JP4187277B2 - グリコシル化し得る抗原結合単鎖タンパク質、それらの生成および使用 - Google Patents
グリコシル化し得る抗原結合単鎖タンパク質、それらの生成および使用 Download PDFInfo
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- JP4187277B2 JP4187277B2 JP54735198A JP54735198A JP4187277B2 JP 4187277 B2 JP4187277 B2 JP 4187277B2 JP 54735198 A JP54735198 A JP 54735198A JP 54735198 A JP54735198 A JP 54735198A JP 4187277 B2 JP4187277 B2 JP 4187277B2
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- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/56—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an organic macromolecular compound, e.g. an oligomeric, polymeric or dendrimeric molecule
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- A61K47/60—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an organic macromolecular compound, e.g. an oligomeric, polymeric or dendrimeric molecule obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds, e.g. polyureas or polyurethanes the organic macromolecular compound being a polyoxyalkylene oligomer, polymer or dendrimer, e.g. PEG, PPG, PEO or polyglycerol
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- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/30—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants from tumour cells
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- C07K2317/40—Immunoglobulins specific features characterized by post-translational modification
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- C07K2317/60—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments
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- C—CHEMISTRY; METALLURGY
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JP54735198A Expired - Lifetime JP4187277B2 (ja) | 1997-04-30 | 1998-04-30 | グリコシル化し得る抗原結合単鎖タンパク質、それらの生成および使用 |
JP2008008563A Withdrawn JP2008115193A (ja) | 1997-04-30 | 2008-01-17 | ポリアルキレンオキシド修飾された単鎖ポリペプチド |
JP2009281051A Withdrawn JP2010051331A (ja) | 1997-04-30 | 2009-12-10 | ポリアルキレンオキシド修飾された単鎖ポリペプチド |
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JP2009281051A Withdrawn JP2010051331A (ja) | 1997-04-30 | 2009-12-10 | ポリアルキレンオキシド修飾された単鎖ポリペプチド |
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Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1998049198A1 (en) * | 1997-04-30 | 1998-11-05 | Enzon, Inc. | Single-chain antigen-binding proteins capable of glycosylation, production and uses thereof |
US20040009166A1 (en) * | 1997-04-30 | 2004-01-15 | Filpula David R. | Single chain antigen-binding polypeptides for polymer conjugation |
US6333396B1 (en) | 1998-10-20 | 2001-12-25 | Enzon, Inc. | Method for targeted delivery of nucleic acids |
MXPA01005562A (es) * | 1998-11-03 | 2003-08-01 | Centocor Inc | Anticuerpos y fragmentos de anticuerpos modificados con mayor duracion de actividad. |
US7122632B2 (en) | 1999-12-23 | 2006-10-17 | Zymogenetics, Inc. | Soluble Interleukin-20 receptor |
US6610286B2 (en) | 1999-12-23 | 2003-08-26 | Zymogenetics, Inc. | Method for treating inflammation using soluble receptors to interleukin-20 |
ES2327606T3 (es) | 2000-01-10 | 2009-11-02 | Maxygen Holdings Ltd | Conjugados de g-csf. |
PL204285B1 (pl) | 2000-02-11 | 2009-12-31 | Bayer Healthcare Llc | Koniugat polipeptydowy, polipeptyd, sekwencja nukleotydowa, wektor ekspresyjny, komórka gospodarz, sposób wytwarzania koniugatu polipeptydowego, środek farmaceutyczny i zastosowanie koniugatu polipeptydowego |
US20030027207A1 (en) * | 2000-02-29 | 2003-02-06 | Filpula David Ray | Anti-platelet binding proteins and polymer conjugates containing the same |
US6410246B1 (en) * | 2000-06-23 | 2002-06-25 | Genetastix Corporation | Highly diverse library of yeast expression vectors |
US6410271B1 (en) * | 2000-06-23 | 2002-06-25 | Genetastix Corporation | Generation of highly diverse library of expression vectors via homologous recombination in yeast |
US7118737B2 (en) * | 2000-09-08 | 2006-10-10 | Amylin Pharmaceuticals, Inc. | Polymer-modified synthetic proteins |
JP2004515471A (ja) * | 2000-09-08 | 2004-05-27 | グリフォン セラピューティクス,インコーポレーテッド | 合成赤血球産生刺激タンパク質 |
US8110218B2 (en) * | 2000-11-30 | 2012-02-07 | The Research Foundation Of State University Of New York | Compositions and methods for less immunogenic protein-lipid complexes |
AU2002223350A1 (en) * | 2000-12-01 | 2002-06-11 | Eleanor N. Fish | Cytokine receptor binding peptides |
US6979556B2 (en) | 2000-12-14 | 2005-12-27 | Genentech, Inc. | Separate-cistron contructs for secretion of aglycosylated antibodies from prokaryotes |
US7195923B2 (en) * | 2001-01-31 | 2007-03-27 | Scripps Laboratories, Inc. | Ratiometric determination of glycated protein |
CA2469846A1 (en) | 2001-02-27 | 2002-09-26 | Maxygen Aps | New interferon beta-like molecules |
ATE382053T1 (de) | 2001-08-27 | 2008-01-15 | Genentech Inc | System zur antikörperexpression und- synthese |
US8008252B2 (en) | 2001-10-10 | 2011-08-30 | Novo Nordisk A/S | Factor VII: remodeling and glycoconjugation of Factor VII |
US7173003B2 (en) | 2001-10-10 | 2007-02-06 | Neose Technologies, Inc. | Granulocyte colony stimulating factor: remodeling and glycoconjugation of G-CSF |
US7214660B2 (en) | 2001-10-10 | 2007-05-08 | Neose Technologies, Inc. | Erythropoietin: remodeling and glycoconjugation of erythropoietin |
US7795210B2 (en) * | 2001-10-10 | 2010-09-14 | Novo Nordisk A/S | Protein remodeling methods and proteins/peptides produced by the methods |
US7157277B2 (en) | 2001-11-28 | 2007-01-02 | Neose Technologies, Inc. | Factor VIII remodeling and glycoconjugation of Factor VIII |
PT1531843E (pt) | 2001-12-17 | 2011-10-27 | Zymogenetics Inc | Método para tratar o cancro cervical |
AU2003202297C1 (en) | 2002-01-25 | 2006-05-18 | G2 Therapies Ltd | Anti-C5aR antibodies and uses thereof |
MXPA04012496A (es) | 2002-06-21 | 2005-09-12 | Novo Nordisk Healthcare Ag | Glicoformos del factor vii pegilados. |
KR101186140B1 (ko) | 2002-06-21 | 2012-09-27 | 노보 노르디스크 헬스 케어 악티엔게젤샤프트 | 페길화된 인자 vii 글리코형태 |
US9321832B2 (en) | 2002-06-28 | 2016-04-26 | Domantis Limited | Ligand |
US20050026866A1 (en) * | 2002-08-02 | 2005-02-03 | Pawelek John M. | Agents and methods for treatment of disease by oligosaccharide targeting agents |
US20040067532A1 (en) | 2002-08-12 | 2004-04-08 | Genetastix Corporation | High throughput generation and affinity maturation of humanized antibody |
DE60321363D1 (de) * | 2002-08-28 | 2008-07-10 | Millipore Corp | Verfahren zur aufreinigung von sequenzierungsreaktionen |
US20040062748A1 (en) | 2002-09-30 | 2004-04-01 | Mountain View Pharmaceuticals, Inc. | Polymer conjugates with decreased antigenicity, methods of preparation and uses thereof |
US8129330B2 (en) | 2002-09-30 | 2012-03-06 | Mountain View Pharmaceuticals, Inc. | Polymer conjugates with decreased antigenicity, methods of preparation and uses thereof |
AU2003303595A1 (en) | 2002-12-30 | 2004-07-29 | Gryphon Therapeutics, Inc. | Water-soluble thioester and selenoester compounds and methods for making and using the same |
US7351688B2 (en) * | 2003-02-05 | 2008-04-01 | The Research Foundation Of State University Of New York | Compositions and methods for less immunogenic protein formulations |
