CN102816241B - 清蛋白融合蛋白 - Google Patents
清蛋白融合蛋白 Download PDFInfo
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- CN102816241B CN102816241B CN201210139189.3A CN201210139189A CN102816241B CN 102816241 B CN102816241 B CN 102816241B CN 201210139189 A CN201210139189 A CN 201210139189A CN 102816241 B CN102816241 B CN 102816241B
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- albumin fusion
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Classifications
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- C—CHEMISTRY; METALLURGY
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- 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
- C07K14/76—Albumins
- C07K14/765—Serum albumin, e.g. HSA
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K19/00—Hybrid peptides, i.e. peptides covalently bound to nucleic acids, or non-covalently bound protein-protein complexes
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- A—HUMAN NECESSITIES
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- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
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- A—HUMAN NECESSITIES
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- A—HUMAN NECESSITIES
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- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P5/00—Drugs for disorders of the endocrine system
-
- 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
- C07K14/76—Albumins
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/62—DNA sequences coding for fusion proteins
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- A—HUMAN NECESSITIES
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- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/31—Fusion polypeptide fusions, other than Fc, for prolonged plasma life, e.g. albumin
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/35—Fusion polypeptide containing a fusion for enhanced stability/folding during expression, e.g. fusions with chaperones or thioredoxin
Landscapes
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Applications Claiming Priority (9)
| Application Number | Priority Date | Filing Date | Title |
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| US54227404P | 2004-02-09 | 2004-02-09 | |
| US60/542,274 | 2004-02-09 | ||
| US54990104P | 2004-03-05 | 2004-03-05 | |
| US60/549,901 | 2004-03-05 | ||
| US55690604P | 2004-03-29 | 2004-03-29 | |
| US60/556,906 | 2004-03-29 | ||
| US63660304P | 2004-12-17 | 2004-12-17 | |
| US60/636,603 | 2004-12-17 | ||
| CN200580012252.5A CN1980687B (zh) | 2004-02-09 | 2005-02-09 | 清蛋白融合蛋白 |
Related Parent Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN200580012252.5A Division CN1980687B (zh) | 2004-02-09 | 2005-02-09 | 清蛋白融合蛋白 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN102816241A CN102816241A (zh) | 2012-12-12 |
| CN102816241B true CN102816241B (zh) | 2015-07-22 |
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Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201210139189.3A Expired - Fee Related CN102816241B (zh) | 2004-02-09 | 2005-02-09 | 清蛋白融合蛋白 |
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| JP (2) | JP5010923B2 (enExample) |
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| PL (1) | PL1729795T3 (enExample) |
| SI (1) | SI1729795T1 (enExample) |
| WO (1) | WO2005077042A2 (enExample) |
Families Citing this family (204)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB9526733D0 (en) | 1995-12-30 | 1996-02-28 | Delta Biotechnology Ltd | Fusion proteins |
| CA2405550A1 (en) | 2000-04-12 | 2001-10-25 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| US20050100991A1 (en) * | 2001-04-12 | 2005-05-12 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| CA2484556A1 (en) | 2001-12-21 | 2003-07-24 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| US20080194481A1 (en) | 2001-12-21 | 2008-08-14 | Human Genome Sciences, Inc. | Albumin Fusion Proteins |
| AU2002364586A1 (en) | 2001-12-21 | 2003-07-30 | Delta Biotechnology Limited | Albumin fusion proteins |
| US20060002935A1 (en) | 2002-06-28 | 2006-01-05 | Domantis Limited | Tumor Necrosis Factor Receptor 1 antagonists and methods of use therefor |
| CA2513213C (en) | 2003-01-22 | 2013-07-30 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| EP1631496B1 (en) * | 2003-04-28 | 2014-02-26 | Medical Instill Technologies, Inc. | Container with valve assembly for filling and dispensing substances, and apparatus and method for filling |
| SI1729795T1 (sl) * | 2004-02-09 | 2016-04-29 | Human Genome Sciences, Inc. | Albuminski fuzijski proteini |
| CN101724071A (zh) | 2004-10-08 | 2010-06-09 | 杜门蒂斯有限公司 | 抗肿瘤坏死因子受体1的单域抗体及其使用方法 |
| KR20080071119A (ko) * | 2005-08-12 | 2008-08-01 | 휴먼 게놈 사이언시즈, 인코포레이티드 | 알부민 융합 단백질 |
| US20090099031A1 (en) * | 2005-09-27 | 2009-04-16 | Stemmer Willem P | Genetic package and uses thereof |
| US20070212703A1 (en) * | 2005-09-27 | 2007-09-13 | Stemmer Willem P | Proteinaceous pharmaceuticals and uses thereof |
| US7846445B2 (en) * | 2005-09-27 | 2010-12-07 | Amunix Operating, Inc. | Methods for production of unstructured recombinant polymers and uses thereof |
| US7855279B2 (en) | 2005-09-27 | 2010-12-21 | Amunix Operating, Inc. | Unstructured recombinant polymers and uses thereof |
| JP2009514900A (ja) * | 2005-11-04 | 2009-04-09 | スミスクライン・ビーチャム・コーポレイション | 血糖降下剤の投与方法 |
