google Patents
RECEPTOR FGF HUMANO Y PROTEINAS ENLAZADAS A ß-KLOTHO.Info
- Publication number
- MX2012011986A MX2012011986A MX2012011986A MX2012011986A MX2012011986A MX 2012011986 A MX2012011986 A MX 2012011986A MX 2012011986 A MX2012011986 A MX 2012011986A MX 2012011986 A MX2012011986 A MX 2012011986A MX 2012011986 A MX2012011986 A MX 2012011986A
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- seq
- antigen
- linked
- protein
- fgf21
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Classifications
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- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
- A61K39/39533—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals
- A61K39/3955—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals against proteinaceous materials, e.g. enzymes, hormones, lymphokines
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- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
- A61P1/16—Drugs for disorders of the alimentary tract or the digestive system for liver or gallbladder disorders, e.g. hepatoprotective agents, cholagogues, litholytics
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- A—HUMAN NECESSITIES
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- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/04—Anorexiants; Antiobesity agents
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- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/06—Antihyperlipidemics
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- A—HUMAN NECESSITIES
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- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
- A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
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- 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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- A—HUMAN NECESSITIES
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- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
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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
- C07K16/2863—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 growth factors, growth regulators
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/40—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against enzymes
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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
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/31—Immunoglobulins specific features characterized by aspects of specificity or valency multispecific
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- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/32—Immunoglobulins specific features characterized by aspects of specificity or valency specific for a neo-epitope on a complex, e.g. antibody-antigen or ligand-receptor
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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
- C07K2317/90—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
- C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
- C07K2319/74—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor
- C07K2319/75—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor containing a fusion for activation of a cell surface receptor, e.g. thrombopoeitin, NPY and other peptide hormones
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
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- Chemical Kinetics & Catalysis (AREA)
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- Mycology (AREA)
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- Heart & Thoracic Surgery (AREA)
- Gastroenterology & Hepatology (AREA)
- Cardiology (AREA)
- Emergency Medicine (AREA)
- Child & Adolescent Psychology (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US32469110P | 2010-04-15 | 2010-04-15 | |
| US39285910P | 2010-10-13 | 2010-10-13 | |
| PCT/US2011/032333 WO2011130417A2 (en) | 2010-04-15 | 2011-04-13 | HUMAN FGF RECEPTOR AND β-KLOTHO BINDING PROTEINS |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| MX2012011986A true MX2012011986A (es) | 2013-03-05 |
Family
ID=44140861
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| MX2012011986A MX2012011986A (es) | 2010-04-15 | 2011-04-13 | RECEPTOR FGF HUMANO Y PROTEINAS ENLAZADAS A ß-KLOTHO. |
Country Status (7)
| Country | Link |
|---|---|
