UA82830C2 - Taci-immunoglobulin fused protein - Google Patents
Taci-immunoglobulin fused protein Download PDFInfo
- Publication number
- UA82830C2 UA82830C2 UA20031110605A UA20031110605A UA82830C2 UA 82830 C2 UA82830 C2 UA 82830C2 UA 20031110605 A UA20031110605 A UA 20031110605A UA 20031110605 A UA20031110605 A UA 20031110605A UA 82830 C2 UA82830 C2 UA 82830C2
- Authority
- UA
- Ukraine
- Prior art keywords
- taci
- immunoglobulin
- amino acid
- fragment
- fusion protein
- Prior art date
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Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- General Chemical & Material Sciences (AREA)
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- Engineering & Computer Science (AREA)
- Immunology (AREA)
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- Molecular Biology (AREA)
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- Mycology (AREA)
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- Microbiology (AREA)
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- Zoology (AREA)
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- Rheumatology (AREA)
- Neurology (AREA)
- Dermatology (AREA)
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Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US29334301P | 2001-05-24 | 2001-05-24 | |
PCT/US2002/015910 WO2002094852A2 (en) | 2001-05-24 | 2002-05-20 | Taci-immunoglobulin fusion proteins |
Publications (1)
Publication Number | Publication Date |
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UA82830C2 true UA82830C2 (en) | 2008-05-26 |
Family
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Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
UA20031110605A UA82830C2 (en) | 2001-05-24 | 2002-05-20 | Taci-immunoglobulin fused protein |
Country Status (28)
Country | Link |
---|---|
US (9) | US20030103986A1 (sh) |
EP (2) | EP1436003B3 (sh) |
JP (2) | JP2004535182A (sh) |
KR (3) | KR100976743B1 (sh) |
CN (2) | CN101628111B (sh) |
AT (2) | ATE542545T1 (sh) |
AU (1) | AU2002305646C1 (sh) |
BR (1) | BRPI0209933B8 (sh) |
CA (1) | CA2448123C (sh) |
CY (2) | CY1109751T1 (sh) |
DE (1) | DE60234202D1 (sh) |
DK (2) | DK2116259T3 (sh) |
EA (2) | EA010594B1 (sh) |
ES (2) | ES2379977T3 (sh) |
HK (2) | HK1076603A1 (sh) |
HR (2) | HRP20030948B1 (sh) |
IL (2) | IL158920A0 (sh) |
ME (1) | MEP21708A (sh) |
MX (1) | MXPA03010687A (sh) |
NO (1) | NO337295B1 (sh) |
NZ (1) | NZ529638A (sh) |
PL (2) | PL403488A1 (sh) |
PT (2) | PT1436003E (sh) |
RS (2) | RS20120253A1 (sh) |
SI (2) | SI1436003T1 (sh) |
UA (1) | UA82830C2 (sh) |
WO (1) | WO2002094852A2 (sh) |
ZA (1) | ZA200308984B (sh) |
Families Citing this family (200)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US8212004B2 (en) | 1999-03-02 | 2012-07-03 | Human Genome Sciences, Inc. | Neutrokine-alpha fusion proteins |
US6812327B1 (en) | 1996-10-25 | 2004-11-02 | Human Genome Sciences, Inc. | Neutrokine-alpha polypeptides |
US7833529B1 (en) * | 1999-01-07 | 2010-11-16 | Zymogenetics, Inc. | Methods for inhibiting B lymphocyte proliferation with soluble ztnf4 receptor |
US6969519B2 (en) | 2000-03-10 | 2005-11-29 | Human Genome Sciences, Inc. | Methods of using an agonistic antibody human tumor necrosis factor receptor (TR17) |
US7879328B2 (en) | 2000-06-16 | 2011-02-01 | Human Genome Sciences, Inc. | Antibodies that immunospecifically bind to B lymphocyte stimulator |
KR101155294B1 (ko) * | 2000-06-16 | 2013-03-07 | 캠브리지 안티바디 테크놀로지 리미티드 | 면역특이적으로 BLyS에 결합하는 항체 |
ATE451390T1 (de) | 2000-08-18 | 2009-12-15 | Dyax Corp | Polypeptide zur bindung an das b-lymphozyten- stimulatorische protein (blys) |
US20030091565A1 (en) | 2000-08-18 | 2003-05-15 | Beltzer James P. | Binding polypeptides and methods based thereon |
ATE542545T1 (de) * | 2001-05-24 | 2012-02-15 | Zymogenetics Inc | Taci-immunoglobulin-fusionsproteine |
CA2446734A1 (en) | 2001-05-24 | 2002-11-28 | Human Genome Sciences, Inc. | Antibodies against tumor necrosis factor delta (april) |
HUP0500992A3 (en) * | 2001-08-03 | 2007-11-28 | Genentech Inc | Tacis and br3 polypeptides and uses thereof |
US7112410B1 (en) | 2001-08-29 | 2006-09-26 | Human Genome Sciences, Inc. | Human tumor necrosis factor TR21 and methods based thereon |
US7256015B2 (en) * | 2001-09-21 | 2007-08-14 | Amgen Inc. | TALL-1 receptor molecules and uses thereof |
EP1495055B1 (en) * | 2002-04-18 | 2013-08-14 | Genencor International, Inc. | Production of functional antibodies in filamentous fungi |
US7262025B2 (en) * | 2002-06-18 | 2007-08-28 | Zymogenetics, Inc. | Hybrid vector having a cytomegalovirus enhancer and myeloproliferative sarcoma virus promoter |
JP2006502715A (ja) * | 2002-10-11 | 2006-01-26 | ザイモジェネティクス,インコーポレイティド | ホモ3量体融合タンパク質の製造 |
