AU736993B2 - Practical in vitro sialylation of recombinant glycoproteins - Google Patents
Practical in vitro sialylation of recombinant glycoproteins Download PDFInfo
- Publication number
- AU736993B2 AU736993B2 AU62427/98A AU6242798A AU736993B2 AU 736993 B2 AU736993 B2 AU 736993B2 AU 62427/98 A AU62427/98 A AU 62427/98A AU 6242798 A AU6242798 A AU 6242798A AU 736993 B2 AU736993 B2 AU 736993B2
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- Australia
- Prior art keywords
- sialyltransferase
- amino acid
- glycoprotein
- recombinant
- acid sequence
- 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.)
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- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
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- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/1048—Glycosyltransferases (2.4)
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- Enzymes And Modification Thereof (AREA)
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Priority Applications (2)
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| AU91343/01A AU771407B2 (en) | 1997-01-16 | 2001-11-15 | Practical in vitro sialylation of recombinant glycoproteins |
| AU2004202707A AU2004202707B2 (en) | 1997-01-16 | 2004-06-18 | Practical in vitro sialylation of recombinant glycoproteins |
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| US3571097P | 1997-01-16 | 1997-01-16 | |
| US60/035710 | 1997-01-16 | ||
| PCT/US1998/000835 WO1998031826A1 (en) | 1997-01-16 | 1998-01-15 | Practical in vitro sialylation of recombinant glycoproteins |
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| AU91343/01A Division AU771407B2 (en) | 1997-01-16 | 2001-11-15 | Practical in vitro sialylation of recombinant glycoproteins |
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| AU6242798A AU6242798A (en) | 1998-08-07 |
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| AU62427/98A Ceased AU736993B2 (en) | 1997-01-16 | 1998-01-15 | Practical in vitro sialylation of recombinant glycoproteins |
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Families Citing this family (101)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE69823046T2 (de) * | 1997-01-16 | 2005-03-31 | Neose Technologies, Inc. | Praktische in vitro sialylierung von rekombinanten glykpproteinen |
| US6689604B1 (en) | 1998-03-20 | 2004-02-10 | National Research Council Of Canada | Lipopolysaccharide α-2,3 sialyltransferase of Campylobacter jejuni and its uses |
| ATE475714T1 (de) | 1998-12-09 | 2010-08-15 | Phyton Holdings Llc | Verfahren zur herstellung von glycoprotein mit menschlichem glycosylierungsbild |
| US7345019B1 (en) * | 1999-04-13 | 2008-03-18 | The Kenneth S. Warren Institute, Inc. | Modulation of excitable tissue function by peripherally administered erythropoietin |
| WO2001031045A1 (en) | 1999-10-26 | 2001-05-03 | Plant Research International B.V. | Mammalian-type glycosylation in plants |
| NZ522320A (en) * | 2000-05-12 | 2007-03-30 | Neose Technologies Inc | In vitro modification of glycosylation patterns of recombinant glycopeptides |
| US7767643B2 (en) | 2000-12-29 | 2010-08-03 | The Kenneth S. Warren Institute, Inc. | Protection, restoration, and enhancement of erythropoietin-responsive cells, tissues and organs |
