ES2362424T3 - Biblioteca del dominio kunitz. - Google Patents
Biblioteca del dominio kunitz. Download PDFInfo
- Publication number
- ES2362424T3 ES2362424T3 ES04700617T ES04700617T ES2362424T3 ES 2362424 T3 ES2362424 T3 ES 2362424T3 ES 04700617 T ES04700617 T ES 04700617T ES 04700617 T ES04700617 T ES 04700617T ES 2362424 T3 ES2362424 T3 ES 2362424T3
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- Prior art keywords
- phage
- library
- protein
- kunitz domain
- amino acid
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
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- 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
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1034—Isolating an individual clone by screening libraries
- C12N15/1037—Screening libraries presented on the surface of microorganisms, e.g. phage display, E. coli display
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- Health & Medical Sciences (AREA)
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Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US43849103P | 2003-01-07 | 2003-01-07 | |
| US438491P | 2003-01-07 |
Publications (1)
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| ES2362424T3 true ES2362424T3 (es) | 2011-07-05 |
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Country Status (11)
| Country | Link |
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| US (2) | US20040209243A1 (OSRAM) |
| EP (2) | EP2290107A1 (OSRAM) |
| JP (2) | JP2007524348A (OSRAM) |
| AT (1) | ATE500345T1 (OSRAM) |
| AU (1) | AU2004204095B2 (OSRAM) |
| CA (1) | CA2512590A1 (OSRAM) |
| DE (1) | DE602004031589D1 (OSRAM) |
| DK (1) | DK1587907T3 (OSRAM) |
| ES (1) | ES2362424T3 (OSRAM) |
| PT (1) | PT1587907E (OSRAM) |
| WO (1) | WO2004063337A2 (OSRAM) |
Families Citing this family (62)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6057287A (en) | 1994-01-11 | 2000-05-02 | Dyax Corp. | Kallikrein-binding "Kunitz domain" proteins and analogues thereof |
| ATE529444T1 (de) * | 1994-01-11 | 2011-11-15 | Dyax Corp | Inhibitoren des humanplasmins, die sich von den kunitz domänen ableiten |
| DE60333758D1 (de) | 2002-06-07 | 2010-09-23 | Dyax Corp | Prevention und Verringerung von Ischemia |
| US7153829B2 (en) | 2002-06-07 | 2006-12-26 | Dyax Corp. | Kallikrein-inhibitor therapies |
| US7235530B2 (en) | 2004-09-27 | 2007-06-26 | Dyax Corporation | Kallikrein inhibitors and anti-thrombolytic agents and uses thereof |
| EP1835926A4 (en) * | 2004-11-22 | 2009-04-01 | Dyax Corp | PLASMINE-INHIBITING THERAPIES |
| AR054165A1 (es) * | 2005-07-13 | 2007-06-06 | Avidia Inc | Proteinas de union a il-6 |
| WO2009026334A2 (en) * | 2007-08-21 | 2009-02-26 | Genzyme Corporation | Treatment with kallikrein inhibitors |
| CN104984319B (zh) | 2008-12-19 | 2025-05-09 | 武田药品工业株式会社 | Tfpi抑制剂和使用方法 |
| JP2013516389A (ja) | 2009-01-06 | 2013-05-13 | ダイアックス コーポレーション | カリクレイン阻害剤による粘膜炎治療 |
| SI3459564T1 (sl) | 2010-01-06 | 2022-06-30 | Takeda Pharmaceutical Company Limited | Proteini, ki vežejo plazemski kalikrein |
| EP3146977B1 (en) | 2010-03-19 | 2024-05-08 | Takeda Pharmaceutical Company Limited | Tfpi inhibitors and methods of use |