BR122018071808B8 (pt) | 2003-11-06 | 2020-06-30 | Seattle Genetics Inc | conjugado |
US7381794B2 (en) | 2004-03-08 | 2008-06-03 | Zymogenetics, Inc. | Dimeric fusion proteins and materials and methods for producing them |
BRPI0510883B8 (pt) | 2004-06-01 | 2021-05-25 | Genentech Inc | composto conjugado de droga e anticorpo, composição farmacêutica, método de fabricação de composto conjugado de droga e anticorpo e usos de uma formulação, de um conjugado de droga e anticorpo e um agente quimioterapêutico e de uma combinação |
ES2426005T3 (es) | 2004-07-23 | 2013-10-18 | Acceleron Pharma Inc. | Polipéptidos del receptor ACTRII, procedimientos y composiciones |
CA2580141C (en) | 2004-09-23 | 2013-12-10 | Genentech, Inc. | Cysteine engineered antibodies and conjugates |
US20100111856A1 (en) | 2004-09-23 | 2010-05-06 | Herman Gill | Zirconium-radiolabeled, cysteine engineered antibody conjugates |
NZ565511A (en) | 2005-07-22 | 2011-03-31 | Five Prime Therapeutics Inc | Compositions and methods of treating disease with FGFR fusion proteins |
AR059025A1 (es) * | 2005-08-09 | 2008-03-12 | Zymogenetics Inc | Metodos para el tratamiento y prevencion de proliferacion de celulas anormales utilizando moleculas de fusion taci |
JP2009507777A (ja) * | 2005-08-09 | 2009-02-26 | ザイモジェネティクス,インコーポレイティド | TACI−Ig融合分子を用いたB細胞性腫瘍の処置方法 |
WO2007019618A1 (en) * | 2005-08-12 | 2007-02-22 | Garvan Institute Of Medical Research | Phrophylactic and/or therapeutic method for treatment of autoimmune disease |
EA015860B1 (ru) | 2005-10-13 | 2011-12-30 | Хьюман Дженом Сайенсиз, Инк. | Способы лечения аутоиммунных заболеваний при использовании антагониста нейтрокина-альфа |
US9168286B2 (en) | 2005-10-13 | 2015-10-27 | Human Genome Sciences, Inc. | Methods and compositions for use in treatment of patients with autoantibody positive disease |
CN105001320A (zh) | 2005-11-23 | 2015-10-28 | 阿塞勒隆制药公司 | Activin-ActRIIa拮抗剂及其促进骨骼生长的应用 |
US8128933B2 (en) | 2005-11-23 | 2012-03-06 | Acceleron Pharma, Inc. | Method of promoting bone growth by an anti-activin B antibody |
CA2629306A1 (en) | 2005-11-23 | 2007-05-31 | Genentech, Inc. | Methods and compositions related to b cell assays |
JP2009525765A (ja) * | 2006-02-10 | 2009-07-16 | ザイモジェネティクス, インコーポレイテッド | 切断型のil−17ra可溶性受容体および炎症において使用する方法 |
WO2007123765A2 (en) | 2006-03-31 | 2007-11-01 | Human Genome Sciences Inc. | Neutrokine-alpha and neutrokine-alpha splice variant |
EA015342B1 (ru) * | 2006-05-15 | 2011-06-30 | Арес Трейдинг С.А. | Способы лечения аутоиммунных заболеваний с использованием слитой молекулы taci-ig |
EP2054441A1 (en) * | 2006-08-25 | 2009-05-06 | Zymogenetics, Inc. | Soluble il-27 receptor |
JP2010501622A (ja) * | 2006-08-28 | 2010-01-21 | アレス トレーディング ソシエテ アノニム | Fc−融合タンパク質の精製法 |
PL2061803T5 (pl) * | 2006-08-28 | 2023-03-27 | Ares Trading S.A. | Proces oczyszczania białek zawierających fc |
CN101541825B (zh) * | 2006-08-28 | 2013-08-14 | 阿雷斯贸易股份有限公司 | Fc融合蛋白的纯化方法 |
BRPI0716382B8 (pt) * | 2006-08-28 | 2021-05-25 | Ares Trading Sa | método para reduzir o teor de porções de fc livres em um fluido compreendendo uma proteína contendo fc, e uso de cromatografia de troca catiônica |
AU2007357448B2 (en) * | 2006-09-18 | 2012-09-06 | Compugen Ltd | Bioactive peptides and method of using same |
US8895016B2 (en) | 2006-12-18 | 2014-11-25 | Acceleron Pharma, Inc. | Antagonists of activin-actriia and uses for increasing red blood cell levels |
EP2121931B1 (en) * | 2007-01-26 | 2011-05-11 | Merck Serono S.A. | Purification of fc-tact fusion proteins using the oilbody technology |
CN101835485B (zh) | 2007-02-01 | 2016-10-26 | 阿塞勒隆制药公司 | 活化素-actriia拮抗剂及在治疗或预防乳腺癌中的用途 |
TW202021980A (zh) | 2007-02-02 | 2020-06-16 | 美商艾瑟勒朗法瑪公司 | 衍生自ActRIIB的變體與其用途 |
ME02333B (me) | 2007-02-09 | 2013-04-30 | Acceleron Pharma Inc | FARMACEUTSKE SMEŠE KOJE SADRŽE AKTIVIN-ActRIIA ANTAGONISTE I NJIHOVA UPOTREBA U PREVENCIJI ILI LEČENJU MULTIPLOG MIJELOMA |
ES2422479T3 (es) * | 2007-03-27 | 2013-09-11 | Zymogenetics Inc | Combinación de inhibición de BLyS y micofenolato de mofetilo para tratamiento de enfermedades autoinmunitarias |
JP2010537623A (ja) * | 2007-03-27 | 2010-12-09 | クリストファー ホーヴェンス | 前立腺癌を治療する方法及び組成物 |
CN101323643B (zh) | 2007-06-15 | 2010-12-01 | 烟台荣昌生物工程有限公司 | 优化的TACI-Fc融合蛋白 |
EP2190469B1 (en) | 2007-09-04 | 2015-02-25 | Compugen Ltd. | Polypeptides and polynucleotides, and uses thereof as a drug target for producing drugs and biologics |
CN101861161B (zh) | 2007-09-18 | 2017-04-19 | 阿塞勒隆制药公司 | 活化素‑actriia拮抗剂和减少或抑制fsh分泌的用途 |
AU2008312406B2 (en) * | 2007-10-16 | 2014-03-06 | Ares Trading S.A. | Combination of BLyS inhibition and anti-CD 20 agents for treatment of autoimmune disease |