| US (1) | US9517264B2 (enExample) |
| EP (2) | EP2558497A2 (enExample) |
| JP (1) | JP2013523184A (enExample) |
| AU (1) | AU2011239689A1 (enExample) |
| CA (1) | CA2796055A1 (enExample) |
| MX (1) | MX2012011986A (enExample) |
| WO (1) | WO2011130417A2 (enExample) |
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| JOP20190083A1 (ar) | 2008-06-04 | 2017-06-16 | Amgen Inc | بولي ببتيدات اندماجية طافرة لـfgf21 واستخداماتها |
| EP2707718A1 (en) * | 2011-05-10 | 2014-03-19 | Amgen Inc. | Method of identifying compounds that specifically modulate the interaction of fgfr1 and beta-klotho |
| US9574002B2 (en) * | 2011-06-06 | 2017-02-21 | Amgen Inc. | Human antigen binding proteins that bind to a complex comprising β-Klotho and an FGF receptor |
| ES2748038T3 (es) | 2011-07-01 | 2020-03-12 | Ngm Biopharmaceuticals Inc | Composiciones, usos y métodos para el tratamiento de trastornos y enfermedades metabólicos |
| US20140213512A1 (en) | 2011-08-31 | 2014-07-31 | Amgen Inc. | Method of Treating or Ameliorating Type 1 Diabetes Using FGF21 |
| EP2925775B1 (en) | 2012-11-28 | 2020-09-16 | NGM Biopharmaceuticals, Inc. | Compositions and methods for treatment of metabolic disorders and diseases |
| US9290557B2 (en) | 2012-11-28 | 2016-03-22 | Ngm Biopharmaceuticals, Inc. | Compositions comprising variants and fusions of FGF19 polypeptides |
| EP2938740B1 (en) | 2012-12-27 | 2022-04-20 | NGM Biopharmaceuticals, Inc. | Chimeric fgf19 peptides for use in treating bile acid disorders |
| US9273107B2 (en) | 2012-12-27 | 2016-03-01 | Ngm Biopharmaceuticals, Inc. | Uses and methods for modulating bile acid homeostasis and treatment of bile acid disorders and diseases |
| KR102178945B1 (ko) | 2013-10-28 | 2020-11-13 | 엔지엠 바이오파마슈티컬스, 아이엔씨. | 암 모델 및 관련 방법 |
| TWI670283B (zh) * | 2013-12-23 | 2019-09-01 | 美商建南德克公司 | 抗體及使用方法 |
| PE20170256A1 (es) | 2014-01-24 | 2017-04-22 | Ngm Biopharmaceuticals Inc | Proteinas de union y sus metodos de uso |
| US20170065678A1 (en) | 2014-03-11 | 2017-03-09 | Novartis Ag | Methods of treating metabolic disorders associated with lipodystrophies and defects in insulin production or signaling |
| EP3122776B1 (en) * | 2014-03-25 | 2021-04-28 | Regeneron Pharmaceuticals, Inc. | Fgf21 receptor agonists and uses thereof |
| US10398758B2 (en) | 2014-05-28 | 2019-09-03 | Ngm Biopharmaceuticals, Inc. | Compositions comprising variants of FGF19 polypeptides and uses thereof for the treatment of hyperglycemic conditions |
| WO2015195509A2 (en) | 2014-06-16 | 2015-12-23 | Ngm Biopharmaceuticals, Inc. | Methods and uses for modulating bile acid homeostasis and treatment of bile acid disorders and diseases |
| IL251834B2 (en) | 2014-10-23 | 2023-09-01 | Ngm Biopharmaceuticals Inc | Pharmaceutical compositions containing peptide variants and methods of using them |
| GB201419094D0 (en) | 2014-10-27 | 2014-12-10 | Agency Science Tech & Res | Anti-TIM-3-antibodies |
| CN107405397B (zh) | 2014-10-27 | 2020-08-25 | 新加坡科技研究局 | 抗tim-3抗体 |
| US10434144B2 (en) | 2014-11-07 | 2019-10-08 | Ngm Biopharmaceuticals, Inc. | Methods for treatment of bile acid-related disorders and prediction of clinical sensitivity to treatment of bile acid-related disorders |
| US11566082B2 (en) | 2014-11-17 | 2023-01-31 | Cytiva Bioprocess R&D Ab | Mutated immunoglobulin-binding polypeptides |
| WO2017019957A2 (en) | 2015-07-29 | 2017-02-02 | Ngm Biopharmaceuticals, Inc. | Binding proteins and methods of use thereof |
| EP3331914A1 (en) | 2015-08-03 | 2018-06-13 | Novartis AG | Methods of treating fgf21-associated disorders |
| KR20180056657A (ko) | 2015-09-24 | 2018-05-29 | 제넨테크, 인크. | 뇌전증의 치료를 위한 방법 |
| ES2871036T3 (es) | 2015-11-09 | 2021-10-28 | Ngm Biopharmaceuticals Inc | Método para el tratamiento de trastornos relacionados con ácidos biliares |
| ES2909833T3 (es) | 2016-05-11 | 2022-05-10 | Cytiva Bioprocess R & D Ab | Método de limpieza y/o desinfección de una matriz de separación |
| CN109311949B (zh) | 2016-05-11 | 2022-09-16 | 思拓凡生物工艺研发有限公司 | 储存分离基质的方法 |
| US10730908B2 (en) | 2016-05-11 | 2020-08-04 | Ge Healthcare Bioprocess R&D Ab | Separation method |
| US10889615B2 (en) | 2016-05-11 | 2021-01-12 | Cytiva Bioprocess R&D Ab | Mutated immunoglobulin-binding polypeptides |
| US10654887B2 (en) | 2016-05-11 | 2020-05-19 | Ge Healthcare Bio-Process R&D Ab | Separation matrix |
| US10703774B2 (en) | 2016-09-30 | 2020-07-07 | Ge Healthcare Bioprocess R&D Ab | Separation method |
