EA014182B1 - КОМПОЗИЦИЯ ПОЛИКЛОНАЛЬНЫХ АНТИ-RhD АНТИТЕЛ, СПОСОБ ЕЁ ПОЛУЧЕНИЯ И ПРИМЕНЕНИЕ КОМПОЗИЦИИ - Google Patents
КОМПОЗИЦИЯ ПОЛИКЛОНАЛЬНЫХ АНТИ-RhD АНТИТЕЛ, СПОСОБ ЕЁ ПОЛУЧЕНИЯ И ПРИМЕНЕНИЕ КОМПОЗИЦИИ Download PDFInfo
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- EA014182B1 EA014182B1 EA200700249A EA200700249A EA014182B1 EA 014182 B1 EA014182 B1 EA 014182B1 EA 200700249 A EA200700249 A EA 200700249A EA 200700249 A EA200700249 A EA 200700249A EA 014182 B1 EA014182 B1 EA 014182B1
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- C07K2317/77—Internalization into the cell
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Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DKPA200401133 | 2004-07-20 | ||
| DKPA200401992 | 2004-12-22 | ||
| PCT/DK2005/000501 WO2006007850A1 (en) | 2004-07-20 | 2005-07-18 | Anti-rhesus d recombinant polyclonal antibody and methods of manufacture |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| EA200700249A1 EA200700249A1 (ru) | 2007-06-29 |
| EA014182B1 true EA014182B1 (ru) | 2010-10-29 |
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| Application Number | Title | Priority Date | Filing Date |
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| EA200700249A EA014182B1 (ru) | 2004-07-20 | 2005-07-18 | КОМПОЗИЦИЯ ПОЛИКЛОНАЛЬНЫХ АНТИ-RhD АНТИТЕЛ, СПОСОБ ЕЁ ПОЛУЧЕНИЯ И ПРИМЕНЕНИЕ КОМПОЗИЦИИ |
Country Status (13)
| Country | Link |
|---|---|
| US (2) | US8198415B2 (enExample) |
| EP (2) | EP1771483A1 (enExample) |
| JP (1) | JP4926054B2 (enExample) |
| KR (1) | KR20070038556A (enExample) |
| AU (1) | AU2005263331B8 (enExample) |
| BR (1) | BRPI0513706A (enExample) |
| CA (1) | CA2574062A1 (enExample) |
| EA (1) | EA014182B1 (enExample) |
| IL (1) | IL179658A (enExample) |
| MX (1) | MX2007000644A (enExample) |
| NO (1) | NO20070927L (enExample) |
| NZ (1) | NZ552265A (enExample) |
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2770654C1 (ru) * | 2021-06-17 | 2022-04-20 | Федеральное государственное бюджетное образовательное учреждение высшего образования "Санкт-Петербургский государственный педиатрический медицинский университет" Министерства здравоохранения Российской Федерации (ФГБОУ ВО СПбГПМУ Минздрава России) | Способ профилактики тяжелой формы гемолитической болезни новорожденных при резус-иммунизации у беременных с соматической патологией и потерями плода в анамнезе |
Families Citing this family (49)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7658924B2 (en) | 2001-10-11 | 2010-02-09 | Amgen Inc. | Angiopoietin-2 specific binding agents |
| CA2512647C (en) * | 2003-01-07 | 2013-10-08 | Symphogen A/S | Method for manufacturing recombinant polyclonal proteins |
| AR045563A1 (es) | 2003-09-10 | 2005-11-02 | Warner Lambert Co | Anticuerpos dirigidos a m-csf |
| TWI333977B (en) | 2003-09-18 | 2010-12-01 | Symphogen As | Method for linking sequences of interest |
| RU2426795C2 (ru) | 2004-07-20 | 2011-08-20 | Симфоген А/С | Способ структурной характеристики рекомбинантного поликлонального белка или поликлональной клеточной линии |
| JP2009518320A (ja) * | 2005-12-05 | 2009-05-07 | シュムフォウエン アクティーゼルスカブ | 抗オルトポックスウイルス組換えポリクローナル抗体 |
| TW200846362A (en) * | 2007-02-09 | 2008-12-01 | Symphogen As | A polyclonal antibody product |