PT2219675E (pt) | 2007-11-12 | 2013-11-18 | Ares Trading Sa | Formulações para proteínas de fusão de taci-imunoglobulina |
WO2009062916A1 (en) * | 2007-11-12 | 2009-05-22 | Ares Trading S.A. | Taci-immunoglobulin fusion proteins for treatment of optic neuritis |
EP2219673A1 (en) * | 2007-11-12 | 2010-08-25 | Ares Trading S.A. | Taci-immunoglobulin fusion proteins for treatment of relapsing multiple sclerosis |
ES2572231T3 (es) | 2007-12-07 | 2016-05-30 | Zymogenetics Inc | Anticuerpos monoclonales anti-IL-21 humana |
WO2009093246A2 (en) * | 2008-01-22 | 2009-07-30 | Compugen Ltd. | Novel clusterin derived peptide |
CA2720682A1 (en) | 2008-04-25 | 2009-10-29 | Zymogenetics, Inc. | Levels of bcma protein expression on b cells and use in diagnostic methods |
US8003335B2 (en) | 2008-04-30 | 2011-08-23 | Universite Paris-SUD11 | Levels of APRIL in serum and use in diagnostic methods |
PL2291657T3 (pl) | 2008-05-01 | 2016-09-30 | Stężenie heterotrimerów blys/april w surowicy oraz zastosowanie w sposobach diagnostycznych | |
EP2313105B1 (en) | 2008-06-27 | 2013-07-24 | ZymoGenetics, Inc. | SOLUBLE HYBRID Fc gamma RECEPTORS AND RELATED METHODS |
US8216997B2 (en) | 2008-08-14 | 2012-07-10 | Acceleron Pharma, Inc. | Methods for increasing red blood cell levels and treating anemia using a combination of GDF traps and erythropoietin receptor activators |
TWI748373B (zh) | 2008-08-14 | 2021-12-01 | 美商艾瑟勒朗法瑪公司 | 使用gdf阱以增加紅血球水平 |
EP2343080B1 (en) | 2008-09-30 | 2017-11-08 | Kyowa Hakko Kirin Co., Ltd. | PHARMACEUTICAL COMPOSITION FOR TREATING BONE DISEASES WHICH COMPRISES PROTEIN COMPRISING Frizzled1, Frizzled2 OR Frizzled7 EXTRACELLULAR CYSTEINE-RICH DOMAIN AND Fc PROTEIN |
US20110311450A1 (en) | 2008-12-08 | 2011-12-22 | Zurit Levine | Polypeptides and polynucleotides, and uses thereof as a drug target for producing drugs and biologics |
WO2010096394A2 (en) * | 2009-02-17 | 2010-08-26 | Redwood Biosciences, Inc. | Aldehyde-tagged protein-based drug carriers and methods of use |
US8338377B2 (en) * | 2009-03-30 | 2012-12-25 | Acceleron Pharma Inc. | BMP-ALK3 antagonists and uses for promoting bone growth |
MX2011013172A (es) | 2009-06-08 | 2012-04-02 | Acceleron Pharma Inc | Metodos para aumentar adipocitos termogenicos. |
EP3805259A1 (en) | 2009-06-12 | 2021-04-14 | Acceleron Pharma Inc. | Truncated actriib-fc fusion proteins |
IN2012DN03025A (sh) | 2009-09-09 | 2015-07-31 | Ct Se Llc | |
DK2498799T3 (en) | 2009-11-13 | 2016-12-05 | Five Prime Therapeutics Inc | Use of the FGFR1 ECD proteins for the treatment of cancer diseases characterized by ligand dependent activating mutations in FGFR2 |
EP3332796A1 (en) | 2009-11-17 | 2018-06-13 | Acceleron Pharma Inc. | Actriib proteins and variants and uses therefore relating to utrophin induction for muscular dystrophy therapy |
EP2507265B1 (en) | 2009-12-01 | 2016-05-11 | Compugen Ltd. | Antibody specific for heparanase splice variant T5 and its use. |
WO2011102845A1 (en) * | 2010-02-18 | 2011-08-25 | Transtech Pharma, Inc. | Rage fusion protein compositions and methods of use |
WO2011109280A1 (en) | 2010-03-05 | 2011-09-09 | Lerner Research Institute | Methods and compositions to treat immune-mediated disorders |
US20150231215A1 (en) | 2012-06-22 | 2015-08-20 | Randolph J. Noelle | VISTA Antagonist and Methods of Use |
US10745467B2 (en) | 2010-03-26 | 2020-08-18 | The Trustees Of Dartmouth College | VISTA-Ig for treatment of autoimmune, allergic and inflammatory disorders |
EP2552947A4 (en) | 2010-03-26 | 2013-11-13 | Dartmouth College | VISTA REGULATORY T CELL MEDIATOR PROTEIN, VISTA BINDING ACTIVE SUBSTANCES AND USE THEREOF |
PE20130342A1 (es) | 2010-04-15 | 2013-04-20 | Spirogen Sarl | Pirrolobenzodiacepinas y conjugados de las mismas |
CN101851278B (zh) * | 2010-05-26 | 2013-03-13 | 石药集团中奇制药技术(石家庄)有限公司 | B细胞激活因子拮抗剂及其制备方法与用途 |
RU2626537C2 (ru) | 2010-06-08 | 2017-07-28 | Дженентек, Инк. | Полученные с помощью генной инженерии антитела с цистеиновыми заменами и их конъюгаты |
BR112012031329A2 (pt) | 2010-06-09 | 2016-10-11 | Zymogenetics Inc | proteínas de fusão diméricas vstm3 e composições e métodos relacionados |
US20130189268A1 (en) | 2010-06-22 | 2013-07-25 | Precision Biologics, Inc. | Colon and pancreas cancer specific antigens and antibodies |
WO2016030888A1 (en) | 2014-08-26 | 2016-03-03 | Compugen Ltd. | Polypeptides and uses thereof as a drug for treatment of autoimmune disorders |
WO2012001647A2 (en) | 2010-06-30 | 2012-01-05 | Compugen Ltd. | Polypeptides and uses thereof as a drug for treatment of multiple sclerosis, rheumatoid arthritis and other autoimmune disorders |
ES2719624T3 (es) | 2010-09-23 | 2019-07-11 | Prec Biologics Inc | Peptidomiméticos de cáncer de colon y de páncreas |