US20040229793A1 (en) * | 2003-02-05 | 2004-11-18 | Balasubramanian Sathyamangalam V. | Compositions and methods for less immunogenic protein formulations |
US7803777B2 (en) | 2003-03-14 | 2010-09-28 | Biogenerix Ag | Branched water-soluble polymers and their conjugates |
US8791070B2 (en) | 2003-04-09 | 2014-07-29 | Novo Nordisk A/S | Glycopegylated factor IX |
EP2055189A1 (en) | 2003-04-09 | 2009-05-06 | Neose Technologies, Inc. | Glycopegylation methods and proteins/peptides produced by the methods |
US7932364B2 (en) * | 2003-05-09 | 2011-04-26 | Novo Nordisk A/S | Compositions and methods for the preparation of human growth hormone glycosylation mutants |
SI1639011T1 (sl) * | 2003-06-30 | 2009-04-30 | Domantis Ltd | Pegilirana protitelesa z enojno domeno (dAb) |
US9005625B2 (en) * | 2003-07-25 | 2015-04-14 | Novo Nordisk A/S | Antibody toxin conjugates |
EP1668358B1 (en) * | 2003-08-05 | 2014-12-10 | The Research Foundation of State University of New York | Reconstitution medium for protein and peptide formulations |
US20050055024A1 (en) * | 2003-09-08 | 2005-03-10 | James Anthony H. | Orthopaedic implant and screw assembly |
EP2263684A1 (en) | 2003-10-10 | 2010-12-22 | Novo Nordisk A/S | IL-21 derivatives |
ES2428358T3 (es) | 2003-10-17 | 2013-11-07 | Novo Nordisk A/S | Terapia de combinación |
WO2005052001A2 (en) * | 2003-11-21 | 2005-06-09 | Zymogenetics, Inc. | Anti-il-20 receptor antibodies and binding partners and methods of using in inflammation |
US8633157B2 (en) | 2003-11-24 | 2014-01-21 | Novo Nordisk A/S | Glycopegylated erythropoietin |
US20080305992A1 (en) | 2003-11-24 | 2008-12-11 | Neose Technologies, Inc. | 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 |
CA2552435A1 (en) | 2003-12-05 | 2005-06-23 | Compound Therapeutics, Inc. | Inhibitors of type 2 vascular endothelial growth factor receptors |
US20080220049A1 (en) * | 2003-12-05 | 2008-09-11 | Adnexus, A Bristol-Myers Squibb R&D Company | Compositions and methods for intraocular delivery of fibronectin scaffold domain proteins |
KR101439880B1 (ko) | 2004-01-08 | 2014-09-12 | 라티오팜 게엠베하 | 펩티드의 오-결합형 글리코실화 |
JP4896745B2 (ja) | 2004-02-02 | 2012-03-14 | アンブレツクス・インコーポレイテツド | 修飾されたヒトインターフェロンポリペプチドおよびこれらの使用 |
WO2006069220A2 (en) | 2004-12-22 | 2006-06-29 | Ambrx, Inc. | Modified human growth hormone |
JP2008503217A (ja) | 2004-06-18 | 2008-02-07 | アンブレツクス・インコーポレイテツド | 新規抗原結合ポリペプチド及びそれらの使用 |
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 |
US20060045866A1 (en) * | 2004-09-01 | 2006-03-02 | Chris Chappelow | Novel high purity and high molecular weight mPEG alcohol compositions |
US8268967B2 (en) | 2004-09-10 | 2012-09-18 | Novo Nordisk A/S | Glycopegylated interferon α |
DK2586456T3 (en) | 2004-10-29 | 2016-03-21 | Ratiopharm Gmbh | Conversion and glycopegylation of fibroblast growth factor (FGF) |
WO2006068802A2 (en) | 2004-12-22 | 2006-06-29 | Ambrx, Inc. | COMPOSITIONS OF AMINOACYL-tRNA SYNTHETASE AND USES THEREOF |
MX2007007587A (es) | 2004-12-22 | 2007-12-11 | Ambrx Inc | Formulaciones de la hormona del crecimiento humano que comprenden un aminoacido codificado de manera no natural. |
KR20070100299A (ko) | 2004-12-22 | 2007-10-10 | 암브룩스, 인코포레이티드 | 재조합 인간 성장 호르몬의 발현 및 정제 방법 |
EP1858543B1 (en) | 2005-01-10 | 2013-11-27 | BioGeneriX AG | Glycopegylated granulocyte colony stimulating factor |
EP1841787A2 (en) * | 2005-01-25 | 2007-10-10 | Cell Therapeutics, Inc. | Conjugates of biologically active proteins having a modified in vivo half-life |
WO2006097682A1 (en) * | 2005-03-18 | 2006-09-21 | Ucl Business Plc | Mechano growth factor peptides and their use |
US20060233740A1 (en) * | 2005-03-23 | 2006-10-19 | Bossard Mary J | Conjugates of an hGH moiety and a polymer |
EP2279756A2 (en) | 2005-04-05 | 2011-02-02 | Instituto di Ricerche di Biologia Molecolare p Angeletti S.P.A. | Method for shielding functional sites or epitopes on proteins |
WO2006121569A2 (en) | 2005-04-08 | 2006-11-16 | Neose Technologies, Inc. | Compositions and methods for the preparation of protease resistant human growth hormone glycosylation mutants |
EP2975135A1 (en) | 2005-05-25 | 2016-01-20 | Novo Nordisk A/S | Glycopegylated factor IX |
US20110003744A1 (en) * | 2005-05-25 | 2011-01-06 | Novo Nordisk A/S | Glycopegylated Erythropoietin Formulations |
EP1888098A2 (en) | 2005-05-25 | 2008-02-20 | Neose Technologies, Inc. | Glycopegylated erythropoietin formulations |
WO2006133089A2 (en) | 2005-06-03 | 2006-12-14 | Ambrx, Inc. | Improved human interferon molecules and their uses |
US8028453B2 (en) * | 2005-06-16 | 2011-10-04 | Hold That Thought, Inc. | Apparatus and methods for displaying a card |
US8633300B2 (en) | 2005-06-17 | 2014-01-21 | Novo Nordisk Healthcare Ag | Selective reduction and derivatization of engineered proteins comprising at least one non-native cysteine |
JP2008543943A (ja) * | 2005-06-20 | 2008-12-04 | ペプゲン コーポレイション | ヒトインターフェロンアルファ類似体とインターフェロンタウの低毒性長期循環性キメラ |
US7695710B2 (en) * | 2005-06-20 | 2010-04-13 | Pepgen Corporation | Antitumor and antiviral combination therapies using low-toxicity, long-circulating human interferon-alpha analogs |
CA2613705A1 (en) * | 2005-06-29 | 2007-01-04 | The Research Foundation Of State University Of New York | Compositions and methods for less immunogenic pr0tein-lip1d complexes |
WO2007021822A2 (en) * | 2005-08-09 | 2007-02-22 | The Research Foundation Of State Of University Of New York At Buffalo | Compositions and methods of preparation of liposomal microparticulate il-12 |
US20070105755A1 (en) | 2005-10-26 | 2007-05-10 | Neose Technologies, Inc. | One pot desialylation and glycopegylation of therapeutic peptides |
WO2007026972A2 (en) * | 2005-09-01 | 2007-03-08 | Canon Kabushiki Kaisha | Binding protein molecule |
US8168592B2 (en) | 2005-10-21 | 2012-05-01 | Amgen Inc. | CGRP peptide antagonists and conjugates |
US20090048440A1 (en) | 2005-11-03 | 2009-02-19 | Neose Technologies, Inc. | Nucleotide Sugar Purification Using Membranes |
JP2009520949A (ja) | 2005-11-16 | 2009-05-28 | アンブルックス,インコーポレイテッド | 非天然アミノ酸を含んでいる組成物および方法 |
CA2660310C (en) * | 2006-03-30 | 2015-04-21 | The Research Foundation Of State University Of New York | Compositions of less immunogenic and long-circulating protein-lipid complexes |
US7875288B2 (en) * | 2006-03-30 | 2011-01-25 | The Research Foundation Of State University Of New York | Method for treating blood coagulation disorders |
US7645860B2 (en) | 2006-03-31 | 2010-01-12 | Baxter Healthcare S.A. | Factor VIII polymer conjugates |
AU2007245190B2 (en) | 2006-03-31 | 2011-07-21 | Takeda Pharmaceutical Company Limited | Pegylated factor VIII |
US7982010B2 (en) * | 2006-03-31 | 2011-07-19 | Baxter International Inc. | Factor VIII polymer conjugates |
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 |
US20080096819A1 (en) * | 2006-05-02 | 2008-04-24 | Allozyne, Inc. | Amino acid substituted molecules |
AU2007248680C1 (en) * | 2006-05-02 | 2014-01-23 | Allozyne, Inc. | Non-natural amino acid substituted polypeptides |