| MX2009008908A (es) | 2007-03-01 | 2009-08-28 | Symphogen As | Metodo para clonacion de anticuerpos analogos. |
| PL2132229T3 (pl) * | 2007-03-01 | 2016-12-30 | Kompozycje rekombinowanych przeciwciał anty-receptor czynnika wzrostu naskórka | |
| CN101679513A (zh) | 2007-03-06 | 2010-03-24 | 西福根有限公司 | 用于治疗呼吸道合胞病毒感染的重组抗体 |
| NZ581316A (en) * | 2007-05-25 | 2012-02-24 | Symphogen As | Method for manufacturing a recombinant polyclonal protein |
| JP2008289483A (ja) * | 2007-05-25 | 2008-12-04 | Symphogen As | 真核生物系において発現可能な形質転換体のスクリーニング |
| CN101821289A (zh) * | 2007-09-07 | 2010-09-01 | 西福根有限公司 | 重组制造抗rsv抗体的方法 |
| EP2045602A1 (en) | 2007-10-04 | 2009-04-08 | Symphogen A/S | Potency assay |
| CA2702322A1 (en) * | 2007-11-22 | 2009-05-28 | Symphogen A/S | A method for characterization of a recombinant polyclonal protein |
| JO2913B1 (en) | 2008-02-20 | 2015-09-15 | امجين إنك, | Antibodies directed towards angiopoietin-1 and angiopoietin-2 proteins and their uses |
| PT2708559T (pt) * | 2008-04-11 | 2018-05-16 | Chugai Pharmaceutical Co Ltd | Molécula de ligação ao antigénio capaz de se ligar repetidamente a duas ou mais moléculas de antigénio |
| BRPI0910454A2 (pt) * | 2008-04-23 | 2018-03-27 | Symphogen As | processo para produção de uma proteína policlonal |
| AR072999A1 (es) | 2008-08-11 | 2010-10-06 | Medarex Inc | Anticuerpos humanos que se unen al gen 3 de activacion linfocitaria (lag-3) y los usos de estos |
| MX2011001929A (es) * | 2008-08-26 | 2011-04-21 | Symphogen As | Tratamiento de trombocitopenia. |
| MX2011001930A (es) * | 2008-08-29 | 2011-04-21 | Symphogen As | Metodo para clonar anticuerpos derivados de aves. |
| EP2331577B1 (en) | 2008-08-29 | 2017-06-07 | Symphogen A/S | Recombinant anti-epidermal growth factor receptor antibody compositions |
| AU2009301505A1 (en) * | 2008-10-06 | 2010-04-15 | Symphogen A/S | Method for identifying and selecting drug candidates for combinatorial drug products |
| FR2942799B1 (fr) * | 2009-03-06 | 2011-02-25 | Lfb Biotechnologies | Anticorps monoclonal anti-rhesus d |
| JP2013507603A (ja) | 2009-10-09 | 2013-03-04 | シムフォゲン・アクティーゼルスカブ | 署名ペプチドおよび質量分析による混合物中の個々の組換えタンパク質の多重定量化 |
| EP3604330A1 (en) | 2011-02-25 | 2020-02-05 | Chugai Seiyaku Kabushiki Kaisha | Fcgammariib-specific fc antibody |
| HRP20190030T1 (hr) * | 2012-06-21 | 2019-02-22 | Synthon Biopharmaceuticals B.V. | Postupak pročišćavanja protutijela |
| EP2711428A1 (en) * | 2012-09-21 | 2014-03-26 | Lonza Biologics plc. | Site-specific integration |
| AR091649A1 (es) | 2012-07-02 | 2015-02-18 | Bristol Myers Squibb Co | Optimizacion de anticuerpos que se fijan al gen de activacion de linfocitos 3 (lag-3) y sus usos |
| US10081681B2 (en) | 2013-09-20 | 2018-09-25 | Bristol-Myers Squibb Company | Combination of anti-LAG-3 antibodies and anti-PD-1 antibodies to treat tumors |
| JOP20200094A1 (ar) | 2014-01-24 | 2017-06-16 | Dana Farber Cancer Inst Inc | جزيئات جسم مضاد لـ pd-1 واستخداماتها |
| ME03558B (me) | 2014-03-14 | 2020-07-20 | Novartis Ag | Molekuli anti-lag-3 antiтela i njihove upotrebe |
| US9683017B2 (en) | 2014-07-17 | 2017-06-20 | University Tennessee Research Foundation | Inhibitory peptides of viral infection |
| EP3186273A4 (en) | 2014-08-26 | 2018-05-02 | University of Tennessee Research Foundation | Targeting immunotherapy for amyloidosis |