| US20030072737A1 (en) * | 2000-12-29 | 2003-04-17 | Michael Brines | Tissue protective cytokines for the protection, restoration, and enhancement of responsive cells, tissues and organs |
| CN100385006C (zh) | 2001-01-19 | 2008-04-30 | 陶氏化学公司 | 利用植物细胞分泌性生产具有人型糖链的糖蛋白的方法 |
| ES2561985T3 (es) | 2001-10-10 | 2016-03-01 | Ratiopharm Gmbh | Remodelación y glicoconjugación de anticuerpos |
| US7795210B2 (en) | 2001-10-10 | 2010-09-14 | Novo Nordisk A/S | Protein remodeling methods and proteins/peptides produced by the methods |
| US7399613B2 (en) | 2001-10-10 | 2008-07-15 | Neose Technologies, Inc. | Sialic acid nucleotide sugars |
| US7157277B2 (en) | 2001-11-28 | 2007-01-02 | Neose Technologies, Inc. | Factor VIII remodeling and glycoconjugation of Factor VIII |
| US7265084B2 (en) | 2001-10-10 | 2007-09-04 | Neose Technologies, Inc. | Glycopegylation methods and proteins/peptides produced by the methods |
| US7125843B2 (en) | 2001-10-19 | 2006-10-24 | Neose Technologies, Inc. | Glycoconjugates including more than one peptide |
| US7214660B2 (en) | 2001-10-10 | 2007-05-08 | Neose Technologies, Inc. | Erythropoietin: remodeling and glycoconjugation of erythropoietin |
| US7439043B2 (en) | 2001-10-10 | 2008-10-21 | Neose Technologies, Inc. | Galactosyl nucleotide sugars |
| US7173003B2 (en) | 2001-10-10 | 2007-02-06 | Neose Technologies, Inc. | Granulocyte colony stimulating factor: remodeling and glycoconjugation of G-CSF |
| US7265085B2 (en) | 2001-10-10 | 2007-09-04 | Neose Technologies, Inc. | Glycoconjugation methods and proteins/peptides produced by the methods |
| US7179617B2 (en) | 2001-10-10 | 2007-02-20 | Neose Technologies, Inc. | Factor IX: remolding and glycoconjugation of Factor IX |
| US8008252B2 (en) * | 2001-10-10 | 2011-08-30 | Novo Nordisk A/S | Factor VII: remodeling and glycoconjugation of Factor VII |
| US7696163B2 (en) | 2001-10-10 | 2010-04-13 | Novo Nordisk A/S | Erythropoietin: remodeling and glycoconjugation of erythropoietin |
| US7297511B2 (en) | 2001-10-10 | 2007-11-20 | Neose Technologies, Inc. | Interferon alpha: remodeling and glycoconjugation of interferon alpha |
| US7226903B2 (en) | 2001-10-10 | 2007-06-05 | Neose Technologies, Inc. | Interferon beta: remodeling and glycoconjugation of interferon beta |
| AU2002340562B2 (en) * | 2001-10-22 | 2008-10-23 | Merck Serono Sa | Compositions of FSH with high sialylation degree and their use for the preparation of medicaments |
| US7473680B2 (en) | 2001-11-28 | 2009-01-06 | Neose Technologies, Inc. | Remodeling and glycoconjugation of peptides |
| JP2005535280A (ja) | 2001-11-28 | 2005-11-24 | ネオーズ テクノロジーズ， インコーポレイテッド | エンドグリカナーゼを用いる糖タンパク質のリモデリング |
| EP1485492B1 (en) | 2002-03-19 | 2011-12-21 | Stichting Dienst Landbouwkundig Onderzoek | Gntiii (udp-n-acetylglucosamine:beta-d mannoside beta(1,4)-n-acetylglucosaminyltransferase iii) expression in plants |
| JP4532118B2 (ja) | 2002-03-19 | 2010-08-25 | スティヒティング ディーンスト ランドバウクンディフ オンデルズーク | 植物体内のグリカンプロセシングの最適化 |
| CN1671420A (zh) | 2002-06-21 | 2005-09-21 | 诺和诺德医疗保健公司 | Peg化因子ⅶ糖型 |
| MXPA04012496A (es) | 2002-06-21 | 2005-09-12 | Novo Nordisk Healthcare Ag | Glicoformos del factor vii pegilados. |
