DE69724428T3 - Humanisierte antikörper die an das gleiche antigen wie antikörper nr-lu-13 binden und deren verwendung in "pretargeting" verfahren - Google Patents
Humanisierte antikörper die an das gleiche antigen wie antikörper nr-lu-13 binden und deren verwendung in "pretargeting" verfahren Download PDFInfo
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- DE69724428T3 DE69724428T3 DE69724428T DE69724428T DE69724428T3 DE 69724428 T3 DE69724428 T3 DE 69724428T3 DE 69724428 T DE69724428 T DE 69724428T DE 69724428 T DE69724428 T DE 69724428T DE 69724428 T3 DE69724428 T3 DE 69724428T3
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Landscapes
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- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
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| US66036296A | 1996-06-07 | 1996-06-07 | |
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| PCT/US1997/010074 WO1997046589A2 (en) | 1996-06-07 | 1997-06-06 | Humanized antibodies that bind to the same antigen as bound by antibody nr-lu-13, and their use in pretargeting methods |
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| DE69724428D1 DE69724428D1 (de) | 2003-10-02 |
| DE69724428T2 DE69724428T2 (de) | 2004-06-09 |
| DE69724428T3 true DE69724428T3 (de) | 2009-07-23 |
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| US7632929B2 (en) | 2000-04-20 | 2009-12-15 | The Board Of Trustees Of The University Of Arkansas | Methamphetamine-like hapten compounds, linkers, carriers and compositions and uses thereof |
| US20020146753A1 (en) * | 2001-04-06 | 2002-10-10 | Henrik Ditzel | Autoantibodies to glucose-6-phosphate isomerase and their participation in autoimmune disease |
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| NZ535425A (en) | 2002-03-13 | 2008-05-30 | Biogen Idec Inc | Anti-alphavbeta6 antibodies |
| US7527966B2 (en) * | 2002-06-26 | 2009-05-05 | Transgenrx, Inc. | Gene regulation in transgenic animals using a transposon-based vector |
| US20040172667A1 (en) * | 2002-06-26 | 2004-09-02 | Cooper Richard K. | Administration of transposon-based vectors to reproductive organs |
| US20040242848A1 (en) * | 2003-04-21 | 2004-12-02 | Owens S. Michael | Mouse/human chimeric anti-phencyclidine antibody and uses thereof |
| US8071364B2 (en) * | 2003-12-24 | 2011-12-06 | Transgenrx, Inc. | Gene therapy using transposon-based vectors |
| US20050260131A1 (en) * | 2004-05-20 | 2005-11-24 | General Electric Company | Pharmaceuticals for enhanced delivery to disease targets |
| EP2302393A1 (en) * | 2004-05-21 | 2011-03-30 | The Institute for Systems Biology | Compositions and methods for quantification of serum glycoproteins |
| US20070009428A1 (en) * | 2005-07-06 | 2007-01-11 | Syud Faisal A | Compounds and methods for enhanced delivery to disease targets |
| US20070009427A1 (en) * | 2005-07-06 | 2007-01-11 | Syud Faisal A | Compounds and methods for enhanced delivery to disease targets |
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| US20070009435A1 (en) * | 2005-07-06 | 2007-01-11 | Syud Faisal A | Compositions and methods for enhanced delivery to target sites |
| CN104072614B (zh) | 2005-07-08 | 2017-04-26 | 生物基因Ma公司 | 抗-αvβ6 抗体及其用途 |
| SG173364A1 (en) | 2006-07-10 | 2011-08-29 | Biogen Idec Inc | Compositions and methods for inhibiting growth of smad4-deficient cancers |