| JP7031934B2 (ja) | 2016-05-11 | 2022-03-08 | サイティバ・バイオプロセス・アールアンドディ・アクチボラグ | 分離マトリックス |
| EP3455243B1 (en) | 2016-05-11 | 2021-03-24 | Cytiva BioProcess R&D AB | Separation matrix |
| CN106279437B (zh) | 2016-08-19 | 2017-10-31 | 安源医药科技（上海）有限公司 | 高糖基化人凝血因子viii融合蛋白及其制备方法与用途 |
| CN107759697B (zh) | 2016-08-19 | 2023-03-24 | 安源医药科技（上海）有限公司 | 制备融合蛋白的方法 |
| US11123438B2 (en) | 2016-08-19 | 2021-09-21 | Ampsource Biopharma Shanghai Inc. | Linker peptide for constructing fusion protein |
| WO2018039557A1 (en) | 2016-08-26 | 2018-03-01 | Ngm Biopharmaceuticals, Inc. | Methods of treating fibroblast growth factor 19-mediated cancers and tumors |
| US12448411B2 (en) | 2016-09-30 | 2025-10-21 | Cytiva Bioprocess R&D Ab | Separation method |
| EP3333179A1 (en) * | 2016-12-07 | 2018-06-13 | Merz Pharma GmbH & Co. KGaA | Novel recombinant botulinum toxin with accelarated onset of effect |
| WO2018138297A1 (en) * | 2017-01-27 | 2018-08-02 | Kymab Limited | Anti-opg antibodies |
| EP3580237B1 (en) | 2017-02-08 | 2025-05-14 | Novartis AG | Fgf21 mimetic antibodies and uses thereof |
| EP3649157A4 (en) | 2017-07-06 | 2021-07-28 | Yale University | COMPOSITIONS AND METHODS FOR THE TREATMENT OR PREVENTION OF DISEASES RELATED TO ENDOCRINE FGF |
| CN119386162A (zh) | 2017-12-22 | 2025-02-07 | 诺华股份有限公司 | 用fgf21变体治疗代谢障碍的方法 |
| US11685766B2 (en) | 2019-05-08 | 2023-06-27 | Creighton University | 14-3-3 targeting peptides for cancer treatment |
| US11518784B2 (en) * | 2019-05-08 | 2022-12-06 | Creighton University | 14-3-3 targeting peptides for cancer treatment |
| WO2021231237A2 (en) * | 2020-05-11 | 2021-11-18 | Augmenta Bioworks, Inc. | Antibodies for sars-cov-2 and uses thereof |
| US11981718B2 (en) | 2020-05-27 | 2024-05-14 | Ampsource Biopharma Shanghai Inc. | Dual-function protein for lipid and blood glucose regulation |
| WO2021262880A2 (en) * | 2020-06-23 | 2021-12-30 | Kadmon Corporation, Llc | Anti-pd-1 antibodies and fusion proteins |
| US12054551B2 (en) | 2020-07-02 | 2024-08-06 | Sanofi | FGFR1/KLB targeting agonistic antigen-binding proteins and conjugates thereof with GLP-1R agonistic peptides |
| IL300537A (en) * | 2020-08-10 | 2023-04-01 | Gv20 Therapeutics Llc | Compositions and methods for treating autoimmune diseases and cancer by targeting IGSF8 |
| CN118451109A (zh) * | 2021-12-30 | 2024-08-06 | 上海津曼特生物科技有限公司 | 抗βKlotho抗体及其应用 |
| US12188328B2 (en) | 2023-05-15 | 2025-01-07 | Saudi Arabian Oil Company | Wellbore back pressure valve with pressure gauge |
Family Cites Families (185)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| 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 |
| US4263428A (en) | 1978-03-24 | 1981-04-21 | The Regents Of The University Of California | Bis-anthracycline nucleic acid function inhibitors and improved method for administering the same |
| JPS6023084B2 (ja) | 1979-07-11 | 1985-06-05 | 味の素株式会社 | 代用血液 |
| US4399216A (en) | 1980-02-25 | 1983-08-16 | The Trustees Of Columbia University | Processes for inserting DNA into eucaryotic cells and for producing proteinaceous materials |
| US4376110A (en) | 1980-08-04 | 1983-03-08 | Hybritech, Incorporated | Immunometric assays using monoclonal antibodies |
| IE52535B1 (en) | 1981-02-16 | 1987-12-09 | Ici Plc | Continuous release pharmaceutical compositions |
| US4640835A (en) | 1981-10-30 | 1987-02-03 | Nippon Chemiphar Company, Ltd. | Plasminogen activator derivatives |
| EP0088046B1 (de) | 1982-02-17 | 1987-12-09 | Ciba-Geigy Ag | Lipide in wässriger Phase |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| HUT35524A (en) | 1983-08-02 | 1985-07-29 | Hoechst Ag | Process for preparing pharmaceutical compositions containing regulatory /regulative/ peptides providing for the retarded release of the active substance |
| EP0143949B1 (en) | 1983-11-01 | 1988-10-12 | TERUMO KABUSHIKI KAISHA trading as TERUMO CORPORATION | Pharmaceutical composition containing urokinase |
| US4496689A (en) | 1983-12-27 | 1985-01-29 | Miles Laboratories, Inc. | Covalently attached complex of alpha-1-proteinase inhibitor with a water soluble polymer |
| US4740461A (en) | 1983-12-27 | 1988-04-26 | Genetics Institute, Inc. | Vectors and methods for transformation of eucaryotic cells |
| DE3572982D1 (en) | 1984-03-06 | 1989-10-19 | Takeda Chemical Industries Ltd | Chemically modified lymphokine and production thereof |