| CA2491567A1 (en) * | 2002-07-01 | 2004-01-08 | The Kenneth S. Warren Institute, Inc. | Recombinant tissue protective cytokines and encoding nucleic acids thereof for protection, restoration, and enhancement of responsive cells, tissues, and organs |
| PL376318A1 (en) * | 2002-10-17 | 2005-12-27 | Pharming Intellectual Property B.V. | Protein modification |
| CL2003002461A1 (es) | 2002-11-27 | 2005-01-07 | Dow Chemical Company Agroscien | Inmunoglobulina que comprende al menos un glicano afucosilado, composicion que la contiene, secuencia nucleotidica y vector que la comprende, procedimiento para producir dicha inmunoglobulina en plantas. |
| CN102212019B (zh) | 2003-03-14 | 2015-05-27 | 蔚所番有限公司 | 支化水溶性聚合物及其缀合物 |
| US8791070B2 (en) | 2003-04-09 | 2014-07-29 | Novo Nordisk A/S | Glycopegylated factor IX |
| SG155777A1 (en) | 2003-04-09 | 2009-10-29 | Neose Technologies Inc | Glycopegylation methods and proteins/peptides produced by the methods |
| WO2004091499A2 (en) | 2003-04-09 | 2004-10-28 | Neose Technologies, Inc. | Intracellular formation of peptide conjugates |
| EP1624847B1 (en) * | 2003-05-09 | 2012-01-04 | BioGeneriX AG | Compositions and methods for the preparation of human growth hormone glycosylation mutants |
| WO2005012484A2 (en) | 2003-07-25 | 2005-02-10 | Neose Technologies, Inc. | Antibody-toxin conjugates |
| KR20070008519A (ko) * | 2003-09-29 | 2007-01-17 | 워렌 파마슈티칼즈 인코포레이티드 | 패혈증 및 유착 형성의 치료 및 예방용 조직 보호성사이토카인 |
| US20080305992A1 (en) * | 2003-11-24 | 2008-12-11 | Neose Technologies, Inc. | Glycopegylated erythropoietin |
| US8633157B2 (en) | 2003-11-24 | 2014-01-21 | Novo Nordisk A/S | Glycopegylated erythropoietin |
| US7842661B2 (en) * | 2003-11-24 | 2010-11-30 | Novo Nordisk A/S | Glycopegylated erythropoietin formulations |
| US20070254834A1 (en) | 2003-11-24 | 2007-11-01 | Defrees Shawn | Glycopegylated Erythropoietin |
| US20060040856A1 (en) | 2003-12-03 | 2006-02-23 | Neose Technologies, Inc. | Glycopegylated factor IX |
| US7956032B2 (en) | 2003-12-03 | 2011-06-07 | Novo Nordisk A/S | Glycopegylated granulocyte colony stimulating factor |
| JP5743368B2 (ja) | 2004-01-08 | 2015-07-01 | ラショファーム ゲーエムベーハー | ペプチドのｏ結合型グリコシル化 |
| EP1720892B1 (en) * | 2004-01-26 | 2013-07-24 | BioGeneriX AG | Branched polymer-modified sugars and nucleotides |
| ES2339953T5 (es) | 2004-05-04 | 2020-05-06 | Novo Nordisk Healthcare Ag | Glicoformas de factor VII ligadas a O y método de fabricación |
| US20080300173A1 (en) | 2004-07-13 | 2008-12-04 | Defrees Shawn | Branched Peg Remodeling and Glycosylation of Glucagon-Like Peptides-1 [Glp-1] |
| WO2006020372A2 (en) * | 2004-07-23 | 2006-02-23 | Neose Technologies, Inc. | Enzymatic modification of glycopeptides |
| US8268967B2 (en) | 2004-09-10 | 2012-09-18 | Novo Nordisk A/S | Glycopegylated interferon α |
| JP4812625B2 (ja) * | 2004-10-18 | 2011-11-09 | 日本たばこ産業株式会社 | 糖転移酵素の酵素活性を向上させる方法 |
| HUE026826T2 (en) | 2004-10-29 | 2016-07-28 | Ratiopharm Gmbh | Modeling and glycopegylation of fibroblast growth factor (FGF) |
| US20090196850A1 (en) | 2005-01-06 | 2009-08-06 | Novo Nordisk A/S | Anti-Kir Combination Treatments and Methods |
| WO2006074279A1 (en) * | 2005-01-06 | 2006-07-13 | Neose Technologies, Inc. | Glycoconjugation using saccharyl fragments |