RU2008145084A (ru) | 2006-05-24 | 2010-06-27 | Ново Нордиск Хелс Кеа Аг (Ch) | Аналоги фактора ix, имеющие пролонгированное время полужизни in vivo |
ES2656359T3 (es) | 2006-06-30 | 2018-02-26 | Novo Nordisk A/S | Anticuerpos anti-NKG2A y usos de los mismos |
EP2049144B8 (en) | 2006-07-21 | 2015-02-18 | ratiopharm GmbH | Glycosylation of peptides via o-linked glycosylation sequences |
AU2007292892B9 (en) | 2006-09-08 | 2013-02-28 | Ambrx, Inc. | Hybrid suppressor tRNA for vertebrate cells |
AU2007292903B2 (en) | 2006-09-08 | 2012-03-29 | Ambrx, Inc. | Modified human plasma polypeptide or Fc scaffolds and their uses |
JP2008069073A (ja) * | 2006-09-12 | 2008-03-27 | Yokohama Tlo Co Ltd | ラクトフェリン複合体及びその製造方法 |
US8367065B2 (en) * | 2006-09-15 | 2013-02-05 | Enzon Pharmaceuticals, Inc. | Targeted polymeric prodrugs containing multifunctional linkers |
AU2007296056B2 (en) * | 2006-09-15 | 2012-09-13 | Enzon Pharmaceuticals, Inc. | Targeted polymeric prodrugs containing multifunctional linkers |
US7985783B2 (en) | 2006-09-21 | 2011-07-26 | The Regents Of The University Of California | Aldehyde tags, uses thereof in site-specific protein modification |
US8969532B2 (en) | 2006-10-03 | 2015-03-03 | Novo Nordisk A/S | Methods for the purification of polypeptide conjugates comprising polyalkylene oxide using hydrophobic interaction chromatography |
WO2008066752A2 (en) * | 2006-11-22 | 2008-06-05 | Adnexus, A Bristol-Myers Squibb R & D Company | Targeted therapeutics based on engineered proteins for tyrosine kinases receptors, including igf-ir |
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 |
CN107011431B (zh) * | 2007-01-30 | 2020-11-06 | 埃皮瓦克斯公司 | 调节性t细胞表位、组合物及其用途 |
EP2111228B1 (en) * | 2007-02-02 | 2011-07-20 | Bristol-Myers Squibb Company | 10Fn3 domain for use in treating diseases associated with inappropriate angiogenesis |
CA2682147C (en) | 2007-03-30 | 2017-08-08 | Ambrx, Inc. | Modified fgf-21 polypeptides and their uses |
PL2144923T3 (pl) | 2007-04-03 | 2013-12-31 | Biogenerix Ag | Sposoby leczenia z użyciem glikopegilowanego G-CSF |
NZ580686A (en) | 2007-05-02 | 2012-11-30 | Ambrx Inc | Modified interferon beta polypeptides and their uses |
US9493499B2 (en) | 2007-06-12 | 2016-11-15 | Novo Nordisk A/S | Process for the production of purified cytidinemonophosphate-sialic acid-polyalkylene oxide (CMP-SA-PEG) as modified nucleotide sugars via anion exchange chromatography |
US7968811B2 (en) * | 2007-06-29 | 2011-06-28 | Harley-Davidson Motor Company Group, Inc. | Integrated ignition and key switch |
JP2010533181A (ja) * | 2007-07-13 | 2010-10-21 | アボツト・バイオテクノロジー・リミテツド | TNFα阻害剤の肺投与のための方法及び組成物 |
CA2707840A1 (en) * | 2007-08-20 | 2009-02-26 | Allozyne, Inc. | Amino acid substituted molecules |
US20090304719A1 (en) | 2007-08-22 | 2009-12-10 | Patrick Daugherty | Activatable binding polypeptides and methods of identification and use thereof |
US8207112B2 (en) | 2007-08-29 | 2012-06-26 | Biogenerix Ag | Liquid formulation of G-CSF conjugate |
CA2697193C (en) | 2007-09-14 | 2017-06-06 | Adimab, Inc. | Rationally designed, synthetic antibody libraries and uses therefor |
US8877688B2 (en) | 2007-09-14 | 2014-11-04 | Adimab, Llc | Rationally designed, synthetic antibody libraries and uses therefor |
US20100285178A1 (en) * | 2007-11-15 | 2010-11-11 | Nestec S.A. | Production of food products with enhanced in mouth and mental refreshment |
CN101918026B (zh) | 2007-11-20 | 2016-03-02 | Ambrx公司 | 经修饰胰岛素多肽和其用途 |
US9097667B2 (en) | 2007-12-14 | 2015-08-04 | Biotium, Inc. | Fluorescent compounds |
EP2222706B2 (en) | 2007-12-14 | 2016-08-10 | Novo Nordisk A/S | Antibodies against human nkg2d and uses thereof |
BRPI0908508A2 (pt) | 2008-01-24 | 2016-03-22 | Novo Nordisk As | anticorpo monoclonal nkg2a anti-humano humanizado |
CN101939443B (zh) | 2008-02-08 | 2014-01-29 | Ambrx公司 | 经修饰瘦素多肽和其用途 |
US8524244B2 (en) | 2008-02-14 | 2013-09-03 | Bristol-Myers Squibb Company | Targeted therapeutics based on engineered proteins that bind EGFR |
WO2009103113A1 (en) | 2008-02-20 | 2009-08-27 | G2 Inflammation Pty Ltd | HUMANIZED ANTI-C5aR ANTIBODIES |
RU2573587C2 (ru) | 2008-02-27 | 2016-01-20 | Ново Нордиск А/С | Конъюгированные молекулы фактора viii |
WO2009142773A2 (en) | 2008-05-22 | 2009-11-26 | Bristol-Myers Squibb Company | Multivalent fibronectin based scaffold domain proteins |
ES2654387T3 (es) | 2008-07-23 | 2018-02-13 | Ambrx, Inc. | Polipéptidos G-CSF bovinos modificados y sus usos |
PT2342223T (pt) | 2008-09-26 | 2017-07-07 | Lilly Co Eli | Polipéptidos de eritropoetina animal modificados e suas utilizações |
MX343802B (es) | 2008-09-26 | 2016-11-23 | Ambrx Inc | Microorganismos y vacunas dependientes de replicacion de aminoacidos no naturales. |
BRPI0921586A2 (pt) | 2008-11-18 | 2019-09-24 | Merrimack Pharmaceuticals Inc | articuladores de albumina de soro humana e conjugados destes |
TWI496582B (zh) | 2008-11-24 | 2015-08-21 | 必治妥美雅史谷比公司 | 雙重專一性之egfr/igfir結合分子 |
RU2562114C2 (ru) | 2008-12-22 | 2015-09-10 | Ново Нордиск А/С | Антитела против ингибитора метаболического пути тканевого фактора |
WO2010081173A2 (en) | 2009-01-12 | 2010-07-15 | Cytomx Therapeutics, Llc | Modified antibody compositions, methods of making and using thereof |
WO2010081890A1 (en) | 2009-01-19 | 2010-07-22 | Innate Pharma | Anti-kir3d antibodies |
WO2010096838A2 (en) | 2009-02-23 | 2010-08-26 | Cytomx Therapeutics, Llc | Proproteins and methods of use thereof |
US8067201B2 (en) * | 2009-04-17 | 2011-11-29 | Bristol-Myers Squibb Company | Methods for protein refolding |
EP2446027A1 (en) * | 2009-06-25 | 2012-05-02 | Danisco A/S | Protein |
JP5946766B2 (ja) | 2009-07-03 | 2016-07-06 | ビオノール イミュノ エーエスBionor Immuno As | Hivワクチン組成物における使用又は診断手段としての使用のためのhiv関連ペプチドの組合せ又は融合物 |
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 |
US8809501B2 (en) | 2009-07-27 | 2014-08-19 | Baxter International Inc. | Nucleophilic catalysts for oxime linkage |
HUE028056T2 (en) | 2009-07-27 | 2016-11-28 | Baxalta GmbH | Blood coagulation protein conjugates |
US8642737B2 (en) | 2010-07-26 | 2014-02-04 | Baxter International Inc. | Nucleophilic catalysts for oxime linkage |
JP5908401B2 (ja) * | 2009-07-27 | 2016-04-26 | 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 | 血液凝固タンパク質複合体 |
WO2011030107A1 (en) | 2009-09-10 | 2011-03-17 | Ucb Pharma S.A. | Multivalent antibodies |
US8658434B2 (en) * | 2009-10-28 | 2014-02-25 | Biotium, Inc. | Fluorescent pyrene compounds |
GB0920127D0 (en) * | 2009-11-17 | 2009-12-30 | Ucb Pharma Sa | Antibodies |
EA201290541A1 (ru) | 2009-12-21 | 2013-05-30 | Амбркс, Инк. | Модифицированные бычьи соматотропиновые полипептиды и их применение |
CA2784800A1 (en) | 2009-12-21 | 2011-07-21 | Ambrx, Inc. | Modified porcine somatotropin polypeptides and their uses |
TWI513466B (zh) | 2010-01-20 | 2015-12-21 | Boehringer Ingelheim Int | 抗凝血劑解毒劑 |
US10080799B2 (en) | 2010-02-12 | 2018-09-25 | Arizona Board Of Regents On Behalf Of Arizona State University | Methods and compositions related to glycoprotein-immunoglobulin fusions |
