CN105131104B - 肽的重构和糖缀合 - Google Patents
肽的重构和糖缀合 Download PDFInfo
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- CN105131104B CN105131104B CN201510483413.4A CN201510483413A CN105131104B CN 105131104 B CN105131104 B CN 105131104B CN 201510483413 A CN201510483413 A CN 201510483413A CN 105131104 B CN105131104 B CN 105131104B
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| US5581476A (en) * | 1993-01-28 | 1996-12-03 | Amgen Inc. | Computer-based methods and articles of manufacture for preparing G-CSF analogs |
| US5545553A (en) * | 1994-09-26 | 1996-08-13 | The Rockefeller University | Glycosyltransferases for biosynthesis of oligosaccharides, and genes encoding them |
| JP2003518075A (ja) | 1999-12-24 | 2003-06-03 | ジェネンテック・インコーポレーテッド | 生理活性化合物の消失半減期延長のための方法及び組成物 |
| EP2275557A1 (en) | 2000-04-12 | 2011-01-19 | Human Genome Sciences, Inc. | Albumin fusion proteins |
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| US7863020B2 (en) | 2000-06-28 | 2011-01-04 | Glycofi, Inc. | Production of sialylated N-glycans in lower eukaryotes |
| US7449308B2 (en) | 2000-06-28 | 2008-11-11 | Glycofi, Inc. | Combinatorial DNA library for producing modified N-glycans in lower eukaryotes |
| US7598055B2 (en) | 2000-06-28 | 2009-10-06 | Glycofi, Inc. | N-acetylglucosaminyltransferase III expression in lower eukaryotes |
| US7723296B2 (en) | 2001-01-18 | 2010-05-25 | Genzyme Corporation | Methods for introducing mannose-6-phosphate and other oligosaccharides onto glycoproteins and its application thereof |
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| US7112410B1 (en) | 2001-08-29 | 2006-09-26 | Human Genome Sciences, Inc. | Human tumor necrosis factor TR21 and methods based thereon |
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| 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 |
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| US7473680B2 (en) * | 2001-11-28 | 2009-01-06 | Neose Technologies, Inc. | Remodeling and glycoconjugation of peptides |
| EP2990417A1 (en) * | 2001-12-21 | 2016-03-02 | Human Genome Sciences, Inc. | Albumin insulin fusion protein |
| EP2399586A1 (en) | 2002-01-11 | 2011-12-28 | Jefferies, Dr., Wilfred | Use of P97 as an enzyme delivery system for the delivery of therapeutic lysosomal enzymes |
| DE10209821A1 (de) | 2002-03-06 | 2003-09-25 | Biotechnologie Ges Mittelhesse | Kopplung von Proteinen an ein modifiziertes Polysaccharid |
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| US7598354B2 (en) * | 2002-08-01 | 2009-10-06 | National Research Council Of Canada | Campylobacter glycans and glycopeptides |
| US7611700B2 (en) * | 2002-09-09 | 2009-11-03 | Hanall Pharmaceuticals, Co., Ltd. | Protease resistant modified interferon alpha polypeptides |
| ATE409048T1 (de) | 2002-10-08 | 2008-10-15 | Fresenius Kabi De Gmbh | Pharmazeutisch aktive oligosaccharid-conjugate |
| SG160203A1 (en) | 2002-10-16 | 2010-04-29 | Scripps Research Inst | Glycoprotein synthesis |
| JP4699028B2 (ja) * | 2002-11-08 | 2011-06-08 | ザ ブライアム アンド ウィミンズ ホスピタル インコーポレーテッド | 血小板の生存を延長するための組成物および方法 |
| US7332299B2 (en) | 2003-02-20 | 2008-02-19 | Glycofi, Inc. | Endomannosidases in the modification of glycoproteins in eukaryotes |
| AU2004221824B2 (en) | 2003-03-14 | 2009-08-27 | Ratiopharm Gmbh | Branched water-soluble polymers and their conjugates |
| US8791070B2 (en) | 2003-04-09 | 2014-07-29 | Novo Nordisk A/S | Glycopegylated factor IX |
| WO2006127896A2 (en) | 2005-05-25 | 2006-11-30 | Neose Technologies, Inc. | Glycopegylated factor ix |
| WO2004091499A2 (en) * | 2003-04-09 | 2004-10-28 | Neose Technologies, Inc. | Intracellular formation of peptide conjugates |
| US20050008580A1 (en) * | 2003-04-09 | 2005-01-13 | Wyeth | Hemophilia treatment by inhalation of coagulation factors |
| CA2522345A1 (en) * | 2003-04-09 | 2004-11-18 | Neose Technologies, Inc. | Glycopegylation methods and proteins/peptides produced by the methods |
| ES2380093T3 (es) | 2003-05-09 | 2012-05-08 | Biogenerix Ag | Composiciones y métodos para la preparación de mutantes de glucosilación de la hormona del crecimiento humana |
| WO2005012484A2 (en) | 2003-07-25 | 2005-02-10 | Neose Technologies, Inc. | Antibody-toxin conjugates |
| WO2005014655A2 (en) | 2003-08-08 | 2005-02-17 | Fresenius Kabi Deutschland Gmbh | Conjugates of hydroxyalkyl starch and a protein |
| US8338373B2 (en) * | 2003-10-24 | 2012-12-25 | Nora Therapeutics, Inc. | Method for reducing the risk of spontaneous abortion in a human female subject |
| EP2441465B1 (en) * | 2003-10-24 | 2014-01-15 | Nora Therapeutics, Inc. | Compositions and methods for healthy pregnancy |
| US20090226397A1 (en) | 2003-10-24 | 2009-09-10 | Nora Therapeutics, Inc. | Compositions and methods for reducing the likelihood of implantation failure or miscarriage in recipients of artificial insemination |
| US7507573B2 (en) | 2003-11-14 | 2009-03-24 | Vib, Vzw | Modification of protein glycosylation in methylotrophic yeast |
| WO2005051429A2 (en) * | 2003-11-19 | 2005-06-09 | Government Of The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Targeted conjugates with a modified saccharide linker |
| WO2005072371A2 (en) * | 2004-01-26 | 2005-08-11 | Neose Technologies, Inc. | Branched polymeric sugars and nucleotides thereof |
| JP4719686B2 (ja) * | 2003-11-24 | 2011-07-06 | バイオジェネリックス アーゲー | GlycoPEG化エリスロポエチン |
| 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 |
| CN1890257A (zh) | 2003-12-01 | 2007-01-03 | 诺和诺德医疗保健公司 | 液体因子ⅶ组合物的病毒过滤 |
| US20060040856A1 (en) | 2003-12-03 | 2006-02-23 | Neose Technologies, Inc. | Glycopegylated factor IX |
| BRPI0417342A (pt) * | 2003-12-03 | 2007-04-17 | Neose Technologies Inc | fator estimulante de colÈnia de granulócitos glicopeguilado |
| US20080318850A1 (en) * | 2003-12-03 | 2008-12-25 | Neose Technologies, Inc. | Glycopegylated Factor Ix |
| CA2549413A1 (en) * | 2003-12-03 | 2005-06-23 | Neose Technologies, Inc. | Glycopegylated factor ix |
| US7956032B2 (en) | 2003-12-03 | 2011-06-07 | Novo Nordisk A/S | Glycopegylated granulocyte colony stimulating factor |
| KR20140093711A (ko) | 2003-12-19 | 2014-07-28 | 노보 노르디스크 헬스 케어 악티엔게젤샤프트 | 인자 vii 폴리펩티드의 안정화된 조성물 |
| BRPI0506741A (pt) | 2004-01-08 | 2007-05-15 | Neose Technologies Inc | glicosilação de peptìdeos ligados a o |
| NZ548308A (en) * | 2004-01-26 | 2010-11-26 | Biogenerix Ag | Branched polymeric sugars and nucleotides thereof |
| BRPI0507169A (pt) * | 2004-02-02 | 2007-06-26 | Ambrx Inc | polipeptìdeos do hormÈnio de crescimento humano modificados e seu usos |
| AU2005211725B2 (en) * | 2004-02-09 | 2010-07-15 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| AR048098A1 (es) * | 2004-03-15 | 2006-03-29 | Wyeth Corp | Conjugados de caliqueamicina |
| EP1744786A2 (en) * | 2004-03-23 | 2007-01-24 | Amgen Inc. | Chemically modified protein compositions and methods |
| MXPA06012676A (es) | 2004-05-04 | 2007-04-02 | Novo Nordisk Healthcare Ag | Glucoformas o-enlazadas de polipeptidos y metodos de fabricacion de los mismos. |
| US20050287639A1 (en) | 2004-05-17 | 2005-12-29 | California Institute Of Technology | Methods of incorporating amino acid analogs into proteins |
| KR101100059B1 (ko) * | 2004-06-30 | 2011-12-29 | 넥타르 테라퓨틱스 | 중합체인자 ix 부분의 접합체 |
| AU2014280936B2 (en) * | 2004-06-30 | 2016-12-15 | Nektar Therapeutics | Polymer-factor ix moiety conjugates |
| EP1771066A2 (en) | 2004-07-13 | 2007-04-11 | Neose Technologies, Inc. | Branched peg remodeling and glycosylation of glucagon-like peptide-1 glp-1 |
| US20090292110A1 (en) * | 2004-07-23 | 2009-11-26 | Defrees Shawn | Enzymatic modification of glycopeptides |
| US20120225044A9 (en) * | 2004-09-07 | 2012-09-06 | Zymequest, Inc. | Compositions and methods for prolonging survival of platelets |
| US8052667B2 (en) * | 2004-09-07 | 2011-11-08 | Velico Medical, Inc. | Apparatus for prolonging survival of platelets |
| EP1799249A2 (en) * | 2004-09-10 | 2007-06-27 | Neose Technologies, Inc. | Glycopegylated interferon alpha |
| KR20070073886A (ko) * | 2004-10-05 | 2007-07-10 | 제넨테크, 인크. | 독성이 감소된 치료제 |
| AU2005295467B2 (en) * | 2004-10-15 | 2011-07-07 | Velico Medical, Inc. | Compositions and methods for prolonging survival of platelets |
| US20080064059A1 (en) | 2004-10-20 | 2008-03-13 | Scripps Research Institute | In Vivo Site-Specific Incorporation of N-Acetyl-Galactosamine Amino Acids in Eubacteria |
| EP3061461A1 (en) * | 2004-10-29 | 2016-08-31 | ratiopharm GmbH | Remodeling and glycopegylation of fibroblast growth factor (fgf) |
| WO2006066258A2 (en) * | 2004-12-17 | 2006-06-22 | Neose Technologies, Inc. | Lipoconjugation of peptides |
| EP2360171A1 (en) | 2004-12-23 | 2011-08-24 | Novo Nordisk Health Care AG | Reduction of the content of protein contaminants in compositions comprising a vitamin K-dependent protein of interest |
| US20100009902A1 (en) * | 2005-01-06 | 2010-01-14 | Neose Technologies, Inc. | Glycoconjugation Using Saccharyl Fragments |
| NZ556436A (en) * | 2005-01-10 | 2010-11-26 | Biogenerix Ag | Glycopegylated granulocyte colony stimulating factor |
| JP2008527980A (ja) * | 2005-01-25 | 2008-07-31 | アポロ ライフ サイエンシズ リミテッド | 分子およびそのキメラ分子 |
| EP1861423A4 (en) * | 2005-02-15 | 2010-01-27 | Apollo Life Sciences Ltd | MOLECULES AND CHIMESE MOLECULES THEREOF |
| KR20070110902A (ko) * | 2005-03-11 | 2007-11-20 | 프레제니우스 카비 도이치란트 게엠베하 | 비활성 출발 물질로부터 생물활성 당단백질의 생산 |
| KR20080021590A (ko) * | 2005-03-24 | 2008-03-07 | 네오스 테크놀로지스, 인크. | 가용성이고 활성인 진핵생물 글리코실트랜스퍼라제의원핵생물 유기체 내에서의 발현 |
| JP2008538181A (ja) * | 2005-03-30 | 2008-10-16 | ネオス テクノロジーズ インコーポレイテッド | 昆虫細胞系において増殖させたペプチドを生産するための製造方法 |
| EP1876441B1 (en) * | 2005-03-31 | 2010-10-06 | The Noguchi Institute | Analysis method for biological sample and screening method for disease marker |
| US9187546B2 (en) | 2005-04-08 | 2015-11-17 | Novo Nordisk A/S | Compositions and methods for the preparation of protease resistant human growth hormone glycosylation mutants |
| JP5628476B2 (ja) | 2005-04-28 | 2014-11-19 | ベンタナ・メデイカル・システムズ・インコーポレーテツド | 抗体コンジュゲート |
| WO2006127910A2 (en) | 2005-05-25 | 2006-11-30 | Neose Technologies, Inc. | Glycopegylated erythropoietin formulations |
| US20110003744A1 (en) * | 2005-05-25 | 2011-01-06 | Novo Nordisk A/S | Glycopegylated Erythropoietin Formulations |
| EP2360170A3 (en) | 2005-06-17 | 2012-03-28 | Novo Nordisk Health Care AG | Selective reduction and derivatization of engineered proteins comprinsing at least one non-native cysteine |
| US7696318B2 (en) | 2005-07-13 | 2010-04-13 | Novo Nordisk Health Care Ag | Host cell protein knock-out cells for production of therapeutic proteins |
| US20070105755A1 (en) | 2005-10-26 | 2007-05-10 | Neose Technologies, Inc. | One pot desialylation and glycopegylation of therapeutic peptides |