| US9029331B2 (en) | 2005-01-10 | 2015-05-12 | Novo Nordisk A/S | Glycopegylated granulocyte colony stimulating factor |
| KR20080021590A (ko) * | 2005-03-24 | 2008-03-07 | 네오스 테크놀로지스, 인크. | 가용성이고 활성인 진핵생물 글리코실트랜스퍼라제의원핵생물 유기체 내에서의 발현 |
| EP1871795A4 (en) * | 2005-04-08 | 2010-03-31 | Biogenerix Ag | COMPOSITIONS AND METHOD FOR PRODUCING GLYCOSYLATION MUTANTS OF A PROTEASE-RESISTANT HUMAN GROWTH HORMONE |
| EP1891231A4 (en) | 2005-05-25 | 2011-06-22 | Novo Nordisk As | GLYCOPEGYLATED FACTOR IX |
| US20110003744A1 (en) * | 2005-05-25 | 2011-01-06 | Novo Nordisk A/S | Glycopegylated Erythropoietin Formulations |
| FI20055398A0 (fi) | 2005-07-08 | 2005-07-08 | Suomen Punainen Risti Veripalv | Menetelmä solupopulaatioiden evaluoimiseksi |
| JP2009515508A (ja) * | 2005-08-19 | 2009-04-16 | ネオス テクノロジーズ インコーポレイテッド | グリコｐｅｇ化因子ｖｉｉおよび因子ｖｉｉａ |
| US20070105755A1 (en) | 2005-10-26 | 2007-05-10 | Neose Technologies, Inc. | One pot desialylation and glycopegylation of therapeutic peptides |
| KR20080048505A (ko) | 2005-08-31 | 2008-06-02 | 센토코 인코포레이티드 | 증진된 작용자 기능을 지닌 항체 불변 영역을 생산하기위한 숙주 세포주 |
| US20090048440A1 (en) | 2005-11-03 | 2009-02-19 | Neose Technologies, Inc. | Nucleotide Sugar Purification Using Membranes |
| FR2901707B1 (fr) * | 2006-05-31 | 2017-09-29 | Lab Francais Du Fractionnement | Composition de facteur vii recombinant ou transgenique, chaque molecule de facteur vii possedant deux sites de n-glycosylation a motifs glycanniques definis |
| AR078117A1 (es) | 2006-06-20 | 2011-10-19 | Protech Pharma S A | Una muteina recombinante del interferon alfa humano glicosilado, un gen que codifica para dicha muteina, un metodo de produccion de dicho gen, un metodo para obtener una celula eucariota productora de dicha muteina, un metodo para producir dicha muteina, un procedimiento para purificar dicha muteina |
| US20080248959A1 (en) | 2006-07-21 | 2008-10-09 | Neose Technologies, Inc. | Glycosylation of peptides via o-linked glycosylation sequences |
| FR2904558B1 (fr) * | 2006-08-01 | 2008-10-17 | Lab Francais Du Fractionnement | "composition de facteur vii recombinant ou transgenique, presentant majoritairement des formes glycanniques biantennees, bisialylees et non fucosylees" |
| JP2010505874A (ja) * | 2006-10-03 | 2010-02-25 | ノヴォ ノルディスク アー／エス | ポリペプチドコンジュゲートの精製方法 |
| US20100041872A1 (en) | 2006-10-04 | 2010-02-18 | Defrees Shawn | Glycerol linked pegylated sugars and glycopeptides |
| JP2010512306A (ja) * | 2006-10-27 | 2010-04-22 | ザ ロックフェラー ユニバーシティー | 抗炎症特性が増強され、細胞毒性特性が減少したポリペプチドおよび関連する方法 |
| FI20075030A0 (fi) * | 2007-01-18 | 2007-01-18 | Suomen Punainen Risti Veripalv | Menetelmä solujen modifioimiseksi |
| RS52845B (sr) | 2007-04-03 | 2013-12-31 | Biogenerix Ag | Postupci tretmana korišćenjem glikopegiliranog g-csf |
| NZ580510A (en) | 2007-04-17 | 2011-06-30 | Stichting Dienst Landbouwkundi | Mammalian-type glycosylation in plants by expression of non-mammalian glycosyltransferases |
| AU2008245524A1 (en) * | 2007-04-26 | 2008-11-06 | Cnj Holdings, Inc. | Recombinant vitamin K dependent proteins with high sialic acid content and methods of preparing same |
| JP5876649B2 (ja) | 2007-06-12 | 2016-03-02 | ラツィオファルム ゲーエムベーハーｒａｔｉｏｐｈａｒｍ ＧｍｂＨ | ヌクレオチド糖の改良製造法 |
| US7968811B2 (en) * | 2007-06-29 | 2011-06-28 | Harley-Davidson Motor Company Group, Inc. | Integrated ignition and key switch |
