CA2417214C - Molecular vaccine linking an endoplasmic reticulum chaperone polypeptide to an antigen - Google Patents
Molecular vaccine linking an endoplasmic reticulum chaperone polypeptide to an antigen Download PDFInfo
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- CA2417214C CA2417214C CA2417214A CA2417214A CA2417214C CA 2417214 C CA2417214 C CA 2417214C CA 2417214 A CA2417214 A CA 2417214A CA 2417214 A CA2417214 A CA 2417214A CA 2417214 C CA2417214 C CA 2417214C
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Classifications
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- C—CHEMISTRY; METALLURGY
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- C07K2319/35—Fusion polypeptide containing a fusion for enhanced stability/folding during expression, e.g. fusions with chaperones or thioredoxin
Landscapes
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- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
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| PCT/US2001/024134 WO2002012281A2 (en) | 2000-08-03 | 2001-08-02 | Molecular vaccine linking an endoplasmic reticulum chaperone polypeptide to an antigen |
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| CA2417214C true CA2417214C (en) | 2016-06-21 |
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| WO (1) | WO2002012281A2 (enExample) |
Families Citing this family (44)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20050100928A1 (en) * | 1999-09-16 | 2005-05-12 | Zycos Inc., A Delaware Corporation | Nucleic acids encoding polyepitope polypeptides |
| US8128922B2 (en) | 1999-10-20 | 2012-03-06 | Johns Hopkins University | Superior molecular vaccine linking the translocation domain of a bacterial toxin to an antigen |
| AU2001290520A1 (en) * | 2000-08-01 | 2002-02-13 | The Johns Hokpins University | Intercellular transport protein linked to an antigen as a molecular vaccine |
| WO2002012281A2 (en) | 2000-08-03 | 2002-02-14 | Johns Hopkins University | Molecular vaccine linking an endoplasmic reticulum chaperone polypeptide to an antigen |
| AU2002242016A1 (en) | 2001-02-01 | 2002-08-12 | The Johns Hopkins University | Nucleic acid derived vaccine that encodes an antigen linked to a polypeptide that promotes antigen presentation |
| US20070026501A1 (en) * | 2003-04-18 | 2007-02-01 | Joe Chiba | Immunogen, composition for immulogical use and process for producing antibody using the same |
| US9701725B2 (en) * | 2003-05-05 | 2017-07-11 | The Johns Hopkins University | Anti-cancer DNA vaccine employing plasmids encoding signal sequence, mutant oncoprotein antigen, and heat shock protein |
| ES2427641T3 (es) | 2003-05-22 | 2013-10-31 | Ibio, Inc. | Molécula vehículo recombinante para la expresión, el suministro y la purificación de polipéptidos diana |
| WO2005081716A2 (en) * | 2003-11-24 | 2005-09-09 | The Johns Hopkins University | DNA VACCINES TARGETING ANTIGENS OF THE SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS (SARS-CoV) |
| AU2003290460A1 (en) * | 2003-12-24 | 2005-07-14 | Leiden University Medical Center | Synthetic protein as tumor-specific vaccine |
| CA2583361C (en) | 2004-10-15 | 2015-08-04 | Sekisui Chemical Co., Ltd. | Gene immunization using an antigen-chaperonin fusion |
| AU2005322960A1 (en) | 2005-01-06 | 2006-07-13 | The Johns Hopkins University | RNA interference that blocks expression of pro-apoptotic proteins potentiates immunity induced by DNA and transfected dendritic cell vaccines |
| EP1846026A4 (en) * | 2005-01-26 | 2008-07-02 | Univ Johns Hopkins | ANTIBODY DNA VACCINE WITH PLASMIDES FOR CODING A MUTATED ONCOPROTEIN ANTIGEN AND CALRETICULIN |