| US20080280328A1 (en) * | 2005-11-18 | 2008-11-13 | Novozymes A/S | Glucoamylase Variants |
| EP1816201A1 (en) | 2006-02-06 | 2007-08-08 | CSL Behring GmbH | Modified coagulation factor VIIa with extended half-life |
| WO2007133865A2 (en) | 2006-04-11 | 2007-11-22 | Novartis Ag | Hcv/hiv inhibitors an their uses |
| EP2013113B1 (en) * | 2006-04-24 | 2018-03-21 | Medical Instill Technologies, Inc. | Needle penetrable and resealable lyophilization device and related method |
| EP2046367A4 (en) * | 2006-06-07 | 2009-11-11 | Human Genome Sciences Inc | ALBUM INFUSION PROTEINS |
| JO2945B1 (en) * | 2006-09-13 | 2016-03-15 | سميث كلاين بيتشام كوربوريشن | Methods of giving prolonged hypoglycemic agents |
| AU2007294805A1 (en) * | 2006-09-14 | 2008-03-20 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| WO2008052043A2 (en) * | 2006-10-24 | 2008-05-02 | Cogenesys, Inc. | Opioid receptor agonist fusion proteins |
| CA2670471A1 (en) | 2006-11-22 | 2008-06-05 | Adnexus, A Bristol-Myers Squibb R&D Company (A Delaware Corporation) | Targeted therapeutics based on engineered proteins for tyrosine kinases receptors, including igf-ir |
| CA2915168C (en) | 2007-01-30 | 2017-05-23 | Epivax, Inc. | Regulatory t cell epitopes, compositions and uses thereof |
| WO2008097497A2 (en) | 2007-02-02 | 2008-08-14 | Adnexus, A Bristol-Myers Squibb R & D Company | Vegf pathway blockade |
| KR20100018040A (ko) | 2007-06-06 | 2010-02-16 | 도만티스 리미티드 | 프로테아제 내성 폴리펩티드를 선택하는 방법 |
| RU2361607C2 (ru) * | 2007-06-09 | 2009-07-20 | Государственное образовательное учреждение высшего профессионального образования "Челябинская государственная медицинская академия Федерального агентства по здравоохранению и социальному развитию Российской Федерации" | Способ локальной иммунотерапии гнойно-воспалительных заболеваний мягких тканей челюстно-лицевой области |
| AU2008275911A1 (en) * | 2007-07-19 | 2009-01-22 | Arizona Board of Regents, a body corporate acting for and on behalf of Arizona State University | Self- anchoring MEMS intrafascicular neural electrode |
| BRPI0815416A2 (pt) * | 2007-08-15 | 2014-10-21 | Amunix Inc | Composições e métodos para modificar propriedades de polipeptídeos biologicamente ativos |
| EP2197550A1 (en) * | 2007-09-05 | 2010-06-23 | Sanofi-Aventis | Use of urate oxidase for the treatment or prophylaxis of disorders or indirect sequelae of the heart caused by ischemic or reperfusion events |
| EP2050764A1 (en) | 2007-10-15 | 2009-04-22 | sanofi-aventis | Novel polyvalent bispecific antibody format and uses thereof |
| GB0723712D0 (en) * | 2007-12-04 | 2008-01-16 | Apitope Technology Bristol Ltd | Peptides |
| EP2072527A1 (en) | 2007-12-21 | 2009-06-24 | Altonabiotec AG | Fusion polypeptides comprising a SHBG dimerization component and uses thereof |
| JPWO2009116557A1 (ja) * | 2008-03-21 | 2011-07-21 | 富士フイルム株式会社 | 薬剤含有組成物 |
| EP2799448A1 (en) | 2008-05-22 | 2014-11-05 | Bristol-Myers Squibb Company | Multivalent fibronectin based scaffold domain proteins |
| WO2009144927A1 (ja) * | 2008-05-27 | 2009-12-03 | 富士フイルム株式会社 | 薬剤含有組成物 |
| SMT201700189T1 (it) | 2008-12-10 | 2017-05-08 | Glaxosmithkline Llc | Composizioni farmaceutiche di albiglutide |
| WO2010091122A1 (en) * | 2009-02-03 | 2010-08-12 | Amunix, Inc. | Extended recombinant polypeptides and compositions comprising same |
| US8703717B2 (en) * | 2009-02-03 | 2014-04-22 | Amunix Operating Inc. | Growth hormone polypeptides and methods of making and using same |
| US8680050B2 (en) * | 2009-02-03 | 2014-03-25 | Amunix Operating Inc. | Growth hormone polypeptides fused to extended recombinant polypeptides and methods of making and using same |
| KR101722961B1 (ko) | 2009-02-11 | 2017-04-04 | 알부메딕스 에이/에스 | 알부민 변이체 및 접합체 |
| BRPI1008014A2 (pt) | 2009-02-19 | 2016-10-04 | Glaxo Group Ltd | domínio variável simples, ligante multiespecífico, antagonistas de tnfr1, e de receptor de tnf-alfa, uso do agonista de tnfr, antagonista anti-tnfr1, polipeptídeo ou ligante multiespecífico, método para tratar e/ou prevenir uma condição ou doença, ácido nucleico, vetor, e, hospedeiro |
| WO2010118169A2 (en) * | 2009-04-08 | 2010-10-14 | The Regents Of The University Of California | Human protein scaffold with controlled serum pharmacokinetics |
| US20110182850A1 (en) | 2009-04-10 | 2011-07-28 | Trixi Brandl | Organic compounds and their uses |
| US8512690B2 (en) | 2009-04-10 | 2013-08-20 | Novartis Ag | Derivatised proline containing peptide compounds as protease inhibitors |
| KR101286721B1 (ko) * | 2009-06-05 | 2013-07-16 | 한국과학기술연구원 | 폴리-시스테인 펩티드 융합 재조합 알부민 및 이의 제조방법 |
| AU2010258898B8 (en) * | 2009-06-08 | 2015-02-05 | Amunix Operating Inc. | Glucose-regulating polypeptides and methods of making and using same |
| US9849188B2 (en) | 2009-06-08 | 2017-12-26 | Amunix Operating Inc. | Growth hormone polypeptides and methods of making and using same |
| JP2012532619A (ja) | 2009-07-16 | 2012-12-20 | グラクソ グループ リミテッド | Ｔｎｆｒ１を部分的に阻害するためのアンタゴニスト、用途および方法 |
| AU2010277629B2 (en) | 2009-07-29 | 2016-05-19 | Glaxo Group Limited | Anti - TGF - beta receptor type II single domain antibodies |
| BR112012004094A2 (pt) | 2009-08-24 | 2016-03-08 | Amunix Operating Inc | composições de fator vii de coagulação e métodos para fazer e usar as mesmas |
| EP2493504B1 (en) | 2009-10-27 | 2015-10-07 | Glaxo Group Limited | Stable anti-tnfr1 polypeptides, antibody variable domains and antagonists |