WO2011104381A2 (en) | 2010-02-26 | 2011-09-01 | Novo Nordisk A/S | Stable antibody containing compositions |
EP3815708A1 (en) | 2010-03-05 | 2021-05-05 | Omeros Corporation | Chimeric inhibitor molecules of complement activation |
TW201138808A (en) | 2010-05-03 | 2011-11-16 | Bristol Myers Squibb Co | Serum albumin binding molecules |
US20120135912A1 (en) | 2010-05-10 | 2012-05-31 | Perseid Therapeutics Llc | Polypeptide inhibitors of vla4 |
EP2576615B1 (en) | 2010-05-26 | 2016-03-30 | Bristol-Myers Squibb Company | Fibronectin based scaffold proteins having improved stability |
EP2575761A1 (en) | 2010-05-28 | 2013-04-10 | Novo Nordisk A/S | Stable multi-dose compositions comprising an antibody and a preservative |
WO2012000994A1 (en) | 2010-06-29 | 2012-01-05 | C.N.R.S. | Llt-1 antibodies with new functional properties |
US9260518B2 (en) | 2010-06-30 | 2016-02-16 | Novo Nordisk A/S | Antibodies that are capable of specifically binding tissue factor pathway inhibitor |
KR101963709B1 (ko) | 2010-07-16 | 2019-04-01 | 아디맵 엘엘씨 | 항체 라이브러리 |
US9567386B2 (en) | 2010-08-17 | 2017-02-14 | Ambrx, Inc. | Therapeutic uses of modified relaxin polypeptides |
MA34521B1 (fr) | 2010-08-17 | 2013-09-02 | Ambrx Inc | Polypeptides de relaxine modifiés et leurs utilisations |
AR083006A1 (es) | 2010-09-23 | 2013-01-23 | Lilly Co Eli | Formulaciones para el factor estimulante de colonias de granulocitos (g-csf) bovino y variantes de las mismas |
EP2654794B8 (en) | 2010-12-22 | 2020-04-22 | Baxalta GmbH | Materials and methods for conjugating a water soluble fatty acid derivative to a protein |
WO2012130834A1 (en) | 2011-03-30 | 2012-10-04 | Boehringer Ingelheim International Gmbh | Anticoagulant antidotes |
EP2699597B1 (en) | 2011-04-21 | 2016-06-01 | Garvan Institute of Medical Research | Modified variable domain molecules and methods for producing and using them b |
EP2714198A1 (en) | 2011-05-31 | 2014-04-09 | Novo Nordisk A/S | Il-21 epitope and il-21 ligands |
EP3424953B1 (en) | 2011-06-06 | 2020-08-05 | Novo Nordisk A/S | Therapeutic antibodies |
KR102047248B1 (ko) | 2011-06-17 | 2019-11-21 | 노보 노르디스크 에이/에스 | 침식성 세포의 선택적 제거 |
KR20140054009A (ko) | 2011-07-01 | 2014-05-08 | 바이엘 인텔렉쳐 프로퍼티 게엠베하 | 릴랙신 융합 폴리펩타이드 및 그의 용도 |
HUE029855T2 (en) | 2011-07-05 | 2017-04-28 | Bioasis Technologies Inc | p97 antibody conjugates |
WO2013011059A1 (en) | 2011-07-18 | 2013-01-24 | Novo Nordisk A/S | Antagonist antibodies against oscar |
WO2013011063A1 (en) | 2011-07-18 | 2013-01-24 | Novo Nordisk A/S | Antagonistic antibodies against oscar |
WO2013011062A2 (en) | 2011-07-18 | 2013-01-24 | Novo Nordisk A/S | Oscar antagonists |
WO2013011061A1 (en) | 2011-07-18 | 2013-01-24 | Novo Nordisk A/S | Antagonistic antibodies against oscar |
CA2858806A1 (en) | 2011-12-23 | 2013-06-27 | Innate Pharma | Enzymatic conjugation of polypeptides |
US9550830B2 (en) | 2012-02-15 | 2017-01-24 | Novo Nordisk A/S | Antibodies that bind and block triggering receptor expressed on myeloid cells-1 (TREM-1) |
EP2814842B1 (en) | 2012-02-15 | 2018-08-22 | Novo Nordisk A/S | Antibodies that bind peptidoglycan recognition protein 1 |
US9000127B2 (en) | 2012-02-15 | 2015-04-07 | Novo Nordisk A/S | Antibodies that bind and block triggering receptor expressed on myeloid cells-1 (TREM-1) |
WO2013182660A1 (en) | 2012-06-06 | 2013-12-12 | Bionor Immuno As | Hiv vaccine |
US9738724B2 (en) | 2012-06-08 | 2017-08-22 | Sutro Biopharma, Inc. | Antibodies comprising site-specific non-natural amino acid residues, methods of their preparation and methods of their use |
WO2014004639A1 (en) | 2012-06-26 | 2014-01-03 | Sutro Biopharma, Inc. | Modified fc proteins comprising site-specific non-natural amino acid residues, conjugates of the same, methods of their preparation and methods of their use |
WO2014006230A1 (en) | 2012-07-06 | 2014-01-09 | Novo Nordisk A/S | Il-20 epitopes and il-20 ligands |
EP2872894B1 (en) | 2012-07-13 | 2019-04-17 | Innate Pharma | Screening of conjugated antibodies |
CA2880162C (en) | 2012-07-31 | 2023-04-04 | Bioasis Technologies, Inc. | Dephosphorylated lysosomal storage disease proteins and methods of use thereof |
US20150202287A1 (en) | 2012-08-30 | 2015-07-23 | Merrimack Pharmaceuticals, Inc. | Combination therapies comprising anti-erbb3 agents |
WO2014036492A1 (en) | 2012-08-31 | 2014-03-06 | Sutro Biopharma, Inc. | Modified amino acids comprising an azido group |
WO2014072482A1 (en) | 2012-11-09 | 2014-05-15 | Innate Pharma | Recognition tags for tgase-mediated conjugation |
EP2916835A4 (en) | 2012-11-12 | 2016-07-27 | Redwood Bioscience Inc | COMPOUNDS AND METHOD FOR PRODUCING A CONJUGATE |
US9310374B2 (en) | 2012-11-16 | 2016-04-12 | Redwood Bioscience, Inc. | Hydrazinyl-indole compounds and methods for producing a conjugate |
EP2920148B1 (en) | 2012-11-16 | 2019-06-12 | The Regents of the University of California | Pictet-spengler ligation for protein chemical modification |
EP2762496A1 (en) | 2013-02-05 | 2014-08-06 | EngMab AG | Method for the selection of antibodies against BCMA |
ES2829499T3 (es) | 2013-02-05 | 2021-06-01 | Engmab Sarl | Método para la selección de anticuerpos contra BCMA |
US9364567B2 (en) | 2013-03-13 | 2016-06-14 | Bioasis Technologies, Inc. | Fragments of p97 and uses thereof |
WO2014140300A1 (en) | 2013-03-15 | 2014-09-18 | Innate Pharma | Solid phase tgase-mediated conjugation of antibodies |
US9896513B2 (en) | 2013-03-15 | 2018-02-20 | Novo Nordisk A/S | Antibodies capable of specifically binding two epitopes on tissue factor pathway inhibitor |
EP2789630A1 (en) | 2013-04-09 | 2014-10-15 | EngMab AG | Bispecific antibodies against CD3e and ROR1 |
EP3010547B1 (en) | 2013-06-20 | 2021-04-21 | Innate Pharma | Enzymatic conjugation of polypeptides |
KR20160042871A (ko) | 2013-06-21 | 2016-04-20 | 이나뜨 파르마, 에스.아. | 폴리펩티드의 효소적 콘쥬게이션 |
WO2015006555A2 (en) | 2013-07-10 | 2015-01-15 | Sutro Biopharma, Inc. | Antibodies comprising multiple site-specific non-natural amino acid residues, methods of their preparation and methods of their use |
WO2015007337A1 (en) | 2013-07-19 | 2015-01-22 | Bionor Immuno As | Method for the vaccination against hiv |
US20150093399A1 (en) | 2013-08-28 | 2015-04-02 | Bioasis Technologies, Inc. | Cns-targeted conjugates having modified fc regions and methods of use thereof |
WO2015054658A1 (en) | 2013-10-11 | 2015-04-16 | Sutro Biopharma, Inc. | Modified amino acids comprising tetrazine functional groups, methods of preparation, and methods of their use |
JP6747971B2 (ja) | 2013-10-15 | 2020-08-26 | シアトル ジェネティックス, インコーポレイテッド | 改善されたリガンド−薬物コンジュゲート薬物動態のためのpeg化薬物−リンカー |
WO2015067755A2 (en) | 2013-11-07 | 2015-05-14 | Novo Nordisk A/S | Novel methods and antibodies for treating coagulapathy |
CA2927806C (en) | 2013-11-27 | 2023-01-10 | Redwood Bioscience, Inc. | Hydrazinyl-pyrrolo compounds and methods for producing a conjugate |
JOP20200094A1 (ar) | 2014-01-24 | 2017-06-16 | Dana Farber Cancer Inst Inc | جزيئات جسم مضاد لـ pd-1 واستخداماتها |
JOP20200096A1 (ar) | 2014-01-31 | 2017-06-16 | Children’S Medical Center Corp | جزيئات جسم مضاد لـ tim-3 واستخداماتها |