| WO2007117264A2 (en) * | 2005-08-03 | 2007-10-18 | Fraunhofer Usa, Inc. | Compositions and methods for production of immunoglobulins |
| CN101395174B (zh) * | 2006-02-13 | 2014-03-19 | 艾比欧公司 | 人类乳头瘤病毒（hpv）抗原、疫苗组合物和相关方法 |
| WO2008048344A2 (en) * | 2006-02-13 | 2008-04-24 | Fraunhofer Usa, Inc. | Bacillus anthracis antigens, vaccine compositions, and related methods |
| WO2008024844A2 (en) * | 2006-08-22 | 2008-02-28 | The Johns Hopkins University | Anticancer combination therapies |
| WO2008046251A1 (fr) * | 2006-10-19 | 2008-04-24 | Sunbio Biotech Pharmaceuticals(Tianjin) Co., Ltd. | Protéines hybrides contenant un domaine n de la calréticuline humaine et des protéines e6 ou e7 du papillomavirus humain de type 16, et utilisations associées |
| US9085638B2 (en) | 2007-03-07 | 2015-07-21 | The Johns Hopkins University | DNA vaccine enhancement with MHC class II activators |
| US20080260765A1 (en) * | 2007-03-15 | 2008-10-23 | Johns Hopkins University | HPV DNA Vaccines and Methods of Use Thereof |
| US20100291683A1 (en) * | 2007-03-27 | 2010-11-18 | Lung-Ji Chang | Modified Antigen Presenting Cells and Methods of Use |
| WO2009009759A2 (en) * | 2007-07-11 | 2009-01-15 | Fraunhofer Usa, Inc. | Yersinia pestis antigens, vaccine compositions, and related methods |
| KR20110011595A (ko) * | 2008-01-28 | 2011-02-08 | 탭이뮨, 인크. | 면역 반응 증진을 위한 타파신 증대 |
| EP2752193B1 (en) | 2008-03-03 | 2017-01-11 | The University of Miami | Allogeneic cancer cell-based immunotherapy |
| WO2009117116A2 (en) | 2008-03-20 | 2009-09-24 | University Of Miami | Heat shock protein gp96 vaccination and methods of using same |
| US20090285861A1 (en) * | 2008-04-17 | 2009-11-19 | Tzyy-Choou Wu | Tumor cell-based cancer immunotherapeutic compositions and methods |
| WO2010030861A2 (en) * | 2008-09-11 | 2010-03-18 | Calretex, Llc | Compositions and methods for purifying calreticulin |
| WO2010037046A1 (en) | 2008-09-28 | 2010-04-01 | Fraunhofer Usa, Inc. | Humanized neuraminidase antibody and methods of use thereof |
| CA2776144C (en) | 2009-09-29 | 2020-10-27 | Fraunhofer Usa, Inc. | Influenza hemagglutinin antibodies, compositions, and related methods |
| PL2591114T3 (pl) * | 2010-07-06 | 2017-08-31 | Glaxosmithkline Biologicals Sa | Immunizacja dużych ssaków małymi dawkami rna |
| KR20140045341A (ko) * | 2011-02-23 | 2014-04-16 | 유니버시티 오브 마이애미 | Siv/hiv로부터의 보호를 위한 조합된 세포 기반의 gp96-ig-siv/hiv, 재조합 gp120 단백질 백신접종 |
| LT3892295T (lt) | 2011-05-24 | 2023-07-10 | BioNTech SE | Individualizuotos vakcinos nuo vėžio |
| EP2752112B1 (en) * | 2011-09-02 | 2016-04-27 | Kaneka Corporation | Transgenic bird expressing foreign gene using endoplasmic reticulum chaperone promoter |
| WO2013093629A2 (en) * | 2011-12-20 | 2013-06-27 | Netherlands Cancer Institute | Modular vaccines, methods and compositions related thereto |
| JP6484558B2 (ja) | 2012-11-28 | 2019-03-13 | バイオエヌテック エールエヌアー ファーマシューティカルズ ゲーエムベーハーＢｉｏｎｔｅｃｈ Ｒｎａ Ｐｈａｒｍａｃｅｕｔｉｃａｌｓ Ｇｍｂｈ | 癌ワクチンの組み合せ物 |
| WO2014164727A1 (en) * | 2013-03-12 | 2014-10-09 | Wisconsin Alumni Research Foundation | A method of treating fungal infection |
| US10676723B2 (en) | 2015-05-11 | 2020-06-09 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| WO2017155981A1 (en) * | 2016-03-07 | 2017-09-14 | Massachusetts Institute Of Technology | Protein-chaperoned t-cell vaccines |
| US11129906B1 (en) | 2016-12-07 | 2021-09-28 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| US11180535B1 (en) | 2016-12-07 | 2021-11-23 | David Gordon Bermudes | Saccharide binding, tumor penetration, and cytotoxic antitumor chimeric peptides from therapeutic bacteria |