| MX2012004793A (es) | 2009-10-30 | 2012-07-20 | Novozymes Biopharma Dk As | Variantes de albumina. |
| NZ598465A (en) | 2009-10-30 | 2013-10-25 | Boehringer Ingelheim Int | Dosage regimens for hcv combination therapy comprising bi201335, interferon alpha and ribavirin |
| US20120308517A1 (en) | 2010-02-09 | 2012-12-06 | Digna Biotech, S.L. | Compositions for the treatment of infectious and tumoural diseases |
| BR112012019881A2 (pt) | 2010-02-18 | 2017-06-27 | Bristol Myers Squibb Co | proteínas de domínio estrutural baseadas na fibronectina que ligam-se à il-23 |
| WO2011123830A2 (en) | 2010-04-02 | 2011-10-06 | Amunix Operating Inc. | Alpha 1-antitrypsin compositions and methods of making and using same |
| JP5969458B2 (ja) | 2010-04-09 | 2016-08-17 | アルブミディクス アクティーゼルスカブ | アルブミン誘導体及び変異体 |
| EP3424949A1 (en) | 2010-04-13 | 2019-01-09 | Bristol-Myers Squibb Company | Fibronectin based scaffold domain proteins that bind pcsk9 |
| WO2011140176A1 (en) | 2010-05-04 | 2011-11-10 | Glaxosmithkline Llc | Methods for treating or preventing cardiovascular disorders and providing cardiovascular protection |
| JP6200806B2 (ja) * | 2010-05-21 | 2017-09-20 | メリマック ファーマシューティカルズ インコーポレーティッド | 二重特異的融合タンパク質 |
| EP2576615B1 (en) | 2010-05-26 | 2016-03-30 | Bristol-Myers Squibb Company | Fibronectin based scaffold proteins having improved stability |
| CN103096891A (zh) | 2010-06-24 | 2013-05-08 | 判米德有限公司 | 利用羟氯喹或羟氯喹和抗病毒剂的组合治疗丙型肝炎病毒相关疾病 |
| WO2012013597A1 (de) * | 2010-07-28 | 2012-02-02 | Justus-Liebig-Universität Giessen | Stoffe und deren verwendung zur beeinflussung natriuretischer peptidrezeptoren |
| AU2011311880B2 (en) | 2010-10-08 | 2014-07-24 | Novartis Ag | Vitamin E formulations of sulfamide NS3 inhibitors |
| EP2655411A1 (en) | 2010-12-22 | 2013-10-30 | Bristol-Myers Squibb Company | Fibronectin based scaffold domain proteins that bind il-23 |
| MX2013007936A (es) | 2011-01-06 | 2013-08-09 | Glaxo Group Ltd | Ligandos que se unen al receptor ii del factor de crecimiento transformante-beta. |
| JP6043629B2 (ja) * | 2011-01-07 | 2016-12-14 | 中外製薬株式会社 | 抗体の物性を改善させる方法 |
| WO2012115772A2 (en) | 2011-02-25 | 2012-08-30 | Medtronic, Inc. | Therapy for kidney disease and/or heart failure |
| AU2012222833B2 (en) | 2011-03-03 | 2017-03-16 | Zymeworks Inc. | Multivalent heteromultimer scaffold design and constructs |
| CA2830660A1 (en) | 2011-05-05 | 2012-11-08 | Novozymes Biopharma Dk A/S | Albumin variants |
| EP2750697A4 (en) | 2011-09-02 | 2015-03-25 | Medtronic Inc | CHIMERIC NATRIURETIC PEPTIDE COMPOSITIONS AND METHOD FOR THE PRODUCTION THEREOF |
| US9522951B2 (en) | 2011-10-31 | 2016-12-20 | Bristol-Myers Squibb Company | Fibronectin binding domains with reduced immunogenicity |
| US20140315817A1 (en) | 2011-11-18 | 2014-10-23 | Eleven Biotherapeutics, Inc. | Variant serum albumin with improved half-life and other properties |
| LT2822577T (lt) | 2012-02-15 | 2019-03-25 | Bioverativ Therapeutics Inc. | Rekombinantiniai faktoriaus viii baltymai |
| HRP20221531T1 (hr) | 2012-02-15 | 2023-02-17 | Bioverativ Therapeutics Inc. | Pripravci faktora viii i postupci dobivanja i korištenja istih |
| CN107496932A (zh) | 2012-02-27 | 2017-12-22 | 阿穆尼克斯运营公司 | Xten缀合组合物和制造其的方法 |
| US9603897B2 (en) | 2012-03-12 | 2017-03-28 | Massachusetts Institute Of Technology | Methods for treating tissue damage associated with ischemia with apolipoprotein D |
| WO2013137869A1 (en) | 2012-03-14 | 2013-09-19 | Boehringer Ingelheim International Gmbh | Combination therapy for treating hcv infection in an hcv-hiv coinfected patient population |
| DK2825556T3 (en) | 2012-03-16 | 2018-04-16 | Albumedix As | albumin Variants |
| JP2015512900A (ja) | 2012-03-28 | 2015-04-30 | 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 | 特別な患者の遺伝子亜型分集団のｈｃｖ感染症を治療するための併用療法 |
| WO2013177187A2 (en) | 2012-05-22 | 2013-11-28 | Massachusetts Institute Of Technology | Synergistic tumor treatment with extended-pk il-2 and therapeutic agents |
| IN2015DN01115A (enExample) | 2012-07-13 | 2015-06-26 | Zymeworks Inc | |
| EP2888279A1 (en) | 2012-08-22 | 2015-07-01 | Glaxo Group Limited | Anti lrp6 antibodies |
| LT3835310T (lt) | 2012-09-13 | 2024-04-25 | Bristol-Myers Squibb Company | Fibronektino pagrindo karkaso domeno baltymai, kurie rišasi prie miostatino |
| KR20150082422A (ko) | 2012-11-08 | 2015-07-15 | 노보자임스 바이오파마 디케이 에이/에스 | 알부민 변이체 |
| US20140205566A1 (en) | 2012-11-30 | 2014-07-24 | Novartis Ag | Cyclic nucleuoside derivatives and uses thereof |
| EP2951206A2 (en) | 2013-02-01 | 2015-12-09 | Bristol-Myers Squibb Company | Fibronectin based scaffold proteins |
| US9255262B2 (en) * | 2013-03-06 | 2016-02-09 | Vision Global Holdings Ltd. | Albumin-binding arginine deminase and the use thereof |
| US9926570B2 (en) | 2013-03-06 | 2018-03-27 | Glaxosmithkline Llc | Host cells and methods of use |
| USRE48805E1 (en) * | 2013-03-06 | 2021-11-02 | Vision Global Holdings Ltd. | Method for cancer targeting treatment and detection of arginine using albumin-binding arginine deiminase fusion protein |
| WO2014165093A2 (en) | 2013-03-13 | 2014-10-09 | Bristol-Myers Squibb Company | Fibronectin based scaffold domains linked to serum albumin or a moiety binding thereto |
| SI2970464T1 (sl) | 2013-03-15 | 2020-08-31 | Glaxosmithkline Intellectual Propety Development Limited | Anti-LAG-3 vezavni proteini |