MX370138B (es) | 2014-02-26 | 2019-12-03 | Univ Texas | Liberación de protones de nitrobenzaldehído para la manipulación de la acidosis celular. |
MX2016011993A (es) | 2014-03-14 | 2016-12-09 | Novartis Ag | Moleculas de anticuerpo que se unen a lag-3 y usos de las mismas. |
ES2939760T3 (es) | 2014-03-15 | 2023-04-26 | Novartis Ag | Tratamiento de cáncer utilizando un receptor quimérico para antígenos |
AU2015231170B2 (en) | 2014-03-20 | 2019-10-03 | Bristol-Myers Squibb Company | Serum albumin-binding fibronectin type III domains |
EP3161002A1 (en) | 2014-06-27 | 2017-05-03 | Innate Pharma | MULTISPECIFIC NKp46 BINDING PROTEINS |
AU2015279321B2 (en) | 2014-06-27 | 2021-03-04 | Innate Pharma, S.A. | Multispecific antigen binding proteins |
US10179814B2 (en) | 2014-07-17 | 2019-01-15 | Novo Nordisk A/S | Site directed mutagenesis of TREM-1 antibodies for decreasing viscosity |
EP3026061A1 (en) | 2014-11-26 | 2016-06-01 | Novo Nordisk A/S | Site directed mutagenesis of trem-1 antibodies for decreasing viscosity. |
EP2975056A1 (en) | 2014-07-17 | 2016-01-20 | Novo Nordisk A/S | Site directed mutagenesis of TREM-1 antibodies for decreasing viscosity |
BR112017001183A2 (pt) | 2014-07-21 | 2017-11-28 | Novartis Ag | tratamento de câncer usando receptor de antígeno quimérico anti-bcma humanizado |
KR102594343B1 (ko) | 2014-07-21 | 2023-10-26 | 노파르티스 아게 | Cd33 키메라 항원 수용체를 사용한 암의 치료 |
JP2017528433A (ja) | 2014-07-21 | 2017-09-28 | ノバルティス アーゲー | 低い免疫増強用量のmTOR阻害剤とCARの組み合わせ |
WO2016014553A1 (en) | 2014-07-21 | 2016-01-28 | Novartis Ag | Sortase synthesized chimeric antigen receptors |
ES2781175T3 (es) | 2014-07-31 | 2020-08-31 | Novartis Ag | Subconjunto optimizado de células T que contienen un receptor de antígeno quimérico |
CA2958200A1 (en) | 2014-08-14 | 2016-02-18 | Novartis Ag | Treatment of cancer using a gfr alpha-4 chimeric antigen receptor |
CN107108744B (zh) | 2014-08-19 | 2020-09-25 | 诺华股份有限公司 | 抗cd123嵌合抗原受体(car)用于癌症治疗 |
BR112017005390A2 (pt) | 2014-09-17 | 2017-12-12 | Novartis Ag | células citotóxicas alvo com receptores quiméricos para imunoterapia adotiva |
US11952421B2 (en) | 2014-10-09 | 2024-04-09 | Bristol-Myers Squibb Company | Bispecific antibodies against CD3EPSILON and ROR1 |
EP4245376A3 (en) | 2014-10-14 | 2023-12-13 | Novartis AG | Antibody molecules to pd-l1 and uses thereof |
LT3412302T (lt) | 2014-10-24 | 2021-07-26 | Bristol-Myers Squibb Company | Modifikuoti fgf-21 polipeptidai ir jų panaudojimai |
WO2016090034A2 (en) | 2014-12-03 | 2016-06-09 | Novartis Ag | Methods for b cell preconditioning in car therapy |
JP2018502084A (ja) | 2014-12-23 | 2018-01-25 | アンスティチュ ナショナル ドゥ ラ サンテ エ ドゥ ラ ルシェルシュ メディカル | ベータ細胞への変換と組み合わせられたアルファ細胞の再生 |
WO2016164731A2 (en) | 2015-04-08 | 2016-10-13 | Novartis Ag | Cd20 therapies, cd22 therapies, and combination therapies with a cd19 chimeric antigen receptor (car) - expressing cell |
WO2016172583A1 (en) | 2015-04-23 | 2016-10-27 | Novartis Ag | Treatment of cancer using chimeric antigen receptor and protein kinase a blocker |
CA2990511A1 (en) | 2015-06-23 | 2016-12-29 | Innate Pharma | Multispecific antigen binding proteins |
EP3313881A1 (en) | 2015-06-23 | 2018-05-02 | Innate Pharma | Multispecific nk engager proteins |
WO2017019897A1 (en) | 2015-07-29 | 2017-02-02 | Novartis Ag | Combination therapies comprising antibody molecules to tim-3 |
DK3317301T3 (da) | 2015-07-29 | 2021-06-28 | Immutep Sas | Kombinationsterapier omfattende antistofmolekyler mod lag-3 |
EA036975B1 (ru) | 2015-08-03 | 2021-01-21 | Энгмаб Сарл | Моноклональные антитела против bcma |
EP3708580B1 (en) | 2015-09-23 | 2023-11-01 | Bristol-Myers Squibb Company | Fast-off rate serum albumin binding fibronectin type iii domains |
US11793880B2 (en) | 2015-12-04 | 2023-10-24 | Seagen Inc. | Conjugates of quaternized tubulysin compounds |
MX2018006218A (es) | 2015-12-04 | 2018-09-05 | Seattle Genetics Inc | Conjugados de compuestos de tubulisina cuaternizada. |
WO2017106810A2 (en) | 2015-12-17 | 2017-06-22 | Novartis Ag | Combination of c-met inhibitor with antibody molecule to pd-1 and uses thereof |
MX2018007423A (es) | 2015-12-17 | 2018-11-09 | Novartis Ag | Moleculas de anticuerpo que se unen a pd-1 y usos de las mismas. |
EP3851457A1 (en) | 2016-01-21 | 2021-07-21 | Novartis AG | Multispecific molecules targeting cll-1 |
CN109153714A (zh) | 2016-03-04 | 2019-01-04 | 诺华股份有限公司 | 表达多重嵌合抗原受体(car)分子的细胞及其用途 |
US11549099B2 (en) | 2016-03-23 | 2023-01-10 | Novartis Ag | Cell secreted minibodies and uses thereof |
EA201892040A1 (ru) | 2016-03-25 | 2019-04-30 | Сиэтл Дженетикс, Инк. | Способ получения пегилированных соединений лекарственный препарат - линкер и их промежуточных соединений |
CA3021027A1 (en) | 2016-04-15 | 2017-10-19 | Novartis Ag | Compositions and methods for selective expression of chimeric antigen receptors |
KR20220103806A (ko) | 2016-05-18 | 2022-07-22 | 베링거 인겔하임 인터내셔날 게엠베하 | 암 치료용 항-pd1 및 항-lag3 항체 |
EP3463449A1 (en) | 2016-05-27 | 2019-04-10 | ALK-Abelló A/S | Immunogenic proteins and fragments thereof from allergenic mites |
US20210177896A1 (en) | 2016-06-02 | 2021-06-17 | Novartis Ag | Therapeutic regimens for chimeric antigen receptor (car)- expressing cells |
EP4269562A3 (en) | 2016-07-12 | 2023-12-27 | Kite Pharma, Inc. | Antigen binding molecules and methods of use thereof |
JP7219376B2 (ja) | 2016-07-15 | 2023-02-08 | ノバルティス アーゲー | キメラ抗原受容体をキナーゼ阻害薬と併用して使用したサイトカイン放出症候群の治療及び予防 |
KR20190034588A (ko) | 2016-07-28 | 2019-04-02 | 노파르티스 아게 | 키메라 항원 수용체 및 pd-1 억제제의 조합 요법 |
EP3490590A2 (en) | 2016-08-01 | 2019-06-05 | Novartis AG | Treatment of cancer using a chimeric antigen receptor in combination with an inhibitor of a pro-m2 macrophage molecule |
BR112019006781A2 (pt) | 2016-10-07 | 2019-07-30 | Novartis Ag | receptores de antígeno quiméricos para o tratamento de câncer |
BR112019008426A2 (pt) | 2016-11-02 | 2019-09-03 | Engmab Sarl | anticorpo biespecífico contra bcma e cd3 e um fármaco imunológico para uso combinado no tratamento de mieloma múltiplo |
US11135307B2 (en) | 2016-11-23 | 2021-10-05 | Mersana Therapeutics, Inc. | Peptide-containing linkers for antibody-drug conjugates |
US11129906B1 (en) | 2016-12-07 | 2021-09-28 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
EP3360898A1 (en) | 2017-02-14 | 2018-08-15 | Boehringer Ingelheim International GmbH | Bispecific anti-tnf-related apoptosis-inducing ligand receptor 2 and anti-cadherin 17 binding molecules for the treatment of cancer |
US20190322767A1 (en) | 2016-12-23 | 2019-10-24 | Innate Pharma | Heterodimeric antigen binding proteins |
US11535662B2 (en) | 2017-01-26 | 2022-12-27 | Novartis Ag | CD28 compositions and methods for chimeric antigen receptor therapy |
SG11201907209QA (en) | 2017-02-08 | 2019-09-27 | Bristol Myers Squibb Co | Modified relaxin polypeptides comprising a pharmacokinetic enhancer and uses thereof |
WO2018160731A1 (en) | 2017-02-28 | 2018-09-07 | Novartis Ag | Shp inhibitor compositions and uses for chimeric antigen receptor therapy |