| WO2018224166A1 (en) | 2017-06-09 | 2018-12-13 | Biontech Rna Pharmaceuticals Gmbh | Methods for predicting the usefulness of disease specific amino acid modifications for immunotherapy |
| SG11201911430PA (en) | 2017-07-04 | 2020-01-30 | Curevac Ag | Novel nucleic acid molecules |
| CN109182339A (zh) * | 2018-09-06 | 2019-01-11 | 青岛农业大学 | 一种许氏平鮋钙网蛋白基因及应用 |
| CA3161800A1 (en) | 2019-11-18 | 2021-05-27 | Janssen Biotech, Inc. | Vaccines based on mutant calr and jak2 and their uses |
Family Cites Families (78)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5744133A (en) * | 1986-08-13 | 1998-04-28 | Transgene S.A. | Expression of a tumor-specific antigen by a recombinant vector virus and use thereof in preventitive or curative treatment of the corresponding tumor |
| US4898730A (en) * | 1987-03-13 | 1990-02-06 | The University Of British Columbia | Method to stimulate the immune response to specific antigens |
| US5582831A (en) * | 1991-11-26 | 1996-12-10 | Yeda Research And Development Co., Ltd. | Anti-tumor vaccines |
| DE68924162T2 (de) | 1988-06-15 | 1996-04-25 | Medical Res Council | Stressproteine und verwendungen dafür. |
| US5217879A (en) * | 1989-01-12 | 1993-06-08 | Washington University | Infectious Sindbis virus vectors |
| DE3907721A1 (de) * | 1989-03-10 | 1990-09-20 | Behringwerke Ag | Immunogene regionen auf dem e7-protein des humanen papillomvierus typ 16 |
| US5545727A (en) * | 1989-05-10 | 1996-08-13 | Somatogen, Inc. | DNA encoding fused di-alpha globins and production of pseudotetrameric hemoglobin |
| US5348945A (en) * | 1990-04-06 | 1994-09-20 | Wake Forest University | Method of treatment with hsp70 |
| US5821088A (en) * | 1990-05-11 | 1998-10-13 | Siga Pharmaceuticals, Inc. | Use of gram-positive bacteria to express recombinant proteins |
| CN1067382A (zh) | 1990-09-26 | 1992-12-30 | 布里斯托尔-迈尔斯斯奎尔公司 | 人类乳头状瘤病毒肽的表达以及在致免疫组合物中的应用 |
| US5674486A (en) * | 1991-06-25 | 1997-10-07 | San Diego Regional Cancer Center | Cancer immunotherapy with carrier cells |
| ATE234860T1 (de) * | 1991-07-13 | 2003-04-15 | Dade Behring Marburg Gmbh | Verwendung von hpv-16 e6 und e7-gen gewonnen peptiden für den diagnostischen zweck |
| GB9207701D0 (en) | 1992-04-08 | 1992-05-27 | Cancer Res Campaign Tech | Papillomavirus e7 protein |
| IL106760A (en) | 1992-08-25 | 1999-12-31 | Miles Inc | Protein-nucleic acid hybrid construct for translocating an exogenous nucleic acid into a target cell and nucleus |
| US5618536A (en) | 1992-09-03 | 1997-04-08 | The United States Of America As Represented By The Department Of Health And Human Services | Chimeric papillomavirus-like particles |
| US5997869A (en) * | 1993-03-15 | 1999-12-07 | The United States Of America As Represented By The Department Of Health And Human Services | Peptides containing a fusion joint of a chimeric protein encoded by DNA spanning a tumor-associated chromosomal translocation and their use as immunogens |
| GB9306731D0 (en) * | 1993-03-31 | 1993-05-26 | Cancer Res Campaign Tech | Vaccines |
| US5426097A (en) * | 1993-04-06 | 1995-06-20 | The Trustees Of Columbia University In The City Of New York | Calreticulin: a novel antithrombotic agent |
| ES2171454T3 (es) | 1993-06-04 | 2002-09-16 | Whitehead Biomedical Inst | Proteinas de estres y sus usos. |
| US5646008A (en) | 1993-06-22 | 1997-07-08 | The Regent Of The University Of Michigan | Vertebrate apoptosis gene: compositions and methods |
| US5591716A (en) * | 1993-11-19 | 1997-01-07 | New York University | Beneficial wound healing applications of calreticulin and other hyaluronan-associated proteins |