| RU2646098C2 (ru) | 2013-04-30 | 2018-03-01 | Интас Фармасьютикалс Лтд | Новый способ клонирования, экспрессии и очистки для получения ранибизумаба |
| WO2015001049A1 (en) | 2013-07-04 | 2015-01-08 | Novartis Ag | O-mannosyltransferase deficient filamentous fungal cells and methods of use thereof |
| WO2015023890A1 (en) * | 2013-08-14 | 2015-02-19 | The Arizona Board Of Regents On Behalf Of The University Of Arizona | Glycosylated pacap/vip analogues with enhanced cns penetration for treatment of neurodegenerative diseases |
| EP3033097B1 (en) | 2013-08-14 | 2021-03-10 | Bioverativ Therapeutics Inc. | Factor viii-xten fusions and uses thereof |
| CN105377882B (zh) * | 2014-03-06 | 2020-05-05 | 葛兰素史密斯克莱有限责任公司 | 宿主细胞和使用方法 |
| WO2015198199A1 (en) | 2014-06-23 | 2015-12-30 | Novartis Ag | Hsa-gdf-15 fusion polypeptide and use thereof. |
| CA2954974A1 (en) | 2014-07-21 | 2016-01-28 | Glykos Finland Oy | Production of glycoproteins with mammalian-like n-glycans in filamentous fungi |
| WO2016025647A1 (en) | 2014-08-12 | 2016-02-18 | Massachusetts Institute Of Technology | Synergistic tumor treatment with il-2, a therapeutic antibody, and a cancer vaccine |
| AU2015301753B2 (en) | 2014-08-12 | 2021-04-08 | Massachusetts Institute Of Technology | Synergistic tumor treatment with IL-2 and integrin-binding-Fc-fusion protein |
| US9616114B1 (en) | 2014-09-18 | 2017-04-11 | David Gordon Bermudes | Modified bacteria having improved pharmacokinetics and tumor colonization enhancing antitumor activity |
| EP3224277B1 (en) | 2014-11-25 | 2020-08-26 | Bristol-Myers Squibb Company | Novel pd-l1 binding polypeptides for imaging |
| CN107207379B (zh) | 2014-11-25 | 2021-08-10 | 百时美施贵宝公司 | 用于生物制品的18f-放射性标记的方法和组合物 |
| WO2016100803A2 (en) | 2014-12-19 | 2016-06-23 | Alexion Pharmaceuticals, Inc. | Methods of treating tissue calcification |
| CR20170482A (es) | 2015-04-24 | 2018-03-07 | Viiv Healthcare Uk No 5 Ltd | Polipéptidos dirigidos a la fusión de vih |
| US10676723B2 (en) | 2015-05-11 | 2020-06-09 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| MX2018001497A (es) | 2015-08-03 | 2018-05-15 | Bioverativ Therapeutics Inc | Proteinas de fusion de factor ix y metodos para producirlas y usarlas. |
| EP3337816B1 (en) | 2015-08-20 | 2024-02-14 | Albumedix Ltd | Albumin variants and conjugates |
| IL319047A (en) | 2015-08-28 | 2025-04-01 | Amunix Operating Inc | Chimeric polypeptide composition and methods for its preparation and use |
| CN108699145A (zh) | 2015-09-02 | 2018-10-23 | 伊缪泰普有限公司 | 抗lag-3抗体 |
| PT3348635T (pt) | 2015-09-08 | 2021-03-15 | Japan Chem Res | Novo mutante de albumina do soro humano |
| KR102443831B1 (ko) * | 2015-09-18 | 2022-09-15 | 고쿠리츠 다이가쿠 호징 미야자키 다이가쿠 | 장시간 작용형 아드레노메둘린 유도체 |
| ES2809125T3 (es) | 2015-09-23 | 2021-03-03 | Bristol Myers Squibb Co | Moléculas de armazón a base de fibronectina de unión a glipicano-3 |
| CN110452295B (zh) * | 2015-11-10 | 2022-10-11 | 孙嘉琳 | 抗肿瘤蛋白内皮抑素的衍生物 |
| WO2017109706A1 (en) | 2015-12-22 | 2017-06-29 | Novartis Ag | Methods of treating or ameliorating metabolic disorders using growth differentiation factor 15 (gdf-15) |
| PL3393496T3 (pl) | 2015-12-23 | 2024-04-22 | The Johns Hopkins University | Długo działający agonista glp-1r jako terapia stanów neurologicznych i neurodegeneracyjnych |
| JP2017165713A (ja) * | 2016-03-14 | 2017-09-21 | Ｊｃｒファーマ株式会社 | 血清アルブミン−２０ｋ成長ホルモン融合タンパク質 |
| WO2017210335A1 (en) | 2016-06-01 | 2017-12-07 | Bristol-Myers Squibb Company | Imaging methods using 18f-radiolabeled biologics |
| EP3471747A1 (en) | 2016-06-16 | 2019-04-24 | Alexion Pharmaceuticals, Inc. | Methods of treating myointimal proliferation |
| WO2018102743A1 (en) | 2016-12-02 | 2018-06-07 | Bioverativ Therapeutics Inc. | Methods of treating hemophilic arthropathy using chimeric clotting factors |
| US11180535B1 (en) | 2016-12-07 | 2021-11-23 | David Gordon Bermudes | Saccharide binding, tumor penetration, and cytotoxic antitumor chimeric peptides from therapeutic bacteria |
| US11129906B1 (en) | 2016-12-07 | 2021-09-28 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| JP2020505438A (ja) | 2017-01-10 | 2020-02-20 | ノダス・セラピューティクスＮｏｄｕｓ Ｔｈｅｒａｐｅｕｔｉｃｓ | インテグリン結合性ポリペプチド−Ｆｃ融合タンパク質および免疫調節物質を用いる併用がん治療法 |
| US10350266B2 (en) | 2017-01-10 | 2019-07-16 | Nodus Therapeutics, Inc. | Method of treating cancer with a multiple integrin binding Fc fusion protein |
| US10767164B2 (en) | 2017-03-30 | 2020-09-08 | The Research Foundation For The State University Of New York | Microenvironments for self-assembly of islet organoids from stem cells differentiation |
| US12134790B2 (en) | 2017-09-27 | 2024-11-05 | Inozyme Pharma, Inc. | Methods of improving cardiovascular function and treating cardiovascular disease using a recombinant ectonucleotide pyrophosphatase phosphodiesterase (NPP1) |
| CN110090295B (zh) * | 2018-01-29 | 2022-12-23 | 武汉康理通科技有限公司 | Ephrin-B1在制备治疗炎症性肠病的药物中的用途 |
| WO2019152827A1 (en) * | 2018-02-02 | 2019-08-08 | AskGene Pharma, Inc. | Novel antibody-drug conjugates (adc), methods of making, and methods of use thereof |
| MX2020008394A (es) | 2018-02-12 | 2020-09-21 | Biontech Rna Pharmaceuticals Gmbh | Tratamiento que usa arn que codifica citoquinas. |
| CN113840832A (zh) | 2018-05-14 | 2021-12-24 | 狼人治疗公司 | 可活化白介素-2多肽及其使用方法 |
| MX2020012252A (es) | 2018-05-14 | 2021-04-28 | Werewolf Therapeutics Inc | Polipeptidos de interleucina 12 activables y metodos de uso de los mismos. |