JP2020512312A (ja) | 2017-03-24 | 2020-04-23 | シアトル ジェネティックス, インコーポレイテッド | グルクロニド薬物−リンカーの調製のためのプロセスおよびその中間体 |
WO2018201056A1 (en) | 2017-04-28 | 2018-11-01 | Novartis Ag | Cells expressing a bcma-targeting chimeric antigen receptor, and combination therapy with a gamma secretase inhibitor |
US20200179511A1 (en) | 2017-04-28 | 2020-06-11 | Novartis Ag | Bcma-targeting agent, and combination therapy with a gamma secretase inhibitor |
AU2018290237A1 (en) | 2017-06-22 | 2020-01-16 | Novartis Ag | Antibody molecules to CD73 and uses thereof |
CA3066747A1 (en) | 2017-06-27 | 2019-01-03 | Novartis Ag | Dosage regimens for anti-tim-3 antibodies and uses thereof |
CA3069438A1 (en) | 2017-07-11 | 2019-01-17 | Compass Therapeutics Llc | Agonist antibodies that bind human cd137 and uses thereof |
CN111163798A (zh) | 2017-07-20 | 2020-05-15 | 诺华股份有限公司 | 用于抗lag-3抗体的给药方案及其用途 |
WO2019089753A2 (en) | 2017-10-31 | 2019-05-09 | Compass Therapeutics Llc | Cd137 antibodies and pd-1 antagonists and uses thereof |
US20200277378A1 (en) | 2017-11-16 | 2020-09-03 | Novartis Ag | Combination therapies |
EP3713961A2 (en) | 2017-11-20 | 2020-09-30 | Compass Therapeutics LLC | Cd137 antibodies and tumor antigen-targeting antibodies and uses thereof |
EP3713959A1 (en) | 2017-11-21 | 2020-09-30 | Innate Pharma | Multispecific antigen binding proteins |
EP3732254A4 (en) | 2017-12-26 | 2021-12-22 | Becton, Dickinson and Company | DEEP UV-EXCITABLE WATER-SOLVATIZED POLYMER DYES |
CA3090249A1 (en) | 2018-01-31 | 2019-08-08 | Novartis Ag | Combination therapy using a chimeric antigen receptor |
US10844228B2 (en) | 2018-03-30 | 2020-11-24 | Becton, Dickinson And Company | Water-soluble polymeric dyes having pendant chromophores |
US11155618B2 (en) | 2018-04-02 | 2021-10-26 | Bristol-Myers Squibb Company | Anti-TREM-1 antibodies and uses thereof |
US20210147547A1 (en) | 2018-04-13 | 2021-05-20 | Novartis Ag | Dosage Regimens For Anti-Pd-L1 Antibodies And Uses Thereof |
EP3784351A1 (en) | 2018-04-27 | 2021-03-03 | Novartis AG | Car t cell therapies with enhanced efficacy |
EP3569618A1 (en) | 2018-05-19 | 2019-11-20 | Boehringer Ingelheim International GmbH | Antagonizing cd73 antibody |
WO2019226658A1 (en) | 2018-05-21 | 2019-11-28 | Compass Therapeutics Llc | Multispecific antigen-binding compositions and methods of use |
TW202003580A (zh) | 2018-05-21 | 2020-01-16 | 美商坎伯斯治療有限責任公司 | 用於增強nk細胞對標靶細胞之殺死之組合物及方法 |
EP3801769A1 (en) | 2018-05-25 | 2021-04-14 | Novartis AG | Combination therapy with chimeric antigen receptor (car) therapies |
WO2019232244A2 (en) | 2018-05-31 | 2019-12-05 | Novartis Ag | Antibody molecules to cd73 and uses thereof |
BR112020025048A2 (pt) | 2018-06-13 | 2021-04-06 | Novartis Ag | Receptores de antígeno quimérico de bcma e usos dos mesmos |
MX2020013798A (es) | 2018-06-19 | 2021-08-11 | Atarga Llc | Moléculas de anticuerpo de componente de complemento 5 y sus usos. |
AR116109A1 (es) | 2018-07-10 | 2021-03-31 | Novartis Ag | Derivados de 3-(5-amino-1-oxoisoindolin-2-il)piperidina-2,6-diona y usos de los mismos |
CA3107332A1 (en) | 2018-07-22 | 2020-01-30 | Bioasis Technologies Inc. | Treatment of lymphatic metastases |
WO2020021465A1 (en) | 2018-07-25 | 2020-01-30 | Advanced Accelerator Applications (Italy) S.R.L. | Method of treatment of neuroendocrine tumors |
SG11202102427XA (en) | 2018-09-11 | 2021-04-29 | Ambrx Inc | Interleukin-2 polypeptide conjugates and their uses |
JP2022512746A (ja) | 2018-10-19 | 2022-02-07 | アンブルックス,インコーポレイテッド | インターロイキン-10ポリペプチド複合体、その二量体、およびそれらの使用 |
GB201818477D0 (en) | 2018-11-13 | 2018-12-26 | Emstopa Ltd | Tissue plasminogen activator antibodies and method of use thereof |
AU2019379576A1 (en) | 2018-11-13 | 2021-06-03 | Compass Therapeutics Llc | Multispecific binding constructs against checkpoint molecules and uses thereof |
JP2022514280A (ja) | 2018-12-20 | 2022-02-10 | ノバルティス アーゲー | Mdm2阻害剤のための延長低用量レジメン |
CN113271945A (zh) | 2018-12-20 | 2021-08-17 | 诺华股份有限公司 | 包含3-(1-氧代异吲哚啉-2-基)哌啶-2,6-二酮衍生物的给药方案和药物组合 |
KR20210136014A (ko) | 2019-02-12 | 2021-11-16 | 암브룩스, 인코포레이티드 | 항체-tlr 작용제 콘쥬게이트를 함유하는 조성물, 방법 및 이의 용도 |
WO2020165833A1 (en) | 2019-02-15 | 2020-08-20 | Novartis Ag | 3-(1-oxo-5-(piperidin-4-yl)isoindolin-2-yl)piperidine-2,6-dione derivatives and uses thereof |
JP2022520448A (ja) | 2019-02-15 | 2022-03-30 | ノバルティス アーゲー | 置換3-(1-オキソイソインドリン-2-イル)ピペリジン-2,6-ジオン誘導体及びその使用 |
US10871640B2 (en) | 2019-02-15 | 2020-12-22 | Perkinelmer Cellular Technologies Germany Gmbh | Methods and systems for automated imaging of three-dimensional objects |
WO2020172553A1 (en) | 2019-02-22 | 2020-08-27 | Novartis Ag | Combination therapies of egfrviii chimeric antigen receptors and pd-1 inhibitors |
US20220185876A1 (en) | 2019-03-29 | 2022-06-16 | Atarga, Llc | Anti fgf23 antibody |
US11208477B2 (en) | 2019-04-01 | 2021-12-28 | Novo Nordisk A/S | Antibodies and use thereof |
EP3999541A1 (en) | 2019-07-15 | 2022-05-25 | Bristol-Myers Squibb Company | Antibodies against human trem-1 and uses thereof |
WO2021011678A1 (en) | 2019-07-15 | 2021-01-21 | Bristol-Myers Squibb Company | Anti-trem-1 antibodies and uses thereof |
KR20220077127A (ko) * | 2019-09-06 | 2022-06-08 | 더 리전츠 오브 더 유니버시티 오브 캘리포니아 | 암 치료를 위한 키메라 항원 수용체 및 관련 방법 및 조성물 |
KR20220087498A (ko) | 2019-10-21 | 2022-06-24 | 노파르티스 아게 | Tim-3 억제제 및 그의 용도 |
CA3158298A1 (en) | 2019-10-21 | 2021-04-29 | Novartis Ag | Combination therapies with venetoclax and tim-3 inhibitors |
EP4065158A2 (en) | 2019-11-26 | 2022-10-05 | Novartis AG | Chimeric antigen receptors binding bcma and cd19 and uses thereof |
CA3165399A1 (en) | 2019-12-20 | 2021-06-24 | Novartis Ag | Uses of anti-tgf-beta antibodies and checkpoint inhibitors for the treatment of proliferative diseases |
CN113186185B (zh) * | 2020-01-14 | 2023-05-26 | 东北林业大学 | 一种从哺乳动物粪便中高效富集宿主dna的方法 |
US20210222244A1 (en) | 2020-01-17 | 2021-07-22 | Becton, Dickinson And Company | Methods and compositions for single cell secretomics |
AU2021207348A1 (en) | 2020-01-17 | 2022-08-11 | Novartis Ag | Combination comprising a TIM-3 inhibitor and a hypomethylating agent for use in treating myelodysplastic syndrome or chronic myelomonocytic leukemia |
JP2023515211A (ja) | 2020-02-27 | 2023-04-12 | ノバルティス アーゲー | キメラ抗原受容体発現細胞を作製する方法 |
IL296099A (en) | 2020-03-11 | 2022-11-01 | Ambrx Inc | Interleukin-2 polypeptide conjugates and methods of using them |
US20210355468A1 (en) | 2020-05-18 | 2021-11-18 | Bioasis Technologies, Inc. | Compositions and methods for treating lewy body dementia |
CN116249555A (zh) | 2020-05-19 | 2023-06-09 | 勃林格殷格翰国际有限公司 | 用于癌症治疗的结合分子 |
CA3180556A1 (en) | 2020-05-29 | 2021-12-02 | Stephan Becker | Neutralizing antibodies against sars-related coronavirus |
US20210393787A1 (en) | 2020-06-17 | 2021-12-23 | Bioasis Technologies, Inc. | Compositions and methods for treating frontotemporal dementia |
IL298262A (en) | 2020-06-23 | 2023-01-01 | Novartis Ag | A dosage regimen that includes derivatives of 3-(1-oxoisoindolin-2-yl)piperidine-2,6-dione |