| CN102719508A (zh) * | 2005-08-19 | 2012-10-10 | 诺和诺德公司 | 糖基聚乙二醇化的因子vii和因子viia |
| AU2006283560B2 (en) * | 2005-08-19 | 2011-12-08 | Centocor, Inc. | Proteolysis resistant antibody preparations |
| EP1924689B1 (en) | 2005-09-01 | 2014-08-13 | Novo Nordisk Health Care AG | Hydrophobic interaction chromatography purification of factor vii polypeptides |
| JP5690047B2 (ja) | 2005-09-14 | 2015-03-25 | ノボ ノルディスク ヘルス ケア アーゲー | ヒト凝固第vii因子ポリペプチド |
| EP1937294A4 (en) * | 2005-10-21 | 2009-11-04 | Synageva Biopharma Corp | GLYCOLIC AND GLYCOSYLATED THERAPEUTIC PROTEINS DERIVED FROM POULTRY |
| US20090048440A1 (en) | 2005-11-03 | 2009-02-19 | Neose Technologies, Inc. | Nucleotide Sugar Purification Using Membranes |
| US8247530B2 (en) * | 2005-11-08 | 2012-08-21 | Palatin Technologies, Inc. | N-alkylated cyclic peptide melanocortin agonists |
| ES2804129T3 (es) * | 2005-11-23 | 2021-02-03 | Ventana Med Syst Inc | Conjugado anticuerpo-enzima |
| EP1816201A1 (en) * | 2006-02-06 | 2007-08-08 | CSL Behring GmbH | Modified coagulation factor VIIa with extended half-life |
| EP2623610B1 (en) † | 2006-02-10 | 2015-04-29 | Life Technologies Corporation | Labeling and detection of post translationally modified proteins |
| CA2647632C (en) | 2006-03-27 | 2017-06-27 | University Of Maryland Biotechnology Institute | Glycoprotein synthesis and remodeling by enzymatic transglycosylation |
| US7645860B2 (en) * | 2006-03-31 | 2010-01-12 | Baxter Healthcare S.A. | Factor VIII polymer conjugates |
| US7982010B2 (en) * | 2006-03-31 | 2011-07-19 | Baxter International Inc. | Factor VIII polymer conjugates |
| CA2647314A1 (en) | 2006-03-31 | 2007-11-08 | Baxter International Inc. | Pegylated factor viii |
| US7985839B2 (en) * | 2006-03-31 | 2011-07-26 | Baxter International Inc. | Factor VIII polymer conjugates |
| WO2007117685A2 (en) | 2006-04-07 | 2007-10-18 | Nektar Therapeutics Al, Corporation | Conjugates of an anti-tnf-alpha antibody |
| JP2009534034A (ja) | 2006-04-19 | 2009-09-24 | ノヴォ ノルディスク アクティーゼルスカブ | 原核微生物におけるo−グリコシル化治療用タンパク質の発現 |
| AU2007248680C1 (en) | 2006-05-02 | 2014-01-23 | Allozyne, Inc. | Non-natural amino acid substituted polypeptides |
| CA2654055A1 (en) | 2006-06-07 | 2007-12-21 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| CA2655246A1 (en) * | 2006-06-09 | 2007-12-21 | University Of Maryland, Baltimore | Glycosylation engineered antibody therapy |
| 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 |
| US9187532B2 (en) | 2006-07-21 | 2015-11-17 | Novo Nordisk A/S | Glycosylation of peptides via O-linked glycosylation sequences |
| JP2009544680A (ja) * | 2006-07-25 | 2009-12-17 | リポクセン テクノロジーズ リミテッド | ポリサッカライドによるタンパク質のn末端誘導体化 |
| WO2008057683A2 (en) * | 2006-10-03 | 2008-05-15 | Novo Nordisk A/S | Methods for the purification of polypeptide conjugates |
| CN101600448B (zh) * | 2006-10-04 | 2015-11-25 | 诺和诺德公司 | 甘油连接的peg化的糖和糖肽 |
| WO2008073620A2 (en) * | 2006-11-02 | 2008-06-19 | Neose Technologies, Inc. | Manufacturing process for the production of polypeptides expressed in insect cell-lines |
| CN101678079B (zh) | 2006-11-28 | 2013-12-25 | 韩诺生物制约株式会社 | 修饰的促红细胞生成素多肽及其治疗用途 |
| JP5876208B2 (ja) | 2006-12-15 | 2016-03-02 | バクスター・インターナショナル・インコーポレイテッドBaxter International Incorp0Rated | 延長されたinvivo半減期を有する第VIIa因子−(ポリ)シアル酸結合体 |
| WO2008089339A2 (en) * | 2007-01-18 | 2008-07-24 | Genzyme Corporation | Oligosaccharide conjugates for cellular targeting |
| IL243117B2 (en) | 2007-01-18 | 2023-03-01 | Genzyme Corp | Oligosaccharides containing an amino group and their conjugates |
| US7960139B2 (en) | 2007-03-23 | 2011-06-14 | Academia Sinica | Alkynyl sugar analogs for the labeling and visualization of glycoconjugates in cells |
| ES2385114T3 (es) * | 2007-03-30 | 2012-07-18 | Ambrx, Inc. | Polipéptidos de FGF-21 modificados y sus usos |
| BRPI0809670A8 (pt) | 2007-04-03 | 2018-12-18 | Biogenerix Ag | métodos para aumentar a produção de célula tronco, para aumentar o número de granulócitos em um indivíduo, para prevenir, tratar e aliviar a mielossupressão que resulta de uma terapia contra o câncer, para tratar uma condição em um indivíduo, para tratar neutropenia e trombocitopenia em um mamífero, para expandir células tronco hematopoiéticas em cultura, para aumentar a hematopoiese em um indivíduo, para aumentar o número de célulars progenitoras hematopoiéticas em um indivíduo, e para fornecer enxerto estável da medula óssea, e, forma de dosagem oral. |
| WO2008124706A2 (en) | 2007-04-06 | 2008-10-16 | Arizona Board Of Regents Acting For And On Behalf Of Arizona State University | Devices and methods for target molecule characterization |
| US20090053167A1 (en) * | 2007-05-14 | 2009-02-26 | Neose Technologies, Inc. | C-, S- and N-glycosylation of peptides |
| MX2009013259A (es) * | 2007-06-12 | 2010-01-25 | Novo Nordisk As | Proceso mejorado para la produccion de azucares de nucleotidos. |
| AU2008275911A1 (en) * | 2007-07-19 | 2009-01-22 | Arizona Board of Regents, a body corporate acting for and on behalf of Arizona State University | Self- anchoring MEMS intrafascicular neural electrode |
| BRPI0815416A2 (pt) * | 2007-08-15 | 2014-10-21 | Amunix Inc | Composições e métodos para modificar propriedades de polipeptídeos biologicamente ativos |
| PL2197919T3 (pl) | 2007-08-27 | 2014-09-30 | Ratiopharm Gmbh | Ciekły preparat koniugatu G-CSF |
| US8207112B2 (en) | 2007-08-29 | 2012-06-26 | Biogenerix Ag | Liquid formulation of G-CSF conjugate |
| EP2222329A1 (en) * | 2007-11-09 | 2010-09-01 | Baxter International Inc. | Modified recombinant factor viii and von willebrand factor and methods of use |
| JP5571576B2 (ja) * | 2008-01-07 | 2014-08-13 | シナジェバ・バイオファーマ・コーポレイション | トリにおけるグリコシル化 |
| JP5647899B2 (ja) * | 2008-01-08 | 2015-01-07 | ラツィオファルム ゲーエムベーハーratiopharm GmbH | オリゴサッカリルトランスフェラーゼを使用するポリペプチドの複合糖質化 |
| RU2573587C2 (ru) | 2008-02-27 | 2016-01-20 | Ново Нордиск А/С | Конъюгированные молекулы фактора viii |
| US8628649B2 (en) | 2008-03-18 | 2014-01-14 | Arizona Board Of Regents Acting For And On Behalf Of Arizona State University | Nanopore and carbon nanotube based DNA sequencer and a serial recognition sequencer |
| WO2009117517A2 (en) | 2008-03-18 | 2009-09-24 | Arizona Board Of Regents Acting For And On Behalf Of Arizona State University | Nanopore and carbon nanotube based dna sequencer |
| KR20110033242A (ko) * | 2008-06-25 | 2011-03-30 | 바이엘 헬스케어 엘엘씨 | 면역원성이 감소된, 인자 ⅷ 뮤테인 |
| JP5986745B2 (ja) | 2008-07-15 | 2016-09-06 | アカデミア シニカAcademia Sinica | Ptfe様のアルミニウム・コート・ガラススライド上のグリカンアレイおよび関連する方法 |
| US8968540B2 (en) | 2008-10-06 | 2015-03-03 | Arizona Board Of Regents, A Body Corporate Of The State Of Arizona Acting For And On Behalf Of Arizona State University | Trans-base tunnel reader for sequencing |
| HUE044381T2 (hu) | 2008-12-16 | 2019-10-28 | Genzyme Corp | Szintetikus intermedierek oligoszacharid-fehérje konjugátumok elõállításához |
| SG193837A1 (en) * | 2009-01-28 | 2013-10-30 | Smartcells Inc | Conjugate based systems for controlled drug delivery |
| PL2393828T3 (pl) | 2009-02-03 | 2017-06-30 | Amunix Operating Inc. | Wydłużone rekombinowane polipeptydy i zawierające je kompozycje |
| US20110046060A1 (en) * | 2009-08-24 | 2011-02-24 | Amunix Operating, Inc., | Coagulation factor IX compositions and methods of making and using same |
| WO2010096394A2 (en) | 2009-02-17 | 2010-08-26 | Redwood Biosciences, Inc. | Aldehyde-tagged protein-based drug carriers and methods of use |
| EP2410846B1 (en) | 2009-03-25 | 2016-09-07 | Seneb Biosciences, Inc. | Glycolipids as treatment for disease |
| EP2417155B1 (en) | 2009-04-06 | 2013-06-19 | Novo Nordisk A/S | Targeted delivery of factor viii proteins to platelets |
| WO2010146362A2 (en) * | 2009-06-16 | 2010-12-23 | The University Of Bath | Materials and methods relating to glycosylation |
| JP5909755B2 (ja) | 2009-07-27 | 2016-04-27 | リポクセン テクノロジーズ リミテッド | 非血液凝固タンパク質の糖ポリシアル酸化 |
| EP3093029A1 (en) | 2009-07-27 | 2016-11-16 | Baxalta GmbH | Blood coagulation protein conjugates |
| US8809501B2 (en) | 2009-07-27 | 2014-08-19 | Baxter International Inc. | Nucleophilic catalysts for oxime linkage |
| SG178141A1 (en) | 2009-07-27 | 2012-03-29 | Baxter Int | Blood coagulation protein conjugates |
| US8642737B2 (en) | 2010-07-26 | 2014-02-04 | Baxter International Inc. | Nucleophilic catalysts for oxime linkage |
| WO2011018515A1 (en) | 2009-08-14 | 2011-02-17 | Novo Nordisk Health Care Ag | Method of purifying pegylated proteins |
| GB0915403D0 (en) * | 2009-09-04 | 2009-10-07 | London School Hygiene & Tropical Medicine | Protein glycosylation |
| WO2011045704A1 (en) | 2009-10-12 | 2011-04-21 | Pfizer Inc. | Cancer treatment |
| US8697844B2 (en) | 2009-11-24 | 2014-04-15 | Novo Nordisk A/S | Method of purifying pegylated proteins |
| US10087236B2 (en) * | 2009-12-02 | 2018-10-02 | Academia Sinica | Methods for modifying human antibodies by glycan engineering |
| US11377485B2 (en) | 2009-12-02 | 2022-07-05 | Academia Sinica | Methods for modifying human antibodies by glycan engineering |
| JP2013512674A (ja) * | 2009-12-02 | 2013-04-18 | アクセルロン ファーマ, インコーポレイテッド | Fc融合タンパク質の血清半減期を増加させるための組成物および方法 |
| US20130040888A1 (en) | 2010-02-16 | 2013-02-14 | Novo Nordisk A/S | Factor VIII Molecules With Reduced VWF Binding |
| EP2977055A1 (en) | 2010-02-16 | 2016-01-27 | Novo Nordisk A/S | Factor viii fusion protein |
| AU2011223627B2 (en) | 2010-03-04 | 2015-06-18 | Pfenex Inc. | Method for producing soluble recombinant interferon protein without denaturing |
| NZ603033A (en) | 2010-04-01 | 2014-06-27 | Pfenex Inc | Methods for g-csf production in a pseudomonas host cell |
| WO2011130332A1 (en) | 2010-04-12 | 2011-10-20 | Academia Sinica | Glycan arrays for high throughput screening of viruses |
| US8962345B2 (en) * | 2010-05-21 | 2015-02-24 | The United States Of America As Represented By The Secretary Of Commerce | Method of characterizing glycans attached to glycoproteins |
| CN103080135B (zh) | 2010-06-30 | 2017-06-13 | 诺沃—诺迪斯克有限公司 | 能够特异性结合组织因子途径抑制剂的抗体 |
| NZ605348A (en) | 2010-07-09 | 2015-01-30 | Biogen Idec Hemophilia Inc | Factor ix polypeptides and methods of use thereof |
| WO2012007324A2 (en) | 2010-07-15 | 2012-01-19 | Novo Nordisk A/S | Stabilized factor viii variants |
| US9074015B2 (en) | 2010-07-28 | 2015-07-07 | Smartcells, Inc. | Recombinantly expressed insulin polypeptides and uses thereof |
| JP2013535198A (ja) | 2010-07-30 | 2013-09-12 | グリコド | 哺乳類のグリコシル化経路を有する酵母人工染色体 |
| ES2534936T3 (es) | 2010-08-02 | 2015-04-30 | Ratiopharm Gmbh | Método para producir y purificar una sialiltransferasa soluble activa |
| JP6173911B2 (ja) | 2010-09-10 | 2017-08-09 | メディミューン リミテド | 抗体誘導体 |
| CN103209992A (zh) | 2010-09-15 | 2013-07-17 | 诺沃—诺迪斯克有限公司 | 具有减少的细胞摄取的因子viii变体 |