| JP2014506257A (ja) | 2011-01-06 | 2014-03-13 | ダイアックス コーポレーション | 血漿カリクレイン結合タンパク質 |
| KR102263685B1 (ko) | 2012-03-21 | 2021-06-11 | 다케다 야쿠힌 고교 가부시키가이샤 | Tfpi 저해제 및 사용 방법 |
| CA2881431C (en) | 2012-08-08 | 2021-10-19 | Daiichi Sankyo Company, Limited | Peptide library and use thereof |
| IL295414B1 (en) | 2014-03-27 | 2025-10-01 | Takeda Pharmaceuticals Co | Compositions and methods for treating macular edema due to diabetes |
| US9982052B2 (en) | 2014-08-05 | 2018-05-29 | MabQuest, SA | Immunological reagents |
| PL3177644T3 (pl) | 2014-08-05 | 2021-06-14 | MabQuest SA | Immunologiczne reagenty wiążące do PD-1 |
| KR102825102B1 (ko) | 2014-12-24 | 2025-06-26 | 넥스이뮨, 인크. | 면역요법을 위한 나노입자 조성물 및 방법 |
| US11702477B2 (en) | 2015-11-06 | 2023-07-18 | Orionis Biosciences BV | Bi-functional chimeric proteins and uses thereof |
| EP3377080B1 (en) | 2015-11-19 | 2024-02-14 | Asclepix Therapeutics, LLC | Peptides with anti-angiogenic, anti-lymphangiogenic, and anti-edemic properties and nanoparticle formulations |
| US11286307B2 (en) | 2015-12-11 | 2022-03-29 | Takeda Pharmaceutical Company Limited | Plasma kallikrein inhibitors and uses thereof for treating hereditary angioedema attack |
| EP3405497A2 (en) | 2016-01-22 | 2018-11-28 | Mabquest SA | Immunological reagents |
| US11214617B2 (en) | 2016-01-22 | 2022-01-04 | MabQuest SA | Immunological reagents |
| CA3013554A1 (en) | 2016-02-05 | 2017-08-10 | Orionis Biosciences Nv | Targeted therapeutic agents and uses thereof |
| CA3016849A1 (en) | 2016-03-07 | 2017-09-14 | Vib Vzw | Cd20 binding single domain antibodies |
| CN109689087B (zh) | 2016-05-13 | 2023-04-04 | 奥里尼斯生物科学私人有限公司 | 靶向性突变干扰素-β及其用途 |
| WO2017194782A2 (en) | 2016-05-13 | 2017-11-16 | Orionis Biosciences Nv | Therapeutic targeting of non-cellular structures |
| SG10202103032QA (en) | 2016-10-04 | 2021-05-28 | Asclepix Therapeutics Inc | Compounds and methods for activating tie2 signaling |
| WO2018077893A1 (en) | 2016-10-24 | 2018-05-03 | Orionis Biosciences Nv | Targeted mutant interferon-gamma and uses thereof |
| US11384154B2 (en) | 2017-02-06 | 2022-07-12 | Orionis Biosciences BV | Targeted chimeric proteins and uses thereof |
| US10906985B2 (en) | 2017-02-06 | 2021-02-02 | Orionis Biosciences, Inc. | Targeted engineered interferon and uses thereof |
| WO2018146074A1 (en) | 2017-02-07 | 2018-08-16 | Vib Vzw | Immune-cell targeted bispecific chimeric proteins and uses thereof |
| EP3661536A4 (en) | 2017-08-03 | 2021-07-21 | Asclepix Therapeutics, Inc. | PROCESSES FOR IDENTIFYING AND PREPARING PHARMACEUTICAL AGENTS TO ACTIVATE THE TIE2 RECEPTOR |
| WO2019075056A1 (en) | 2017-10-10 | 2019-04-18 | The Johns Hopkins University | BIODEGRADABLE BIOMIMETIC PARTICLES |
| WO2019094648A1 (en) | 2017-11-08 | 2019-05-16 | L.E.A.F. Holdings Group Llc | Platinum complexes and uses thereof |
| CA3082410A1 (en) | 2017-11-14 | 2019-05-23 | Arcellx, Inc. | Multifunctional immune cell therapies |
| WO2019148089A1 (en) | 2018-01-26 | 2019-08-01 | Orionis Biosciences Inc. | Xcr1 binding agents and uses thereof |
| CA3090406A1 (en) | 2018-02-05 | 2019-08-08 | Orionis Biosciences, Inc. | Fibroblast binding agents and use thereof |