| US4945050A (en) | 1984-11-13 | 1990-07-31 | Cornell Research Foundation, Inc. | Method for transporting substances into living cells and tissues and apparatus therefor |
| US4751180A (en) | 1985-03-28 | 1988-06-14 | Chiron Corporation | Expression using fused genes providing for protein product |
| EP0206448B1 (en) | 1985-06-19 | 1990-11-14 | Ajinomoto Co., Inc. | Hemoglobin combined with a poly(alkylene oxide) |
| US4935233A (en) | 1985-12-02 | 1990-06-19 | G. D. Searle And Company | Covalently linked polypeptide cell modulators |
| WO1987005330A1 (en) | 1986-03-07 | 1987-09-11 | Michel Louis Eugene Bergh | Method for enhancing glycoprotein stability |
| CA1310924C (en) | 1986-04-24 | 1992-12-01 | Francis P. Mccormick | Infective drug delivery system |
| US4791192A (en) | 1986-06-26 | 1988-12-13 | Takeda Chemical Industries, Ltd. | Chemically modified protein with polyethyleneglycol |
| US4959455A (en) | 1986-07-14 | 1990-09-25 | Genetics Institute, Inc. | Primate hematopoietic growth factors IL-3 and pharmaceutical compositions |
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| US4912040A (en) | 1986-11-14 | 1990-03-27 | Genetics Institute, Inc. | Eucaryotic expression system |
| US5011912A (en) | 1986-12-19 | 1991-04-30 | Immunex Corporation | Hybridoma and monoclonal antibody for use in an immunoaffinity purification system |
| US4970154A (en) | 1987-10-09 | 1990-11-13 | Baylor College Of Medicine | Method for inserting foreign genes into cells using pulsed radiofrequency |
| US4965195A (en) | 1987-10-26 | 1990-10-23 | Immunex Corp. | Interleukin-7 |
| EP0315456B1 (en) | 1987-11-05 | 1994-06-01 | Hybritech Incorporated | Polysaccharide-modified immunoglobulins having reduced immunogenic potential or improved pharmacokinetics |
| US4892538A (en) | 1987-11-17 | 1990-01-09 | Brown University Research Foundation | In vivo delivery of neurotransmitters by implanted, encapsulated cells |
| US5106627A (en) | 1987-11-17 | 1992-04-21 | Brown University Research Foundation | Neurological therapy devices |
| US5158881A (en) | 1987-11-17 | 1992-10-27 | Brown University Research Foundation | Method and system for encapsulating cells in a tubular extrudate in separate cell compartments |
| US4968607A (en) | 1987-11-25 | 1990-11-06 | Immunex Corporation | Interleukin-1 receptors |
| US5011472A (en) | 1988-09-06 | 1991-04-30 | Brown University Research Foundation | Implantable delivery system for biological factors |
| GB8823869D0 (en) | 1988-10-12 | 1988-11-16 | Medical Res Council | Production of antibodies |
| WO1990005183A1 (en) | 1988-10-31 | 1990-05-17 | Immunex Corporation | Interleukin-4 receptors |
| JP2989002B2 (ja) | 1988-12-22 | 1999-12-13 | キリン―アムジエン・インコーポレーテツド | 化学修飾顆粒球コロニー刺激因子 |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US5288855A (en) | 1989-01-23 | 1994-02-22 | Farmitalia Carlo Erba | Extracellular form of the human fibroblast growth factor receptor |
| JP3039802B2 (ja) | 1989-07-06 | 2000-05-08 | ザ リージェンツ オブザ ユニバーシティ オブ カリフォルニア | 繊維芽細胞成長因子のための受容体 |
| US5683888A (en) | 1989-07-22 | 1997-11-04 | University Of Wales College Of Medicine | Modified bioluminescent proteins and their use |
| US5676954A (en) | 1989-11-03 | 1997-10-14 | Vanderbilt University | Method of in vivo delivery of functioning foreign genes |
| US5272071A (en) | 1989-12-22 | 1993-12-21 | Applied Research Systems Ars Holding N.V. | Method for the modification of the expression characteristics of an endogenous gene of a given cell line |
| ATE156189T1 (de) | 1989-12-22 | 1997-08-15 | Applied Research Systems | Modifikation der endogenen genexpression mit hilfe eines regulatorischen elements mittels homologe rekombination |
| US5292658A (en) | 1989-12-29 | 1994-03-08 | University Of Georgia Research Foundation, Inc. Boyd Graduate Studies Research Center | Cloning and expressions of Renilla luciferase |
| WO1991010470A1 (en) | 1990-01-08 | 1991-07-25 | Brown University Research Foundation | Devices and methods for enhanced delivery of active factors |
| ATE139258T1 (de) | 1990-01-12 | 1996-06-15 | Cell Genesys Inc | Erzeugung xenogener antikörper |
| US6673986B1 (en) | 1990-01-12 | 2004-01-06 | Abgenix, Inc. | Generation of xenogeneic antibodies |
| US6713610B1 (en) | 1990-01-12 | 2004-03-30 | Raju Kucherlapati | Human antibodies derived from immunized xenomice |
| US5672510A (en) | 1990-01-19 | 1997-09-30 | Genetic Therapy, Inc. | Retroviral vectors |