BR112023000482A2 (pt) | 2020-07-16 | 2023-01-31 | Novartis Ag | Anticorpos antibetacelulina, fragmentos dos mesmos e moléculas de ligação multiespecíficas |
WO2022026592A2 (en) | 2020-07-28 | 2022-02-03 | Celltas Bio, Inc. | Antibody molecules to coronavirus and uses thereof |
EP4188549A1 (en) | 2020-08-03 | 2023-06-07 | Novartis AG | Heteroaryl substituted 3-(1-oxoisoindolin-2-yl)piperidine-2,6-dione derivatives and uses thereof |
EP4192876A1 (en) | 2020-08-10 | 2023-06-14 | Innate Pharma | Cell surface mica and micb detection using antibodies |
AU2021327396A1 (en) | 2020-08-20 | 2023-03-23 | Ambrx, Inc. | Antibody-TLR agonist conjugates, methods and uses thereof |
WO2022043557A1 (en) | 2020-08-31 | 2022-03-03 | Advanced Accelerator Applications International Sa | Method of treating psma-expressing cancers |
EP4204020A1 (en) | 2020-08-31 | 2023-07-05 | Advanced Accelerator Applications International S.A. | Method of treating psma-expressing cancers |
JP2023546228A (ja) | 2020-10-21 | 2023-11-01 | ベーリンガー インゲルハイム インターナショナル ゲゼルシャフト ミット ベシュレンクテル ハフツング | 眼の疾患の処置のための二重特異性抗VEGF及び抗TrkB結合分子 |
IL302277A (en) | 2020-10-22 | 2023-06-01 | Janssen Biotech Inc | Proteins containing delta-like ligand antigen binding domains (DLL3) and uses thereof |
JP2023547499A (ja) | 2020-11-06 | 2023-11-10 | ノバルティス アーゲー | 抗体Fc変異体 |
JP2023549504A (ja) | 2020-11-13 | 2023-11-27 | ノバルティス アーゲー | キメラ抗原受容体(car)発現細胞との組合せ療法 |
WO2022162569A1 (en) | 2021-01-29 | 2022-08-04 | Novartis Ag | Dosage regimes for anti-cd73 and anti-entpd2 antibodies and uses thereof |
WO2022182872A2 (en) | 2021-02-24 | 2022-09-01 | Alladapt Immunotherapeutics, Inc. | Compositions and methods for identification of cross-reactive allergenic proteins and treatment of allergies |
CA3214440A1 (en) | 2021-03-26 | 2022-09-29 | Rupesh Nanjunda | Humanized antibodies against paired helical filament tau and uses thereof |
KR20230162013A (ko) | 2021-03-26 | 2023-11-28 | 이나뜨 파르마 에스.에이. | Nk 세포 관여를 위해 사이토카인에 융합된 nkp46-결합 부위, 암 항원 결합 부위를 포함하는 다중특이적 단백질 |
WO2022212899A1 (en) | 2021-04-03 | 2022-10-06 | Ambrx, Inc. | Anti-her2 antibody-drug conjugates and uses thereof |
CN117242093A (zh) | 2021-04-05 | 2023-12-15 | 先天制药公司 | 免疫组织化学方法和kir3dl2特异性试剂 |
TW202304979A (zh) | 2021-04-07 | 2023-02-01 | 瑞士商諾華公司 | 抗TGFβ抗體及其他治療劑用於治療增殖性疾病之用途 |
AR125874A1 (es) | 2021-05-18 | 2023-08-23 | Novartis Ag | Terapias de combinación |
EP4095156A1 (en) | 2021-05-28 | 2022-11-30 | Universität zu Köln | Neutralizing antibodies against hepatitis c virus |
WO2022258662A1 (en) | 2021-06-09 | 2022-12-15 | Innate Pharma | Multispecific proteins binding to nkp46, a cytokine receptor, a tumour antigen and cd16a |
WO2022258678A1 (en) | 2021-06-09 | 2022-12-15 | Innate Pharma | Multispecific proteins binding to nkp30, a cytokine receptor, a tumour antigen and cd16a |
WO2022258691A1 (en) | 2021-06-09 | 2022-12-15 | Innate Pharma | Multispecific proteins binding to nkg2d, a cytokine receptor, a tumour antigen and cd16a |
EP4351733A1 (en) | 2021-06-09 | 2024-04-17 | Innate Pharma | Multispecific antibodies binding to cd20, nkp46, cd16 and conjugated to il-2 |
WO2022263507A1 (en) | 2021-06-17 | 2022-12-22 | Boehringer Ingelheim International Gmbh | Novel tri-specific binding molecules |
WO2023044483A2 (en) | 2021-09-20 | 2023-03-23 | Voyager Therapeutics, Inc. | Compositions and methods for the treatment of her2 positive cancer |
EP4155349A1 (en) | 2021-09-24 | 2023-03-29 | Becton, Dickinson and Company | Water-soluble yellow green absorbing dyes |
WO2023092004A1 (en) | 2021-11-17 | 2023-05-25 | Voyager Therapeutics, Inc. | Compositions and methods for the treatment of tau-related disorders |
WO2023099688A1 (en) | 2021-12-01 | 2023-06-08 | Universität Zu Köln | Neutralizing antibodies against sars-related coronavirus |
EP4190810A1 (en) | 2021-12-01 | 2023-06-07 | Universität zu Köln | Neutralizing antibodies against sars-related coronavirus |
WO2023150778A1 (en) | 2022-02-07 | 2023-08-10 | Visterra, Inc. | Anti-idiotype antibody molecules and uses thereof |
WO2023170291A1 (en) | 2022-03-11 | 2023-09-14 | Janssen Pharmaceutica Nv | Multispecific antibodies and uses thereof |
WO2023170295A1 (en) | 2022-03-11 | 2023-09-14 | Janssen Pharmaceutica Nv | Multispecific antibodies and uses thereof |
WO2023170290A1 (en) | 2022-03-11 | 2023-09-14 | Janssen Pharmaceutica Nv | Multispecific antibodies and uses thereof |
WO2023220695A2 (en) | 2022-05-13 | 2023-11-16 | Voyager Therapeutics, Inc. | Compositions and methods for the treatment of her2 positive cancer |
WO2024007016A2 (en) | 2022-07-01 | 2024-01-04 | Beckman Coulter, Inc. | Novel fluorescent dyes and polymers from dihydrophenanthrene derivatives |
US20240052065A1 (en) | 2022-07-15 | 2024-02-15 | Boehringer Ingelheim International Gmbh | Binding molecules for the treatment of cancer |
WO2024030976A2 (en) | 2022-08-03 | 2024-02-08 | Voyager Therapeutics, Inc. | Compositions and methods for crossing the blood brain barrier |
WO2024044327A1 (en) | 2022-08-26 | 2024-02-29 | Beckman Coulter, Inc. | Dhnt monomers and polymer dyes with modified photophysical properties |
WO2024056861A1 (en) | 2022-09-15 | 2024-03-21 | Avidicure Ip B.V. | Multispecific antigen binding proteins for stimulating nk cells and use thereof |
Family Cites Families (58)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4179337A (en) | 1973-07-20 | 1979-12-18 | Davis Frank F | Non-immunogenic polypeptides |
US5202236A (en) | 1984-09-13 | 1993-04-13 | Enzon Labs Inc. | Method of producing bioadhesive protein |
US5049504A (en) | 1986-11-24 | 1991-09-17 | Genex Corporation | Bioadhesive coding sequences |
US5202256A (en) * | 1984-09-13 | 1993-04-13 | Enzon Labs, Inc. | Bioadhesive precursor protein expression vectors |
US4946778A (en) * | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
US4881175A (en) | 1986-09-02 | 1989-11-14 | Genex Corporation | Computer based system and method for determining and displaying possible chemical structures for converting double- or multiple-chain polypeptides to single-chain polypeptides |
US5869620A (en) * | 1986-09-02 | 1999-02-09 | Enzon, Inc. | Multivalent antigen-binding proteins |
US5260203A (en) | 1986-09-02 | 1993-11-09 | Enzon, Inc. | Single polypeptide chain binding molecules |
US4704692A (en) | 1986-09-02 | 1987-11-03 | Ladner Robert C | Computer based system and method for determining and displaying possible chemical structures for converting double- or multiple-chain polypeptides to single-chain polypeptides |
US5166320A (en) * | 1987-04-22 | 1992-11-24 | University Of Connecticut | Carrier system and method for the introduction of genes into mammalian cells |
US5091513A (en) * | 1987-05-21 | 1992-02-25 | Creative Biomolecules, Inc. | Biosynthetic antibody binding sites |
US5258498A (en) | 1987-05-21 | 1993-11-02 | Creative Biomolecules, Inc. | Polypeptide linkers for production of biosynthetic proteins |
US4904582A (en) * | 1987-06-11 | 1990-02-27 | Synthetic Genetics | Novel amphiphilic nucleic acid conjugates |
US5122614A (en) * | 1989-04-19 | 1992-06-16 | Enzon, Inc. | Active carbonates of polyalkylene oxides for modification of polypeptides |