| EP0659438A1 (en) | 1993-12-23 | 1995-06-28 | Boehringer Mannheim Gmbh | Conjugates consisting of peptidic T cell antigens and cell binding groups, and their use for therapy |
| US5750119A (en) * | 1994-01-13 | 1998-05-12 | Mount Sinai School Of Medicine Of The City University Of New York | Immunotherapeutic stress protein-peptide complexes against cancer |
| AUPM566794A0 (en) * | 1994-05-17 | 1994-06-09 | University Of Queensland, The | Process and product |
| US5854202A (en) | 1995-01-24 | 1998-12-29 | Dedhar; Shoukat | Peptide fragments of calreticulin, peptide mimetics thereof, and pharmaceutical compostions comprising same |
| AU5512096A (en) | 1995-05-17 | 1996-11-29 | University Of Alberta | Method of inhibiting restenosis using calreticulin |
| US5792462A (en) * | 1995-05-23 | 1998-08-11 | University Of North Carolina At Chapel Hill | Alphavirus RNA replicon systems |
| AU6504596A (en) | 1995-07-21 | 1997-02-18 | Rhone-Poulenc Rorer Pharmaceuticals Inc. | Adeno-associated viral liposomes and their use in transfecting dendritic cells to stimulate specific immunity |
| CA2229543A1 (en) | 1995-08-18 | 1997-02-27 | Sloan-Kettering Institute For Cancer Research | Heat shock protein-based vaccines and immunotherapies |
| US5935576A (en) * | 1995-09-13 | 1999-08-10 | Fordham University | Compositions and methods for the treatment and prevention of neoplastic diseases using heat shock proteins complexed with exogenous antigens |
| US5837251A (en) * | 1995-09-13 | 1998-11-17 | Fordham University | Compositions and methods using complexes of heat shock proteins and antigenic molecules for the treatment and prevention of neoplastic diseases |
| DE19534348C2 (de) | 1995-09-15 | 1997-07-10 | Wieland Heinrich Prof Dr Med | Verfahren zur Bestimmung von Autoimmunphänomenen |
| WO1997020854A1 (en) * | 1995-12-05 | 1997-06-12 | University Of Massachusetts | Recombinant gas vesicles and uses thereof |
| BR9708387A (pt) * | 1996-03-28 | 2000-01-04 | Genitrix Llc | Processo para vacinação de um mamìfero a um antìgeno selecionado, células patogênica e hospedeira, composição de vacina, ácido nucleico, e, opsonina engenheirada. |
| AU738649B2 (en) | 1996-04-26 | 2001-09-20 | Rijksuniversiteit Te Leiden | Methods for selecting and producing T cell peptide epitopes and vaccines incorporating said selected epitopes |
| US5951975A (en) * | 1996-06-28 | 1999-09-14 | University Of Pittsburgh | Induction of CTLs specific for natural antigens by cross priming immunization |
| CA2265935C (en) * | 1996-09-20 | 2006-09-05 | The University Of New Mexico | Heat shock protein complexes |
| US5962318A (en) * | 1996-11-15 | 1999-10-05 | St. Jude Children's Research Hospital | Cytotoxic T lymphocyte-mediated immunotherapy |
| EP0941315B1 (en) | 1996-11-26 | 2006-03-01 | Stressgen Biotechnologies Corporation | Fusion proteins containing stress proteins for inducing immune responses |
| US6046158A (en) * | 1996-12-20 | 2000-04-04 | Board Of Regents The University Of Texas Systems | Unique dendritic cell-associated C-type lectins, dectin-1 and dectin-2; compositions and uses thereof |
| US6017735A (en) | 1997-01-23 | 2000-01-25 | Marie Curie Cancer Care | Materials and methods for intracellular transport and their uses |
| US5830464A (en) * | 1997-02-07 | 1998-11-03 | Fordham University | Compositions and methods for the treatment and growth inhibition of cancer using heat shock/stress protein-peptide complexes in combination with adoptive immunotherapy |