| EP3890773A4 (en) | 2018-11-08 | 2022-11-09 | Orionis Biosciences, Inc. | MODULATION OF DENDRITIC CELL LINES |
| WO2020168024A1 (en) | 2019-02-15 | 2020-08-20 | Integral Molecular, Inc. | Antibodies comprising a common light chain and uses thereof |
| JP7570338B2 (ja) | 2019-02-15 | 2024-10-21 | インテグラル・モレキュラー・インコーポレイテッド | クローディン６抗体及びその使用 |
| EP4010031A1 (en) | 2019-08-06 | 2022-06-15 | L.E.A.F Holdings Group LLC | Processes of preparing polyglutamated antifolates and uses of their compositions |
| GB202004514D0 (en) | 2020-03-27 | 2020-05-13 | Inst De Medicina Molecular Joaeo Lobo Antunes | Treatment of Immunosuppressive Cancer |
| CN119792512A (zh) | 2020-10-14 | 2025-04-11 | 维里迪安治疗公司 | 用于治疗甲状腺眼病的组合物和方法 |
| GB202019817D0 (en) * | 2020-12-15 | 2021-01-27 | Univ Oxford Innovation Ltd | Ligand-binding polypeptides and uses thereof |
| AU2022242842A1 (en) | 2021-03-26 | 2023-10-05 | Arcellx, Inc. | Multifunctional immune cell therapies |
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| US20250304677A1 (en) | 2022-07-04 | 2025-10-02 | Vib Vzw | Blood-Cerebrospinal Fluid Barrier Crossing Antibodies |
| WO2024077118A2 (en) | 2022-10-06 | 2024-04-11 | Bicara Therapeutics Inc. | Multispecific proteins and related methods |
| IL319951A (en) | 2022-11-30 | 2025-05-01 | Integral Molecular Inc | Antibodies targeting claudin 6, including its bispecific formats |
| WO2024208816A1 (en) | 2023-04-03 | 2024-10-10 | Vib Vzw | Blood-brain barrier crossing antibodies |
| WO2025014774A1 (en) | 2023-07-07 | 2025-01-16 | Viridian Therapeutics, Inc. | Methods of treating active and chronic thyroid eye disease |
| WO2025024334A1 (en) | 2023-07-21 | 2025-01-30 | Marrow Therapeutics, Inc. | Hematopoietic cell targeting conjugates and related methods |
| WO2025093683A1 (en) | 2023-11-03 | 2025-05-08 | Neuvasq Biotechnologies Sa | Wnt7 signaling agonists |
| TW202535948A (zh) | 2023-12-17 | 2025-09-16 | 美商維里迪恩醫療股份有限公司 | 用於治療甲狀腺眼病之組合物、劑量及方法 |
| WO2025151502A1 (en) | 2024-01-09 | 2025-07-17 | Viridian Therapeutics, Inc. | Modified antibodies |
| WO2025151492A1 (en) | 2024-01-09 | 2025-07-17 | Viridian Therapeutics, Inc. | Compositions and methods for treatment of thyroid eye disease |
| WO2025151496A1 (en) | 2024-01-09 | 2025-07-17 | Viridian Therapeutics, Inc. | Compositions and methods for treatment of thyroid eye disease |
| US20250375499A1 (en) | 2024-01-26 | 2025-12-11 | Flagship Pioneering Innovations Vii, Llc | Immunoreceptor inhibitory proteins and related methods |
| WO2025240680A1 (en) | 2024-05-16 | 2025-11-20 | Flagship Pioneering Innovations Vii, Llc | Immunoreceptor inhibitory proteins and related methods |
| WO2025245111A1 (en) | 2024-05-22 | 2025-11-27 | Flagship Pioneering Innovations Vii, Llc | Immunoreceptor targeting proteins and related methods |
Family Cites Families (64)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US53206A (en) * | 1866-03-13 | Improvement in linings for artificial limbs | ||
| US38893A (en) * | 1863-06-16 | Improvement in apparatus for the manufacture of salt | ||
| US9690A (en) * | 1853-04-26 | Eadiator fob stoves | ||
| US4475196A (en) | 1981-03-06 | 1984-10-02 | Zor Clair G | Instrument for locating faults in aircraft passenger reading light and attendant call control system |