| RS66972B1 (sr) | 2018-05-18 | 2025-07-31 | Bioverativ Therapeutics Inc | Metode lečenja hemofilije a |
| KR20210022004A (ko) | 2018-06-18 | 2021-03-02 | 안위타 바이오사이언시스, 인코포레이티드 | 항-메소텔린 작제물 및 이의 용도 |
| CA3106858A1 (en) | 2018-07-24 | 2020-01-30 | Biontech Rna Pharmaceuticals Gmbh | Il2 agonists |
| KR20250154552A (ko) | 2018-09-27 | 2025-10-28 | 실리오 디벨럽먼트, 인크. | 마스킹된 사이토카인 폴리펩타이드 |
| AU2019346335B2 (en) | 2018-09-28 | 2024-07-25 | Massachusetts Institute Of Technology | Collagen-localized immunomodulatory molecules and methods thereof |
| US11235032B2 (en) | 2019-01-23 | 2022-02-01 | Massachusetts Institute Of Technology | Combination immunotherapy dosing regimen for immune checkpoint blockade |
| WO2020152367A1 (en) | 2019-01-25 | 2020-07-30 | Ospedale San Raffaele S.R.L. | Inhibitor of dux4 and uses thereof |
| EP3920960B1 (en) | 2019-02-08 | 2024-04-17 | Biontech Cell & Gene Therapies Gmbh | Treatment involving car-engineered t cells and cytokines |
| MX2021011258A (es) | 2019-03-18 | 2021-12-10 | Biontech Cell & Gene Therapies Gmbh | Variantes de interleucina-2 (il2) y receptor de interleucina-2 (il2r) para la activacion especifica de celulas efectoras inmunitarias. |
| WO2020200481A1 (en) | 2019-04-05 | 2020-10-08 | Biontech Rna Pharmaceuticals Gmbh | Treatment involving interleukin-2 (il2) and interferon (ifn) |
| CA3136602A1 (en) | 2019-04-15 | 2020-10-22 | Qwixel Therapeutics Llc | Fusion protein composition(s) comprising targeted masked type i interferons (ifna and ifnb) and an antibody against tumor antigen, for use in the treatment of cancer |
| EP3969035A4 (en) | 2019-05-14 | 2023-06-21 | Werewolf Therapeutics, Inc. | SEPARATION UNITS AND METHODS AND THEIR USE |
| CN111944036B (zh) * | 2019-05-14 | 2024-09-06 | 上海盖浦生物科技有限公司 | 一种增殖免疫细胞的突变体蛋白 |
| TW202115105A (zh) | 2019-06-24 | 2021-04-16 | 德商拜恩迪克Ｒｎａ製藥有限公司 | Ｉｌ２激動劑 |
| EP3990491A1 (en) | 2019-06-26 | 2022-05-04 | Massachusetts Institute of Technology | Immunomodulatory fusion protein-metal hydroxide complexes and methods thereof |
| RU2714392C1 (ru) * | 2019-07-09 | 2020-02-14 | Екатерина Олеговна Кудасова | Способ модификации поверхности метилметакрилата стоматологического протеза низкотемпературной газоразрядной плазмой кислорода низкого давления за счет изменения контактного угла смачивания по воде и свободной поверхностной энергии |
| AU2020329290A1 (en) | 2019-08-13 | 2022-03-24 | Elpis Biopharmaceuticals | Engineered interleukin-2 receptor beta agonists |
| WO2021058091A1 (en) | 2019-09-24 | 2021-04-01 | Biontech Rna Pharmaceuticals Gmbh | Treatment involving therapeutic antibody and interleukin-2 (il2) |
| WO2021097376A1 (en) | 2019-11-14 | 2021-05-20 | Werewolf Therapeutics, Inc. | Activatable cytokine polypeptides and methods of use thereof |
| WO2021129927A1 (en) | 2019-12-23 | 2021-07-01 | Biontech Cell & Gene Therapies Gmbh | Treatment with immune effector cells engineered to express an antigen receptor |
| WO2021129945A1 (en) | 2019-12-27 | 2021-07-01 | Biontech Cell & Gene Therapies Gmbh | In vitro and in vivo gene delivery to immune effector cells using nanoparticles functionalized with designed ankyrin repeat proteins (darpins) |
| CN116568341A (zh) | 2020-02-28 | 2023-08-08 | 百时美施贵宝公司 | 基于纤连蛋白的放射性标记的支架和抗体及其治疗诊断用途 |
| AU2021238582A1 (en) | 2020-03-16 | 2022-09-22 | Biontech Cell & Gene Therapies Gmbh | Antigen-specific T cell receptors and T cell epitopes |
| WO2021197589A1 (en) | 2020-03-31 | 2021-10-07 | BioNTech SE | Treatment involving non-immunogenic rna for antigen vaccination |
| LT4157876T (lt) | 2020-05-26 | 2024-10-25 | Boehringer Ingelheim International Gmbh | Anti-pd-1 antikūnai |
| WO2022030580A1 (ja) * | 2020-08-06 | 2022-02-10 | 国立大学法人宮崎大学 | 長時間作用型新規アドレノメデュリン誘導体、その製造方法及びその医薬用途 |
| KR102467827B1 (ko) * | 2020-08-31 | 2022-11-16 | 연세대학교 산학협력단 | 미생물 에어로졸화 과정 중 발생하는 손상 방지 방법 |
| CN112724259B (zh) * | 2020-11-16 | 2022-12-20 | 天津林达生物科技有限公司 | 人血清白蛋白与白介素2的融合蛋白及其用途 |
| EP4251187A4 (en) | 2020-11-25 | 2025-09-10 | Xilio Dev Inc | TUMOR-SPECIFIC CLASSIBLE LINKERS |
| WO2022135667A1 (en) | 2020-12-21 | 2022-06-30 | BioNTech SE | Therapeutic rna for treating cancer |
| WO2022135666A1 (en) | 2020-12-21 | 2022-06-30 | BioNTech SE | Treatment schedule for cytokine proteins |
| TW202245808A (zh) | 2020-12-21 | 2022-12-01 | 德商拜恩迪克公司 | 用於治療癌症之治療性ｒｎａ |
| CN112753846B (zh) * | 2021-01-27 | 2023-08-29 | 吉林农业大学 | 一种超持水大豆分离蛋白凝胶及其制备方法 |
| CA3215103A1 (en) | 2021-04-12 | 2022-10-20 | Steffen Panzner | Rna compositions comprising a buffer substance and methods for preparing, storing and using the same |
| AU2022260466A1 (en) | 2021-04-20 | 2023-11-02 | BioNTech SE | Virus vaccine |
| CA3218973A1 (en) * | 2021-05-14 | 2022-11-17 | Antlia Bioscience, Inc. | Modified b-type natriuretic peptide |
| EP4347653A1 (en) | 2021-06-04 | 2024-04-10 | Boehringer Ingelheim International GmbH | Anti-sirp-alpha antibodies |
| CN113391067B (zh) * | 2021-06-16 | 2023-07-25 | 军事科学院军事医学研究院军事兽医研究所 | 抗尼帕病毒g蛋白抗体的间接elisa检测方法 |
| WO2023051926A1 (en) | 2021-09-30 | 2023-04-06 | BioNTech SE | Treatment involving non-immunogenic rna for antigen vaccination and pd-1 axis binding antagonists |
| JP2024540949A (ja) | 2021-10-21 | 2024-11-06 | ビオンテック・ソシエタス・エウロパエア | コロナウイルスワクチン |
| AU2022374004A1 (en) | 2021-10-22 | 2024-05-02 | BioNTech SE | Compositions for administration of different doses of rna |