US20120258496A1 (en) * | 2010-09-27 | 2012-10-11 | Boehringer Ingelheim International Gmbh | Production of low fucose antibodies in h4-ii-e rat cells |
CN103298832A (zh) | 2010-11-08 | 2013-09-11 | 阿塞勒隆制药公司 | Actriia结合剂及其用途 |
US8481038B2 (en) | 2010-11-15 | 2013-07-09 | Five Prime Therapeutics, Inc. | Treatment of cancer with elevated dosages of soluble FGFR1 fusion proteins |
ES2544608T3 (es) | 2010-11-17 | 2015-09-02 | Genentech, Inc. | Conjugados de anticuerpo y de alaninil-maitansinol |
EP2643016A2 (en) | 2010-11-23 | 2013-10-02 | Alder Biopharmaceuticals, Inc. | Anti-il-6 antibodies for the treatment of anemia |
US8951972B2 (en) | 2010-12-09 | 2015-02-10 | Five Prime Therapeutics, Inc. | FGFR1 extracellular domain combination therapies for lung cancer |
WO2012090150A2 (en) | 2010-12-27 | 2012-07-05 | Compugen Ltd | New cell-penetrating peptides and uses thereof |
JP6162606B2 (ja) | 2011-01-14 | 2017-07-12 | レッドウッド バイオサイエンス, インコーポレイテッド | アルデヒド−タグ付き免疫グロブリンポリペプチド及びその使用方法 |
CN102085367B (zh) * | 2011-01-19 | 2012-08-22 | 烟台荣昌生物工程有限公司 | 优化的TACI-Fc融合蛋白用于制备治疗类风湿性关节炎药物的应用 |
SG194099A1 (en) | 2011-04-15 | 2013-11-29 | Compugen Ltd | Polypeptides and polynucleotides, and uses thereof for treatment of immune related disorders and cancer |
WO2012155019A1 (en) | 2011-05-12 | 2012-11-15 | Genentech, Inc. | Multiple reaction monitoring lc-ms/ms method to detect therapeutic antibodies in animal samples using framework signature pepides |
AU2012260601B2 (en) | 2011-05-25 | 2018-02-01 | Innate Pharma, S.A. | Anti-KIR antibodies for the treatment of inflammatory disorders |
WO2013001517A1 (en) | 2011-06-30 | 2013-01-03 | Compugen Ltd. | Polypeptides and uses thereof for treatment of autoimmune disorders and infection |
EP2750713B1 (en) | 2011-10-14 | 2015-09-16 | Spirogen Sàrl | Pyrrolobenzodiazepines and conjugates thereof |
US10016484B2 (en) | 2011-11-14 | 2018-07-10 | Five Prime Therapeutics, Inc. | Methods of treating lung cancer |
SG2014008304A (en) | 2012-02-01 | 2014-06-27 | Compugen Ltd | C10rf32 antibodies, and uses thereof for treatment of cancer |
WO2013130093A1 (en) | 2012-03-02 | 2013-09-06 | Genentech, Inc. | Biomarkers for treatment with anti-tubulin chemotherapeutic compounds |
WO2013192504A1 (en) | 2012-06-22 | 2013-12-27 | The Trustees Of Dartmouth College | Novel vista-ig constructs and the use of vista-ig for treatment of autoimmune, allergic and inflammatory disorders |
US9890215B2 (en) | 2012-06-22 | 2018-02-13 | King's College London | Vista modulators for diagnosis and treatment of cancer |
CA2884704C (en) | 2012-09-07 | 2023-04-04 | Randolph J. Noelle | Vista modulators for diagnosis and treatment of cancer |
CN105102068B (zh) | 2012-10-12 | 2018-06-01 | Adc疗法责任有限公司 | 吡咯并苯并二氮杂卓-抗体结合物 |
MX364329B (es) | 2012-10-12 | 2019-04-23 | Medimmune Ltd | Conjugados del anticuerpo pirrolobenzodiazepina. |
AU2013328628B2 (en) | 2012-10-12 | 2016-12-15 | Adc Therapeutics Sa | Pyrrolobenzodiazepine-anti-CD22 antibody conjugates |
ES2660029T3 (es) | 2012-10-12 | 2018-03-20 | Medimmune Limited | Conjugados de anticuerpo-pirrolobenzodiazepinas |
PL2906253T3 (pl) | 2012-10-12 | 2019-02-28 | Adc Therapeutics Sa | Koniugaty pirolobenzodiazepina-przeciwciało anty-psma |
KR101819404B1 (ko) | 2012-10-12 | 2018-02-28 | 메디뮨 리미티드 | 피롤로벤조디아제핀 및 그의 컨주게이트 |
EP2906250B1 (en) | 2012-10-12 | 2018-05-30 | ADC Therapeutics SA | Pyrrolobenzodiazepine-anti-psma antibody conjugates |
CA2890217C (en) | 2012-11-02 | 2021-07-20 | Yifu FANG | Activin-actrii antagonists and uses for treating bone and other disorders |
CN103833856B (zh) * | 2012-11-22 | 2017-05-03 | 上海康岱生物医药技术股份有限公司 | 抑制taci‑baff复合物形成的融合蛋白及其制法和用途 |
CN110452242A (zh) | 2012-12-21 | 2019-11-15 | 麦迪穆有限责任公司 | 吡咯并苯并二氮杂卓及其结合物 |
CA2894959C (en) | 2012-12-21 | 2022-01-11 | Spirogen Sarl | Unsymmetrical pyrrolobenzodiazepines-dimers for use in the treatment of proliferative and autoimmune diseases |
JP6444902B2 (ja) | 2013-03-13 | 2018-12-26 | メドイミューン・リミテッドMedImmune Limited | ピロロベンゾジアゼピン及びその結合体 |
BR112015023070B1 (pt) | 2013-03-13 | 2022-06-07 | Genentech, Inc. | Conjugados e compostos de pirrolobenzodiazepinas, composição farmacêutica que compreende os mesmo, bem como seus usos para o tratamento de uma doença proliferativa |
KR102066318B1 (ko) | 2013-03-13 | 2020-01-14 | 메디뮨 리미티드 | 피롤로벤조디아제핀 및 그의 컨쥬게이트 |
BR112016002829A2 (pt) | 2013-08-12 | 2017-09-19 | Genentech Inc | Composto e processo para preparar o composto de conjugado anticorpo-¿droga, composição farmacêutica, método de tratamento do câncer, kit para o tratamento do câncer, intermediário ligante¿-droga, porção e composto de porção droga de dímero cbi |
US9950078B2 (en) | 2013-10-11 | 2018-04-24 | Medimmune Limited | Pyrrolobenzodiazepine-antibody conjugates |