| EP2619228A1 (en) | 2010-09-22 | 2013-07-31 | Novo Nordisk A/S | Therapeutic factor viii antibodies |
| RU2604490C2 (ru) | 2010-11-05 | 2016-12-10 | Займворкс Инк. | ДИЗАЙН УСТОЙЧИВОГО ГЕТЕРОДИМЕРНОГО АНТИТЕЛА С МУТАЦИЯМИ В Fc ДОМЕНЕ |
| RU2013131911A (ru) | 2010-12-16 | 2015-01-27 | Ново Нордиск А/С | Водный раствор фактора viii |
| DK2654794T3 (da) | 2010-12-22 | 2020-06-08 | Baxalta GmbH | Materialer og fremgangsmåder til konjugering af et vandopløseligt fedtsyrederivat til et protein |
| MX2013006234A (es) * | 2011-01-06 | 2013-08-01 | Univ Johns Hopkins | Metodo para la produccion de glicoproteinas recombinantes con semivida en circulacion incrementada en celulas de mamifero. |
| CN103415621A (zh) | 2011-01-14 | 2013-11-27 | 雷德伍德生物科技股份有限公司 | 醛标记免疫球蛋白多肽及其使用方法 |
| CA2827732A1 (en) * | 2011-02-25 | 2012-08-30 | Merck Sharp & Dohme Corp. | Yeast strain for the production of proteins with modified o-glycosylation |
| KR20140043720A (ko) | 2011-03-01 | 2014-04-10 | 노보 노르디스크 에이/에스 | 길항성 dr3 리간드 |
| RU2013142015A (ru) | 2011-03-02 | 2015-04-10 | Ново Нордиск А/С | Нацеливание факторов свертывания крови на рецептор tlt-1 на поверхности активированных тромбоцитов |
| JP6101638B2 (ja) | 2011-03-03 | 2017-03-22 | ザイムワークス,インコーポレイテッド | 多価ヘテロマルチマー足場設計及び構築物 |
| JP2014509864A (ja) | 2011-03-23 | 2014-04-24 | グリコド | Gdp−フコースを産生可能な酵母組換え細胞 |
| US20140178368A1 (en) | 2011-04-19 | 2014-06-26 | Leslie Lynne SHARP | Combinations of anti-4-1bb antibodies and adcc-inducing antibodies for the treatment of cancer |
| KR20240110072A (ko) | 2011-05-18 | 2024-07-12 | 메더리스 다이어비티즈, 엘엘씨 | 인슐린 저항성에 대한 개선된 펩티드 제약 |
| WO2012158962A2 (en) | 2011-05-18 | 2012-11-22 | Eumederis Pharmaceuticals, Inc. | Improved peptide pharmaceuticals |
| AU2012264696A1 (en) | 2011-05-31 | 2013-12-12 | Probiogen Ag | Methods for preparation of fucose-linked site specific conjugates of proteins with toxins, adjuvants, detection labels and pharmacokinetic half life extenders |
| WO2012170938A1 (en) | 2011-06-08 | 2012-12-13 | Acceleron Pharma Inc. | Compositions and methods for increasing serum half-life |
| PT2717898T (pt) | 2011-06-10 | 2019-05-20 | Bioverativ Therapeutics Inc | Compostos pró-coagulantes e processos para a sua utilização |
| US9150846B2 (en) | 2011-07-05 | 2015-10-06 | Bioasis Technologies, Inc. | P97-antibody conjugates and methods of use |
| DK2739649T3 (en) | 2011-08-05 | 2018-01-08 | Bioasis Technologies Inc | P97 FRAGMENTS WITH TRANSFER ACTIVITY |
| AR087433A1 (es) * | 2011-08-08 | 2014-03-26 | Merck Sharp & Dohme | Analogos de insulina n-glicosilados |
| CN104093735B (zh) | 2011-09-23 | 2018-07-06 | 诺沃—诺迪斯克有限公司 | 新的胰高血糖素类似物 |
| CN109134642A (zh) * | 2011-10-01 | 2019-01-04 | 株式会社糖锁工学研究所 | 加成糖链的多肽及含有该多肽的医药组合物 |
| WO2013058582A2 (ko) * | 2011-10-18 | 2013-04-25 | 한국생명공학연구원 | 당전이 효소를 이용한 안사마이신 배당체의 제조방법 |
| KR101456174B1 (ko) * | 2011-10-18 | 2014-11-03 | 한국생명공학연구원 | 용해도가 증가된 비―퀴논 젤다나마이신 당전이 유도체 또는 이의 약학적으로 허용가능한 염, 이의 제조방법 및 이의 열충격 단백질(Hsp90) 에이티피아제(ATPase) 활성 저해용 약학적 조성물 |
| US9034829B1 (en) * | 2011-10-27 | 2015-05-19 | Northwestern University | pH-sensitive polymer-drug conjugates for targeted delivery of therapeutics |
| EP2773671B1 (en) | 2011-11-04 | 2021-09-15 | Zymeworks Inc. | Stable heterodimeric antibody design with mutations in the fc domain |
| WO2013123457A1 (en) | 2012-02-15 | 2013-08-22 | Biogen Idec Ma Inc. | Recombinant factor viii proteins |
| CN119192402A (zh) | 2012-02-15 | 2024-12-27 | 比奥贝拉蒂治疗公司 | 因子viii组合物及其制备和使用方法 |
| US10265388B2 (en) | 2012-02-21 | 2019-04-23 | Cytonics Corporation | Systems, compositions, and methods for transplantation |
| US10130714B2 (en) | 2012-04-14 | 2018-11-20 | Academia Sinica | Enhanced anti-influenza agents conjugated with anti-inflammatory activity |
| WO2013160005A1 (en) | 2012-04-24 | 2013-10-31 | Novo Nordisk A/S | Pharmaceutical composition suitable for treatment of haemophilia |
| JP2015515482A (ja) | 2012-04-24 | 2015-05-28 | ノヴォ ノルディスク アー/エス | 血友病の治療に適する化合物 |
| WO2014004586A1 (en) | 2012-06-25 | 2014-01-03 | Zymeworks Inc. | Process and methods for efficient manufacturing of highly pure asymmetric antibodies in mammalian cells |
| CN102786030B (zh) * | 2012-07-06 | 2014-03-12 | 江苏大学 | 一种通过溶剂处理制备多肽纳米薄膜的方法 |
| WO2014012082A2 (en) | 2012-07-13 | 2014-01-16 | Zymeworks Inc. | Multivalent heteromultimer scaffold design an constructs |
| AU2013296557B2 (en) | 2012-07-31 | 2019-04-18 | Bioasis Technologies Inc. | Dephosphorylated lysosomal storage disease proteins and methods of use thereof |
| JP6302909B2 (ja) | 2012-08-18 | 2018-03-28 | アカデミア シニカAcademia Sinica | シアリダーゼの同定および画像化のための細胞透過性プローブ |
| SG10201702387YA (en) | 2012-09-24 | 2017-04-27 | Medimmune Ltd | Cell lines |
| WO2014057068A1 (en) | 2012-10-10 | 2014-04-17 | Novo Nordisk Health Care Ag | Liquid pharmaceutical composition of factor vii polypeptide |
| US9274430B2 (en) | 2012-10-10 | 2016-03-01 | Arizona Board Of Regents On Behalf Of Arizona State University | Systems and devices for molecule sensing and method of manufacturing thereof |
| JP2015532307A (ja) | 2012-10-15 | 2015-11-09 | ノヴォ・ノルディスク・ヘルス・ケア・アーゲー | 凝固因子viiポリペプチド |
| CN104661685A (zh) | 2012-10-15 | 2015-05-27 | 诺和诺德保健Ag(股份有限公司) | 因子vii缀合物 |
| JP6525456B2 (ja) * | 2012-11-20 | 2019-06-05 | メデリス ダイアビーティーズ,エルエルシー | インスリン抵抗性のための改善されたペプチド製剤 |
| WO2014081864A1 (en) | 2012-11-20 | 2014-05-30 | Eumederis Pharmaceuticals, Inc. | Improved peptide pharmaceuticals |
| US9914785B2 (en) | 2012-11-28 | 2018-03-13 | Zymeworks Inc. | Engineered immunoglobulin heavy chain-light chain pairs and uses thereof |
| EP2925345B1 (en) | 2012-12-03 | 2018-09-05 | Merck Sharp & Dohme Corp. | Method for making o-glycosylated carboxy terminal portion (ctp) peptide-based insulin and insulin analogues |
| CN103044509B (zh) * | 2013-01-05 | 2015-04-01 | 宁辉 | γ-胞嘧啶核苷-5’-三磷酸二钠结晶化合物、其制备方法及其药物组合物 |
| MX2015010428A (es) * | 2013-02-13 | 2016-04-13 | Lab Francais Du Fractionnement | Anticuerpos anti-her2 altamente galactosilados y sus usos. |
| US10174110B2 (en) | 2013-02-13 | 2019-01-08 | Laboratoire Français Du Fractionnement Et Des Biotechnologies | Highly galactosylated anti-TNF-α antibodies and uses thereof |
| WO2014140927A2 (en) | 2013-02-13 | 2014-09-18 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Proteins with modified glycosylation and methods of production thereof |
| RU2708314C2 (ru) * | 2013-03-11 | 2019-12-05 | Джензим Корпорейшн | Гипергликозилированные связывающие полипептиды |
| EP2970433B1 (en) | 2013-03-13 | 2019-09-18 | Bioasis Technologies Inc. | Fragments of p97 and uses thereof |
| ES2926773T3 (es) | 2013-03-15 | 2022-10-28 | Novo Nordisk As | Anticuerpos capaces de unirse específicamente a dos epítopos en el inhibidor de la ruta del factor tisular |
| WO2014170496A1 (en) | 2013-04-18 | 2014-10-23 | Novo Nordisk A/S | Stable, protracted glp-1/glucagon receptor co-agonists for medical use |
| PL2991683T3 (pl) | 2013-05-02 | 2020-03-31 | Glykos Finland Oy | Koniugaty glikoproteiny lub glikanu z toksycznym ładunkiem |
| WO2014182970A1 (en) * | 2013-05-08 | 2014-11-13 | Zymeworks Inc. | Bispecific her2 and her3 antigen binding constructs |
| EP2996772B1 (en) | 2013-05-13 | 2018-12-19 | Momenta Pharmaceuticals, Inc. | Methods for the treatment of neurodegeneration |
| EP3013365B1 (en) | 2013-06-26 | 2019-06-05 | Academia Sinica | Rm2 antigens and use thereof |
| WO2014210564A1 (en) | 2013-06-27 | 2014-12-31 | Academia Sinica | Glycan conjugates and use thereof |
| WO2015023891A2 (en) | 2013-08-14 | 2015-02-19 | Biogen Idec Ma Inc. | Factor viii-xten fusions and uses thereof |
| EP3038635A4 (en) | 2013-08-28 | 2017-04-05 | Cytonics Corporation | Systems, compositions, and methods for transplantation and treating conditions |
| CN105682666B (zh) | 2013-09-06 | 2021-06-01 | 中央研究院 | 使用醣脂激活人类iNKT细胞 |
| US9884125B2 (en) | 2013-10-04 | 2018-02-06 | Merck Sharp & Dohme Corp. | Glucose-responsive insulin conjugates |
| US9987373B2 (en) | 2013-10-14 | 2018-06-05 | Synaffix B.V. | Modified glycoprotein, protein-conjugate and process for the preparation thereof |
| WO2015057065A1 (en) * | 2013-10-14 | 2015-04-23 | Synaffix B.V. | Glycoengineered antibody, antibody-conjugate and methods for their preparation |
| BR112016008039A2 (pt) | 2013-10-15 | 2017-10-17 | Novo Nordisk Healthcare Ag | polipeptídeos do fator vii da coagulação |
| WO2015057622A1 (en) | 2013-10-16 | 2015-04-23 | Momenta Pharmaceuticals, Inc. | Sialylated glycoproteins |
| JP2017507118A (ja) | 2014-01-16 | 2017-03-16 | アカデミア シニカAcademia Sinica | がんの処置および検出のための組成物および方法 |
| US10150818B2 (en) | 2014-01-16 | 2018-12-11 | Academia Sinica | Compositions and methods for treatment and detection of cancers |
| US11168085B2 (en) | 2014-01-24 | 2021-11-09 | Synaffix B.V. | Process for the cycloaddition of a hetero(aryl) 1,3-dipole compound with a (hetero)cycloalkyne |
| WO2015112016A1 (en) | 2014-01-24 | 2015-07-30 | Synaffix B.V. | Process for the cycloaddition of a halogenated 1,3-dipole compound with a (hetero)cycloalkyne |
| EP3097200A1 (en) * | 2014-01-24 | 2016-11-30 | SynAffix B.V. | Process for the attachment of a galnac moiety comprising a (hetero)aryl group to a glcnac moiety, and product obtained thereby |
| EP3102608B1 (en) | 2014-02-03 | 2019-09-18 | Bioasis Technologies Inc. | P97 fusion proteins |
| AR099340A1 (es) * | 2014-02-12 | 2016-07-13 | Novo Nordisk As | Conjugados del factor de coagulación ix |
| EP3107562B1 (en) | 2014-02-19 | 2019-09-18 | Bioasis Technologies Inc. | P97-ids fusion proteins |
| US10188739B2 (en) | 2014-02-27 | 2019-01-29 | Xenetic Biosciences, Inc. | Compositions and methods for administering insulin or insulin-like protein to the brain |
| EP3129067B1 (en) | 2014-03-19 | 2023-01-04 | Genzyme Corporation | Site-specific glycoengineering of targeting moieties |
| CN106415244B (zh) | 2014-03-27 | 2020-04-24 | 中央研究院 | 反应性标记化合物及其用途 |
| CA2944539A1 (en) | 2014-04-08 | 2015-10-15 | University Of Georgia Research Foundation, Inc. | Site-specific antibody-drug glycoconjugates and methods |
| JP6750148B2 (ja) * | 2014-04-25 | 2020-09-02 | 公益財団法人野口研究所 | 糖鎖切断抗体の製造方法及び均一糖鎖抗体 |
| JP6847664B2 (ja) | 2014-05-01 | 2021-03-24 | バイオアシス テクノロジーズ インコーポレイテッド | P97−ポリヌクレオチド複合体 |
| US20150344585A1 (en) | 2014-05-27 | 2015-12-03 | Academia Sinica | Anti-cd20 glycoantibodies and uses thereof |
| TWI717319B (zh) | 2014-05-27 | 2021-02-01 | 中央研究院 | 得自類桿菌屬之岩藻糖苷酶及其用途 |
| US10118969B2 (en) | 2014-05-27 | 2018-11-06 | Academia Sinica | Compositions and methods relating to universal glycoforms for enhanced antibody efficacy |
| TWI679020B (zh) | 2014-05-27 | 2019-12-11 | 中央研究院 | 抗her2醣抗體及其用途 |
| US9856306B2 (en) | 2014-05-28 | 2018-01-02 | Spitfire Pharma, Inc. | Peptide pharmaceuticals for insulin resistance |