| WO1991018982A1 (en) | 1990-06-05 | 1991-12-12 | Immunex Corporation | Type ii interleukin-1 receptors |
| GB9014932D0 (en) | 1990-07-05 | 1990-08-22 | Celltech Ltd | Recombinant dna product and method |
| US5874299A (en) | 1990-08-29 | 1999-02-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5661016A (en) | 1990-08-29 | 1997-08-26 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US5877397A (en) | 1990-08-29 | 1999-03-02 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US5625126A (en) | 1990-08-29 | 1997-04-29 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US6300129B1 (en) | 1990-08-29 | 2001-10-09 | Genpharm International | Transgenic non-human animals for producing heterologous antibodies |
| US5789650A (en) | 1990-08-29 | 1998-08-04 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| AU8507191A (en) | 1990-08-29 | 1992-03-30 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US6255458B1 (en) | 1990-08-29 | 2001-07-03 | Genpharm International | High affinity human antibodies and human antibodies against digoxin |
| US5770429A (en) | 1990-08-29 | 1998-06-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
| US5814318A (en) | 1990-08-29 | 1998-09-29 | Genpharm International Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5217889A (en) | 1990-10-19 | 1993-06-08 | Roninson Igor B | Methods and applications for efficient genetic suppressor elements |
| US5252714A (en) | 1990-11-28 | 1993-10-12 | The University Of Alabama In Huntsville | Preparation and use of polyethylene glycol propionaldehyde |
| US5229501A (en) | 1991-01-11 | 1993-07-20 | Chiron Corporation | Expression and use of human fibroblast growth factor receptor |
| ES2142801T3 (es) | 1991-03-11 | 2000-05-01 | Univ Georgia Res Found | Clonacion y expresion de luciferasa de renilla. |
| US6565841B1 (en) | 1991-03-15 | 2003-05-20 | Amgen, Inc. | Pulmonary administration of granulocyte colony stimulating factor |
| CA2111348A1 (en) | 1991-06-14 | 1992-12-23 | John S. Logan | Production of human hemoglobin in transgenic pigs |
| WO1994004679A1 (en) | 1991-06-14 | 1994-03-03 | Genentech, Inc. | Method for making humanized antibodies |
| EP0593592B1 (en) | 1991-07-08 | 1998-03-25 | The University Of Massachusetts At Amherst | Thermotropic liquid crystal segmented block copolymer |
| US5262522A (en) | 1991-11-22 | 1993-11-16 | Immunex Corporation | Receptor for oncostatin M and leukemia inhibitory factor |
| IL100219A0 (en) | 1991-12-02 | 1992-09-06 | Yeda Res & Dev | Variable region within fibroblast growth factor receptors that confers ligand specificity |
| JPH05244982A (ja) | 1991-12-06 | 1993-09-24 | Sumitomo Chem Co Ltd | 擬人化ｂ−ｂ１０ |
| WO1993015722A1 (en) | 1992-02-07 | 1993-08-19 | Syntex (Usa) Inc. | Controlled delivery of pharmaceuticals from preformed porous microparticles |
| US5234784A (en) | 1992-04-01 | 1993-08-10 | Eastman Kodak Company | Method of making a projection viewable transparency comprising an electrostatographic toner image |
| US5364791A (en) | 1992-05-14 | 1994-11-15 | Elisabetta Vegeto | Progesterone receptor having C. terminal hormone binding domain truncations |
| WO1994000599A2 (en) | 1992-06-18 | 1994-01-06 | Whittier Institute For Diabetes And Endocrinology | Process for detection of neoplastic disease |
| NZ255101A (en) | 1992-07-24 | 1997-08-22 | Cell Genesys Inc | A yeast artificial chromosome (yac) vector containing an hprt minigene expressible in murine stem cells and genetically modified rodent therefor |
| JP3589665B2 (ja) | 1992-10-23 | 2004-11-17 | イミュネックス・コーポレーション | 可溶性オリゴマー蛋白質の調製法 |
| US5489743A (en) | 1993-01-19 | 1996-02-06 | Amgen Inc. | Transgenic animal models for thrombocytopenia |
| US5581476A (en) | 1993-01-28 | 1996-12-03 | Amgen Inc. | Computer-based methods and articles of manufacture for preparing G-CSF analogs |
| US6664107B1 (en) | 1993-05-26 | 2003-12-16 | Ontario Cancer Institute, University Health Network | CD45 disrupted nucleic acid |
| CA2161015A1 (en) | 1993-05-26 | 1994-12-08 | Tak Wah Mak | Transgenic mammals lacking expression of particular cd45 isoforms |
| US5589362A (en) | 1993-06-14 | 1996-12-31 | Basf Aktiengesellschaft | Tetracycline regulated transcriptional modulators with altered DNA binding specificities |
| US5654168A (en) | 1994-07-01 | 1997-08-05 | Basf Aktiengesellschaft | Tetracycline-inducible transcriptional activator and tetracycline-regulated transcription units |