| WO2017184973A1 (en) * | 2016-04-22 | 2017-10-26 | University Of Tennessee Research Foundation | Identifying amyloidogenic proteins & amyloidogenic risk |
| HUE065242T2 (hu) | 2017-05-30 | 2024-05-28 | Bristol Myers Squibb Co | LAG-3-pozitív tumorok kezelése |
| BR112019021847A2 (pt) | 2017-05-30 | 2020-06-02 | Bristol-Myers Squibb Company | Composições compreendendo um anticorpo anti-lag-3 ou um anticorpo anti-lag-3 e um anticorpo anti-pd-1 ou anti-pd-l1 |
| MA52945A (fr) * | 2018-06-22 | 2021-04-28 | Genmab As | Procédé de production d'un mélange contrôlé d'au moins deux anticorps différents |
| SG11202103334YA (en) | 2018-10-26 | 2021-05-28 | Hoffmann La Roche | Multispecific antibody screening method using recombinase mediated cassette exchange |
| WO2020205775A1 (en) * | 2019-03-29 | 2020-10-08 | H. Lee Moffitt Cancer Center And Research Institute, Inc. | Antibodies against programmed cell death protein 1 (pd1) and uses thereof |
| AU2020253023B2 (en) | 2019-03-29 | 2022-07-14 | F. Hoffmann-La Roche Ag | Method for the generation of an FcRn expressing cell by targeted integration of multiple expression cassettes in a defined organization |
| WO2020254351A1 (en) | 2019-06-19 | 2020-12-24 | F. Hoffmann-La Roche Ag | Method for the generation of a multivalent, multispecific antibody expressing cell by targeted integration of multiple expression cassettes in a defined organization |
| CA3140318A1 (en) | 2019-06-19 | 2020-12-24 | Johannes Auer | Method for the generation of a bivalent, bispecific antibody expressing cell by targeted integration of multiple expression cassettes in a defined organization |
| KR20220024637A (ko) | 2019-06-19 | 2022-03-03 | 에프. 호프만-라 로슈 아게 | 정의된 조직의 다수 발현 카세트들의 표적화 통합에 의한 3가 항체 발현 세포의 생성 방법 |
| CA3140323A1 (en) | 2019-06-19 | 2020-12-24 | Johannes Auer | Method for the generation of a multivalent, bispecific antibody expressing cell by targeted integration of multiple expression cassettes in a defined organization |
| CA3140297A1 (en) | 2019-06-19 | 2020-12-24 | Simon Auslaender | Method for the generation of a protein expressing cell by targeted integration using cre mrna |
| TW202237642A (zh) * | 2021-01-08 | 2022-10-01 | 美商１０Ｘ基因組學有限公司 | 對冠狀病毒具有特異性的抗原結合多肽及其用途 |
| WO2025039046A1 (en) * | 2023-08-23 | 2025-02-27 | The Walter And Eliza Hall Institute Of Medical Research | Anti-rhesus d human monoclonal antibodies |
| CN119176879B (zh) * | 2024-09-05 | 2025-08-05 | 西安市中心血站（陕西省血液中心） | 一种中和抗d抗体的抗独特型抗体及其应用 |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1995020401A1 (en) * | 1994-01-31 | 1995-08-03 | Trustees Of Boston University | Polyclonal antibody libraries |
| WO1997049809A1 (en) * | 1996-06-24 | 1997-12-31 | Rotkreuzstiftung Zentrallaboratorium Blutspendedienst Srk | Polypeptides capable of forming antigen binding structures with specificity for the rhesus d antigens, the dna encoding them and the process for their preparation and use |
| WO2002044361A2 (en) * | 2000-11-28 | 2002-06-06 | Applied Molecular Evolution, Inc. | Eukaryotic expression libraries based on double lox recombination and methods of use |
| WO2004061104A2 (en) * | 2003-01-07 | 2004-07-22 | Symphogen A/S | Method for manufacturing recombinant polyclonal proteins |