US5358932A (en) * | 1989-12-29 | 1994-10-25 | Zymogenetics, Inc. | Hybrid protein C |
GB9012995D0 (en) * | 1990-06-11 | 1990-08-01 | Celltech Ltd | Multivalent antigen-binding proteins |
US5766897A (en) * | 1990-06-21 | 1998-06-16 | Incyte Pharmaceuticals, Inc. | Cysteine-pegylated proteins |
CA2101918A1 (en) | 1991-03-18 | 1992-09-19 | Samuel Zalipsky | Hydrazine containing conjugates of polypeptides and glycopolypeptides with polymers |
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 |
US5872222A (en) * | 1991-04-19 | 1999-02-16 | Tanox Biosystems, Inc. | Conjugates of polymers and antibodies specific for T lymphocytes, and their use as adjuvants |
US6787153B1 (en) * | 1991-06-28 | 2004-09-07 | Mitsubishi Chemical Corporation | Human monoclonal antibody specifically binding to surface antigen of cancer cell membrane |
US5981273A (en) | 1991-09-30 | 1999-11-09 | Boehringer Ingelheim Int'l. Gmbh | Composition comprising an endosomolytic agent for introducing nucleic acid complexes into higher eucaryotic cells |
NZ244306A (en) | 1991-09-30 | 1995-07-26 | Boehringer Ingelheim Int | Composition for introducing nucleic acid complexes into eucaryotic cells, complex containing nucleic acid and endosomolytic agent, peptide with endosomolytic domain and nucleic acid binding domain and preparation |
US5521291A (en) | 1991-09-30 | 1996-05-28 | Boehringer Ingelheim International, Gmbh | Conjugates for introducing nucleic acid into higher eucaryotic cells |
US6027725A (en) * | 1991-11-25 | 2000-02-22 | Enzon, Inc. | Multivalent antigen-binding proteins |
EP0617706B1 (en) | 1991-11-25 | 2001-10-17 | Enzon, Inc. | Multivalent antigen-binding proteins |
WO1993016185A2 (en) | 1992-02-06 | 1993-08-19 | Creative Biomolecules, Inc. | Biosynthetic binding protein for cancer marker |
US5714350A (en) | 1992-03-09 | 1998-02-03 | Protein Design Labs, Inc. | Increasing antibody affinity by altering glycosylation in the immunoglobulin variable region |
US6113946A (en) | 1992-04-03 | 2000-09-05 | The Regents Of The University Of California | Self-assembling polynucleotide delivery system comprising dendrimer polycations |
US6329507B1 (en) | 1992-08-21 | 2001-12-11 | The Dow Chemical Company | Dimer and multimer forms of single chain polypeptides |
AU5670194A (en) | 1992-11-20 | 1994-06-22 | Enzon, Inc. | Linker for linked fusion polypeptides |
US5359030A (en) * | 1993-05-10 | 1994-10-25 | Protein Delivery, Inc. | Conjugation-stabilized polypeptide compositions, therapeutic delivery and diagnostic formulations comprising same, and method of making and using the same |
US5880131A (en) | 1993-10-20 | 1999-03-09 | Enzon, Inc. | High molecular weight polymer-based prodrugs |
JPH09504033A (ja) | 1993-10-20 | 1997-04-22 | エンゾン,インコーポレーテッド | 2’−及び/又は7−置換タキソイド類 |
US5443953A (en) * | 1993-12-08 | 1995-08-22 | Immunomedics, Inc. | Preparation and use of immunoconjugates |
US5844107A (en) * | 1994-03-23 | 1998-12-01 | Case Western Reserve University | Compacted nucleic acids and their delivery to cells |
US5656465A (en) | 1994-05-04 | 1997-08-12 | Therion Biologics Corporation | Methods of in vivo gene delivery |
US5730990A (en) * | 1994-06-24 | 1998-03-24 | Enzon, Inc. | Non-antigenic amine derived polymers and polymer conjugates |
US5888773A (en) | 1994-08-17 | 1999-03-30 | The United States Of America As Represented By The Department Of Health And Human Services | Method of producing single-chain Fv molecules |
US5670132A (en) | 1994-09-20 | 1997-09-23 | Immunomedics, Inc. | Modified radioantibody fragments for reduced renal uptake |
US5763733A (en) | 1994-10-13 | 1998-06-09 | Enzon, Inc. | Antigen-binding fusion proteins |
WO1996013599A1 (en) | 1994-11-01 | 1996-05-09 | Winfried Wels | Nucleic acid transfer system |
AU6255096A (en) | 1995-06-07 | 1996-12-30 | Mount Sinai School Of Medicine Of The City University Of New York, The | Pegylated modified proteins |
KR19990063648A (ko) * | 1995-09-21 | 1999-07-26 | 프레드한 아룬디프 에스 | 글루타민산 데카복실라제에 대한 항체와 폴리(에틸렌 글리콜)공액물을 섬세포에 제공하는 방법 |
CN1173878A (zh) | 1995-10-16 | 1998-02-18 | 尤尼利弗公司 | 双功能或双价抗体片段类似物 |
US6090382A (en) * | 1996-02-09 | 2000-07-18 | Basf Aktiengesellschaft | Human antibodies that bind human TNFα |
HU230515B1 (hu) * | 1996-02-09 | 2016-10-28 | Abbvie Biotechnology Ltd | Humán TNFalfa-kötő antitestek alkalmazásai |
GB9625640D0 (en) | 1996-12-10 | 1997-01-29 | Celltech Therapeutics Ltd | Biological products |
AU746819B2 (en) | 1997-02-21 | 2002-05-02 | Genentech Inc. | Antibody fragment-polymer conjugates and humanized anti-IL-8 monoclonal antibodies |
US6025158A (en) | 1997-02-21 | 2000-02-15 | Genentech, Inc. | Nucleic acids encoding humanized anti-IL-8 monoclonal antibodies |
US6117980A (en) * | 1997-02-21 | 2000-09-12 | Genentech, Inc. | Humanized anti-IL-8 monoclonal antibodies |
US5830698A (en) * | 1997-03-14 | 1998-11-03 | Idec Pharmaceuticals Corporation | Method for integrating genes at specific sites in mammalian cells via homologous recombination and vectors for accomplishing the same |
WO1998049198A1 (en) * | 1997-04-30 | 1998-11-05 | Enzon, Inc. | Single-chain antigen-binding proteins capable of glycosylation, production and uses thereof |
GB9812545D0 (en) | 1998-06-10 | 1998-08-05 | Celltech Therapeutics Ltd | Biological products |
US6333396B1 (en) * | 1998-10-20 | 2001-12-25 | Enzon, Inc. | Method for targeted delivery of nucleic acids |
US6908963B2 (en) * | 2001-10-09 | 2005-06-21 | Nektar Therapeutics Al, Corporation | Thioester polymer derivatives and method of modifying the N-terminus of a polypeptide therewith |
DE60236536D1 (de) * | 2001-11-12 | 2010-07-08 | Merck Patent Gmbh | Modifizierter anti-tnf antikörper |
US7101978B2 (en) * | 2003-01-08 | 2006-09-05 | Applied Molecular Evolution | TNF-α binding molecules |
-
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- 1998-04-30 EP EP98920001A patent/EP0979102A4/en not_active Withdrawn
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EP0981548A4 (en) | 2005-11-23 |
US6824782B2 (en) | 2004-11-30 |
US20050008650A1 (en) | 2005-01-13 |
AU7266698A (en) | 1998-11-24 |
JP2010051331A (ja) | 2010-03-11 |
WO1998048837A1 (en) | 1998-11-05 |
CA2288992A1 (en) | 1998-11-05 |
EP0979102A1 (en) | 2000-02-16 |
US7632504B2 (en) | 2009-12-15 |
US20050042680A1 (en) | 2005-02-24 |
JP2002516610A (ja) | 2002-06-04 |
US20020155498A1 (en) | 2002-10-24 |
JP2008115193A (ja) | 2008-05-22 |
WO1998049198A1 (en) | 1998-11-05 |
CA2288992C (en) | 2012-06-12 |
US20020098192A1 (en) | 2002-07-25 |
US6323322B1 (en) | 2001-11-27 |
US6872393B2 (en) | 2005-03-29 |
CA2288994C (en) | 2011-07-05 |
US20020061307A1 (en) | 2002-05-23 |
US20050048064A1 (en) | 2005-03-03 |
JP2002505574A (ja) | 2002-02-19 |
US6743908B2 (en) | 2004-06-01 |
AU7266898A (en) | 1998-11-24 |
WO1998048837A9 (en) | 1999-04-22 |
EP0979102A4 (en) | 2005-11-23 |
US20020161201A1 (en) | 2002-10-31 |
CA2288994A1 (en) | 1998-11-05 |
US6743896B2 (en) | 2004-06-01 |
EP0981548A1 (en) | 2000-03-01 |
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