| US6017540A (en) * | 1997-02-07 | 2000-01-25 | Fordham University | Prevention and treatment of primary and metastatic neoplastic diseases and infectious diseases with heat shock/stress protein-peptide complexes |
| AU7022898A (en) | 1997-04-23 | 1998-11-13 | Ontario Cancer Treatment & Research Foundation | Calreticulin-deficient cells |
| US6319503B1 (en) | 1998-02-19 | 2001-11-20 | Proteinix Company | Heat shock fusion-based vaccine system |
| HUP0003601A3 (en) | 1997-08-05 | 2003-03-28 | Stressgen Biotechnologies Corp | Immune responses against hpv antigens elicited by compositions comprising an hpv antigen and a stress protein or an expression vector capable of expression of these proteins |
| AU3910097A (en) | 1997-08-05 | 1999-03-01 | Government Of The United States Of America, As Represented By The Secretary Of The Department Of Health And Human Services, The | Live recombinant vaccine comprising inefficiently or non-replicating vir us |
| US6007821A (en) * | 1997-10-16 | 1999-12-28 | Fordham University | Method and compositions for the treatment of autoimmune disease using heat shock proteins |
| US6331388B1 (en) * | 1997-10-17 | 2001-12-18 | Wisconsin Alumni Research Foundation | Immune response enhancer |
| US5948646A (en) * | 1997-12-11 | 1999-09-07 | Fordham University | Methods for preparation of vaccines against cancer comprising heat shock protein-peptide complexes |
| US6534482B1 (en) | 1998-05-13 | 2003-03-18 | Epimmune, Inc. | Expression vectors for stimulating an immune response and methods of using the same |
| EP1086129A1 (en) | 1998-06-17 | 2001-03-28 | Beth Israel Deaconess Medical Center | Anti-angiogenic proteins and methods of use thereof |
| US6235523B1 (en) * | 1998-09-04 | 2001-05-22 | Connaught Laboratories Limited | Vectors for DNA immunization against cervical cancer |
| US7001995B1 (en) * | 1999-08-25 | 2006-02-21 | Merck & Co., Inc. | Synthetic human papillomavirus genes |
| CN1411512A (zh) | 1999-10-20 | 2003-04-16 | 约翰霍普金斯大学医学院 | 嵌合的免疫原性组合物及其编码核酸 |
| US6734173B1 (en) * | 1999-10-20 | 2004-05-11 | Johns Hopkins University | HSP DNA vaccines |
| US8128922B2 (en) | 1999-10-20 | 2012-03-06 | Johns Hopkins University | Superior molecular vaccine linking the translocation domain of a bacterial toxin to an antigen |
| US20010034042A1 (en) * | 2000-01-20 | 2001-10-25 | Srivastava Pramod K. | Complexes of peptide-binding fragments of heat shock proteins and their use as immunotherapeutic agents |
| US6967075B2 (en) * | 2000-04-07 | 2005-11-22 | Schering Corporation | HCV replicase complexes |
| US7030219B2 (en) * | 2000-04-28 | 2006-04-18 | Johns Hopkins University | B7-DC, Dendritic cell co-stimulatory molecules |
| SK18362002A3 (sk) | 2000-06-26 | 2004-02-03 | Stressgen Biotechnologies Corporation | Použitie prostriedku s obsahom fúzneho proteínu |
| AU2001290520A1 (en) * | 2000-08-01 | 2002-02-13 | The Johns Hokpins University | Intercellular transport protein linked to an antigen as a molecular vaccine |
| WO2002012281A2 (en) | 2000-08-03 | 2002-02-14 | Johns Hopkins University | Molecular vaccine linking an endoplasmic reticulum chaperone polypeptide to an antigen |
| JP3930243B2 (ja) * | 2000-11-06 | 2007-06-13 | 本田技研工業株式会社 | マグネットポンプ |
| CZ302719B6 (cs) * | 2000-12-01 | 2011-09-21 | MAX-PLANCK-Gesellschaft zur Förderung der Wissenschaften e.V. | Izolovaná molekula dvouretezcové RNA, zpusob její výroby a její použití |
| US7892730B2 (en) * | 2000-12-22 | 2011-02-22 | Sagres Discovery, Inc. | Compositions and methods for cancer |