Family Cites Families (36)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0162918A1 (en) | 1983-11-28 | 1985-12-04 | The Board Of Trustees Of The Leland Stanford Junior University | HUMAN MONOCLONAL ANTIBODY AGAINST Rh(D) ANTIGEN AND ITS USES |
| US5126130A (en) | 1986-11-24 | 1992-06-30 | The Childrens Hospital Incorporated | Monoclonal antibodies reactive with specific antigenic sites on human cytomegalovirus glycoprotein a |
| GB8722020D0 (en) | 1987-09-18 | 1987-10-28 | Central Blood Lab Authority | Human anti-rh(d)monoclonal antibodies |
| GB8722018D0 (en) | 1987-09-18 | 1987-10-28 | Central Blood Lab Authority | Human anti-rh(d)monoclonal antibodies |
| GB8722019D0 (en) | 1987-09-18 | 1987-10-28 | Central Blood Lab Authority | Human anti-rh(d)monoclonal antibodies |
| WO1990005144A1 (en) | 1988-11-11 | 1990-05-17 | Medical Research Council | Single domain ligands, receptors comprising said ligands, methods for their production, and use of said ligands and receptors |
| GB8906129D0 (en) | 1989-03-17 | 1989-05-04 | Central Blood Lab Authority | Pharmaceutical preparations |
| GB8919761D0 (en) | 1989-09-01 | 1989-10-18 | Central Blood Lab Authority | Chemical compounds |
| WO1992015694A1 (en) | 1991-03-08 | 1992-09-17 | The Salk Institute For Biological Studies | Flp-mediated gene modification in mammalian cells, and compositions and cells useful therefor |
| US5837268A (en) | 1991-10-16 | 1998-11-17 | University Of Saskatchewan | GnRH-leukotoxin chimeras |
| PL302438A1 (en) | 1992-06-26 | 1994-07-25 | Aetsrn | Human anti-rh(d) monoclonal antibodies and cellular lines producing them |
| ES2191677T3 (es) | 1992-10-21 | 2003-09-16 | Stefan Miltenyi | Seleccion directa de celulas mediante un producto de secrecion. |
| US5538848A (en) | 1994-11-16 | 1996-07-23 | Applied Biosystems Division, Perkin-Elmer Corp. | Method for detecting nucleic acid amplification using self-quenching fluorescence probe |
| FR2724182B1 (fr) | 1994-09-02 | 1996-12-13 | Pasteur Institut | Obtention d'un anticorps monoclonal recombinant a partir d'un anticorps monoclonal humain anti-rhesus d, sa production en cellules d'insecte, et ses utilisations |
| US6025155A (en) | 1996-04-10 | 2000-02-15 | Chromos Molecular Systems, Inc. | Artificial chromosomes, uses thereof and methods for preparing artificial chromosomes |
| US5876925A (en) | 1996-10-11 | 1999-03-02 | The Trustees Of The University Of Pennsylvania | Magnetically activated cell sorting for production of proteins |
| US6255455B1 (en) | 1996-10-11 | 2001-07-03 | The Trustees Of The University Of Pennsylvania | Rh(D)-binding proteins and magnetically activated cell sorting method for production thereof |
| GB9703369D0 (en) | 1997-02-18 | 1997-04-09 | Lindqvist Bjorn H | Process |
| ATE401410T1 (de) | 1997-11-18 | 2008-08-15 | Pioneer Hi Bred Int | Zusammensetzungen und verfahren für die genetische modifizierung von pflanzen |
| WO2000005393A2 (en) | 1998-07-21 | 2000-02-03 | Cobra Therapeutics Limited | A polynucleotide comprising a ubiquitous chromatin opening element (ucoe) |
| US20020155114A1 (en) | 1998-08-31 | 2002-10-24 | James D. Marks | Therapeutic monoclonal antibodies that neutralize botulinum neurotoxins |