| TWI732738B (zh) | 2014-05-28 | 2021-07-11 | 中央研究院 | 抗TNF-α醣抗體及其用途 |
| US10570184B2 (en) | 2014-06-04 | 2020-02-25 | Novo Nordisk A/S | GLP-1/glucagon receptor co-agonists for medical use |
| DK3160513T3 (da) | 2014-06-30 | 2020-04-06 | Glykos Finland Oy | Saccharidderivat af en toksisk payload og antistofkonjugater deraf |
| CN106714817A (zh) * | 2014-07-10 | 2017-05-24 | 中央研究院 | 多药物递送系统及其用途 |
| BR112017002090B1 (pt) | 2014-08-04 | 2021-06-01 | Csl Limited | Composição aquosa de fator viii de coagulação e método de estabilizar uma molécula de fviii |
| TWI745275B (zh) | 2014-09-08 | 2021-11-11 | 中央研究院 | 使用醣脂激活人類iNKT細胞 |
| CN108025083B (zh) * | 2014-10-09 | 2021-09-03 | 建新公司 | 糖工程化的抗体药物缀合物 |
| SG11201702824UA (en) | 2014-10-24 | 2017-05-30 | Bristol Myers Squibb Co | Modified fgf-21 polypeptides and uses thereof |
| US10889631B2 (en) | 2014-11-20 | 2021-01-12 | Cytonics Corporation | Therapeutic variant alpha-2-macroglobulin compositions |
| WO2016091268A2 (en) | 2014-12-12 | 2016-06-16 | University Of Copenhagen | N-glycosylation |
| EP3835312A1 (en) | 2014-12-31 | 2021-06-16 | Checkmate Pharmaceuticals, Inc. | Combination tumor immunotherapy |
| US9975965B2 (en) | 2015-01-16 | 2018-05-22 | Academia Sinica | Compositions and methods for treatment and detection of cancers |
| US10495645B2 (en) | 2015-01-16 | 2019-12-03 | Academia Sinica | Cancer markers and methods of use thereof |
| CA2972072A1 (en) | 2015-01-24 | 2016-07-28 | Academia Sinica | Novel glycan conjugates and methods of use thereof |
| CN107406493B (zh) | 2015-03-06 | 2021-08-13 | 康诺贝林伦瑙有限公司 | 具有改善的半衰期的经修饰的血管性血友病因子 |
| FR3038517B1 (fr) | 2015-07-06 | 2020-02-28 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Utilisation de fragments fc modifies en immunotherapie |
| CA2994547A1 (en) | 2015-08-03 | 2017-02-09 | Bioverativ Therapeutics Inc. | Factor ix fusion proteins and methods of making and using same |
| WO2017118704A1 (en) | 2016-01-08 | 2017-07-13 | Ascendis Pharma Growth Disorders A/S | Controlled-release cnp agonists with low npr-c binding |
| WO2017118693A1 (en) | 2016-01-08 | 2017-07-13 | Ascendis Pharma Growth Disorders A/S | Cnp prodrugs with large carrier moieties |
| SMT202200466T1 (it) | 2016-01-08 | 2023-01-13 | Ascendis Pharma Growth Disorders As | Profarmaci di cnp con legame a supporto in corrispondenza del raggruppamento ciclico |
| CA3008017C (en) * | 2016-01-08 | 2024-01-02 | Ascendis Pharma Growth Disorders A/S | Controlled-release cnp agonists with reduced side-effects |
| EP3400022A1 (en) | 2016-01-08 | 2018-11-14 | Ascendis Pharma Growth Disorders A/S | Controlled-release cnp agonists with low initial npr-b activity |
| NZ743487A (en) | 2016-01-08 | 2023-02-24 | Ascendis Pharma Growth Disorders As | Controlled-release cnp agonists with increased nep stability |
| CN105505884B (zh) * | 2016-01-26 | 2017-10-03 | 郑州师范学院 | 进行抗体表达和组装的重组系统及应用 |
| TW201808978A (zh) | 2016-03-08 | 2018-03-16 | 中央研究院 | N-聚醣及其陣列之模組化合成方法 |
| MA45473A (fr) * | 2016-04-04 | 2019-02-13 | Shire Human Genetic Therapies | Inhibiteur de c1 estérase conjugué et ses utilisations |
| EP3448885A4 (en) | 2016-04-26 | 2020-01-08 | R.P. Scherer Technologies, LLC | ANTIBODY CONJUGATES AND METHOD FOR THE PRODUCTION AND USE THEREOF |
| MY194619A (en) | 2016-06-02 | 2022-12-07 | Abbvie Inc | Glucocorticoid receptor agonist and immunoconjugates thereof |
| EP3500594A4 (en) | 2016-08-22 | 2020-03-11 | Cho Pharma Inc. | ANTIBODIES, BINDING FRAGMENTS AND METHOD FOR USE |
| IL321464A (en) | 2016-09-29 | 2025-08-01 | Ascendis Pharma Growth Disorders As | Combination therapy with controlled-release cnp agonists |
| US12161696B2 (en) | 2016-12-02 | 2024-12-10 | Bioverativ Therapeutics Inc. | Methods of treating hemophilic arthropathy using chimeric clotting factors |
| JP6852397B2 (ja) * | 2016-12-28 | 2021-03-31 | 株式会社島津製作所 | 分析用試料の調製方法および分析方法 |
| TWI673363B (zh) * | 2016-12-29 | 2019-10-01 | 財團法人生物技術開發中心 | 製備醣蛋白-藥物共軛物之方法 |
| WO2018148419A1 (en) | 2017-02-08 | 2018-08-16 | Bristol-Myers Squibb Company | Modified relaxin polypeptides comprising a pharmacokinetic enhancer and uses thereof |
| FI3583120T3 (fi) | 2017-02-17 | 2023-01-13 | Muunneltuja transferriinireseptoria sitovia polypeptidejä | |
| JP2020511499A (ja) | 2017-03-20 | 2020-04-16 | エフ.ホフマン−ラ ロシュ アーゲーF. Hoffmann−La Roche Aktiengesellschaft | 赤血球生成刺激タンパク質のインビトロでの糖鎖改変のための方法 |
| CN111051512A (zh) | 2017-07-11 | 2020-04-21 | 辛索克斯公司 | 非天然核苷酸的掺入及其方法 |
| SG11202000939PA (en) | 2017-08-03 | 2020-02-27 | Synthorx Inc | Cytokine conjugates for the treatment of proliferative and infectious diseases |
| ES2930534T3 (es) | 2017-09-04 | 2022-12-16 | 89Bio Ltd | Conjugados de péptidos de FGF-21 mutantes y usos de los mismos |
| PH12020550661A1 (en) | 2017-11-21 | 2021-04-19 | Univ Leland Stanford Junior | Partial agonists of interleukin-2 |
| BR112020010694A2 (pt) | 2017-12-01 | 2020-11-10 | Abbvie Inc. | agonista de receptor de glicocorticoides e imunoconjugados do mesmo |
| EP3735295B1 (en) | 2018-01-03 | 2024-08-21 | Mederis Diabetes, LLC | Improved peptide pharmaceuticals for treatment of nash and other disorders |
| EP3752194A4 (en) | 2018-02-13 | 2022-03-16 | Checkmate Pharmaceuticals, Inc. | COMPOSITIONS AND METHODS FOR TUMOR IMMUNOTHERAPY |
| IL277680B2 (en) | 2018-04-09 | 2025-08-01 | Checkmate Pharmaceuticals Inc | Packaging oligonucleotides into virus-like particles |
| TW202015723A (zh) | 2018-05-18 | 2020-05-01 | 美商百歐維拉提夫治療公司 | 治療a型血友病的方法 |
| WO2019232283A1 (en) * | 2018-05-30 | 2019-12-05 | Purdue Research Foundation | Targeting anabolic drugs for accelerated fracture repair |
| CN113301925A (zh) | 2018-12-19 | 2021-08-24 | 小利兰·斯坦福大学理事会 | 用于溶酶体靶向的双官能分子以及相关的组合物和方法 |
| AU2020218203A1 (en) | 2019-02-06 | 2021-08-26 | Synthorx, Inc. | IL-2 conjugates and methods of use thereof |
| US12377133B2 (en) | 2019-02-11 | 2025-08-05 | Ascendis Pharma Growth Disorders A/S | Dry pharmaceutical formulations of CNP conjugates |
| AU2020300820A1 (en) | 2019-07-04 | 2022-03-03 | CSL Behring Lengnau AG | A truncated von willebrand factor (vWF) for increasing the in vitro stability of coagulation factor VIII |
| WO2021094344A1 (en) | 2019-11-11 | 2021-05-20 | CSL Behring Lengnau AG | Polypeptides for inducing tolerance to factor viii |
| AU2020411480B2 (en) | 2019-12-23 | 2023-12-21 | Denali Therapeutics Inc. | Progranulin variants |
| JP7303391B2 (ja) | 2020-01-14 | 2023-07-04 | シンセカイン インコーポレイテッド | バイアス型il2ムテイン、方法、および組成物 |
| US12122845B2 (en) * | 2020-08-07 | 2024-10-22 | Eutilex Co., Ltd. | Anti-HER2/anti-4-1BB bispecific antibodies and uses thereof |
| US20230235082A1 (en) * | 2020-08-21 | 2023-07-27 | Glyco-Therapy Biotechnology Co., Ltd. | Site-specific antibody conjugates and the methods for preparation of the same |
| WO2022079211A1 (en) * | 2020-10-16 | 2022-04-21 | Adc Therapeutics Sa | Glycoconjugates |
| EP4228703A1 (en) * | 2020-10-16 | 2023-08-23 | University of Georgia Research Foundation, Inc. | Glycoconjugates |
| US12171806B2 (en) | 2021-09-28 | 2024-12-24 | Spitfire Pharma Llc | Therapeutic regimens and methods for lowering blood glucose and/or body weight using GLP-1R and GCGR balanced agonists |
| WO2022136705A1 (en) * | 2020-12-24 | 2022-06-30 | Synaffix B.V. | Glycan-conjugated antibodies binding to fc-gamma receptor |
| KR20230128534A (ko) * | 2021-02-22 | 2023-09-05 | 상하이 인스티튜트 오브 마테리아 메디카 차이니즈 아카데미 오브 싸이언시즈 | 이당류 링커, 이당류-소분자 약물 접합체 및 당쇄 부위특이적 항체-약물 접합체, 그 제조 방법 및 용도 |
| CN113429443B (zh) * | 2021-07-08 | 2023-07-25 | 江南大学 | 一种双唾液酸-甘露寡糖复合物及其合成方法 |
| JP2024524614A (ja) | 2021-07-14 | 2024-07-05 | ライシア セラピューティクス, インコーポレイテッド | Asgpr細胞表面受容体結合化合物及びコンジュゲート |
| WO2023122616A1 (en) * | 2021-12-20 | 2023-06-29 | 89Bio, Inc. | Chemical synthesis of cytidine-5'-monophospho-n-glycyl-sialic acid |
| EP4285934A1 (en) | 2022-05-30 | 2023-12-06 | CER Groupe | Modified trimannose-oligosacharides, bisected n-glycans comprising said trimannose core and method for obtaining them |
| KR20250052370A (ko) | 2022-06-24 | 2025-04-18 | 89바이오 인코포레이티드 | 중증 고중성지방혈증용 조성물 및 치료 방법 |
| KR20250126089A (ko) * | 2022-12-29 | 2025-08-22 | 허니베어 바이오사이언시스 인코포레이티드 | 당단백질 변형 방법 |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE2432518A1 (de) * | 1973-07-05 | 1975-01-30 | Beecham Group Ltd | Arzneimittel und verfahren zu seiner herstellung |
| WO1994029370A1 (en) * | 1993-06-08 | 1994-12-22 | Enzon, Inc. | Factor ix - polymeric conjugates |
| US5405753A (en) * | 1990-03-26 | 1995-04-11 | Brossmer; Reinhard | CMP-activated, fluorescing sialic acids, as well as processes for their preparation |
| WO2000044785A1 (en) * | 1999-01-29 | 2000-08-03 | F. Hoffmann-La Roche Ag | Gcsf conjugates |
Family Cites Families (292)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3691016A (en) | 1970-04-17 | 1972-09-12 | Monsanto Co | Process for the preparation of insoluble enzymes |
| CA1023287A (en) | 1972-12-08 | 1977-12-27 | Boehringer Mannheim G.M.B.H. | Process for the preparation of carrier-bound proteins |
| US4179337A (en) | 1973-07-20 | 1979-12-18 | Davis Frank F | Non-immunogenic polypeptides |
| DE2433883C2 (de) * | 1973-07-20 | 1986-03-27 | Research Corp., New York, N.Y. | Verwendung von physiologisch aktiven Polypeptiden |
| CH596313A5 (enExample) | 1975-05-30 | 1978-03-15 | Battelle Memorial Institute | |
| US4385260A (en) | 1975-09-09 | 1983-05-24 | Beckman Instruments, Inc. | Bargraph display |
| US4235871A (en) | 1978-02-24 | 1980-11-25 | Papahadjopoulos Demetrios P | Method of encapsulating biologically active materials in lipid vesicles |
| US4342832A (en) | 1979-07-05 | 1982-08-03 | Genentech, Inc. | Method of constructing a replicable cloning vehicle having quasi-synthetic genes |
| IL63270A0 (en) | 1980-08-05 | 1981-10-30 | Univ Leland Stanford Junior | Eukaryotic autonomously replicating segment |
| US4414147A (en) | 1981-04-17 | 1983-11-08 | Massachusetts Institute Of Technology | Methods of decreasing the hydrophobicity of fibroblast and other interferons |
| JPS57206622A (en) | 1981-06-10 | 1982-12-18 | Ajinomoto Co Inc | Blood substitute |
| US4579821A (en) | 1981-11-23 | 1986-04-01 | University Patents, Inc. | Control of DNA sequence transcription |
| US4656134A (en) | 1982-01-11 | 1987-04-07 | Board Of Trustees Of Leland Stanford Jr. University | Gene amplification in eukaryotic cells |
| US4975276A (en) | 1982-01-15 | 1990-12-04 | Cetus Corporation | Interferon-alpha 54 |
| US4695543A (en) | 1982-03-23 | 1987-09-22 | Bristol-Myers Company | Alpha Interferon GX-1 |
| US4748233A (en) | 1982-03-23 | 1988-05-31 | Bristol-Myers Company | Alpha-interferon Gx-1 |
| US6936694B1 (en) | 1982-05-06 | 2005-08-30 | Intermune, Inc. | Manufacture and expression of large structural genes |
| WO1983004050A1 (en) | 1982-05-19 | 1983-11-24 | Gist-Brocades N.V. | Cloning system for kluyveromyces species |