| AU2002242016A1 (en) * | 2001-02-01 | 2002-08-12 | The Johns Hopkins University | Nucleic acid derived vaccine that encodes an antigen linked to a polypeptide that promotes antigen presentation |
| WO2002074920A2 (en) | 2001-03-16 | 2002-09-26 | Johns Hopkins University | A replication-defective alphavirus vaccine linking antigen with an immunogenicity-potentiating polypeptide and a method of delivery the same |
| US20030144221A1 (en) | 2001-07-17 | 2003-07-31 | Isis Pharmaceuticals Inc. | Antisense modulation of BCL2-associated X protein expression |
| CN100335121C (zh) * | 2001-07-20 | 2007-09-05 | 得克萨斯大学体系董事会 | 涉及hpv相关的癌前期的和癌的生长(包括cin)的方法和组合物 |
| US20060040262A1 (en) | 2002-12-27 | 2006-02-23 | Morris David W | Novel compositions and methods in cancer |
| AU2003224732A1 (en) | 2002-03-25 | 2003-10-13 | The Trustees Of Boston University | Method of using anti-apoptotic factors in gene expression |
| DK1553966T3 (da) | 2002-10-03 | 2012-09-17 | Wyeth Corp | Fusionspeptider omfattende human papillomavirus E7- og E6- polypeptider samt immunogene sammensætninger deraf |
| US20070026076A1 (en) * | 2003-02-24 | 2007-02-01 | Tzyy-Choou Wu | Molecular vaccines employing nucleic acid encoding anti-apoptotic proteins |
| US9701725B2 (en) | 2003-05-05 | 2017-07-11 | The Johns Hopkins University | Anti-cancer DNA vaccine employing plasmids encoding signal sequence, mutant oncoprotein antigen, and heat shock protein |
| WO2005081716A2 (en) | 2003-11-24 | 2005-09-09 | The Johns Hopkins University | DNA VACCINES TARGETING ANTIGENS OF THE SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS (SARS-CoV) |
| AU2005322960A1 (en) | 2005-01-06 | 2006-07-13 | The Johns Hopkins University | RNA interference that blocks expression of pro-apoptotic proteins potentiates immunity induced by DNA and transfected dendritic cell vaccines |
| EP1846026A4 (en) | 2005-01-26 | 2008-07-02 | Univ Johns Hopkins | ANTIBODY DNA VACCINE WITH PLASMIDES FOR CODING A MUTATED ONCOPROTEIN ANTIGEN AND CALRETICULIN |
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2001
- 2001-08-02 WO PCT/US2001/024134 patent/WO2002012281A2/en not_active Ceased
- 2001-08-02 US US10/343,448 patent/US7342002B2/en not_active Expired - Lifetime
- 2001-08-02 CA CA2417214A patent/CA2417214C/en not_active Expired - Lifetime
- 2001-08-02 ES ES01956081.2T patent/ES2454640T3/es not_active Expired - Lifetime
- 2001-08-02 DK DK01956081.2T patent/DK1363938T3/en active
- 2001-08-02 JP JP2002518253A patent/JP5087201B2/ja not_active Expired - Lifetime
- 2001-08-02 EP EP01956081.2A patent/EP1363938B1/en not_active Expired - Lifetime
- 2001-08-02 AU AU2001278117A patent/AU2001278117A1/en not_active Abandoned
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2008
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- 2008-07-31 JP JP2008197856A patent/JP2009017883A/ja active Pending
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2012
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| JP2004527213A (ja) | 2004-09-09 |
| WO2002012281A3 (en) | 2003-07-10 |
| CA2417214A1 (en) | 2002-02-14 |
| AU2001278117A1 (en) | 2002-02-18 |
| EP1363938B1 (en) | 2013-12-11 |
| WO2002012281A9 (en) | 2003-03-06 |
| ES2454640T3 (es) | 2014-04-11 |
| JP5087201B2 (ja) | 2012-12-05 |
| US20090148471A1 (en) | 2009-06-11 |
| US20130203961A1 (en) | 2013-08-08 |
| US8007781B2 (en) | 2011-08-30 |
| EP1363938A2 (en) | 2003-11-26 |
| US20050054820A1 (en) | 2005-03-10 |
| WO2002012281A2 (en) | 2002-02-14 |
| DK1363938T3 (en) | 2014-03-24 |
| JP2009017883A (ja) | 2009-01-29 |
| US7342002B2 (en) | 2008-03-11 |
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Effective date: 20210803 |