| US4447233A (en) | 1981-04-10 | 1984-05-08 | Parker-Hannifin Corporation | Medication infusion pump |
| US4439196A (en) | 1982-03-18 | 1984-03-27 | Merck & Co., Inc. | Osmotic drug delivery system |
| US4447224A (en) | 1982-09-20 | 1984-05-08 | Infusaid Corporation | Variable flow implantable infusion apparatus |
| US4487603A (en) | 1982-11-26 | 1984-12-11 | Cordis Corporation | Implantable microinfusion pump system |
| US4486194A (en) | 1983-06-08 | 1984-12-04 | James Ferrara | Therapeutic device for administering medicaments through the skin |
| US4760025A (en) | 1984-05-29 | 1988-07-26 | Genencor, Inc. | Modified enzymes and methods for making same |
| AU560584B2 (en) * | 1983-07-28 | 1987-04-09 | Bayer Aktiengesellschaft | Homologues of aprotinin |
| US4657893A (en) * | 1984-05-09 | 1987-04-14 | Syntex (U.S.A.) Inc. | 4H-3,1-benzoxazin-4-ones and related compounds and use as enzyme inhibitors |
| US4845242A (en) * | 1987-04-28 | 1989-07-04 | Georgia Tech Research Corporation | Isocoumarins with basic substituents as serine proteases inhibitors, anticoagulants and anti-inflammatory agents |
| US4596556A (en) | 1985-03-25 | 1986-06-24 | Bioject, Inc. | Hypodermic injection apparatus |
| US5654176A (en) | 1987-05-28 | 1997-08-05 | Amrad Corporation Limited | Fusion proteins containing glutathione-s-transferase |
| US4790824A (en) | 1987-06-19 | 1988-12-13 | Bioject, Inc. | Non-invasive hypodermic injection device |
| US4941880A (en) | 1987-06-19 | 1990-07-17 | Bioject, Inc. | Pre-filled ampule and non-invasive hypodermic injection device assembly |
| GB2208511A (en) * | 1987-08-07 | 1989-04-05 | Bayer Ag | Variants of bovine pancreatic trypsin inhibitor produced by recombinant dna technology |
| DK225488D0 (da) * | 1988-04-26 | 1988-04-26 | Novo Industri As | Polypeptid |
| DE68927933T2 (de) | 1988-09-02 | 1997-08-14 | Dyax Corp | Herstellung und auswahl von rekombinantproteinen mit verschiedenen bindestellen |
| US5223409A (en) * | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| EP0401508B1 (de) * | 1989-05-13 | 1994-11-23 | Bayer Ag | Proteinaseninhibitoren, Verfahren zu ihrer Herstellung sowie diese enthaltende Arzneimittel |
| US5312335A (en) | 1989-11-09 | 1994-05-17 | Bioject Inc. | Needleless hypodermic injection device |
| US5064413A (en) | 1989-11-09 | 1991-11-12 | Bioject, Inc. | Needleless hypodermic injection device |
| US5278285A (en) * | 1990-02-01 | 1994-01-11 | Bayer Aktiengesellschaft | Variant of Kunitz-type inhibitor derived from the α3-chain of human type VI collagen produced by recombinant DNA technology |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| AU665190B2 (en) | 1990-07-10 | 1995-12-21 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| US5278144A (en) * | 1990-09-04 | 1994-01-11 | Cor Therapeutics, Inc. | Antithrombosis agents |
| US5583107A (en) * | 1990-09-04 | 1996-12-10 | Cor Therapeutics, Inc. | Agents affecting thrombosis and hemostasis |
| US5409895A (en) * | 1990-11-13 | 1995-04-25 | Mochida Pharmaceutical Co., Ltd. | Protease inhibitory polypeptides derived from urinary trypsin inhibitor and compositions thereof |