| WO2008092041A2 (en) | 2007-01-24 | 2008-07-31 | Carnegie Mellon University | Optical biosensors |
| ES2619647T3 (es) * | 2007-04-20 | 2017-06-26 | Bioventures Llc | Compuestos de hapteno y composiciones y usos de los mismos |
| EP2342224A2 (en) * | 2008-09-25 | 2011-07-13 | TransGenRx, Inc. | Novel vectors for production of interferon |
| WO2010036976A2 (en) * | 2008-09-25 | 2010-04-01 | Transgenrx, Inc. | Novel vectors for production of antibodies |
| WO2010036978A2 (en) * | 2008-09-25 | 2010-04-01 | Transgenrx, Inc. | Novel vectors for production of growth hormone |
| US9150881B2 (en) * | 2009-04-09 | 2015-10-06 | Proteovec Holding, L.L.C. | Production of proteins using transposon-based vectors |
| EP2556163B1 (en) | 2010-04-07 | 2016-08-10 | Momenta Pharmaceuticals, Inc. | Method for quantifying high mannose containing glycoforms |
| WO2012125553A2 (en) | 2011-03-12 | 2012-09-20 | Momenta Pharmaceuticals, Inc. | N-acetylhexosamine-containing n-glycans in glycoprotein products |
| EP2856159A4 (en) | 2012-06-01 | 2016-04-13 | Momenta Pharmaceuticals Inc | METHODS RELATING TO DENOSUMAB |
| US9023353B2 (en) | 2013-03-13 | 2015-05-05 | The Board Of Trustees Of The University Of Arkansas | Anti-(+)—methamphetamine monoclonal antibodies |
| US10035860B2 (en) | 2013-03-15 | 2018-07-31 | Biogen Ma Inc. | Anti-alpha V beta 6 antibodies and uses thereof |
| WO2014144466A1 (en) | 2013-03-15 | 2014-09-18 | Biogen Idec Ma Inc. | Anti-alpha v beta 6 antibodies and uses thereof |
| EP2855533A4 (en) | 2013-03-15 | 2015-11-25 | Momenta Pharmaceuticals Inc | METHODS RELATING TO CTLA4-FC FUSION PROTEINS |
| US10464996B2 (en) | 2013-05-13 | 2019-11-05 | Momenta Pharmaceuticals, Inc. | Methods for the treatment of neurodegeneration |
| US20160257754A1 (en) | 2013-10-16 | 2016-09-08 | Momenta Pharmaceuticals Inc. | Sialylated glycoproteins |
| DK2970413T3 (en) | 2014-04-01 | 2018-10-15 | Swedish Orphan Biovitrum Ab Publ | Modified sulfamidase and its preparation |
| US20180265885A1 (en) * | 2015-01-29 | 2018-09-20 | Plantvax, Inc. | Highly expressed protective plant-derived broadly neutralizing hiv monoclonal antibodies for use in passive immunotherapy |
| CN109628531A (zh) * | 2018-12-25 | 2019-04-16 | 上海药明生物技术有限公司 | 抗体人源化改造方法 |
| EP4582810A3 (en) * | 2020-12-25 | 2025-12-31 | Denka Company Limited | METHOD FOR MEASURING TARGET ANTIGEN, AND INSOLUBLE PARTICLES AND TARGET ANTIGEN MEASUREMENT KIT USED THEREIN |
| CN116693672B (zh) * | 2023-06-15 | 2025-08-08 | 郑州伊美诺生物技术有限公司 | 抗3型人副流感病毒单克隆抗体及其制备方法和应用 |
Family Cites Families (96)
| Publication number | Priority date | Publication date | Assignee | Title |
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| US4468464A (en) | 1974-11-04 | 1984-08-28 | The Board Of Trustees Of The Leland Stanford Junior University | Biologically functional molecular chimeras |
| US4237224A (en) | 1974-11-04 | 1980-12-02 | Board Of Trustees Of The Leland Stanford Jr. University | Process for producing biologically functional molecular chimeras |
| US4634665A (en) | 1980-02-25 | 1987-01-06 | The Trustees Of Columbia University In The City Of New York | Processes for inserting DNA into eucaryotic cells and for producing proteinaceous materials |