| SI2197919T1 (sl) | 2007-08-27 | 2014-09-30 | Ratiopharm Gmbh | Tekoäśa formulacija g-csf konjugata |
| US8207112B2 (en) | 2007-08-29 | 2012-06-26 | Biogenerix Ag | Liquid formulation of G-CSF conjugate |
| ES2476690T3 (es) | 2008-02-27 | 2014-07-15 | Novo Nordisk A/S | Moléculas conjugadas del Factor VIII |
| TWI488640B (zh) | 2008-04-16 | 2015-06-21 | Ferring Int Ct Sa | 藥學製劑 |
| EP2166085A1 (en) | 2008-07-16 | 2010-03-24 | Suomen Punainen Risti Veripalvelu | Divalent modified cells |
| US20100240871A1 (en) | 2008-10-29 | 2010-09-23 | Raju T Shantha | Galactose Alpha(1-3) Galactose Compositions |
| US9234192B2 (en) | 2010-02-16 | 2016-01-12 | Novo Nordisk A/S | Conjugated proteins |
| CA2850469C (en) | 2011-10-01 | 2020-07-07 | Glytech, Inc. | Glycosylated polypeptide and pharmaceutical composition containing same |
| AU2013222414B2 (en) | 2012-02-21 | 2018-02-15 | Cytonics Corporation | Systems, compositions, and methods for transplantation |
| AU2014245917B2 (en) | 2013-03-29 | 2017-09-28 | Glytech, Inc. | Polypeptide having sialylated sugar chains attached thereto |
| US10464996B2 (en) | 2013-05-13 | 2019-11-05 | Momenta Pharmaceuticals, Inc. | Methods for the treatment of neurodegeneration |
| EP3038635A4 (en) | 2013-08-28 | 2017-04-05 | Cytonics Corporation | Systems, compositions, and methods for transplantation and treating conditions |
| US20160257754A1 (en) | 2013-10-16 | 2016-09-08 | Momenta Pharmaceuticals Inc. | Sialylated glycoproteins |
| US9616114B1 (en) | 2014-09-18 | 2017-04-11 | David Gordon Bermudes | Modified bacteria having improved pharmacokinetics and tumor colonization enhancing antitumor activity |
| US10889631B2 (en) | 2014-11-20 | 2021-01-12 | Cytonics Corporation | Therapeutic variant alpha-2-macroglobulin compositions |
| US10676723B2 (en) | 2015-05-11 | 2020-06-09 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| CN107810194B (zh) | 2015-05-22 | 2021-10-08 | 康诺贝林伦瑙有限公司 | 用于制备经修饰的血管性血友病因子的方法 |
| 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 |
| EP3678687B1 (en) | 2017-09-04 | 2022-08-17 | 89Bio Ltd. | Mutant fgf-21 peptide conjugates and uses thereof |
| US20220251619A1 (en) * | 2019-03-29 | 2022-08-11 | Agency For Science, Technology And Research | Method of Sialylating a Protein |
Family Cites Families (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5272066A (en) | 1986-03-07 | 1993-12-21 | Massachusetts Institute Of Technology | Synthetic method for enhancing glycoprotein stability |
| JPS63258591A (ja) * | 1987-04-17 | 1988-10-26 | Oji Paper Co Ltd | 配糖体の製造方法 |
| US5047335A (en) | 1988-12-21 | 1991-09-10 | The Regents Of The University Of Calif. | Process for controlling intracellular glycosylation of proteins |
| US5541083A (en) | 1989-10-24 | 1996-07-30 | The Regents Of The University Of California | Method for producing secretable glycosyltransferases and other golgi processing enzymes |
| AU668505B2 (en) | 1991-03-18 | 1996-05-09 | Scripps Research Institute, The | Oligosaccharide enzyme substrates and inhibitors: methods and compositions |
| US5352670A (en) * | 1991-06-10 | 1994-10-04 | Alberta Research Council | Methods for the enzymatic synthesis of alpha-sialylated oligosaccharide glycosides |