| US4486533A (en) | 1982-09-02 | 1984-12-04 | St. Louis University | Filamentous fungi functional replicating extrachromosomal element |
| US4522811A (en) | 1982-07-08 | 1985-06-11 | Syntex (U.S.A.) Inc. | Serial injection of muramyldipeptides and liposomes enhances the anti-infective activity of muramyldipeptides |
| US4599311A (en) | 1982-08-13 | 1986-07-08 | Kawasaki Glenn H | Glycolytic promotersfor regulated protein expression: protease inhibitor |
| US5151511A (en) | 1982-09-16 | 1992-09-29 | Amgen Inc. | DNA encoding avian growth hormones |
| US4737462A (en) | 1982-10-19 | 1988-04-12 | Cetus Corporation | Structural genes, plasmids and transformed cells for producing cysteine depleted muteins of interferon-β |
| US4588585A (en) | 1982-10-19 | 1986-05-13 | Cetus Corporation | Human recombinant cysteine depleted interferon-β muteins |
| US4966843A (en) | 1982-11-01 | 1990-10-30 | Cetus Corporation | Expression of interferon genes in Chinese hamster ovary cells |
| US4438253A (en) | 1982-11-12 | 1984-03-20 | American Cyanamid Company | Poly(glycolic acid)/poly(alkylene glycol) block copolymers and method of manufacturing the same |
| US4501728A (en) | 1983-01-06 | 1985-02-26 | Technology Unlimited, Inc. | Masking of liposomes from RES recognition |
| US4603044A (en) | 1983-01-06 | 1986-07-29 | Technology Unlimited, Inc. | Hepatocyte Directed Vesicle delivery system |
| US4713339A (en) | 1983-01-19 | 1987-12-15 | Genentech, Inc. | Polycistronic expression vector construction |
| US4518584A (en) | 1983-04-15 | 1985-05-21 | Cetus Corporation | Human recombinant interleukin-2 muteins |
| US4745051A (en) | 1983-05-27 | 1988-05-17 | The Texas A&M University System | Method for producing a recombinant baculovirus expression vector |
| US5639639A (en) | 1983-11-02 | 1997-06-17 | Genzyme Corporation | Recombinant heterodimeric human fertility hormones, and methods, cells, vectors and DNA for the production thereof |
| US5156957A (en) | 1983-11-02 | 1992-10-20 | Genzyme Corporation | Follicle stimulating hormone |
| US4840896A (en) | 1983-11-02 | 1989-06-20 | Integrated Genetics, Inc. | Heteropolymeric protein |
| US4923805A (en) | 1983-11-02 | 1990-05-08 | Integrated Genetics, Inc. | Fsh |
| US4758656A (en) | 1983-12-26 | 1988-07-19 | Kyowa Hakko Kogyo Co., Ltd. | Novel human interferon-gamma polypeptide derivative |
| US4496689A (en) | 1983-12-27 | 1985-01-29 | Miles Laboratories, Inc. | Covalently attached complex of alpha-1-proteinase inhibitor with a water soluble polymer |
| DE3572982D1 (en) | 1984-03-06 | 1989-10-19 | Takeda Chemical Industries Ltd | Chemically modified lymphokine and production thereof |
| US4965199A (en) | 1984-04-20 | 1990-10-23 | Genentech, Inc. | Preparation of functional human factor VIII in mammalian cells using methotrexate based selection |
| IL71691A (en) | 1984-04-27 | 1991-04-15 | Yeda Res & Dev | Production of interferon-ypsilon |
| US4879236A (en) | 1984-05-16 | 1989-11-07 | The Texas A&M University System | Method for producing a recombinant baculovirus expression vector |
| US4931373A (en) | 1984-05-25 | 1990-06-05 | Zymogenetics, Inc. | Stable DNA constructs for expression of α-1 antitrypsin |
| US4589402A (en) | 1984-07-26 | 1986-05-20 | Serono Laboratories, Inc. | Method of in vitro fertilization |
| US4970300A (en) * | 1985-02-01 | 1990-11-13 | New York University | Modified factor VIII |
| US4761371A (en) | 1985-02-12 | 1988-08-02 | Genentech, Inc. | Insulin receptor |
| US5034506A (en) | 1985-03-15 | 1991-07-23 | Anti-Gene Development Group | Uncharged morpholino-based polymers having achiral intersubunit linkages |
| US4683202A (en) | 1985-03-28 | 1987-07-28 | Cetus Corporation | Process for amplifying nucleic acid sequences |
| US4683195A (en) | 1986-01-30 | 1987-07-28 | Cetus Corporation | Process for amplifying, detecting, and/or-cloning nucleic acid sequences |
| GR860984B (en) | 1985-04-17 | 1986-08-18 | Zymogenetics Inc | Expression of factor vii and ix activities in mammalian cells |
| AU5864086A (en) | 1985-04-22 | 1986-11-18 | Genetics Institute Inc. | High yield production of active factor ix |
| WO1986006358A1 (fr) | 1985-04-30 | 1986-11-06 | Büro Patent Ag | Installation et procede d'amenee automatique de pots remplis et d'evacuation automatique de pots vides dans un metier a filer |
| WO1987000056A1 (en) | 1985-06-26 | 1987-01-15 | Cetus Corporation | Solubilization of proteins for pharmaceutical compositions using polymer conjugation |
| JPS6238172A (ja) | 1985-08-12 | 1987-02-19 | 株式会社 高研 | 抗血栓性医用材料の製造方法 |
| US6004548A (en) | 1985-08-23 | 1999-12-21 | Amgen, Inc. | Analogs of pluripotent granulocyte colony-stimulating factor |
| US4810643A (en) | 1985-08-23 | 1989-03-07 | Kirin- Amgen Inc. | Production of pluripotent granulocyte colony-stimulating factor |
| JPS62236497A (ja) | 1985-09-17 | 1987-10-16 | Chugai Pharmaceut Co Ltd | 顆粒球コロニー刺激因子活性を有する糖蛋白質の製造方法 |
| JPS63502795A (ja) | 1985-10-03 | 1988-10-20 | バイオジェン インコーポレイテッド | 顆粒球‐マクロファージコロニー刺激因子‐様ポリペプチド、dna配列、組換えdna分子並びに微生物細胞中でヒト顆粒球−マクロファ−ジコロニ−刺激因子−様ポリペプチドを高収量で生産する方法 |
| IL80529A0 (en) | 1985-11-14 | 1987-02-27 | Daiichi Seiyaku Co | Method of producing peptides |
| DE3712985A1 (de) | 1987-04-16 | 1988-11-03 | Hoechst Ag | Bifunktionelle proteine |
| US4935349A (en) | 1986-01-17 | 1990-06-19 | Zymogenetics, Inc. | Expression of higher eucaryotic genes in aspergillus |
| WO1987005330A1 (en) | 1986-03-07 | 1987-09-11 | Michel Louis Eugene Bergh | Method for enhancing glycoprotein stability |
| US4925796A (en) | 1986-03-07 | 1990-05-15 | Massachusetts Institute Of Technology | Method for enhancing glycoprotein stability |
| IT1203758B (it) | 1986-03-27 | 1989-02-23 | Univ Roma | Vettori di clonazione e di espressione di geni eterologhi in lieviti e lieviti trasformati con tali vettori |
| GB8610600D0 (en) | 1986-04-30 | 1986-06-04 | Novo Industri As | Transformation of trichoderma |
| US4902505A (en) | 1986-07-30 | 1990-02-20 | Alkermes | Chimeric peptides for neuropeptide delivery through the blood-brain barrier |
| US5075109A (en) | 1986-10-24 | 1991-12-24 | Southern Research Institute | Method of potentiating an immune response |
| US4894330A (en) | 1986-12-23 | 1990-01-16 | Cetus Corporation | Purification of recombinant beta-interferon incorporating RP-HPLC |
| US4837028A (en) | 1986-12-24 | 1989-06-06 | Liposome Technology, Inc. | Liposomes with enhanced circulation time |
| IL85035A0 (en) | 1987-01-08 | 1988-06-30 | Int Genetic Eng | Polynucleotide molecule,a chimeric antibody with specificity for human b cell surface antigen,a process for the preparation and methods utilizing the same |
| US4857505A (en) * | 1987-03-09 | 1989-08-15 | American Cyanamid Company | Sustained release compositions for parenteral administration and their use |
| DK175243B1 (da) | 1987-03-23 | 2004-07-19 | Zymogenetics Inc | Ekspressionsvektor, der er i stand til at styre ekspression af heterologe gener eller cDNA i gær, gærværtscelle samt fremgangsmåde til öget produktion af proteiner i gærværtsceller |
| US5149637A (en) | 1987-04-06 | 1992-09-22 | Scripps Clinic & Research Foundation | Recombinant Factor VIIIC fragments |
| DE3712564A1 (de) * | 1987-04-14 | 1988-11-24 | Bioferon Biochem Substanz | Verfahren zur konstruktion einer animalen zellinie fuer die herstellung von humanem interferon-beta |
| IL82834A (en) | 1987-06-09 | 1990-11-05 | Yissum Res Dev Co | Biodegradable polymeric materials based on polyether glycols,processes for the preparation thereof and surgical artiicles made therefrom |
| HU208553B (en) | 1987-07-28 | 1993-11-29 | Gist Brocades Nv | Process for producing polypeptides, plasmides coding them and transformed kluyveromyces |
| US4897268A (en) | 1987-08-03 | 1990-01-30 | Southern Research Institute | Drug delivery system and method of making the same |
| US5252726A (en) | 1987-09-04 | 1993-10-12 | Novo Nordisk A/S | Promoters for use in aspergillus |
| GB8725529D0 (en) | 1987-10-30 | 1987-12-02 | Delta Biotechnology Ltd | Polypeptides |
| US4847325A (en) * | 1988-01-20 | 1989-07-11 | Cetus Corporation | Conjugation of polymer to colony stimulating factor-1 |
| US5153265A (en) * | 1988-01-20 | 1992-10-06 | Cetus Corporation | Conjugation of polymer to colony stimulating factor-1 |
| GB8810808D0 (en) | 1988-05-06 | 1988-06-08 | Wellcome Found | Vectors |
| JP2511494B2 (ja) | 1988-05-12 | 1996-06-26 | 善治 松浦 | 日本脳炎ウイルス表面抗原蛋白質の製造法 |
| US5770198A (en) | 1988-05-18 | 1998-06-23 | The Research Foundation Of The State Of New York | Platelet-specific chimeric 7E3 immunoglobulin |
| FR2631974B1 (fr) | 1988-05-31 | 1992-12-11 | Agronomique Inst Nat Rech | Baculovirus modifie, son procede de preparation et son application en tant que vecteur d'expression de genes |
| FR2649991B2 (fr) | 1988-08-05 | 1994-03-04 | Rhone Poulenc Sante | Utilisation de derives stables du plasmide pkd1 pour l'expression et la secretion de proteines heterologues dans les levures du genre kluyveromyces |
| US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| US5162215A (en) | 1988-09-22 | 1992-11-10 | Amgen Inc. | Method of gene transfer into chickens and other avian species |
| US5218092A (en) * | 1988-09-29 | 1993-06-08 | Kyowa Hakko Kogyo Co., Ltd. | Modified granulocyte-colony stimulating factor polypeptide with added carbohydrate chains |
| US5534617A (en) | 1988-10-28 | 1996-07-09 | Genentech, Inc. | Human growth hormone variants having greater affinity for human growth hormone receptor at site 1 |
| FR2638643B1 (fr) | 1988-11-09 | 1991-04-12 | Transgene Sa | Sequence d'adn codant pour le facteur ix humain ou une proteine analogue, vecteur d'expression, cellules transformees, procede de preparation du facteur ix et produits obtenus correspondants |
| US5047335A (en) | 1988-12-21 | 1991-09-10 | The Regents Of The University Of Calif. | Process for controlling intracellular glycosylation of proteins |
| US6166183A (en) | 1992-11-30 | 2000-12-26 | Kirin-Amgen, Inc. | Chemically-modified G-CSF |
| EP0853121B1 (en) | 1988-12-23 | 2007-03-28 | Genentech, Inc. | Human DNase |
| US5162228A (en) | 1988-12-28 | 1992-11-10 | Takeda Chemical Industries, Ltd. | Gylceraldehyde-3-phosphate dehydrogenase gene and promoter |
| US5198346A (en) | 1989-01-06 | 1993-03-30 | Protein Engineering Corp. | Generation and selection of novel DNA-binding proteins and polypeptides |
| US5096815A (en) | 1989-01-06 | 1992-03-17 | Protein Engineering Corporation | Generation and selection of novel dna-binding proteins and polypeptides |
| US4957773A (en) | 1989-02-13 | 1990-09-18 | Syracuse University | Deposition of boron-containing films from decaborane |