| US5179017A (en) | 1980-02-25 | 1993-01-12 | The Trustees Of Columbia University In The City Of New York | Processes for inserting DNA into eucaryotic cells and for producing proteinaceous materials |
| 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 |
| US4656134A (en) | 1982-01-11 | 1987-04-07 | Board Of Trustees Of Leland Stanford Jr. University | Gene amplification in eukaryotic cells |
| GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US4879236A (en) | 1984-05-16 | 1989-11-07 | The Texas A&M University System | Method for producing a recombinant baculovirus expression vector |
| DE3584341D1 (de) | 1984-08-24 | 1991-11-14 | Upjohn Co | Rekombinante dna-verbindungen und expression von polypeptiden wie tpa. |
| GB8422238D0 (en) | 1984-09-03 | 1984-10-10 | Neuberger M S | Chimeric proteins |
| EP0200746B1 (en) | 1984-10-01 | 1991-01-30 | The General Hospital Corporation | Plant cells resistant to herbicidal glutamine synthetase inhibitors |
| US5168062A (en) | 1985-01-30 | 1992-12-01 | University Of Iowa Research Foundation | Transfer vectors and microorganisms containing human cytomegalovirus immediate-early promoter-regulatory DNA sequence |
| DE3668186D1 (de) | 1985-04-01 | 1990-02-15 | Celltech Ltd | Transformierte myeloma-zell-linie und dieselbe verwendendes verfahren zur expression eines gens, das ein eukaryontisches polypeptid kodiert. |
| US5169939A (en) | 1985-05-21 | 1992-12-08 | Massachusetts Institute Of Technology & Pres. & Fellows Of Harvard College | Chimeric antibodies |
| IL80529A0 (en) | 1985-11-14 | 1987-02-27 | Daiichi Seiyaku Co | Method of producing peptides |
| US5266314A (en) | 1985-12-02 | 1993-11-30 | Susumu Maeda | Insecticide making use of viruses and preparation process thereof |
| GB8601597D0 (en) | 1986-01-23 | 1986-02-26 | Wilson R H | Nucleotide sequences |
| US5057313A (en) * | 1986-02-25 | 1991-10-15 | The Center For Molecular Medicine And Immunology | Diagnostic and therapeutic antibody conjugates |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| GB8607679D0 (en) | 1986-03-27 | 1986-04-30 | Winter G P | Recombinant dna product |
| US5084396A (en) | 1986-06-20 | 1992-01-28 | Neorx Corporation | Enhanced production of antibodies utilizing insolubilized immune complexes |
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| US5869620A (en) * | 1986-09-02 | 1999-02-09 | Enzon, Inc. | Multivalent antigen-binding proteins |
| ATE87659T1 (de) | 1986-09-02 | 1993-04-15 | Enzon Lab Inc | Bindungsmolekuele mit einzelpolypeptidkette. |
| US5260203A (en) | 1986-09-02 | 1993-11-09 | Enzon, Inc. | Single polypeptide chain binding molecules |
| US5071748A (en) | 1986-09-09 | 1991-12-10 | Genetics Institute, Inc. | Mixed baculovirus compositions and uses thereof |
| NZ221790A (en) | 1986-09-12 | 1990-07-26 | Genentech Inc | Method for the continuous production of a heterologous protein in a eukaryotic host cell |
| US5120657A (en) | 1986-12-05 | 1992-06-09 | Agracetus, Inc. | Apparatus for genetic transformation |
| US5015580A (en) | 1987-07-29 | 1991-05-14 | Agracetus | Particle-mediated transformation of soybean plants and lines |
| EP0279582A3 (en) | 1987-02-17 | 1989-10-18 | Pharming B.V. | Dna sequences to target proteins to the mammary gland for efficient secretion |
| DE3852304T3 (de) | 1987-03-02 | 1999-07-01 | Enzon Labs Inc., Piscataway, N.J. | Organismus als Träger für "Single Chain Antibody Domain (SCAD)". |