| DK0564531T3 (da) | 1990-12-03 | 1998-09-28 | Genentech Inc | Berigelsesfremgangsmåde for variantproteiner med ændrede bindingsegenskaber |
| JP3267293B2 (ja) * | 1990-12-03 | 2002-03-18 | ジェネンテク，インコーポレイテッド | 改変された結合性を有する変異タンパク質の豊富化法 |
| DK1279731T3 (da) | 1991-03-01 | 2007-09-24 | Dyax Corp | Fremgangsmåde til udvikling af bindende miniproteiner |
| DK1471142T3 (da) | 1991-04-10 | 2009-03-09 | Scripps Research Inst | Heterodimere receptor-biblioteker under anvendelse af fagemider |
| US5166133A (en) * | 1991-04-17 | 1992-11-24 | Cetus Corporation | Method for inhibing adhesion of white blood cells to endothelial cells |
| DE4122599C2 (de) | 1991-07-08 | 1993-11-11 | Deutsches Krebsforsch | Phagemid zum Screenen von Antikörpern |
| US5866344A (en) * | 1991-11-15 | 1999-02-02 | Board Of Regents, The University Of Texas System | Antibody selection methods using cell surface expressed libraries |
| IL104314A0 (en) * | 1992-01-07 | 1993-05-13 | Novo Nordisk As | Human kunitz-type protease inhibitor and variants thereof,their production and pharmaceutical compositions containing them |
| IL104325A (en) * | 1992-01-07 | 2000-10-31 | Novo Nordisk As | Variants of human kunitz-type protease inhibitor domain II of tissue factor pathway inhibitor (TFPI) pharmaceutical compositions containing them a DNA construct encoding them their expression vectors a cell containing said DNA constructs and methods for the production of all the above |
| IL104327A0 (en) * | 1992-01-07 | 1993-05-13 | Novo Nordisk As | Variant of human kunitz-type protease inhibitor |
| US5869644A (en) | 1992-04-15 | 1999-02-09 | The Johns Hopkins University | Synthesis of diverse and useful collections of oligonucleotidies |
| US5383851A (en) | 1992-07-24 | 1995-01-24 | Bioject Inc. | Needleless hypodermic injection device |
| EP0719334A1 (en) * | 1993-09-14 | 1996-07-03 | Genentech, Inc. | Pharmaceutical compositions containing ecotin and homologs thereof |
| ES2227545T3 (es) * | 1994-01-11 | 2005-04-01 | Dyax Corporation | Proteinas y sus analogos del "dominio de kunitz" inhibidores de calicreina. |
| US6057287A (en) * | 1994-01-11 | 2000-05-02 | Dyax Corp. | Kallikrein-binding "Kunitz domain" proteins and analogues thereof |
| ATE529444T1 (de) * | 1994-01-11 | 2011-11-15 | Dyax Corp | Inhibitoren des humanplasmins, die sich von den kunitz domänen ableiten |
| US5795954A (en) * | 1994-03-04 | 1998-08-18 | Genentech, Inc. | Factor VIIa inhibitors from Kunitz domain proteins |
| US5589359A (en) * | 1994-08-05 | 1996-12-31 | Chiron Corporation | Chimeric proteins |
| DE19507166C1 (de) | 1995-03-01 | 1996-04-18 | Deutsches Krebsforsch | Antikörper gegen ein Histidin-Fusionspolypeptid, das einen Histidin-Anteil aufweist |
| US5786328A (en) * | 1995-06-05 | 1998-07-28 | Genentech, Inc. | Use of kunitz type plasma kallikrein inhibitors |
| AU7071896A (en) * | 1995-09-14 | 1997-04-01 | Lxr Biotechnology Inc. | Compositions with anti-apoptotic activity, containing a mixture of phospholipids |
| US5770265A (en) * | 1995-09-26 | 1998-06-23 | Triangle Laboratories, Inc. | Environmentally friendly treatments to extend the functional life of wood structures and novel treated wood structures |