| WO1994029442A2 (en) | 1993-06-14 | 1994-12-22 | Basf Aktiengesellschaft | Tight control of gene expression in eucaryotic cells by tetracycline-responsive promoters |
| US5457035A (en) | 1993-07-23 | 1995-10-10 | Immunex Corporation | Cytokine which is a ligand for OX40 |
| AU7568094A (en) | 1993-08-12 | 1995-03-14 | Cytotherapeutics, Inc. | Improved compositions and methods for the delivery of biologically active molecules using genetically altered cells contained in biocompatible immunoisolatory capsules |
| DE69435112D1 (de) | 1993-09-10 | 2008-08-21 | Univ Columbia | Verwendung von grünem fluoreszenzprotein |
| WO1995021191A1 (en) | 1994-02-04 | 1995-08-10 | William Ward | Bioluminescent indicator based upon the expression of a gene for a modified green-fluorescent protein |
| US5658785A (en) | 1994-06-06 | 1997-08-19 | Children's Hospital, Inc. | Adeno-associated virus materials and methods |
| US5484720A (en) | 1994-09-08 | 1996-01-16 | Genentech, Inc. | Methods for calcium phosphate transfection |
| US5824784A (en) | 1994-10-12 | 1998-10-20 | Amgen Inc. | N-terminally chemically modified protein compositions and methods |
| US5777079A (en) | 1994-11-10 | 1998-07-07 | The Regents Of The University Of California | Modified green fluorescent proteins |
| 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 |
| EP0822830B1 (en) | 1995-04-27 | 2008-04-02 | Amgen Fremont Inc. | Human anti-IL-8 antibodies, derived from immunized xenomice |
| CZ372297A3 (cs) | 1995-05-26 | 1998-03-18 | Zeneca Limited | Přepínání genové exprese využívající receptoru pro ekdyson |
| WO1996040958A1 (en) | 1995-06-07 | 1996-12-19 | Baylor College Of Medicine | Nucleic acid transporters for delivery of nucleic acids into a cell |
| WO1996041865A1 (en) | 1995-06-07 | 1996-12-27 | Ariad Gene Therapeutics, Inc. | Rapamcycin-based regulation of biological events |
| US5874304A (en) | 1996-01-18 | 1999-02-23 | University Of Florida Research Foundation, Inc. | Humanized green fluorescent protein genes and methods |
| US5804387A (en) | 1996-02-01 | 1998-09-08 | The Board Of Trustees Of The Leland Stanford Junior University | FACS-optimized mutants of the green fluorescent protein (GFP) |
| US5876995A (en) | 1996-02-06 | 1999-03-02 | Bryan; Bruce | Bioluminescent novelty items |
| ATE465149T1 (de) | 1996-02-28 | 2010-05-15 | Ariad Pharma Inc | Synthetische rapamycinderivate als multimerisierende wirkstoffe für chimere proteine mit von immunophilin abgeleiteten domänen |
| JP4046354B2 (ja) | 1996-03-18 | 2008-02-13 | 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 | 増大した半減期を有する免疫グロブリン様ドメイン |
| US5679559A (en) | 1996-07-03 | 1997-10-21 | University Of Utah Research Foundation | Cationic polymer and lipoprotein-containing system for gene delivery |
| US5925558A (en) | 1996-07-16 | 1999-07-20 | The Regents Of The University Of California | Assays for protein kinases using fluorescent protein substrates |
| US5976796A (en) | 1996-10-04 | 1999-11-02 | Loma Linda University | Construction and expression of renilla luciferase and green fluorescent protein fusion genes |
| US6214795B1 (en) | 1996-11-12 | 2001-04-10 | Praecis Pharmaceuticals, Inc. | Peptide compounds useful for modulating FGF receptor activity |
| EP1500329B1 (en) | 1996-12-03 | 2012-03-21 | Amgen Fremont Inc. | Human antibodies that specifically bind human TNF alpha |
| JP3795533B2 (ja) | 1996-12-12 | 2006-07-12 | プロルーム・リミテツド | 感染性物質を検出及び同定するための方法及び装置 |
| KR20000062345A (ko) | 1996-12-26 | 2000-10-25 | 히라타 다다시 | 신규 폴리펩타이드, 신규 ｄｎａ 및 신규 항체 |
| CA2196496A1 (en) | 1997-01-31 | 1998-07-31 | Stephen William Watson Michnick | Protein fragment complementation assay for the detection of protein-protein interactions |
| US6133426A (en) | 1997-02-21 | 2000-10-17 | Genentech, Inc. | Humanized anti-IL-8 monoclonal antibodies |
| US6235883B1 (en) * | 1997-05-05 | 2001-05-22 | Abgenix, Inc. | Human monoclonal antibodies to epidermal growth factor receptor |
| US6342220B1 (en) | 1997-08-25 | 2002-01-29 | Genentech, Inc. | Agonist antibodies |
| GB9722131D0 (en) | 1997-10-20 | 1997-12-17 | Medical Res Council | Method |
| US6150098A (en) | 1998-02-20 | 2000-11-21 | Amgen Inc. | Methods for identifying novel secreted mammalian polypeptides |
| WO1999049019A2 (en) | 1998-03-27 | 1999-09-30 | Prolume, Ltd. | Luciferases, fluorescent proteins, nucleic acids encoding the luciferases and fluorescent proteins and the use thereof in diagnostics |