GB201317982D0 (en) | 2013-10-11 | 2013-11-27 | Spirogen Sarl | Pyrrolobenzodiazepines and conjugates thereof |
WO2015052535A1 (en) | 2013-10-11 | 2015-04-16 | Spirogen Sàrl | Pyrrolobenzodiazepine-antibody conjugates |
US10010624B2 (en) | 2013-10-11 | 2018-07-03 | Medimmune Limited | Pyrrolobenzodiazepine-antibody conjugates |
MX371092B (es) | 2013-12-16 | 2020-01-16 | Genentech Inc | Compuestos peptidomimeticos y conjugados de anticuerpo-farmaco de los mismos. |
KR20160092024A (ko) | 2013-12-16 | 2016-08-03 | 제넨테크, 인크. | 1-(클로로메틸)-2,3-디히드로-1H-벤조[e]인돌 이량체 항체-약물 접합체 화합물, 및 사용 및 치료 방법 |
EA201691023A1 (ru) | 2013-12-16 | 2016-10-31 | Дженентек, Инк. | Пептидомиметические соединения и их конъюгаты антитела с лекарственным средством |
US11014987B2 (en) | 2013-12-24 | 2021-05-25 | Janssen Pharmaceutics Nv | Anti-vista antibodies and fragments, uses thereof, and methods of identifying same |
CN106661107B (zh) | 2013-12-24 | 2021-12-24 | 杨森制药公司 | 抗vista抗体及片段 |
WO2015191881A2 (en) | 2014-06-11 | 2015-12-17 | Green Kathy A | Use of vista agonists and antagonists to suppress or enhance humoral immunity |
EP3154566B1 (en) | 2014-06-13 | 2022-08-03 | Acceleron Pharma Inc. | Actrii antagonist for the treatment or prevention of a cutaneous ulcer in a subject that has anemia |
CN106687141A (zh) | 2014-09-10 | 2017-05-17 | 麦迪穆有限责任公司 | 吡咯并苯并二氮杂卓及其缀合物 |
KR20170052600A (ko) | 2014-09-12 | 2017-05-12 | 제넨테크, 인크. | 시스테인 가공된 항체 및 콘주게이트 |
US10149913B2 (en) | 2014-09-12 | 2018-12-11 | Genentech, Inc. | Anthracycline disulfide intermediates, antibody-drug conjugates and methods |
GB201416112D0 (en) | 2014-09-12 | 2014-10-29 | Medimmune Ltd | Pyrrolobenzodiazepines and conjugates thereof |
AU2015317653A1 (en) | 2014-09-17 | 2017-04-06 | Genentech, Inc. | Pyrrolobenzodiazepines and antibody disulfide conjugates thereof |
MA41052A (fr) | 2014-10-09 | 2017-08-15 | Celgene Corp | Traitement d'une maladie cardiovasculaire à l'aide de pièges de ligands d'actrii |
JP6656243B2 (ja) | 2014-10-28 | 2020-03-04 | メルク パテント ゲゼルシャフト ミット ベシュレンクテル ハフツングMerck Patent Gesellschaft mit beschraenkter Haftung | 細胞表面での非共有結合Fcドメイン含有タンパク質ディスプレイの方法及びそのスクリーニング方法 |
EP3215531A1 (en) | 2014-11-03 | 2017-09-13 | Merck Patent GmbH | Methods for generating bispecific shark variable antibody domains and use thereof |
CN107148285B (zh) | 2014-11-25 | 2022-01-04 | Adc治疗股份有限公司 | 吡咯并苯并二氮杂䓬-抗体缀合物 |
EP4233889A3 (en) | 2014-12-03 | 2023-10-11 | Celgene Corporation | Activin-actrii antagonists and uses for treating myelodysplastic syndrome |
CN107206101B (zh) | 2014-12-03 | 2021-06-25 | 基因泰克公司 | 季铵化合物及其抗体-药物缀合物 |
CN107405398A (zh) | 2014-12-05 | 2017-11-28 | 伊穆奈克斯特股份有限公司 | 鉴定vsig8作为推定vista受体及其用以产生vista/vsig8激动剂和拮抗剂的用途 |
GB201506411D0 (en) | 2015-04-15 | 2015-05-27 | Bergenbio As | Humanized anti-axl antibodies |
GB201506402D0 (en) | 2015-04-15 | 2015-05-27 | Berkel Patricius H C Van And Howard Philip W | Site-specific antibody-drug conjugates |
DK3313882T3 (da) | 2015-06-24 | 2020-05-11 | Janssen Pharmaceutica Nv | Anti-VISTA antistoffer og fragmenter |
US11130818B2 (en) | 2015-08-07 | 2021-09-28 | Merck Patent Gmbh | Transglutamine tag for efficient site-specific bioconjugation |
DK3328881T3 (da) | 2015-09-08 | 2019-10-07 | Theripion Inc | Apoa-1 fusionspolypeptider og relaterede sammensætninger og fremgangsmåder |
MA43345A (fr) | 2015-10-02 | 2018-08-08 | Hoffmann La Roche | Conjugués anticorps-médicaments de pyrrolobenzodiazépine et méthodes d'utilisation |
MA43354A (fr) | 2015-10-16 | 2018-08-22 | Genentech Inc | Conjugués médicamenteux à pont disulfure encombré |
MA45326A (fr) | 2015-10-20 | 2018-08-29 | Genentech Inc | Conjugués calichéamicine-anticorps-médicament et procédés d'utilisation |
GB201601431D0 (en) | 2016-01-26 | 2016-03-09 | Medimmune Ltd | Pyrrolobenzodiazepines |
GB201602359D0 (en) | 2016-02-10 | 2016-03-23 | Medimmune Ltd | Pyrrolobenzodiazepine Conjugates |
GB201602356D0 (en) | 2016-02-10 | 2016-03-23 | Medimmune Ltd | Pyrrolobenzodiazepine Conjugates |
CA3014013A1 (en) | 2016-02-12 | 2017-08-17 | Janssen Pharmaceutica Nv | Anti-vista (b7h5) antibodies |
JP6943872B2 (ja) | 2016-03-25 | 2021-10-06 | ジェネンテック, インコーポレイテッド | 多重全抗体及び抗体複合体化薬物定量化アッセイ |
TWI770020B (zh) | 2016-04-15 | 2022-07-11 | 丹麥商H朗德貝克公司 | 人類化抗pacap 抗體及其用途 |
CR20180537A (es) | 2016-04-15 | 2019-03-04 | Immunext Inc | Anticuerpos vista antihumanos y su uso |
WO2017189432A1 (en) | 2016-04-26 | 2017-11-02 | R.P. Scherer Technologies, Llc | Antibody conjugates and methods of making and using the same |
GB201607478D0 (en) | 2016-04-29 | 2016-06-15 | Medimmune Ltd | Pyrrolobenzodiazepine Conjugates |
WO2017201449A1 (en) | 2016-05-20 | 2017-11-23 | Genentech, Inc. | Protac antibody conjugates and methods of use |