| US5475090A (en) | 1989-02-21 | 1995-12-12 | Boyce Thompson Institute For Plant Research | Gene coded for a polypeptide which enhances virus infection of host insects |
| US5338835A (en) | 1989-02-21 | 1994-08-16 | Washington University | CTP-extended form of FSH |
| US5194376A (en) | 1989-02-28 | 1993-03-16 | University Of Ottawa | Baculovirus expression system capable of producing foreign gene proteins at high levels |
| DE3906540A1 (de) | 1989-03-02 | 1990-09-13 | Behringwerke Ag | Expressionsvektoren zur synthese von proteinen in der spalthefe schizosaccharomyces pombe |
| US5179023A (en) | 1989-03-24 | 1993-01-12 | Research Corporation Technologies, Inc. | Recombinant α-galactosidase a therapy for Fabry disease |
| US5122614A (en) | 1989-04-19 | 1992-06-16 | Enzon, Inc. | Active carbonates of polyalkylene oxides for modification of polypeptides |
| US5324844A (en) | 1989-04-19 | 1994-06-28 | Enzon, Inc. | Active carbonates of polyalkylene oxides for modification of polypeptides |
| ATE181732T1 (de) | 1989-04-19 | 1999-07-15 | Novo Nordisk As | Aktive karbonate von polyalkylenoxyden zur modifizierung von polypeptiden |
| DE68927344T2 (de) | 1989-04-28 | 1997-02-20 | Rhein Biotech Proz & Prod Gmbh | Hefezellen der Gattung-Schwanniomyces |
| US5766883A (en) | 1989-04-29 | 1998-06-16 | Delta Biotechnology Limited | Polypeptides |
| US5244805A (en) | 1989-05-17 | 1993-09-14 | University Of Georgia Research Foundation, Inc. | Baculovirus expression vectors |
| 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 |
| US5179007A (en) | 1989-07-07 | 1993-01-12 | The Texas A & M University System | Method and vector for the purification of foreign proteins |
| FR2650598B1 (fr) | 1989-08-03 | 1994-06-03 | Rhone Poulenc Sante | Derives de l'albumine a fonction therapeutique |
| US5023328A (en) | 1989-08-04 | 1991-06-11 | The Texas A&M University System | Lepidopteran AKH signal sequence |
| 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 |
| US5182107A (en) | 1989-09-07 | 1993-01-26 | Alkermes, Inc. | Transferrin receptor specific antibody-neuropharmaceutical or diagnostic agent conjugates |
| US5672683A (en) | 1989-09-07 | 1997-09-30 | Alkermes, Inc. | Transferrin neuropharmaceutical agent fusion protein |
| US5527527A (en) | 1989-09-07 | 1996-06-18 | Alkermes, Inc. | Transferrin receptor specific antibody-neuropharmaceutical agent conjugates |
| US5977307A (en) | 1989-09-07 | 1999-11-02 | Alkermes, Inc. | Transferrin receptor specific ligand-neuropharmaceutical agent fusion proteins |
| US5154924A (en) | 1989-09-07 | 1992-10-13 | Alkermes, Inc. | Transferrin receptor specific antibody-neuropharmaceutical agent conjugates |
| US5032519A (en) | 1989-10-24 | 1991-07-16 | The Regents Of The Univ. Of California | Method for producing secretable glycosyltransferases and other Golgi processing enzymes |
| US5580560A (en) | 1989-11-13 | 1996-12-03 | Novo Nordisk A/S | Modified factor VII/VIIa |
| US5312808A (en) | 1989-11-22 | 1994-05-17 | Enzon, Inc. | Fractionation of polyalkylene oxide-conjugated hemoglobin solutions |
| FR2657884B1 (fr) | 1990-02-05 | 1994-09-02 | Tm Innovation | Procede pour la preparation du facteur viii humain et d'analogues du facteur viii. |
| JP2975632B2 (ja) * | 1990-03-30 | 1999-11-10 | 生化学工業株式会社 | グリコサミノグリカン修飾プロテイン |
| US5606031A (en) | 1990-04-06 | 1997-02-25 | Lile; Jack | Production and purification of biologically active recombinant neurotrophic protein in bacteria |
| GB9107846D0 (en) | 1990-04-30 | 1991-05-29 | Ici Plc | Polypeptides |
| US5951972A (en) * | 1990-05-04 | 1999-09-14 | American Cyanamid Company | Stabilization of somatotropins and other proteins by modification of cysteine residues |
| US5399345A (en) | 1990-05-08 | 1995-03-21 | Boehringer Mannheim, Gmbh | Muteins of the granulocyte colony stimulating factor |
| US5219564A (en) | 1990-07-06 | 1993-06-15 | Enzon, Inc. | Poly(alkylene oxide) amino acid copolymers and drug carriers and charged copolymers based thereon |
| DK0538300T3 (da) * | 1990-07-10 | 1994-10-10 | Boehringer Ingelheim Int | O-Glycosyleret IFN-alfa |
| FR2664905B1 (fr) | 1990-07-18 | 1994-08-12 | Agronomique Inst Nat Rech | Baculovirus modifie, son procede d'obtention, et vecteurs d'expression obtenus a partir dudit baculovirus. |
| US5169784A (en) | 1990-09-17 | 1992-12-08 | The Texas A & M University System | Baculovirus dual promoter expression vector |
| US5529914A (en) | 1990-10-15 | 1996-06-25 | The Board Of Regents The Univeristy Of Texas System | Gels for encapsulation of biological materials |
| US5410016A (en) | 1990-10-15 | 1995-04-25 | Board Of Regents, The University Of Texas System | Photopolymerizable biodegradable hydrogels as tissue contacting materials and controlled-release carriers |
| GB9023111D0 (en) | 1990-10-24 | 1990-12-05 | Wellcome Found | Expression system |
| US5401650A (en) | 1990-10-24 | 1995-03-28 | The Mount Sinai School Of Medicine Of The City University Of New York | Cloning and expression of biologically active α-galactosidase A |
| WO1992008790A1 (en) * | 1990-11-14 | 1992-05-29 | Cargill, Incorporated | Conjugates of poly(vinylsaccharide) with proteins for the stabilization of proteins |
| US5420027A (en) | 1991-01-10 | 1995-05-30 | Board Of Regents, The University Of Texas System | Methods and compositions for the expression of biologically active fusion proteins comprising a eukaryotic cytochrome P450 fused to a reductase in bacteria |
| US5948682A (en) | 1991-02-22 | 1999-09-07 | Sembiosys Genetics Inc. | Preparation of heterologous proteins on oil bodies |
| US5650554A (en) | 1991-02-22 | 1997-07-22 | Sembiosys Genetics Inc. | Oil-body proteins as carriers of high-value peptides in plants |
| US6288304B1 (en) | 1991-02-22 | 2001-09-11 | Sembiosys Genetics Inc. | Expression of somatotropin in plant seeds |
| US5833982A (en) | 1991-02-28 | 1998-11-10 | Zymogenetics, Inc. | Modified factor VII |
| US5788965A (en) | 1991-02-28 | 1998-08-04 | Novo Nordisk A/S | Modified factor VII |
| US5997864A (en) | 1995-06-07 | 1999-12-07 | Novo Nordisk A/S | Modified factor VII |
| US5861374A (en) | 1991-02-28 | 1999-01-19 | Novo Nordisk A/S | Modified Factor VII |
| US5817788A (en) | 1991-02-28 | 1998-10-06 | Zymogenetics, Inc. | Modified factor VII |
| US5661008A (en) | 1991-03-15 | 1997-08-26 | Kabi Pharmacia Ab | Recombinant human factor VIII derivatives |
| JP3476455B2 (ja) | 1991-03-18 | 2003-12-10 | ザ スクリップス リサーチ インスティテュート | NeuAcα2、6Galβ1、4GlcNAc及びシアリルLexの合成法 |
| US5278299A (en) * | 1991-03-18 | 1994-01-11 | Scripps Clinic And Research Foundation | Method and composition for synthesizing sialylated glycosyl compounds |
| US5212075A (en) | 1991-04-15 | 1993-05-18 | The Regents Of The University Of California | Compositions and methods for introducing effectors to pathogens and cells |
| US5472858A (en) | 1991-06-04 | 1995-12-05 | Wisconsin Alumni Research Foundation | Production of recombinant proteins in insect larvae |
| US5352670A (en) | 1991-06-10 | 1994-10-04 | Alberta Research Council | Methods for the enzymatic synthesis of alpha-sialylated oligosaccharide glycosides |
| US5374655A (en) | 1991-06-10 | 1994-12-20 | Alberta Research Council | Methods for the synthesis of monofucosylated oligosaccharides terminating in di-N-acetyllactosaminyl structures |
| KR950014915B1 (ko) | 1991-06-19 | 1995-12-18 | 주식회사녹십자 | 탈시알로당단백-포함화합물 |
| US5352570A (en) | 1991-06-28 | 1994-10-04 | Eastman Kodak Company | Method and photographic material and process comprising a benzotriazole compound |
| WO1993000109A1 (en) * | 1991-06-28 | 1993-01-07 | Genentech, Inc. | Method of stimulating immune response using growth hormone |
| US5633146A (en) | 1991-07-02 | 1997-05-27 | Rhone-Poulenc Rorer S.A. | Method for producing recombinant proteins and host cells used therein |
| US5281698A (en) | 1991-07-23 | 1994-01-25 | Cetus Oncology Corporation | Preparation of an activated polymer ester for protein conjugation |
| US5777085A (en) | 1991-12-20 | 1998-07-07 | Protein Design Labs, Inc. | Humanized antibodies reactive with GPIIB/IIIA |
| DK8892D0 (da) | 1992-01-23 | 1992-01-23 | Symbicom Ab | Humant proteingen |
| IT1260468B (it) | 1992-01-29 | 1996-04-09 | Metodo per mantenere l'attivita' di enzimi proteolitici modificati con polietilenglicole | |
| US6039944A (en) | 1992-02-28 | 2000-03-21 | Zymogenetics, Inc. | Modified Factor VII |
| US5965106A (en) | 1992-03-04 | 1999-10-12 | Perimmune Holdings, Inc. | In vivo binding pair pretargeting |
| DE69332538T2 (de) | 1992-04-02 | 2003-11-06 | Sembiosys Genetics, Inc. | Cis elemente des ölkörperproteins als regulationische signale |
| US6037452A (en) | 1992-04-10 | 2000-03-14 | Alpha Therapeutic Corporation | Poly(alkylene oxide)-Factor VIII or Factor IX conjugate |
| US5516657A (en) | 1992-05-11 | 1996-05-14 | Cambridge Biotech Corporation | Baculovirus vectors for expression of secretory and membrane-bound proteins |
| US5614184A (en) | 1992-07-28 | 1997-03-25 | New England Deaconess Hospital | Recombinant human erythropoietin mutants and therapeutic methods employing them |
| EP0664710A4 (en) * | 1992-08-07 | 1998-09-30 | Progenics Pharm Inc | CD4-GAMMA2 AND CD4-IgG2 NON-PEPTIDYL CONJUGATE IMMUNOCONJUGATES AND USES THEREOF. |
| AU5006993A (en) | 1992-08-21 | 1994-03-15 | Enzon, Inc. | Novel attachment of polyalkylene oxides to bio-effecting substances |
| WO1994005332A2 (en) | 1992-09-01 | 1994-03-17 | Berlex Laboratories, Inc. | Glycolation of glycosylated macromolecules |
| US5348886A (en) | 1992-09-04 | 1994-09-20 | Monsanto Company | Method of producing recombinant eukaryotic viruses in bacteria |
| US5736137A (en) | 1992-11-13 | 1998-04-07 | Idec Pharmaceuticals Corporation | Therapeutic application of chimeric and radiolabeled antibodies to human B lymphocyte restricted differentiation antigen for treatment of B cell lymphoma |
| WO1994012646A1 (en) | 1992-11-27 | 1994-06-09 | Ciba-Geigy Ag | Proteins having glycosyltransferase activity |
| US6210671B1 (en) | 1992-12-01 | 2001-04-03 | Protein Design Labs, Inc. | Humanized antibodies reactive with L-selectin |
| NZ250375A (en) * | 1992-12-09 | 1995-07-26 | Ortho Pharma Corp | Peg hydrazone and peg oxime linkage forming reagents and protein derivatives |
| AU6029594A (en) | 1993-01-15 | 1994-08-15 | Enzon, Inc. | Factor viii - polymeric conjugates |
| US5349001A (en) | 1993-01-19 | 1994-09-20 | Enzon, Inc. | Cyclic imide thione activated polyalkylene oxides |
| US5321095A (en) | 1993-02-02 | 1994-06-14 | Enzon, Inc. | Azlactone activated polyalkylene oxides |
| US5202413A (en) | 1993-02-16 | 1993-04-13 | E. I. Du Pont De Nemours And Company | Alternating (ABA)N polylactide block copolymers |
| AUPN154295A0 (en) | 1995-03-06 | 1995-03-30 | Commonwealth Scientific And Industrial Research Organisation | Nucleic acid molecule encoding a protein with avian gamma-interferon activity |