| US20020142374A1 (en) | 1998-08-17 | 2002-10-03 | Michael Gallo | Generation of modified molecules with increased serum half-lives |
| US6548634B1 (en) | 1998-09-30 | 2003-04-15 | Chiron Corporation | Synthetic peptides having FGF receptor affinity |
| US6660843B1 (en) | 1998-10-23 | 2003-12-09 | Amgen Inc. | Modified peptides as therapeutic agents |
| WO2000054813A2 (en) | 1999-03-15 | 2000-09-21 | Chiron Corporation | Use of recombinant gene delivery vectors for treating or preventing diseases of the eye |
| US6833268B1 (en) | 1999-06-10 | 2004-12-21 | Abgenix, Inc. | Transgenic animals for producing specific isotypes of human antibodies via non-cognate switch regions |
| CA2311201A1 (en) | 1999-08-05 | 2001-02-05 | Genset S.A. | Ests and encoded human proteins |
| US7408047B1 (en) | 1999-09-07 | 2008-08-05 | Amgen Inc. | Fibroblast growth factor-like polypeptides |
| US7459540B1 (en) | 1999-09-07 | 2008-12-02 | Amgen Inc. | Fibroblast growth factor-like polypeptides |
| AU7368100A (en) | 1999-09-10 | 2001-04-10 | Curagen Corporation | Fibroblast growth factor polypeptide and nucleic acids encoding same |
| WO2001032678A1 (en) | 1999-11-05 | 2001-05-10 | Smithkline Beecham Corporation | sbgFGF-19a |
| US6716626B1 (en) | 1999-11-18 | 2004-04-06 | Chiron Corporation | Human FGF-21 nucleic acids |
| ES2335386T3 (es) | 1999-11-18 | 2010-03-26 | Novartis Vaccines And Diagnostics, Inc. | Gen fgf-21 humano y productos de expresion genica. |
| AU1628101A (en) | 1999-11-22 | 2001-06-04 | Millennium Pharmaceuticals, Inc. | Jaffa, a novel fibroblast growth factor family member and uses therefor |
| GB9928787D0 (en) | 1999-12-03 | 2000-02-02 | Medical Res Council | Direct screening method |
| US7108984B2 (en) | 2000-01-12 | 2006-09-19 | Mount Sinai School Of Medicine | Methods of identifying modulators of the FGF receptor |
| US20020081663A1 (en) | 2000-01-05 | 2002-06-27 | Conklin Darrell C. | Novel FGF homolog ZFGF11 |
| WO2001049849A1 (en) | 2000-01-05 | 2001-07-12 | Zymogenetics, Inc. | Novel fgf homolog zfgf11 |
| AU5056501A (en) | 2000-03-31 | 2001-10-08 | Nobuyuki Itoh | Fibroblast growth factor-like molecules and uses thereof |
| GB0025144D0 (en) | 2000-10-13 | 2000-11-29 | Medical Res Council | Concatenated nucleic acid sequences |
| IL139380A0 (en) | 2000-10-31 | 2001-11-25 | Prochon Biotech Ltd | Active variants of fibroblast growth factor |
| US20060223114A1 (en) | 2001-04-26 | 2006-10-05 | Avidia Research Institute | Protein scaffolds and uses thereof |
| US20030157561A1 (en) | 2001-11-19 | 2003-08-21 | Kolkman Joost A. | Combinatorial libraries of monomer domains |
| US20040018499A1 (en) | 2001-06-06 | 2004-01-29 | Lal Preeti G | Extracellular messengers |
| JP4444652B2 (ja) | 2001-07-11 | 2010-03-31 | マキシゲン・ホールディングズ・リミテッド | Ｇ−ｃｓｆ結合体 |
| AU2002322394A1 (en) | 2001-07-30 | 2003-02-17 | Eli Lilly And Company | Method for treating diabetes and obesity |
| WO2003038054A2 (en) | 2001-10-31 | 2003-05-08 | New York University | Structure-based design and synthesis of fgf inhibitors and fgf modulator compounds |
| JP2005519891A (ja) | 2002-01-15 | 2005-07-07 | イーライ・リリー・アンド・カンパニー | 危篤状態の患者における罹病率および死亡率を低下させる方法 |
| DE60336452D1 (de) | 2002-01-31 | 2011-05-05 | Max Planck Gesellschaft | Fgfr agoniste |
| EP1332761A1 (en) | 2002-01-31 | 2003-08-06 | Max-Planck-Gesellschaft zur Förderung der Wissenschaften e.V. | Agonists of fibroblast growth factor receptors (FGFR) |
| IL149562A0 (en) | 2002-05-09 | 2002-11-10 | Prochon Ltd | Fgf variants and methods for use thereof |
| US20040202995A1 (en) | 2003-04-09 | 2004-10-14 | Domantis | Nucleic acids, proteins, and screening methods |
| NZ543292A (en) | 2003-06-12 | 2008-04-30 | Lilly Co Eli | GLP-1 analog fusion proteins |
| US20070253966A1 (en) | 2003-06-12 | 2007-11-01 | Eli Lilly And Company | Fusion Proteins |
| PL1680140T3 (pl) | 2003-10-16 | 2011-11-30 | Imclone Llc | Inhibitory receptora-1 czynnika wzrostu fibroblastów i związane z nim sposoby leczenia |
| WO2005061712A1 (en) | 2003-12-10 | 2005-07-07 | Eli Lilly And Company | Muteins of fibroblast growth factor 21 |
| WO2005072769A1 (en) | 2004-01-26 | 2005-08-11 | Eli Lilly And Company | Use of fgf-21 and thiazolidinedione for treating type 2 diabetes |
| CA2557782A1 (en) | 2004-03-17 | 2005-10-06 | Eli Lilly And Company | Glycol linked fgf-21 compounds |