| JPH05166757A (ja) * | 1991-12-13 | 1993-07-02 | Tokyo Electron Ltd | 被処理体の温調装置 |
| GB9225054D0 (en) * | 1992-11-30 | 1993-01-20 | Baxenden Chem | Enzymatic synthesis |
| US5374541A (en) * | 1993-05-04 | 1994-12-20 | The Scripps Research Institute | Combined use of β-galactosidase and sialyltransferase coupled with in situ regeneration of CMP-sialic acid for one pot synthesis of oligosaccharides |
| US5409817A (en) | 1993-05-04 | 1995-04-25 | Cytel, Inc. | Use of trans-sialidase and sialyltransferase for synthesis of sialylα2→3βgalactosides |
| US5834251A (en) * | 1994-12-30 | 1998-11-10 | Alko Group Ltd. | Methods of modifying carbohydrate moieties |
| JPH11503328A (ja) * | 1995-04-11 | 1999-03-26 | サイテル コーポレイション | オリゴ糖類の改善された酵素合成法 |
| DE69823046T2 (de) * | 1997-01-16 | 2005-03-31 | Neose Technologies, Inc. | Praktische in vitro sialylierung von rekombinanten glykpproteinen |
-
1998
- 1998-01-15 DE DE69823046T patent/DE69823046T2/de not_active Expired - Fee Related
- 1998-01-15 NZ NZ336780A patent/NZ336780A/xx unknown
- 1998-01-15 IL IL13096498A patent/IL130964A0/xx not_active IP Right Cessation
- 1998-01-15 AU AU62427/98A patent/AU736993B2/en not_active Ceased
- 1998-01-15 EP EP98904583A patent/EP1015622B1/en not_active Expired - Lifetime
- 1998-01-15 CA CA2278178A patent/CA2278178C/en not_active Expired - Fee Related
- 1998-01-15 US US09/007,741 patent/US6399336B1/en not_active Expired - Lifetime
- 1998-01-15 WO PCT/US1998/000835 patent/WO1998031826A1/en not_active Ceased
- 1998-01-15 AT AT98904583T patent/ATE263841T1/de not_active IP Right Cessation
- 1998-01-15 JP JP51870998A patent/JP2001507215A/ja not_active Withdrawn
- 1998-01-15 ES ES98904583T patent/ES2218806T3/es not_active Expired - Lifetime
- 1998-01-15 DK DK98904583T patent/DK1015622T3/da active
-
1999
- 1999-07-15 IL IL130964A patent/IL130964A/en unknown
-
2001
- 2001-11-09 US US10/007,331 patent/US20020119516A1/en not_active Abandoned
-
2002
- 2002-02-21 US US10/081,456 patent/US20020160460A1/en not_active Abandoned
- 2002-02-21 US US10/081,455 patent/US7220555B2/en not_active Expired - Fee Related
- 2002-08-13 US US10/219,120 patent/US20030124645A1/en not_active Abandoned
-
2010
- 2010-10-08 JP JP2010229044A patent/JP2011024597A/ja not_active Withdrawn
Non-Patent Citations (1)
| Title |
|---|
| WILLIAMS ET AL,1995.GLYCOCONJUGATE JOURNAL, 12:755-761 * |
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| AU6242798A (en) | 1998-08-07 |
| ES2218806T3 (es) | 2004-11-16 |
| EP1015622A4 (en) | 2002-06-19 |
| US6399336B1 (en) | 2002-06-04 |
| US7220555B2 (en) | 2007-05-22 |
| DE69823046T2 (de) | 2005-03-31 |
| CA2278178A1 (en) | 1998-07-23 |
| ATE263841T1 (de) | 2004-04-15 |
| US20020160460A1 (en) | 2002-10-31 |
| WO1998031826A1 (en) | 1998-07-23 |
| EP1015622B1 (en) | 2004-04-07 |
| IL130964A (en) | 2006-06-11 |
| US20020119516A1 (en) | 2002-08-29 |
| EP1015622A1 (en) | 2000-07-05 |
| DE69823046D1 (de) | 2004-05-13 |
| NZ336780A (en) | 2000-12-22 |
| JP2001507215A (ja) | 2001-06-05 |
| IL130964A0 (en) | 2001-01-28 |
| US20030124645A1 (en) | 2003-07-03 |
| CA2278178C (en) | 2012-09-25 |
| JP2011024597A (ja) | 2011-02-10 |
| DK1015622T3 (da) | 2004-08-02 |
| US20020142370A1 (en) | 2002-10-03 |
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