| WO2023083434A1 (en) | 2021-11-09 | 2023-05-19 | BioNTech SE | Rna encoding peptidoglycan hydrolase and use thereof for treating bacterial infection |
| WO2023126053A1 (en) | 2021-12-28 | 2023-07-06 | BioNTech SE | Lipid-based formulations for administration of rna |
| US20250114337A1 (en) * | 2022-01-21 | 2025-04-10 | The Methodist Hospital | Methods for vascular regeneration and wound treatment |
| WO2023165681A1 (en) | 2022-03-01 | 2023-09-07 | BioNTech SE | Rna lipid nanoparticles (lnps) comprising a polyoxazoline and/or polyoxazine polymer |
| WO2023193892A1 (en) | 2022-04-05 | 2023-10-12 | BioNTech SE | Nucleic acid compositions comprising an inorganic polyphosphate and methods for preparing, storing and using the same |
| US20250326813A1 (en) | 2022-05-10 | 2025-10-23 | Elpis Biopharmaceuticals | Engineered interleukin-2 receptor beta reduced-binding agonist |
| US11878055B1 (en) | 2022-06-26 | 2024-01-23 | BioNTech SE | Coronavirus vaccine |
| WO2024017479A1 (en) | 2022-07-21 | 2024-01-25 | BioNTech SE | Multifunctional cells transiently expressing an immune receptor and one or more cytokines, their use and methods for their production |
| IL317565A (en) | 2022-08-01 | 2025-02-01 | BioNTech SE | Nucleic acid compositions containing amphiphilic oligoethylene glycol (OEG) conjugated compounds and methods for using such compounds and compositions |
| EP4565266A1 (en) | 2022-08-03 | 2025-06-11 | Nanoramic, Inc. | Rna for preventing or treating tuberculosis |
| WO2024027910A1 (en) | 2022-08-03 | 2024-02-08 | BioNTech SE | Rna for preventing or treating tuberculosis |
| CN115960175A (zh) * | 2022-08-08 | 2023-04-14 | 江南大学 | 一种强化乳铁蛋白表达的毕赤酵母及其构建方法与应用 |
| JP2024056667A (ja) * | 2022-10-11 | 2024-04-23 | Ｊｃｒファーマ株式会社 | 血清アルブミンと生理活性を有する蛋白質との融合蛋白質 |
| WO2024080304A1 (ja) * | 2022-10-11 | 2024-04-18 | Ｊｃｒファーマ株式会社 | 血清アルブミンと生理活性を有する蛋白質との融合蛋白質 |
| EP4389762A1 (en) | 2022-12-23 | 2024-06-26 | Ospedale San Raffaele S.r.l. | Inhibitors of dux4 activity and their use in therapy. |
| WO2024153324A1 (en) | 2023-01-18 | 2024-07-25 | BioNTech SE | Rna formulations for pharmaceutical use |
| WO2024213776A1 (en) | 2023-04-14 | 2024-10-17 | BioNTech SE | Rna for preventing or treating tuberculosis |
| WO2024216214A1 (en) | 2023-04-14 | 2024-10-17 | BioNTech SE | Rna for preventing or treating tuberculosis |
| WO2024216212A1 (en) | 2023-04-14 | 2024-10-17 | BioNTech SE | Rna for preventing or treating tuberculosis |
| WO2025006676A2 (en) | 2023-06-27 | 2025-01-02 | Firecyte Therapeutics, Inc. | Insulin-like growth factor binding protein like 1 (igfbpl1) compositions and methods of use thereof |
| WO2025021277A1 (en) | 2023-07-21 | 2025-01-30 | BioNTech SE | Agents and methods for targeted delivery of cytokines to immune cells |
| WO2025026866A1 (en) | 2023-07-28 | 2025-02-06 | BioNTech SE | Rna therapeutics with reduced toxicity |
| TW202535460A (zh) | 2023-10-06 | 2025-09-16 | 德商百靈佳殷格翰國際股份有限公司 | 抗ＳＩＲＰ－α抗體用於治療癌症之用途 |
| TW202535461A (zh) | 2023-10-06 | 2025-09-16 | 德商百靈佳殷格翰國際股份有限公司 | 使用抗ｓｉｒｐａ抗體治療肝臟疾病或病症 |
| WO2025106754A1 (en) | 2023-11-15 | 2025-05-22 | BioNTech SE | Coronavirus vaccine |
| WO2025181215A1 (en) | 2024-03-01 | 2025-09-04 | Boehringer Ingelheim International Gmbh | Antibodies to connective tissue growth factor (ctgf) and uses thereof |
| CN120591344A (zh) * | 2025-06-13 | 2025-09-05 | 广州景旸生物科技有限公司 | Col3a1蛋白的制备方法及其应用 |
Family Cites Families (186)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4179337A (en) | 1973-07-20 | 1979-12-18 | Davis Frank F | Non-immunogenic polypeptides |
| US4002531A (en) | 1976-01-22 | 1977-01-11 | Pierce Chemical Company | Modifying enzymes with polyethylene glycol and product produced thereby |
| US4444887A (en) | 1979-12-10 | 1984-04-24 | Sloan-Kettering Institute | Process for making human antibody producing B-lymphocytes |
| US4714681A (en) | 1981-07-01 | 1987-12-22 | The Board Of Reagents, The University Of Texas System Cancer Center | Quadroma cells and trioma cells and methods for the production of same |
| US4474893A (en) | 1981-07-01 | 1984-10-02 | The University of Texas System Cancer Center | Recombinant monoclonal antibodies |
| US4716111A (en) | 1982-08-11 | 1987-12-29 | Trustees Of Boston University | Process for producing human antibodies |
| US4741900A (en) | 1982-11-16 | 1988-05-03 | Cytogen Corporation | Antibody-metal ion complexes |
| NZ207394A (en) | 1983-03-08 | 1987-03-06 | Commw Serum Lab Commission | Detecting or determining sequence of amino acids |
| GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US5807715A (en) | 1984-08-27 | 1998-09-15 | The Board Of Trustees Of The Leland Stanford Junior University | Methods and transformed mammalian lymphocyte cells for producing functional antigen-binding protein including chimeric immunoglobulin |
| EP0216846B2 (en) | 1985-04-01 | 1995-04-26 | Celltech Limited | Transformed myeloma cell-line and a process for the expression of a gene coding for a eukaryotic polypeptide employing same |
| US4980286A (en) | 1985-07-05 | 1990-12-25 | Whitehead Institute For Biomedical Research | In vivo introduction and expression of foreign genetic material in epithelial cells |
| US4676980A (en) | 1985-09-23 | 1987-06-30 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Target specific cross-linked heteroantibodies |
| GB8601597D0 (en) | 1986-01-23 | 1986-02-26 | Wilson R H | Nucleotide sequences |