| US5041379A (en) | 1987-03-16 | 1991-08-20 | American Biogenetic Science, Inc. | Heliothis expression systems |
| US4870023A (en) | 1987-03-16 | 1989-09-26 | American Biogenetic Sciences, Inc. | Recombinant baculovirus occlusion bodies in vaccines and biological insecticides |
| EP0307434B2 (en) | 1987-03-18 | 1998-07-29 | Scotgen Biopharmaceuticals, Inc. | Altered antibodies |
| US5132405A (en) | 1987-05-21 | 1992-07-21 | Creative Biomolecules, Inc. | Biosynthetic antibody binding sites |
| ATE120761T1 (de) | 1987-05-21 | 1995-04-15 | Creative Biomolecules Inc | Multifunktionelle proteine mit vorbestimmter zielsetzung. |
| US5091513A (en) | 1987-05-21 | 1992-02-25 | Creative Biomolecules, Inc. | Biosynthetic antibody binding sites |
| EP0393045B1 (en) | 1987-09-09 | 1995-03-29 | Celltech Therapeutics Limited | Fv antibody fragment production |
| US5196351A (en) | 1987-09-30 | 1993-03-23 | Beckman Instruments, Inc. | Bidentate conjugate and method of use thereof |
| EP0319206A3 (en) | 1987-11-30 | 1990-04-18 | Berlex Laboratories, Inc. | Gene amplification |
| IL89102A0 (en) | 1988-01-29 | 1989-08-15 | Lilly Co Eli | Vectors,compounds and methods for expression of a human adenocarcinoma antigen |
| US4937183A (en) * | 1988-02-03 | 1990-06-26 | Cytogen Corporation | Method for the preparation of antibody-fragment conjugates |
| US5047227A (en) * | 1988-02-08 | 1991-09-10 | Cytogen Corporation | Novel and improved antibodies for site specific attachment of compounds |
| ATE95068T1 (de) | 1988-02-12 | 1993-10-15 | British Tech Group | Modifizierte antikoerper. |
| JP3105898B2 (ja) | 1988-04-16 | 2000-11-06 | セルテック リミテッド | 組換えdnaタンパクの製造方法 |
| GB8809129D0 (en) | 1988-04-18 | 1988-05-18 | Celltech Ltd | Recombinant dna methods vectors and host cells |
| US4975369A (en) | 1988-04-21 | 1990-12-04 | Eli Lilly And Company | Recombinant and chimeric KS1/4 antibodies directed against a human adenocarcinoma antigen |
| GB8810808D0 (en) | 1988-05-06 | 1988-06-08 | Wellcome Found | Vectors |
| GB8823869D0 (en) | 1988-10-12 | 1988-11-16 | Medical Res Council | Production of antibodies |
| US5175384A (en) | 1988-12-05 | 1992-12-29 | Genpharm International | Transgenic mice depleted in mature t-cells and methods for making transgenic mice |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| IL162181A (en) | 1988-12-28 | 2006-04-10 | Pdl Biopharma Inc | A method of producing humanized immunoglubulin, and polynucleotides encoding the same |
| US5185254A (en) | 1988-12-29 | 1993-02-09 | The Wistar Institute | Gene family of tumor-associated antigens |
| WO1990010457A1 (en) * | 1989-03-14 | 1990-09-20 | New York University | Method of treating hiv infections using immunotoxins |
| US5179007A (en) | 1989-07-07 | 1993-01-12 | The Texas A & M University System | Method and vector for the purification of foreign proteins |
| US5077214A (en) | 1989-07-07 | 1991-12-31 | The Texas A&M University System | Use of baculovirus early promoters for expression of foreign genes in stably transformed insect cells |
| US5162222A (en) | 1989-07-07 | 1992-11-10 | Guarino Linda A | Use of baculovirus early promoters for expression of foreign genes in stably transformed insect cells or recombinant baculoviruses |