| US5736364A (en) * | 1995-12-04 | 1998-04-07 | Genentech, Inc. | Factor viia inhibitors |
| US6017723A (en) * | 1998-03-27 | 2000-01-25 | Long Island Jewish Medical Center | Method for isolating inhibitors of protease activity |
| CA2323638A1 (en) | 1998-04-03 | 1999-10-14 | Phylos, Inc. | Addressable protein arrays |
| US6190908B1 (en) * | 1998-08-12 | 2001-02-20 | The Scripps Research Institute | Modulation of polypeptide display on modified filamentous phage |
| JP3763505B2 (ja) | 1998-09-22 | 2006-04-05 | Ｔｄｋ株式会社 | 薄膜磁気ヘッドの製造方法 |
| US6472147B1 (en) | 1999-05-25 | 2002-10-29 | The Scripps Research Institute | Methods for display of heterodimeric proteins on filamentous phage using pVII and pIX, compositions, vectors and combinatorial libraries |
| PT1144607E (pt) | 1999-07-20 | 2009-04-22 | Morphosys Ag | Novos métodos para apresentar (poli)peptídeos/ proteínas em partículas bacteriofágicas através de ligações dissulfureto |
| GB9928787D0 (en) | 1999-12-03 | 2000-02-02 | Medical Res Council | Direct screening method |
| EP1360490B1 (en) | 2001-01-23 | 2011-12-21 | President and Fellows of Harvard College | Nucleic-acid programmable protein arrays |
| US20030186374A1 (en) | 2001-10-01 | 2003-10-02 | Hufton Simon E. | Multi-chain eukaryotic display vectors and uses thereof |
| US20030129659A1 (en) | 2001-12-03 | 2003-07-10 | Whelihan E. Fayelle | Library screening |
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2004
- 2004-01-07 PT PT04700617T patent/PT1587907E/pt unknown
- 2004-01-07 AU AU2004204095A patent/AU2004204095B2/en not_active Ceased
- 2004-01-07 EP EP10012620A patent/EP2290107A1/en not_active Withdrawn
- 2004-01-07 EP EP04700617A patent/EP1587907B1/en not_active Expired - Lifetime
- 2004-01-07 JP JP2006500832A patent/JP2007524348A/ja active Pending
- 2004-01-07 WO PCT/US2004/000333 patent/WO2004063337A2/en not_active Ceased
- 2004-01-07 DK DK04700617.6T patent/DK1587907T3/da active
- 2004-01-07 US US10/753,544 patent/US20040209243A1/en not_active Abandoned
- 2004-01-07 DE DE602004031589T patent/DE602004031589D1/de not_active Expired - Lifetime
- 2004-01-07 CA CA002512590A patent/CA2512590A1/en not_active Abandoned
- 2004-01-07 ES ES04700617T patent/ES2362424T3/es not_active Expired - Lifetime
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2007
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2010
- 2010-02-22 JP JP2010036225A patent/JP2010162030A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| EP2290107A1 (en) | 2011-03-02 |
| US20040209243A1 (en) | 2004-10-21 |
| WO2004063337A2 (en) | 2004-07-29 |
| EP1587907A2 (en) | 2005-10-26 |
| CA2512590A1 (en) | 2004-07-29 |
| ATE500345T1 (de) | 2011-03-15 |
| DK1587907T3 (da) | 2011-04-04 |
| JP2007524348A (ja) | 2007-08-30 |
| EP1587907B1 (en) | 2011-03-02 |
| JP2010162030A (ja) | 2010-07-29 |
| EP1587907A4 (en) | 2007-11-14 |
| PT1587907E (pt) | 2011-04-08 |
| WO2004063337A3 (en) | 2007-01-25 |
| DE602004031589D1 (de) | 2011-04-14 |
| AU2004204095A1 (en) | 2004-07-29 |
| AU2004204095B2 (en) | 2009-07-30 |
| US20080020394A1 (en) | 2008-01-24 |
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