| 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 |
| US6174530B1 (en) | 1993-05-05 | 2001-01-16 | Gryphon Sciences | Homogeneous polyoxime compositions and their preparation by parallel assembly |
| US6001364A (en) | 1993-05-05 | 1999-12-14 | Gryphon Sciences | Hetero-polyoxime compounds and their preparation by parallel assembly |
| WO1994028024A1 (en) * | 1993-06-01 | 1994-12-08 | Enzon, Inc. | Carbohydrate-modified polymer conjugates with erythropoietic activity |
| EP0785988A1 (en) * | 1993-07-15 | 1997-07-30 | Neose Pharmaceuticals, Inc | Method of synthesizing saccharide compositions |
| DE4325317C2 (de) * | 1993-07-29 | 1998-05-20 | Univ Dresden Tech | Verfahren zur radioaktiven Markierung von Immunglobulinen |
| JPH0770195A (ja) * | 1993-08-23 | 1995-03-14 | Yutaka Mizushima | 糖修飾インターフェロン |
| US5446090A (en) | 1993-11-12 | 1995-08-29 | Shearwater Polymers, Inc. | Isolatable, water soluble, and hydrolytically stable active sulfones of poly(ethylene glycol) and related polymers for modification of surfaces and molecules |
| US5827690A (en) | 1993-12-20 | 1998-10-27 | Genzyme Transgenics Corporatiion | Transgenic production of antibodies in milk |
| AU1377395A (en) | 1993-12-23 | 1995-07-10 | University Technologies International Inc. | Methods of expressing proteins in insect cells and methods of killing insects |
| US5597709A (en) | 1994-01-27 | 1997-01-28 | Human Genome Sciences, Inc. | Human growth hormone splice variants hGHV-2(88) and hGHV-3(53) |
| US5369017A (en) * | 1994-02-04 | 1994-11-29 | The Scripps Research Institute | Process for solid phase glycopeptide synthesis |
| US6117679A (en) | 1994-02-17 | 2000-09-12 | Maxygen, Inc. | Methods for generating polynucleotides having desired characteristics by iterative selection and recombination |
| US5837458A (en) | 1994-02-17 | 1998-11-17 | Maxygen, Inc. | Methods and compositions for cellular and metabolic engineering |
| US6165793A (en) | 1996-03-25 | 2000-12-26 | Maxygen, Inc. | Methods for generating polynucleotides having desired characteristics by iterative selection and recombination |
| US5605793A (en) | 1994-02-17 | 1997-02-25 | Affymax Technologies N.V. | Methods for in vitro recombination |
| US5834252A (en) | 1995-04-18 | 1998-11-10 | Glaxo Group Limited | End-complementary polymerase reaction |
| JP3090586B2 (ja) | 1994-03-15 | 2000-09-25 | 片倉工業株式会社 | システインプロテアーゼ遺伝子欠損バキュロウイルスおよびその製造法並びにこれを利用する有用タンパク質の製造法 |
| US5545723A (en) | 1994-03-15 | 1996-08-13 | Biogen Inc. | Muteins of IFN-β |
| US5432059A (en) | 1994-04-01 | 1995-07-11 | Specialty Laboratories, Inc. | Assay for glycosylation deficiency disorders |
| GB9408717D0 (en) | 1994-05-03 | 1994-06-22 | Biotech & Biolog Scien Res | DNA sequences |
| DE69526395D1 (de) | 1994-08-13 | 2002-05-23 | Roche Diagnostics Gmbh | Verwendung von Interferon-gamma zur Vermeidung der Proliferation und Differenzierung der primitiven Hämapoietischen Vorläuferzellen |
| US5871986A (en) | 1994-09-23 | 1999-02-16 | The General Hospital Corporation | Use of a baculovirus to express and exogenous gene in a mammalian cell |
| US5545553A (en) | 1994-09-26 | 1996-08-13 | The Rockefeller University | Glycosyltransferases for biosynthesis of oligosaccharides, and genes encoding them |
| US6010871A (en) * | 1994-09-29 | 2000-01-04 | Ajinomoto Co., Inc. | Modification of peptide and protein |
| US5521299A (en) | 1994-11-22 | 1996-05-28 | National Science Council | Oligonucleotides for detection of baculovirus infection |
| US5834251A (en) | 1994-12-30 | 1998-11-10 | Alko Group Ltd. | Methods of modifying carbohydrate moieties |
| US5932462A (en) | 1995-01-10 | 1999-08-03 | Shearwater Polymers, Inc. | Multiarmed, monofunctional, polymer for coupling to molecules and surfaces |
| IL116730A0 (en) * | 1995-01-13 | 1996-05-14 | Amgen Inc | Chemically modified interferon |
| AU711121B2 (en) | 1995-02-21 | 1999-10-07 | Cantab Pharmaceuticals Research Limited | Viral preparations, vectors, immunogens, and vaccines |
| US5843705A (en) | 1995-02-21 | 1998-12-01 | Genzyme Transgenic Corporation | Transgenically produced antithrombin III |
| GB9506249D0 (en) | 1995-03-27 | 1995-05-17 | Karobio Ab | Media for insect cell cultures |
| US5876980A (en) | 1995-04-11 | 1999-03-02 | Cytel Corporation | Enzymatic synthesis of oligosaccharides |
| US5728554A (en) | 1995-04-11 | 1998-03-17 | Cytel Corporation | Enzymatic synthesis of glycosidic linkages |
| US6030815A (en) | 1995-04-11 | 2000-02-29 | Neose Technologies, Inc. | Enzymatic synthesis of oligosaccharides |
| US5922577A (en) | 1995-04-11 | 1999-07-13 | Cytel Corporation | Enzymatic synthesis of glycosidic linkages |
| CA2227326A1 (en) * | 1995-05-15 | 1996-11-21 | Philip Dehazya | Carbohydrate-mediated coupling of peptides to immunoglobulins |
| US6015555A (en) | 1995-05-19 | 2000-01-18 | Alkermes, Inc. | Transferrin receptor specific antibody-neuropharmaceutical or diagnostic agent conjugates |
| US5770191A (en) | 1995-05-24 | 1998-06-23 | University Of Florida | Active C-terminal peptides of interferon--gamma and their use |
| AU6255096A (en) | 1995-06-07 | 1996-12-30 | Mount Sinai School Of Medicine Of The City University Of New York, The | Pegylated modified proteins |
| US5858752A (en) * | 1995-06-07 | 1999-01-12 | The General Hospital Corporation | Fucosyltransferase genes and uses thereof |
| US5672662A (en) | 1995-07-07 | 1997-09-30 | Shearwater Polymers, Inc. | Poly(ethylene glycol) and related polymers monosubstituted with propionic or butanoic acids and functional derivatives thereof for biotechnical applications |
| US5811634A (en) | 1995-09-12 | 1998-09-22 | Thomas G. O'Brien | Transgenic mammal encoding ornithine decarboxylase |
| DK0851925T3 (da) * | 1995-09-21 | 2005-11-28 | Genentech Inc | Humane Væksthormonvarianter |
| SE9503380D0 (sv) * | 1995-09-29 | 1995-09-29 | Pharmacia Ab | Protein derivatives |
| US5767379A (en) | 1995-11-06 | 1998-06-16 | John Howard | Commercial production of avidin in plants |
| CA2237039A1 (en) | 1995-11-09 | 1997-05-15 | Zymogenetics, Inc. | Production of gad65 in methylotrophic yeast |
| US5965408A (en) | 1996-07-09 | 1999-10-12 | Diversa Corporation | Method of DNA reassembly by interrupting synthesis |
| US6171820B1 (en) | 1995-12-07 | 2001-01-09 | Diversa Corporation | Saturation mutagenesis in directed evolution |
| US6361974B1 (en) | 1995-12-07 | 2002-03-26 | Diversa Corporation | Exonuclease-mediated nucleic acid reassembly in directed evolution |
| US5716812A (en) | 1995-12-12 | 1998-02-10 | The University Of British Columbia | Methods and compositions for synthesis of oligosaccharides, and the products formed thereby |
| US5728580A (en) | 1996-02-20 | 1998-03-17 | Cornell Research Foundation, Inc. | Methods and culture media for inducing single cell suspension in insect cell lines |
| US6096548A (en) | 1996-03-25 | 2000-08-01 | Maxygen, Inc. | Method for directing evolution of a virus |
| AT403765B (de) | 1996-04-12 | 1998-05-25 | Immuno Ag | Verfahren zur herstellung einer präparation enthaltend einen hochgereinigten komplex |
| US5734024A (en) | 1996-04-19 | 1998-03-31 | Boris Y. Zaslavsky | Method for determining the biological activity of recombinant human growth hormone |
| US5750383A (en) | 1996-05-14 | 1998-05-12 | Boyce Thompson Institute For Plant Research, Inc. | Baculovirus cloning system |
| AU708572B2 (en) | 1996-07-17 | 1999-08-05 | Zymogenetics Inc. | Preparation of (pichia methanolica) auxotrophic mutants |
| AU718510B2 (en) | 1996-07-17 | 2000-04-13 | Zymogenetics Inc. | Transformation of pichia methanolica |
| US5682823A (en) | 1996-08-23 | 1997-11-04 | Bethlehem Steel Corporation | Removable insulated cover and method for transporting hot oversized steel ingots |
| US20020064546A1 (en) | 1996-09-13 | 2002-05-30 | J. Milton Harris | Degradable poly(ethylene glycol) hydrogels with controlled half-life and precursors therefor |
| AU735695B2 (en) | 1996-10-10 | 2001-07-12 | Neose Technologies, Inc. | Carbohydrate purification using ultrafiltration, reverse osmosis and nanofiltration |
| US5856452A (en) | 1996-12-16 | 1999-01-05 | Sembiosys Genetics Inc. | Oil bodies and associated proteins as affinity matrices |
| BR9606270A (pt) | 1996-12-18 | 1998-09-22 | Univ Minas Gerais | Processo para a produção da proteína do interferon beta-cis humano recombinante e proteína de interferon beta-cis humano recombinante |
| US6399336B1 (en) | 1997-01-16 | 2002-06-04 | Neose Technologies, Inc. | Practical in vitro sialylation of recombinant glycoproteins |
| US5945314A (en) | 1997-03-31 | 1999-08-31 | Abbott Laboratories | Process for synthesizing oligosaccharides |
| US5804420A (en) | 1997-04-18 | 1998-09-08 | Bayer Corporation | Preparation of recombinant Factor VIII in a protein free medium |
| US6183738B1 (en) * | 1997-05-12 | 2001-02-06 | Phoenix Pharamacologics, Inc. | Modified arginine deiminase |
| US7585645B2 (en) | 1997-05-27 | 2009-09-08 | Sembiosys Genetics Inc. | Thioredoxin and thioredoxin reductase containing oil body based products |
| ES2235336T3 (es) | 1997-06-13 | 2005-07-01 | Gryphon Therapeutics, Inc. | Ligacion quimica nativa en fase solida de peptidos desprotegidos o protegidos en la cisteina n-terminal en solucion acuosa. |
| US6210736B1 (en) | 1997-06-17 | 2001-04-03 | Genzyme Transgenics Corporation | Transgenically produced prolactin |
| JP2002506353A (ja) | 1997-06-24 | 2002-02-26 | ジェネンテック・インコーポレーテッド | ガラクトシル化糖タンパク質の方法及び組成物 |
| WO1999000150A2 (en) | 1997-06-27 | 1999-01-07 | Regents Of The University Of California | Drug targeting of a peptide radiopharmaceutical through the primate blood-brain barrier in vivo with a monoclonal antibody to the human insulin receptor |
| US6090584A (en) | 1997-08-21 | 2000-07-18 | University Technologies International Inc. | Baculovirus artificial chromosomes and methods of use |
| GB9722604D0 (en) * | 1997-10-28 | 1997-12-24 | Cancer Res Campaign Tech | Heparin-binding growth factor derivatives |
| WO1999022764A1 (en) | 1997-10-31 | 1999-05-14 | Genentech, Inc. | Methods and compositions comprising glycoprotein glycoforms |
| WO1999029835A1 (en) | 1997-12-08 | 1999-06-17 | Board Of Trustees Of The University Of Arkansas | PURIFIED β1,2-XYLOSYLTRANSFERASE AND USES THEREOF |
| US7244601B2 (en) | 1997-12-15 | 2007-07-17 | National Research Council Of Canada | Fusion proteins for use in enzymatic synthesis of oligosaccharides |
| US6362276B1 (en) | 1998-01-07 | 2002-03-26 | Debio Recherche Pharmaceutique S.A. | Degradable heterobifunctional poly(ethylene glycol) acrylates and gels and conjugates derived therefrom |