| US5413923A (en) | 1989-07-25 | 1995-05-09 | Cell Genesys, Inc. | Homologous recombination for universal donor cells and chimeric mammalian hosts |
| US5580774A (en) | 1989-07-31 | 1996-12-03 | Eli Lilly And Company | Chimeric antibodies directed against a human glycoprotein antigen |
| US5155037A (en) | 1989-08-04 | 1992-10-13 | The Texas A&M University System | Insect signal sequences useful to improve the efficiency of processing and secretion of foreign genes in insect systems |
| US5464764A (en) | 1989-08-22 | 1995-11-07 | University Of Utah Research Foundation | Positive-negative selection methods and vectors |
| GB8924021D0 (en) | 1989-10-25 | 1989-12-13 | Celltech Ltd | Recombinant dna method and vectors for the use therein |
| US5202422A (en) * | 1989-10-27 | 1993-04-13 | The Scripps Research Institute | Compositions containing plant-produced glycopolypeptide multimers, multimeric proteins and method of their use |
| GB8928874D0 (en) | 1989-12-21 | 1990-02-28 | Celltech Ltd | Humanised antibodies |
| CA2036935A1 (en) | 1990-02-26 | 1991-08-27 | Paul Christou | Plant transformation process with early identification of germ line transformation events |
| US5349053A (en) | 1990-06-01 | 1994-09-20 | Protein Design Labs, Inc. | Chimeric ligand/immunoglobulin molecules and their uses |
| US5149655A (en) | 1990-06-21 | 1992-09-22 | Agracetus, Inc. | Apparatus for genetic transformation |
| CA2089661C (en) | 1990-08-29 | 2007-04-03 | Nils Lonberg | 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 |
| GB9019812D0 (en) | 1990-09-11 | 1990-10-24 | Scotgen Ltd | Novel antibodies for treatment and prevention of infection in animals and man |
| US5169784A (en) | 1990-09-17 | 1992-12-08 | The Texas A & M University System | Baculovirus dual promoter expression vector |
| GB9022543D0 (en) | 1990-10-17 | 1990-11-28 | Wellcome Found | Antibody production |
| GB9023111D0 (en) | 1990-10-24 | 1990-12-05 | Wellcome Found | Expression system |
| US5191066A (en) * | 1990-12-07 | 1993-03-02 | Abbott Laboratories | Site-specific conjugation of immunoglobulins and detectable labels |
| ATE247168T1 (de) | 1991-03-06 | 2003-08-15 | Merck Patent Gmbh | Humanisierte monoklonale antikörper |
| DE122004000008I1 (de) | 1991-06-14 | 2005-06-09 | Genentech Inc | Humanisierter Heregulin Antikörper. |
| IT1248361B (it) | 1991-06-28 | 1995-01-05 | Enea | Vettori plasmidici per l'espressione di geni in piante |
| US5714350A (en) * | 1992-03-09 | 1998-02-03 | Protein Design Labs, Inc. | Increasing antibody affinity by altering glycosylation in the immunoglobulin variable region |
| GB9206422D0 (en) | 1992-03-24 | 1992-05-06 | Bolt Sarah L | Antibody preparation |
| EP0578515A3 (en) | 1992-05-26 | 1995-05-10 | Bristol Myers Squibb Co | Humanized monoclonal antibodies. |
| US6022966A (en) * | 1993-11-22 | 2000-02-08 | Neorx Corporation | Pretargeting methods and compounds |
| US5578287A (en) | 1992-06-09 | 1996-11-26 | Neorx Corporation | Three-step pretargeting methods using improved biotin-active agent |
| US5348886A (en) | 1992-09-04 | 1994-09-20 | Monsanto Company | Method of producing recombinant eukaryotic viruses in bacteria |
| US5639641A (en) | 1992-09-09 | 1997-06-17 | Immunogen Inc. | Resurfacing of rodent antibodies |
| IT1270866B (it) | 1993-03-10 | 1997-05-13 | Eniricerche Spa | Vettore ricombinante e suo impiego per la preparazione esocellulare di anticorpi in forma di singola molecola da bacillus subtilis |