| GB8607679D0 (en) | 1986-03-27 | 1986-04-30 | Winter G P | Recombinant dna product |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| BR8806573A (pt) * | 1987-04-09 | 1989-10-31 | Delta Biotechnology Ltd | Vetor de levedo |
| US5258498A (en) | 1987-05-21 | 1993-11-02 | Creative Biomolecules, Inc. | Polypeptide linkers for production of biosynthetic proteins |
| US5489425A (en) | 1987-06-24 | 1996-02-06 | The Dow Chemical Company | Functionalized polyamine chelants |
| US4994560A (en) | 1987-06-24 | 1991-02-19 | The Dow Chemical Company | Functionalized polyamine chelants and radioactive rhodium complexes thereof for conjugation to antibodies |
| GB8717430D0 (en) | 1987-07-23 | 1987-08-26 | Celltech Ltd | Recombinant dna product |
| PT88641B (pt) | 1987-10-02 | 1993-04-30 | Genentech Inc | Metodo para a preparacao de uma variante de adesao |
| GB8725529D0 (en) | 1987-10-30 | 1987-12-02 | Delta Biotechnology Ltd | Polypeptides |
| JPH01215289A (ja) | 1988-02-22 | 1989-08-29 | Toa Nenryo Kogyo Kk | 遺伝子組換えによる正常ヒト血清アルブミンａの製造方法 |
| GB8809129D0 (en) | 1988-04-18 | 1988-05-18 | Celltech Ltd | Recombinant dna methods vectors and host cells |
| US5756065A (en) | 1988-06-24 | 1998-05-26 | The Dow Chemical Company | Macrocyclic tetraazacyclododecane conjugates and their use as diagnostic and therapeutic agents |
| DE353450T1 (de) | 1988-06-24 | 1990-09-06 | The Dow Chemical Co., Midland, Mich. | Macrocyclische bifunktionelle chelatbildner, komplexe davon und ihre konjugierten antikoerper. |
| CN1033030C (zh) | 1988-06-24 | 1996-10-16 | 唐化学原料公司 | 大环双官能螯合剂及其配合物和抗体共轭物的制备方法 |
| US5274119A (en) | 1988-07-01 | 1993-12-28 | The Dow Chemical Company | Vicinal diols |
| US4925648A (en) | 1988-07-29 | 1990-05-15 | Immunomedics, Inc. | Detection and treatment of infectious and inflammatory lesions |
| FR2649991B2 (fr) | 1988-08-05 | 1994-03-04 | Rhone Poulenc Sante | Utilisation de derives stables du plasmide pkd1 pour l'expression et la secretion de proteines heterologues dans les levures du genre kluyveromyces |
| JPH04501204A (ja) | 1988-08-11 | 1992-03-05 | サイオス ノバ インコーポレイテッド | 異種タンパク発現を安定させる方法およびそれに使用するベクター |
| US5601819A (en) | 1988-08-11 | 1997-02-11 | The General Hospital Corporation | Bispecific antibodies for selective immune regulation and for selective immune cell binding |
| EP1997891A1 (en) | 1988-09-02 | 2008-12-03 | Dyax Corporation | Generation and selection of recombinant varied binding proteins |
| US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| US5349052A (en) | 1988-10-20 | 1994-09-20 | Royal Free Hospital School Of Medicine | Process for fractionating polyethylene glycol (PEG)-protein adducts and an adduct for PEG and granulocyte-macrophage colony stimulating factor |
| US5342604A (en) | 1988-10-31 | 1994-08-30 | The Dow Chemical Company | Complexes possessing ortho ligating functionality |
| US5696239A (en) | 1988-10-31 | 1997-12-09 | The Dow Chemical Company | Conjugates possessing ortho ligating functionality and complexes thereof |
| EP0401384B1 (en) | 1988-12-22 | 1996-03-13 | Kirin-Amgen, Inc. | Chemically modified granulocyte colony stimulating factor |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US5705363A (en) * | 1989-03-02 | 1998-01-06 | The Women's Research Institute | Recombinant production of human interferon τ polypeptides and nucleic acids |
| US5231020A (en) | 1989-03-30 | 1993-07-27 | Dna Plant Technology Corporation | Genetic engineering of novel plant phenotypes |
| US5324844A (en) | 1989-04-19 | 1994-06-28 | Enzon, Inc. | Active carbonates of polyalkylene oxides for modification of polypeptides |
| US5766883A (en) * | 1989-04-29 | 1998-06-16 | Delta Biotechnology Limited | Polypeptides |
| US5808003A (en) | 1989-05-26 | 1998-09-15 | Perimmune Holdings, Inc. | Polyaminocarboxylate chelators |
| ATE144793T1 (de) | 1989-06-29 | 1996-11-15 | Medarex Inc | Bispezifische reagenzien für die aids-therapie |
| US5413923A (en) | 1989-07-25 | 1995-05-09 | Cell Genesys, Inc. | Homologous recombination for universal donor cells and chimeric mammalian hosts |
| FR2650598B1 (fr) * | 1989-08-03 | 1994-06-03 | Rhone Poulenc Sante | Derives de l'albumine a fonction therapeutique |
| US5073627A (en) | 1989-08-22 | 1991-12-17 | Immunex Corporation | Fusion proteins comprising GM-CSF and IL-3 |
| KR100221066B1 (ko) | 1989-10-13 | 1999-10-01 | 스튜어트 엘.왓트 | 에리트로포이에틴 유사체와 그를 포함하는 제약학적 조성물 |
| US5667986A (en) * | 1989-10-18 | 1997-09-16 | Delta Biotechnology Limited | Yeast promoter for expressing heterologous polypeptides |
| GB8924021D0 (en) | 1989-10-25 | 1989-12-13 | Celltech Ltd | Recombinant dna method and vectors for the use therein |
| GB8928874D0 (en) | 1989-12-21 | 1990-02-28 | Celltech Ltd | Humanised antibodies |
| WO1991010737A1 (en) | 1990-01-11 | 1991-07-25 | Molecular Affinities Corporation | Production of antibodies using gene libraries |
| US5780225A (en) | 1990-01-12 | 1998-07-14 | Stratagene | Method for generating libaries of antibody genes comprising amplification of diverse antibody DNAs and methods for using these libraries for the production of diverse antigen combining molecules |
| DE69133566T2 (de) | 1990-01-12 | 2007-12-06 | Amgen Fremont Inc. | Bildung von xenogenen Antikörpern |