| DK1234022T3 (da) | 1999-07-23 | 2010-07-19 | Univ California | DNA-rekombination i eukaryote celler med bakteriofag PHIC31-rekombinationssystemet |
| EP1106625A1 (en) | 1999-11-17 | 2001-06-13 | ZLB Bioplasma AG | Rhesus D specific peptide sequences |
| JP2003534533A (ja) | 2000-02-08 | 2003-11-18 | ザ リージェンツ オブ ザ ユニバーシティ オブ ミシガン | タンパク質のディファレンシャルディスプレイのマッピング |
| EP1358202A2 (en) | 2000-02-08 | 2003-11-05 | The Regents Of The University Of Michigan | Protein separation and display |
| AU2001234893A1 (en) | 2000-02-08 | 2001-08-20 | The Regents Of The University Of Michigan | Protein mapping |
| EP1283720B1 (en) | 2000-05-26 | 2007-04-18 | Symphogen A/S | Recombinant or purified polyclonal antibodies for treating allergy |
| AU2001277076A1 (en) | 2000-07-21 | 2002-02-05 | The United States Of America As Represented By The Secretary Of Agriculture | Methods for the replacement, translocation and stacking of DNA in eukaryotic genomes |
| US6610472B1 (en) | 2000-10-31 | 2003-08-26 | Genetastix Corporation | Assembly and screening of highly complex and fully human antibody repertoire in yeast |
| DE60142650D1 (de) | 2000-12-26 | 2010-09-02 | Inst Systems Biology Seattle | Schnelle und quantitative Proteomanalyse und entsprechende Verfahren |
| AU2003237282A1 (en) | 2002-05-31 | 2003-12-19 | The Regents Of The University Of Michigan | Automated protein analysis system comprising capillary electrophoresis-tandem mass spectrometry |
| SI1523496T1 (sl) | 2002-07-18 | 2011-11-30 | Merus B V | Rekombinantno proizvajanje zmesi protiteles |
| WO2004035169A2 (en) | 2002-10-15 | 2004-04-29 | The Regents Of The University Of Michigan | Multidimensional protein separation system |
| US20060275766A1 (en) | 2003-01-07 | 2006-12-07 | Haurum John S | Method for manufacturing recombinant polyclonal proteins |
| TWI333977B (en) | 2003-09-18 | 2010-12-01 | Symphogen As | Method for linking sequences of interest |
| RU2426795C2 (ru) | 2004-07-20 | 2011-08-20 | Симфоген А/С | Способ структурной характеристики рекомбинантного поликлонального белка или поликлональной клеточной линии |
-
2005
- 2005-07-18 BR BRPI0513706-3A patent/BRPI0513706A/pt not_active IP Right Cessation
- 2005-07-18 WO PCT/DK2005/000501 patent/WO2006007850A1/en not_active Ceased
- 2005-07-18 US US11/632,937 patent/US8198415B2/en not_active Expired - Fee Related
- 2005-07-18 KR KR1020077003955A patent/KR20070038556A/ko not_active Ceased
- 2005-07-18 CA CA002574062A patent/CA2574062A1/en not_active Abandoned
- 2005-07-18 JP JP2007521793A patent/JP4926054B2/ja not_active Expired - Fee Related
- 2005-07-18 EP EP05760588A patent/EP1771483A1/en not_active Withdrawn
- 2005-07-18 EA EA200700249A patent/EA014182B1/ru not_active IP Right Cessation
- 2005-07-18 EP EP08157871A patent/EP1967529A1/en not_active Withdrawn
- 2005-07-18 AU AU2005263331A patent/AU2005263331B8/en not_active Ceased
- 2005-07-18 MX MX2007000644A patent/MX2007000644A/es active IP Right Grant
- 2005-07-18 NZ NZ552265A patent/NZ552265A/en not_active IP Right Cessation
-
2006
- 2006-11-28 IL IL179658A patent/IL179658A/en not_active IP Right Cessation
-
2007
- 2007-02-19 NO NO20070927A patent/NO20070927L/no not_active Application Discontinuation
-
2012
- 2012-06-11 US US13/493,623 patent/US20120322690A1/en not_active Abandoned