CN109313200B (zh) | 2016-05-27 | 2022-10-04 | 豪夫迈·罗氏有限公司 | 用于表征位点特异性抗体-药物缀合物的生物分析性方法 |
US10639378B2 (en) | 2016-06-06 | 2020-05-05 | Genentech, Inc. | Silvestrol antibody-drug conjugates and methods of use |
WO2018027042A1 (en) | 2016-08-03 | 2018-02-08 | Bio-Techne Corporation | Identification of vsig3/vista as a novel immune checkpoint and use thereof for immunotherapy |
WO2018031662A1 (en) | 2016-08-11 | 2018-02-15 | Genentech, Inc. | Pyrrolobenzodiazepine prodrugs and antibody conjugates thereof |
CN110139674B (zh) | 2016-10-05 | 2023-05-16 | 豪夫迈·罗氏有限公司 | 制备抗体药物缀合物的方法 |
GB201617466D0 (en) | 2016-10-14 | 2016-11-30 | Medimmune Ltd | Pyrrolobenzodiazepine conjugates |
WO2018136163A2 (en) | 2016-12-09 | 2018-07-26 | Theripion, Inc. | Tandem apoa-1 fusion polypeptides |
GB201702031D0 (en) | 2017-02-08 | 2017-03-22 | Medlmmune Ltd | Pyrrolobenzodiazepine-antibody conjugates |
PL3544636T3 (pl) | 2017-02-08 | 2021-12-06 | Adc Therapeutics Sa | Koniugaty pirolobenzodiazepina-przeciwciało |
RS63502B1 (sr) | 2017-04-18 | 2022-09-30 | Medimmune Ltd | Konjugati pirolobenzodiazepina |
CA3057748A1 (en) | 2017-04-20 | 2018-10-25 | Adc Therapeutics Sa | Combination therapy with an anti-axl antibody-drug conjugate |
CN117683836A (zh) | 2017-05-09 | 2024-03-12 | 辛利斯生物制药有限责任公司 | 用于修饰微囊藻毒素和节球藻毒素的方法 |
JP7265788B2 (ja) | 2017-05-09 | 2023-04-27 | シアノ バイオテック ゲーエムベーハー | 修飾ミクロシスチンおよびノジュラリン |
US11318211B2 (en) | 2017-06-14 | 2022-05-03 | Adc Therapeutics Sa | Dosage regimes for the administration of an anti-CD19 ADC |
NZ761175A (en) | 2017-08-18 | 2024-07-26 | Medimmune Ltd | Pyrrolobenzodiazepine conjugates |
TW201920192A (zh) | 2017-09-20 | 2019-06-01 | 韓商Ph製藥公司 | 泰蘭他汀(thailanstatin)類似物 |
CN111868082A (zh) | 2018-02-02 | 2020-10-30 | 博奥泰克尼公司 | 调节vista和vsig3的相互作用的化合物及其制备和使用方法 |
GB201803342D0 (en) | 2018-03-01 | 2018-04-18 | Medimmune Ltd | Methods |
GB201806022D0 (en) | 2018-04-12 | 2018-05-30 | Medimmune Ltd | Pyrrolobenzodiazepines and conjugates thereof |
GB201814281D0 (en) | 2018-09-03 | 2018-10-17 | Femtogenix Ltd | Cytotoxic agents |
WO2020086858A1 (en) | 2018-10-24 | 2020-04-30 | Genentech, Inc. | Conjugated chemical inducers of degradation and methods of use |
WO2020123275A1 (en) | 2018-12-10 | 2020-06-18 | Genentech, Inc. | Photocrosslinking peptides for site specific conjugation to fc-containing proteins |
GB201901197D0 (en) | 2019-01-29 | 2019-03-20 | Femtogenix Ltd | G-A Crosslinking cytotoxic agents |
CN114144436A (zh) | 2019-07-24 | 2022-03-04 | H.隆德贝克有限公司 | 抗mGluR5抗体及其用途 |
CA3131790A1 (en) * | 2019-12-24 | 2021-07-01 | Remegen Co., Ltd. | Taci-fc fusion protein and use thereof |
MX2022013998A (es) | 2020-05-08 | 2023-02-16 | Alpine Immune Sciences Inc | Proteinas inmunomoduladoras inhibidoras de april y baff con y sin una proteina inhibidora de celulas t y metodos de uso de las mismas. |
AU2021285813A1 (en) * | 2020-06-02 | 2023-02-02 | Ares Trading S.A. | Methods related to the treatment of IGA nephropathy |
GB2597532A (en) | 2020-07-28 | 2022-02-02 | Femtogenix Ltd | Cytotoxic compounds |
WO2022178090A2 (en) | 2021-02-19 | 2022-08-25 | Theripion, Inc. | Dnase fusion polypeptides and related compositions and methods |
US20240279310A1 (en) | 2021-05-07 | 2024-08-22 | Alpine Immune Sciences, Inc. | Methods of dosing and treatment with a taci-fc fusion immunomodulatory protein |
JP2024518410A (ja) | 2021-05-07 | 2024-05-01 | ビエラ バイオ インコーポレイテッド | 重症筋無力症を治療するための抗cd19抗体の使用 |
EP4296287A1 (en) * | 2021-09-30 | 2023-12-27 | RemeGen Co., Ltd. | Method for treating sjogren's syndrome using taci-fc fusion protein |
WO2023051798A1 (zh) * | 2021-09-30 | 2023-04-06 | 江苏恒瑞医药股份有限公司 | 抗il23抗体融合蛋白及用途 |
EP4442702A1 (en) * | 2022-06-08 | 2024-10-09 | RemeGen Co., Ltd. | Method for treating myasthenia gravis with taci-fc fusion protein |
TW202421653A (zh) * | 2022-09-30 | 2024-06-01 | 大陸商榮昌生物製藥(煙臺)股份有限公司 | 用TACI-Fc融合蛋白治療膜性腎病的方法 |
WO2024077018A2 (en) | 2022-10-04 | 2024-04-11 | Alpine Immune Sciences, Inc. | Methods and uses of taci-fc fusion immunomodulatory protein |
WO2024114777A1 (zh) * | 2022-12-02 | 2024-06-06 | 荣昌生物制药(烟台)股份有限公司 | 用TACI-Fc融合蛋白治疗微小病变型肾病的方法 |
WO2024123675A2 (en) * | 2022-12-05 | 2024-06-13 | Alexion Pharmaceuticals, Inc. | Taci-fc fusion proteins for multifunctional inhibition of baff, april, and neonatal fc receptor |
WO2024138128A2 (en) | 2022-12-23 | 2024-06-27 | Genentech, Inc. | Cereblon degrader conjugates, and uses thereof |
Family Cites Families (73)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US846A (en) | 1838-07-17 | Improvement in revolving fire-arms | ||
US5738A (en) | 1848-08-29 | Francis kelsey | ||
IE54046B1 (en) | 1981-08-25 | 1989-05-24 | Celltech Ltd | Expression vectors |