| US5405779A (en) | 1993-04-09 | 1995-04-11 | Agracetus, Inc. | Apparatus for genetic transformation |
| US5670349A (en) * | 1993-08-02 | 1997-09-23 | Virginia Tech Intellectual Properties, Inc. | HMG2 promoter expression system and post-harvest production of gene products in plants and plant cell cultures |
| US5443953A (en) | 1993-12-08 | 1995-08-22 | Immunomedics, Inc. | Preparation and use of immunoconjugates |
| US5506125A (en) | 1993-12-22 | 1996-04-09 | Agracetus, Inc. | Gene delivery instrument with replaceable cartridges |
| ES2192573T3 (es) | 1994-01-21 | 2003-10-16 | Powderject Vaccines Inc | Instrumento de deposito de genes mediante arrastre gaseoso. |
| CU22615A1 (es) | 1994-06-30 | 2000-02-10 | Centro Inmunologia Molecular | Procedimiento de obtención de anticuerpos monoclonales murinos menos inmunogénicos. anticuerpos monoclonales obtenidos |
| US5525510A (en) | 1995-06-02 | 1996-06-11 | Agracetus, Inc. | Coanda effect gene delivery instrument |
| US5856106A (en) * | 1995-11-01 | 1999-01-05 | Biotransplant, Inc. | Determination of antibody production against administered therapeutic glycoproteins, especially monoclonal antibodies |
| WO1997046589A2 (en) * | 1996-06-07 | 1997-12-11 | Neorx Corporation | Humanized antibodies that bind to the same antigen as bound by antibody nr-lu-13, and their use in pretargeting methods |
| US7738094B2 (en) * | 2007-01-26 | 2010-06-15 | Becton, Dickinson And Company | Method, system, and compositions for cell counting and analysis |
-
1997
- 1997-06-06 WO PCT/US1997/010074 patent/WO1997046589A2/en not_active Ceased
- 1997-06-06 AT AT97931103T patent/ATE248192T1/de not_active IP Right Cessation
- 1997-06-06 JP JP50092698A patent/JP4503706B2/ja not_active Expired - Fee Related
- 1997-06-06 DE DE69724428T patent/DE69724428T3/de not_active Expired - Lifetime
- 1997-06-06 EP EP03010910A patent/EP1378525A3/en not_active Withdrawn
- 1997-06-06 EP EP97931103A patent/EP0909277B2/en not_active Expired - Lifetime
- 1997-06-06 CA CA2257357A patent/CA2257357C/en not_active Expired - Fee Related
- 1997-06-09 US US08/871,488 patent/US6358710B1/en not_active Expired - Fee Related
-
2002
- 2002-01-24 US US10/056,794 patent/US20030119078A1/en not_active Abandoned
-
2003
- 2003-07-31 US US10/631,660 patent/US20050100545A1/en not_active Abandoned
-
2004
- 2004-02-25 US US10/787,067 patent/US20050008635A1/en not_active Abandoned
-
2008
- 2008-03-19 US US12/051,805 patent/US20090094715A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| US20050100545A1 (en) | 2005-05-12 |
| EP1378525A2 (en) | 2004-01-07 |
| WO1997046589A2 (en) | 1997-12-11 |
| EP0909277B2 (en) | 2008-12-24 |
| DE69724428D1 (de) | 2003-10-02 |
| EP0909277B1 (en) | 2003-08-27 |
| US20090094715A1 (en) | 2009-04-09 |
| JP2001503017A (ja) | 2001-03-06 |
| CA2257357A1 (en) | 1997-12-11 |
| US6358710B1 (en) | 2002-03-19 |
| JP4503706B2 (ja) | 2010-07-14 |
| DE69724428T2 (de) | 2004-06-09 |
| EP0909277A2 (en) | 1999-04-21 |
| EP1378525A3 (en) | 2004-01-14 |
| WO1997046589A3 (en) | 2002-09-19 |
| CA2257357C (en) | 2010-04-13 |
| US20050008635A1 (en) | 2005-01-13 |
| US20030119078A1 (en) | 2003-06-26 |
| ATE248192T1 (de) | 2003-09-15 |
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