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1995020401A1 (en) * | 1994-01-31 | 1995-08-03 | Trustees Of Boston University | Polyclonal antibody libraries |
| US5789208A (en) * | 1994-01-31 | 1998-08-04 | The Trustees Of Boston University | Polyclonal antibody libraries |
| WO1997049809A1 (en) * | 1996-06-24 | 1997-12-31 | Rotkreuzstiftung Zentrallaboratorium Blutspendedienst Srk | Polypeptides capable of forming antigen binding structures with specificity for the rhesus d antigens, the dna encoding them and the process for their preparation and use |
| WO2002044361A2 (en) * | 2000-11-28 | 2002-06-06 | Applied Molecular Evolution, Inc. | Eukaryotic expression libraries based on double lox recombination and methods of use |
| WO2004061104A2 (en) * | 2003-01-07 | 2004-07-22 | Symphogen A/S | Method for manufacturing recombinant polyclonal proteins |
Non-Patent Citations (4)
| Title |
|---|
| BREGENHOLT S. ET AL.: "PATHOGEN-SPECIFIC RECOMBINANT HUMAN POLYCLONAL ANTIBODIES: BIODEFENCE APPLICATIONS". EXPERT OPINION ON BIOLOGICAL THERAPY, ASHLEY, LONDON, GB, vol. 4, no. 3, March 2004 (2004-03), pages 387-396, XP008030716, ISSN: 1471-2598, the whole document * |
| HAURUM JOHN ET AL.: "Recombinant polyclonal antibodies: therapeutic antibody technologies come full circle". IDRUGS: THE INVESTIGATIONAL DRUGS JOURNAL. MAY 2005, vol. 8, no. 5, May 2005 (2005-05), pages 404-409, XP002352885, ISSN: 1369-7056, the whole document * |
| SELINGER M.: "Immunoprophylaxis for rhesus disease-expensive but worth it?". BRITISH JOURNAL OF OBSTETRICS AND GYNAECOLOGY. JUN. 1991, vol. 98, no. 6, June 1991 (1991-06), pages 509-512, XP009056635, ISSN: 0306-5456, the whole document * |
| SHARON J. ET AL.: "CONSTRUCTION OF POLYCLONAL ANTIBODY LIBRARIES USING PHAGE DISPLAY". METHODS IN MOLECULAR BIOLOGY, HUMANA PRESS INC., CLIFTON, NJ, US, vol. 178, 2002, pages 101-112, XP008053600, the whole document * |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2770654C1 (ru) * | 2021-06-17 | 2022-04-20 | Федеральное государственное бюджетное образовательное учреждение высшего образования "Санкт-Петербургский государственный педиатрический медицинский университет" Министерства здравоохранения Российской Федерации (ФГБОУ ВО СПбГПМУ Минздрава России) | Способ профилактики тяжелой формы гемолитической болезни новорожденных при резус-иммунизации у беременных с соматической патологией и потерями плода в анамнезе |
Also Published As
| Publication number | Publication date |
|---|---|
| EP1967529A1 (en) | 2008-09-10 |
| NZ552265A (en) | 2009-04-30 |
| KR20070038556A (ko) | 2007-04-10 |
| AU2005263331B2 (en) | 2011-05-26 |
| US20090017017A1 (en) | 2009-01-15 |
| NO20070927L (no) | 2007-04-19 |
| BRPI0513706A (pt) | 2008-05-13 |
| MX2007000644A (es) | 2007-03-28 |
| AU2005263331A1 (en) | 2006-01-26 |
| CA2574062A1 (en) | 2006-01-26 |
| IL179658A0 (en) | 2007-05-15 |
| IL179658A (en) | 2011-08-31 |
| JP2008509658A (ja) | 2008-04-03 |
| AU2005263331B8 (en) | 2011-06-16 |
| EA200700249A1 (ru) | 2007-06-29 |
| US8198415B2 (en) | 2012-06-12 |
| JP4926054B2 (ja) | 2012-05-09 |
| EP1771483A1 (en) | 2007-04-11 |
| AU2005263331A8 (en) | 2011-06-16 |
| WO2006007850A1 (en) | 2006-01-26 |
| US20120322690A1 (en) | 2012-12-20 |
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