US4769331A (en) | 1981-09-16 | 1988-09-06 | University Patents, Inc. | Recombinant methods and materials |
US4486533A (en) | 1982-09-02 | 1984-12-04 | St. Louis University | Filamentous fungi functional replicating extrachromosomal element |
US4599311A (en) | 1982-08-13 | 1986-07-08 | Kawasaki Glenn H | Glycolytic promotersfor regulated protein expression: protease inhibitor |
US4977092A (en) | 1985-06-26 | 1990-12-11 | Amgen | Expression of exogenous polypeptides and polypeptide products including hepatitis B surface antigen in yeast cells |
US4603044A (en) | 1983-01-06 | 1986-07-29 | Technology Unlimited, Inc. | Hepatocyte Directed Vesicle delivery system |
US5139936A (en) | 1983-02-28 | 1992-08-18 | Collaborative Research, Inc. | Use of the GAL1 yeast promoter |
US4661454A (en) | 1983-02-28 | 1987-04-28 | Collaborative Research, Inc. | GAL1 yeast promoter linked to non galactokinase gene |
US4870008A (en) | 1983-08-12 | 1989-09-26 | Chiron Corporation | Secretory expression in eukaryotes |
DE3572982D1 (en) | 1984-03-06 | 1989-10-19 | Takeda Chemical Industries Ltd | Chemically modified lymphokine and production thereof |
US4931373A (en) | 1984-05-25 | 1990-06-05 | Zymogenetics, Inc. | Stable DNA constructs for expression of α-1 antitrypsin |
US5288641A (en) | 1984-06-04 | 1994-02-22 | Arch Development Corporation | Herpes Simplex virus as a vector |
US4859587A (en) | 1984-06-04 | 1989-08-22 | Institut Merieux | Recombinant herpes simplex viruses, vaccines and methods |
US4766073A (en) | 1985-02-25 | 1988-08-23 | Zymogenetics Inc. | Expression of biologically active PDGF analogs in eucaryotic cells |
DE3578435D1 (de) | 1984-12-06 | 1990-08-02 | Labofina Sa | Promotoren fuer die expression von fremden genen in hefe, plasmide, die diese promotoren enthalten, sowie deren verwendung zur herstellung von polypeptiden. |
US4751181A (en) | 1984-12-31 | 1988-06-14 | Duke University | Methods and compositions useful in the diagnosis and treatment of autoimmune diseases |
US4882279A (en) | 1985-10-25 | 1989-11-21 | Phillips Petroleum Company | Site selective genomic modification of yeast of the genus pichia |
US4935349A (en) | 1986-01-17 | 1990-06-19 | Zymogenetics, Inc. | Expression of higher eucaryotic genes in aspergillus |
US5063154A (en) | 1987-06-24 | 1991-11-05 | Whitehead Institute For Biomedical Research | Pheromone - inducible yeast promoter |
US5037743A (en) | 1988-08-05 | 1991-08-06 | Zymogenetics, Inc. | BAR1 secretion signal |
US5162228A (en) | 1988-12-28 | 1992-11-10 | Takeda Chemical Industries, Ltd. | Gylceraldehyde-3-phosphate dehydrogenase gene and promoter |
US5399346A (en) | 1989-06-14 | 1995-03-21 | The United States Of America As Represented By The Department Of Health And Human Services | Gene therapy |
US5328688A (en) | 1990-09-10 | 1994-07-12 | Arch Development Corporation | Recombinant herpes simplex viruses vaccines and methods |
US5252714A (en) | 1990-11-28 | 1993-10-12 | The University Of Alabama In Huntsville | Preparation and use of polyethylene glycol propionaldehyde |
JP3202999B2 (ja) | 1991-01-31 | 2001-08-27 | 協和醗酵工業株式会社 | 肝移行性リポソーム製剤 |
US5298418A (en) | 1991-09-16 | 1994-03-29 | Boyce Thompson Institute For Plant Research, Inc. | Cell line isolated from larval midgut tissue of Trichoplusia ni |
US5861151A (en) * | 1991-12-20 | 1999-01-19 | Bristol-Myers Squibb Co | Soluble fusion molecules with binding specificity for cell adhesion molecules |
ZA932523B (en) * | 1992-04-10 | 1994-10-08 | Res Dev Foundation | Immunotoxins directed against cd33 related surface antigens |
ZA932522B (en) * | 1992-04-10 | 1993-12-20 | Res Dev Foundation | Immunotoxins directed against c-erbB-2(HER/neu) related surface antigens |
US5382657A (en) | 1992-08-26 | 1995-01-17 | Hoffmann-La Roche Inc. | Peg-interferon conjugates |
WO1994009137A1 (en) | 1992-10-15 | 1994-04-28 | Genentech, Inc. | Antibodies against type 2 tumor necrosis factor receptor |
US5650550A (en) | 1993-10-01 | 1997-07-22 | The United States Of America As Represented By The Department Of Health And Human Services | Mutant mice having a deficit of functional estrogen receptors |
US5523227A (en) | 1994-06-17 | 1996-06-04 | The Board Of Trustees Of The Leland Stanford Junior Univ. | DNA encoding calcium-signal modulating cyclophilin ligand |
ES2292172T3 (es) | 1994-12-15 | 2008-03-01 | Yeda Research And Development Co., Ltd. | Moduladores de la funcion de los receptores fas/apo1. |
US5731168A (en) | 1995-03-01 | 1998-03-24 | Genentech, Inc. | Method for making heteromultimeric polypeptides |
US5739277A (en) | 1995-04-14 | 1998-04-14 | Genentech Inc. | Altered polypeptides with increased half-life |