| JP4505631B2 (ja) | 2004-03-31 | 2010-07-21 | 独立行政法人産業技術総合研究所 | ヘパラン硫酸糖鎖を付加したヘパリン結合性タンパク質、その製造方法及びそれを含有する医薬組成物 |
| PT1751184E (pt) | 2004-05-13 | 2009-11-10 | Lilly Co Eli | Proteínas de fusão de fgf-21 |
| WO2006028714A1 (en) | 2004-09-02 | 2006-03-16 | Eli Lilly And Company | Muteins of fibroblast growth factor 21 |
| SI1789442T1 (sl) | 2004-09-02 | 2010-01-29 | Lilly Co Eli | Proteinske mutante fibroblastnega rastnega faktorja 21 |
| EP3061461A1 (en) | 2004-10-29 | 2016-08-31 | ratiopharm GmbH | Remodeling and glycopegylation of fibroblast growth factor (fgf) |
| EP1831371A2 (en) | 2004-12-14 | 2007-09-12 | Eli Lilly And Company | Muteins of fibroblast growth factor 21 |
| EP1846019A2 (en) | 2005-01-21 | 2007-10-24 | Eli Lilly And Company | Method for treating cardiovascular disease |
| JP2006246823A (ja) | 2005-03-11 | 2006-09-21 | Kyoto Univ | 造血因子としてのＦｇｆ２１の使用 |
| WO2006130527A2 (en) | 2005-05-31 | 2006-12-07 | Novartis Ag | Mutations and polymorphisms of fibroblast growth factor receptor 1 |
| EP1910542B1 (en) | 2005-07-22 | 2009-12-02 | Five Prime Therapeutics, Inc. | Compositions and methods of treating disease with fgfr fusion proteins |
| US8043833B2 (en) | 2005-10-31 | 2011-10-25 | Novo Nordisk A/S | Expression of soluble therapeutic proteins |
| CA2644046A1 (en) | 2006-02-28 | 2007-09-07 | Trustees Of Boston University | Metabolic regulators and uses thereof |
| US9187532B2 (en) | 2006-07-21 | 2015-11-17 | Novo Nordisk A/S | Glycosylation of peptides via O-linked glycosylation sequences |
| WO2008057683A2 (en) | 2006-10-03 | 2008-05-15 | Novo Nordisk A/S | Methods for the purification of polypeptide conjugates |
| WO2008066498A1 (en) | 2006-12-01 | 2008-06-05 | Agency For Science, Technology And Research | Cancer-related protein kinases |
| ES2385114T3 (es) | 2007-03-30 | 2012-07-18 | Ambrx, Inc. | Polipéptidos de FGF-21 modificados y sus usos |
| ES2665996T3 (es) | 2007-04-02 | 2018-04-30 | Genentech, Inc. | Anticuerpo agonista de klotho-beta para utilizar en el tratamiento de diabetes mellitus o resistencia a la insulina |
| JP5187837B2 (ja) | 2007-04-06 | 2013-04-24 | 独立行政法人産業技術総合研究所 | 補助因子による受容体の活性化方法並びにリガンド活性の利用方法 |
| US7537903B2 (en) * | 2007-04-23 | 2009-05-26 | Board Of Regents, The University Of Texas System | FGF21 upregulates expression of GLUT-1 in a βklotho-dependent manner |
| KR20100017169A (ko) | 2007-05-22 | 2010-02-16 | 노파르티스 아게 | Ｆｇｆ２１-관련 장애의 치료, 진단 및 검출 방법 |
| WO2008151258A2 (en) | 2007-06-04 | 2008-12-11 | Neose Technologies, Inc. | O-linked glycosylation using n-acetylglucosaminyl transferases |
| JP2010535781A (ja) | 2007-08-03 | 2010-11-25 | イーライ リリー アンド カンパニー | 肥満に対する処置 |
| TW200936156A (en) | 2008-01-28 | 2009-09-01 | Novartis Ag | Methods and compositions using Klotho-FGF fusion polypeptides |
| JOP20190083A1 (ar) | 2008-06-04 | 2017-06-16 | Amgen Inc | بولي ببتيدات اندماجية طافرة لـfgf21 واستخداماتها |
| WO2010006214A1 (en) | 2008-07-09 | 2010-01-14 | Ambrx, Inc. | Fgf-21 neutralizing antibodies and their uses |
| SG10201402038WA (en) | 2009-05-05 | 2014-07-30 | Amgen Inc | FGF21 Mutants And Uses Thereof |
| WO2013180295A1 (ja) | 2012-06-01 | 2013-12-05 | 日本電信電話株式会社 | パケット転送処理方法およびパケット転送処理装置 |
| US9300829B2 (en) | 2014-04-04 | 2016-03-29 | Canon Kabushiki Kaisha | Image reading apparatus and correction method thereof |
-
2011
- 2011-04-13 JP JP2013505101A patent/JP2013523184A/ja active Pending
- 2011-04-13 AU AU2011239689A patent/AU2011239689A1/en not_active Abandoned
- 2011-04-13 MX MX2012011986A patent/MX2012011986A/es not_active Application Discontinuation
- 2011-04-13 WO PCT/US2011/032333 patent/WO2011130417A2/en not_active Ceased
- 2011-04-13 CA CA2796055A patent/CA2796055A1/en not_active Abandoned
- 2011-04-13 US US13/641,041 patent/US9517264B2/en active Active
- 2011-04-13 EP EP11715374A patent/EP2558497A2/en not_active Ceased
- 2011-04-13 EP EP19200863.9A patent/EP3670534A3/en active Pending
Also Published As
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|---|---|
| EP3670534A3 (en) | 2020-09-09 |
| US20130129725A1 (en) | 2013-05-23 |
| JP2013523184A (ja) | 2013-06-17 |
| US9517264B2 (en) | 2016-12-13 |
| AU2011239689A1 (en) | 2012-11-08 |
| EP3670534A2 (en) | 2020-06-24 |
| WO2011130417A3 (en) | 2012-03-08 |
| WO2011130417A2 (en) | 2011-10-20 |
| EP2558497A2 (en) | 2013-02-20 |
| CA2796055A1 (en) | 2011-10-20 |
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