| AU2559799A (en) * | 1998-01-22 | 1999-08-09 | Genentech Inc. | Antibody fragment-polymer conjugates and humanized anti-il-8 monoclonal antibodies and uses of same |
| AR014491A1 (es) | 1998-01-29 | 2001-02-28 | Dow Agrosciences Llc | Metodo para obtener plantas transgenicas fertiles de gossypium hirsutum. |
| ATE268609T1 (de) | 1998-03-12 | 2004-06-15 | Nektar Therapeutics Al Corp | Polyethylenglycolderivate mit benachbarten reaktiven gruppen |
| US6689604B1 (en) | 1998-03-20 | 2004-02-10 | National Research Council Of Canada | Lipopolysaccharide α-2,3 sialyltransferase of Campylobacter jejuni and its uses |
| DK1071700T3 (da) | 1998-04-20 | 2010-06-07 | Glycart Biotechnology Ag | Glykosylerings-modifikation af antistoffer til forbedring af antistofafhængig cellulær cytotoksicitet |
| CN1230546C (zh) | 1998-10-06 | 2005-12-07 | 马克·阿龙·埃马尔法尔布 | 丝状真菌宿主领域的转化系统 |
| US6245539B1 (en) | 1998-10-06 | 2001-06-12 | Board Of Trustees Operating Michigan State University | Human asparaginyl-tRNA synthetase DNA |
| EA004789B9 (ru) * | 1998-10-16 | 2017-05-31 | Байоджен, Инк. | Полимерные конъюгаты бета-1а-интерферона и их использование |
| US6374295B2 (en) * | 1998-10-29 | 2002-04-16 | Nortel Networks Limited | Active server management |
| DE19852729A1 (de) * | 1998-11-16 | 2000-05-18 | Werner Reutter | Rekombinante Glycoproteine, Verfahren zu ihrer Herstellung, sie enthaltende Arzneimittel und ihre Verwendung |
| GB9825105D0 (en) * | 1998-11-16 | 1999-01-13 | Andaris Ltd | Pharamaceutical conjugates |
| AU773845B2 (en) * | 1998-11-18 | 2004-06-10 | Neose Technologies, Inc. | Low cost manufacture of oligosaccharides |
| MXPA01005515A (es) | 1998-12-01 | 2003-07-14 | Protein Design Labs Inc | Anticuerpos humanizados para gamma-interferon. |
| US6365410B1 (en) | 1999-05-19 | 2002-04-02 | Genencor International, Inc. | Directed evolution of microorganisms |
| JO2291B1 (en) * | 1999-07-02 | 2005-09-12 | اف . هوفمان لاروش ايه جي | Erythropoietin derivatives |
| WO2001005434A2 (en) * | 1999-07-20 | 2001-01-25 | Amgen Inc. | Hyaluronic acid-protein conjugates |
| US6348558B1 (en) | 1999-12-10 | 2002-02-19 | Shearwater Corporation | Hydrolytically degradable polymers and hydrogels made therefrom |
| EP2070968A3 (en) | 1999-12-22 | 2013-07-24 | Nektar Therapeutics | Method for the Preparation of 1-Benzotriazolyl Carbonate Esters of Poly(ethylene glycol) |
| AU2352201A (en) | 1999-12-30 | 2001-07-16 | Maxygen Aps | Improved lysosomal enzymes and lysosomal enzyme activators |
| EP2133098A1 (en) * | 2000-01-10 | 2009-12-16 | Maxygen Holdings Ltd | G-CSF conjugates |
| US6423488B1 (en) | 2000-01-15 | 2002-07-23 | Avigenics, Inc | High throughput screening assay for detecting a DNA sequence |
| PL206148B1 (pl) * | 2000-02-11 | 2010-07-30 | Bayer HealthCare LLCBayer HealthCare LLC | Koniugat polipeptydowy, polipeptyd, sekwencja nukleotydowa, wektor ekspresyjny, komórka gospodarz, sposób wytwarzania koniugatu polipeptydowego, środek farmaceutyczny i zastosowanie koniugatu polipeptydowego |
| WO2001060411A1 (en) | 2000-02-18 | 2001-08-23 | Kanagawa Academy Of Science And Technology | Pharmaceutical composition, reagent and method for intracerebral delivery of pharmaceutically active ingredient or labeling substance |
| US7029872B2 (en) | 2000-06-28 | 2006-04-18 | Glycofi, Inc | Methods for producing modified glycoproteins |
| JP2004504016A (ja) | 2000-06-30 | 2004-02-12 | マキシゲン・エイピーエス | ペプチド拡張されたグリコシル化ポリペプチド |
| WO2002004512A2 (en) | 2000-07-10 | 2002-01-17 | Diosynth Rtp, Inc. | Purification of human troponin i |
| AU2001285020A1 (en) | 2000-08-17 | 2002-02-25 | Synapse Technologies, Inc. | P97-active agent conjugates and their methods of use |
| WO2002013843A2 (en) | 2000-08-17 | 2002-02-21 | University Of British Columbia | Chemotherapeutic agents conjugated to p97 and their methods of use in treating neurological tumours |
| WO2002074806A2 (en) | 2001-02-27 | 2002-09-26 | Maxygen Aps | New interferon beta-like molecules |
| ES2411007T3 (es) | 2001-10-10 | 2013-07-04 | Novo Nordisk A/S | Remodelación y glicoconjugación de péptidos |
| JP3894776B2 (ja) | 2001-11-09 | 2007-03-22 | 富士通メディアデバイス株式会社 | 吐出装置および吐出方法 |
| ATE503498T1 (de) * | 2002-06-21 | 2011-04-15 | Novo Nordisk Healthcare Ag | Pegylierte glykoformen von faktor vii |
| WO2004091499A2 (en) * | 2003-04-09 | 2004-10-28 | Neose Technologies, Inc. | Intracellular formation of peptide conjugates |
| JP4251399B2 (ja) * | 2004-05-21 | 2009-04-08 | 独立行政法人産業技術総合研究所 | O結合型糖鎖が付加されたペプチドのスクリーニング方法 |
-
2002
- 2002-10-09 ES ES02795509T patent/ES2411007T3/es not_active Expired - Lifetime
- 2002-10-09 HK HK06100136.9A patent/HK1080090B/zh not_active IP Right Cessation
- 2002-10-09 EP EP09151346.5A patent/EP2080525B1/en not_active Expired - Lifetime
- 2002-10-09 PT PT100125368T patent/PT2279753E/pt unknown
- 2002-10-09 SG SG200605529-7A patent/SG159381A1/en unknown
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- 2002-10-09 DK DK02795509.5T patent/DK1578771T3/da active
- 2002-10-09 AU AU2002360264A patent/AU2002360264B2/en not_active Expired
- 2002-10-09 DK DK10012536.8T patent/DK2279753T3/en active
- 2002-10-09 ES ES10012536.8T patent/ES2556338T3/es not_active Expired - Lifetime
- 2002-10-09 CN CN200910145812.4A patent/CN101724075B/zh not_active Expired - Lifetime
- 2002-10-09 MX MXPA04003333A patent/MXPA04003333A/es active IP Right Grant
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- 2002-10-09 EP EP02795509A patent/EP1578771B1/en not_active Expired - Lifetime
- 2002-10-09 US US10/492,261 patent/US7416858B2/en not_active Expired - Lifetime
- 2002-10-09 EP EP10184886.9A patent/EP2322229B1/en not_active Expired - Lifetime
- 2002-10-09 EP EP10012938.6A patent/EP2279754B1/en not_active Expired - Lifetime
- 2002-10-09 ES ES10012938.6T patent/ES2516041T3/es not_active Expired - Lifetime
- 2002-10-09 DK DK10184886.9T patent/DK2322229T3/en active
- 2002-10-09 ES ES10184886T patent/ES2619371T3/es not_active Expired - Lifetime
- 2002-10-09 CN CN2011100354568A patent/CN102180944A/zh active Pending
- 2002-10-09 ES ES10012794.3T patent/ES2538342T3/es not_active Expired - Lifetime
- 2002-10-09 EP EP10185505A patent/EP2292273A3/en not_active Withdrawn
- 2002-10-09 ES ES10012939.4T patent/ES2466024T3/es not_active Expired - Lifetime
- 2002-10-09 ES ES09000818.6T patent/ES2606840T3/es not_active Expired - Lifetime
- 2002-10-09 EP EP20100012793 patent/EP2305311A3/en not_active Withdrawn
- 2002-10-09 NZ NZ532027A patent/NZ532027A/en not_active IP Right Cessation
- 2002-10-09 EP EP10012794.3A patent/EP2305312B1/en not_active Expired - Lifetime
- 2002-10-09 EP EP10012796.8A patent/EP2298354B1/en not_active Expired - Lifetime
- 2002-10-09 ES ES09151346.5T patent/ES2564688T3/es not_active Expired - Lifetime
- 2002-10-09 ES ES10012798T patent/ES2561985T3/es not_active Expired - Lifetime
- 2002-10-09 JP JP2003534446A patent/JP5232352B2/ja not_active Expired - Lifetime
- 2002-10-09 BR BRPI0213207-9A patent/BRPI0213207B1/pt not_active IP Right Cessation
- 2002-10-09 CN CN02820073XA patent/CN1635901B/zh not_active Expired - Lifetime
- 2002-10-09 EP EP10012795A patent/EP2292271A3/en not_active Withdrawn
- 2002-10-09 SG SG2006055305A patent/SG177002A1/en unknown
- 2002-10-09 CA CA2462930A patent/CA2462930C/en not_active Expired - Lifetime
- 2002-10-09 EP EP10012939.4A patent/EP2279755B1/en not_active Expired - Lifetime
- 2002-10-09 IL IL16125102A patent/IL161251A0/xx unknown
- 2002-10-09 WO PCT/US2002/032263 patent/WO2003031464A2/en not_active Ceased
- 2002-10-09 DK DK10012939.4T patent/DK2279755T3/da active
- 2002-10-09 EP EP10012536.8A patent/EP2279753B1/en not_active Expired - Lifetime
- 2002-10-09 EP EP10012797.6A patent/EP2305313B1/en not_active Expired - Lifetime
- 2002-10-09 PT PT100129394T patent/PT2279755E/pt unknown
- 2002-10-09 EP EP09000818.6A patent/EP2042196B1/en not_active Expired - Lifetime
- 2002-10-09 EP EP10012798.4A patent/EP2305314B1/en not_active Expired - Lifetime
- 2002-11-05 US US10/287,994 patent/US7138371B2/en active Active
-
2004
- 2004-04-01 IL IL161251A patent/IL161251A/en active IP Right Grant
- 2004-04-05 ZA ZA200402673A patent/ZA200402673B/en unknown
-
2006
- 2006-04-12 US US11/404,266 patent/US7276475B2/en not_active Expired - Lifetime
-
2008
- 2008-11-20 JP JP2008297209A patent/JP5376912B2/ja not_active Expired - Lifetime
-
2009
- 2009-06-16 AU AU2009202405A patent/AU2009202405B2/en not_active Expired
-
2010
- 2010-02-05 JP JP2010024516A patent/JP5258809B2/ja not_active Expired - Lifetime
- 2010-09-28 JP JP2010217733A patent/JP5739632B2/ja not_active Expired - Fee Related
- 2010-12-23 IL IL210257A patent/IL210257A/en not_active IP Right Cessation
-
2012
- 2012-05-07 JP JP2012106130A patent/JP2012143250A/ja active Pending
-
2014
- 2014-01-23 LU LU92359C patent/LU92359I2/fr unknown
- 2014-01-24 BE BE2014C004C patent/BE2014C004I2/fr unknown
- 2014-01-24 FR FR14C0007C patent/FR14C0007I2/fr active Active
- 2014-01-28 JP JP2014013799A patent/JP2014087370A/ja not_active Ceased
-
2015
- 2015-09-17 JP JP2015184218A patent/JP6316784B2/ja not_active Expired - Lifetime
-
2016
- 2016-06-14 JP JP2016118316A patent/JP6321724B2/ja not_active Expired - Lifetime
-
2017
- 2017-11-21 NL NL300912C patent/NL300912I2/nl unknown
- 2017-11-28 BE BE2017C059C patent/BE2017C059I2/nl unknown
- 2017-11-30 FR FR17C1053C patent/FR17C1053I2/fr active Active
Patent Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE2432518A1 (de) * | 1973-07-05 | 1975-01-30 | Beecham Group Ltd | Arzneimittel und verfahren zu seiner herstellung |
| US4055635A (en) * | 1973-07-05 | 1977-10-25 | Beecham Group Limited | Fibrinolytic compositions |
| US5405753A (en) * | 1990-03-26 | 1995-04-11 | Brossmer; Reinhard | CMP-activated, fluorescing sialic acids, as well as processes for their preparation |
| WO1994029370A1 (en) * | 1993-06-08 | 1994-12-22 | Enzon, Inc. | Factor ix - polymeric conjugates |
| WO2000044785A1 (en) * | 1999-01-29 | 2000-08-03 | F. Hoffmann-La Roche Ag | Gcsf conjugates |
| SK10352001A3 (sk) * | 1999-01-29 | 2002-06-04 | Amgen, Inc. | Fyziologicky aktívny konjugát, prostriedok a spôsob prípravy |
Non-Patent Citations (4)
| Title |
|---|
| 《Enzymatic introduction of a fluorescent sialic acid into oligosaccharide chains》;GROSS H J 等;《EUROPEAN JOURNAL OF BIOCHEMISTRY》;19881115;第177卷(第3期);第583-589页 * |
| 《Preparation of Antibody-Linked Cytotoxic Agents》;GHOSE T 等;《Methods In Enzymology》;19830101;第93卷(第1期);第280-333页 * |
| 《Transfer of synthetic sial i c acid analogues to N-and O-linked glycoprotein glycans using four different mammalian sialyltransferases》;GROSS H J 等;《Biochemistry》;19890101;第28卷(第1期);第7392-7400页 * |
| 《Utilization of Glycosyltransferases》;Guo Z. 等;《Applied Biochemistry and Biotechnology》;19971001;第68卷;第1-20页 * |
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