DE19533447C1 (de) | 1995-09-09 | 1996-12-05 | Bbs Kraftfahrzeugtechnik | Verfahren und Vorrichtung zum Befüllen eines Gießwerkzeugs mit einer Metallschmelze |
EP0889966A1 (en) | 1995-11-09 | 1999-01-13 | ZymoGenetics, Inc. | Compositions and methods for producing heterologous polypeptides in pichia methanolica |
US5716808A (en) | 1995-11-09 | 1998-02-10 | Zymogenetics, Inc. | Genetic engineering of pichia methanolica |
JP2001501453A (ja) | 1996-03-14 | 2001-02-06 | ヒューマン ジノーム サイエンシーズ,インコーポレイテッド | ヒト腫瘍壊死因子δおよびε |
WO1998002565A1 (en) | 1996-07-17 | 1998-01-22 | Zymogenetics, Inc. | TRANSFORMATION OF $i(PICHIA METHANOLICA) |
IL128072A0 (en) | 1996-07-17 | 1999-11-30 | Zymogenetics Inc | Preparation of pichia methanolica auxotrophic mutants |
US5736383A (en) | 1996-08-26 | 1998-04-07 | Zymogenetics, Inc. | Preparation of Pichia methanolica auxotrophic mutants |
JP2001503263A (ja) | 1996-10-25 | 2001-03-13 | ヒューマン ジノーム サイエンシーズ,インコーポレイテッド | ニュートロカインα |
WO1998027114A2 (en) | 1996-12-17 | 1998-06-25 | Schering Corporation | Mammalian cell surface antigens; related reagents |
US5969102A (en) | 1997-03-03 | 1999-10-19 | St. Jude Children's Research Hospital | Lymphocyte surface receptor that binds CAML, nucleic acids encoding the same and methods of use thereof |
CA2232743A1 (en) | 1997-04-02 | 1998-10-02 | Smithkline Beecham Corporation | A tnf homologue, tl5 |
DE69838061T2 (de) * | 1997-04-18 | 2008-03-13 | Biogen Idec Ma Inc., Cambridge | Typ ii tgf-beta receptor/immunoglobulin konstante domäne fusionsproteine |
AU7608898A (en) | 1997-06-06 | 1998-12-21 | Regeneron Pharmaceuticals, Inc. | Ntn-2 member of tnf ligand family |
JP2002504818A (ja) | 1997-06-06 | 2002-02-12 | リジェネロン ファーマシューティカルズ,インコーポレイテッド | リガンドファミリーのntn−2メンバー |
WO1999004001A1 (en) * | 1997-07-21 | 1999-01-28 | Zymogenetics, Inc. | Tumor necrosis factor receptor ztnfr-5 |
WO1999011791A2 (en) | 1997-09-05 | 1999-03-11 | University Of Washington | Tumor necrosis factor family receptors and ligands, encoding nucleic acids and related binding agents |
TR200000669T2 (tr) | 1997-09-12 | 2000-08-21 | Apotech R & D Sa | Büyüme etkinliğine sahip yeni bir protein-APRIL. |
CZ303272B6 (cs) * | 1999-01-07 | 2012-07-11 | Zymogenetics, Inc. | Farmaceutický prostredek obsahující fúzní protein, izolovaná molekula polynukleotidu, expresní vektor, kultivovaná bunka, zpusob prípravy polypeptidu a izolovaný polypeptid |
US20060067933A1 (en) | 1999-01-07 | 2006-03-30 | Gross Jane A | Soluble receptor BR43x2 and methods of using |
EA006108B1 (ru) | 1999-01-25 | 2005-08-25 | Байоджен, Инк. | Способы стимуляции и ингибирования роста в-клеток, продуцирования иммуноглобулинов и коррекции нарушений, связанных с baff-лигандом, у животного |
WO2000062790A2 (en) | 1999-04-19 | 2000-10-26 | Immunex Corporation | Soluble tumor necrosis factor receptor treatment of medical disorders |
US20030022233A1 (en) | 1999-04-30 | 2003-01-30 | Raymond G. Goodwin | Methods of use of the taci/taci-l interaction |
SK782002A3 (en) * | 1999-07-21 | 2003-08-05 | Lexigen Pharm Corp | FC fusion proteins for enhancing the immunogenicity of protein and peptide antigens |
BR0013391A (pt) | 1999-08-17 | 2002-07-09 | Biogen Inc | Uso do receptor baff (bcma) como um agente imunoregulador |
WO2001021631A2 (en) * | 1999-09-20 | 2001-03-29 | Millennium Pharmaceuticals, Inc. | Secreted proteins and uses thereof |
UA74798C2 (uk) | 1999-10-06 | 2006-02-15 | Байоджен Айдек Ма Інк. | Спосіб лікування раку у ссавця за допомогою поліпептиду, що протидіє взаємодії april з його рецепторами |
DE60028830T2 (de) | 2000-02-16 | 2007-01-18 | Genentech, Inc., South San Francisco | Anti-april antikörper und hybridomazellen |
EP1272647B1 (en) | 2000-04-11 | 2014-11-12 | Genentech, Inc. | Multivalent antibodies and uses therefor |
ES2271004T3 (es) * | 2000-04-27 | 2007-04-16 | Biogen Idec Ma Inc. | Uso de taci como agente antitumoral. |
DE60128216T2 (de) * | 2000-05-12 | 2008-01-10 | Amgen Inc., Thousand Oaks | Polypeptide zum Hemmen der April-vermittelten Proliferation von B- und T- Zellen |
DE60142239D1 (de) | 2000-08-11 | 2010-07-08 | Kyowa Hakko Kirin Co Ltd | DEN PHOSPHORSÄURE-METABOLISMUS, DEN KALZIUM-METABOLISMUS, VERKALKUNG UND DEN VITAMIN D-METABOLISMUS KONTROLLIERENDE POLYPEPTIDE SOWIE FüR DIESE KODIERENDE DNA-MOLEKÜLE |
CA2428242A1 (en) | 2000-11-07 | 2002-05-16 | Zymogenetics, Inc. | Human tumor necrosis factor receptor |
CA2438682A1 (en) * | 2001-02-20 | 2002-08-29 | Zymogenetics, Inc. | Antibodies that bind both bcma and taci |
ATE542545T1 (de) | 2001-05-24 | 2012-02-15 | Zymogenetics Inc | Taci-immunoglobulin-fusionsproteine |
PT2219675E (pt) | 2007-11-12 | 2013-11-18 | Ares Trading Sa | Formulações para proteínas de fusão de taci-imunoglobulina |
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