| US6075181A (en) | 1990-01-12 | 2000-06-13 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US5545618A (en) * | 1990-01-24 | 1996-08-13 | Buckley; Douglas I. | GLP-1 analogs useful for diabetes treatment |
| US5747334A (en) | 1990-02-15 | 1998-05-05 | The University Of North Carolina At Chapel Hill | Random peptide library |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| GB9013017D0 (en) * | 1990-06-11 | 1990-08-01 | Mars Uk Ltd | Compounds |
| GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| US5225341A (en) | 1990-07-19 | 1993-07-06 | The Regents Of The University Of California | Biologically safe plant transformation system using a ds transposon |
| US5202239A (en) * | 1990-08-07 | 1993-04-13 | Scios Nova Inc. | Expression of recombinant polypeptides with improved purification |
| KR100272077B1 (ko) | 1990-08-29 | 2000-11-15 | 젠팜인터내셔날,인코포레이티드 | 이종 항체를 생산할 수 있는 전이유전자를 가진 인간이외의 동물 |
| US5625126A (en) | 1990-08-29 | 1997-04-29 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5814318A (en) | 1990-08-29 | 1998-09-29 | Genpharm International Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5661016A (en) | 1990-08-29 | 1997-08-26 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
| US5698426A (en) | 1990-09-28 | 1997-12-16 | Ixsys, Incorporated | Surface expression libraries of heteromeric receptors |
| AU667460B2 (en) | 1990-10-05 | 1996-03-28 | Medarex, Inc. | Targeted immunostimulation with bispecific reagents |
| JPH07108232B2 (ja) * | 1990-10-09 | 1995-11-22 | エム・ディ・リサーチ株式会社 | ペプチド又は蛋白質の製造方法 |
| AU8727291A (en) | 1990-10-29 | 1992-06-11 | Cetus Oncology Corporation | Bispecific antibodies, method of production, and uses thereof |
| WO1992009690A2 (en) | 1990-12-03 | 1992-06-11 | Genentech, Inc. | Enrichment method for variant proteins with altered binding properties |
| DE69233750D1 (de) | 1991-04-10 | 2009-01-02 | Scripps Research Inst | Bibliotheken heterodimerer Rezeptoren mittels Phagemiden |
| WO1992019973A1 (en) | 1991-04-26 | 1992-11-12 | Surface Active Limited | Novel antibodies, and methods for their use |
| US5646012A (en) * | 1991-04-30 | 1997-07-08 | Rhone-Poulenc Rorer S.A. | Yeast promoter and use thereof |
| DE69233482T2 (de) | 1991-05-17 | 2006-01-12 | Merck & Co., Inc. | Verfahren zur Verminderung der Immunogenität der variablen Antikörperdomänen |
| WO1992022324A1 (en) | 1991-06-14 | 1992-12-23 | Xoma Corporation | Microbially-produced antibody fragments and their conjugates |
| US5565332A (en) | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| ATE408012T1 (de) | 1991-12-02 | 2008-09-15 | Medical Res Council | Herstellung von autoantikörpern auf phagenoberflächen ausgehend von antikörpersegmentbibliotheken |
| US5428139A (en) | 1991-12-10 | 1995-06-27 | The Dow Chemical Company | Bicyclopolyazamacrocyclophosphonic acid complexes for use as radiopharmaceuticals |
| FR2686620B1 (fr) * | 1992-01-27 | 1995-06-23 | Rhone Poulenc Rorer Sa | Serum-albumine humaine, preparation et utilisation. |
| FR2686900B1 (fr) * | 1992-01-31 | 1995-07-21 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides ayant une activite de stimulation des colonies de granulocytes, leur preparation et compositions pharmaceutiques les contenant. |
| FR2686899B1 (fr) * | 1992-01-31 | 1995-09-01 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides biologiquement actifs, leur preparation et compositions pharmaceutiques les contenant. |
| CA2131528C (en) | 1992-03-05 | 2004-07-13 | Philip E. Thorpe | Methods and compositions for targeting the vasculature of solid tumors |
| US5733743A (en) | 1992-03-24 | 1998-03-31 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| US5573905A (en) | 1992-03-30 | 1996-11-12 | The Scripps Research Institute | Encoded combinatorial chemical libraries |
| ATE182651T1 (de) | 1992-06-09 | 1999-08-15 | Hoppe Ag | Riegel und türschloss |
| US5505931A (en) | 1993-03-04 | 1996-04-09 | The Dow Chemical Company | Acid cleavable compounds, their preparation and use as bifunctional acid-labile crosslinking agents |
| ES2153385T5 (es) | 1992-07-31 | 2008-09-01 | Genentech, Inc. | Composicion acuosa a base de hormona del crecimiento humana. |
| US5639641A (en) | 1992-09-09 | 1997-06-17 | Immunogen Inc. | Resurfacing of rodent antibodies |
| US5441050A (en) | 1992-12-18 | 1995-08-15 | Neoprobe Corporation | Radiation responsive surgical instrument |
| DK82893D0 (da) * | 1993-07-08 | 1993-07-08 | Novo Nordisk As | Peptid |
| US5512459A (en) | 1993-07-20 | 1996-04-30 | Bionebraska, Inc. | Enzymatic method for modification or recombinant polypeptides |
| GB9317618D0 (en) | 1993-08-24 | 1993-10-06 | Royal Free Hosp School Med | Polymer modifications |
| US5643575A (en) | 1993-10-27 | 1997-07-01 | Enzon, Inc. | Non-antigenic branched polymer conjugates |
| WO1995015982A2 (en) | 1993-12-08 | 1995-06-15 | Genzyme Corporation | Process for generating specific antibodies |
| US5705483A (en) * | 1993-12-09 | 1998-01-06 | Eli Lilly And Company | Glucagon-like insulinotropic peptides, compositions and methods |
| DK144093D0 (enExample) * | 1993-12-23 | 1993-12-23 | Novo Nordisk As | |
| DK1231268T3 (da) | 1994-01-31 | 2005-11-21 | Univ Boston | Polyklonale antistofbiblioteker |
| US5516637A (en) | 1994-06-10 | 1996-05-14 | Dade International Inc. | Method involving display of protein binding pairs on the surface of bacterial pili and bacteriophage |
| US5985660A (en) | 1994-06-15 | 1999-11-16 | Systemix, Inc. | Method of identifying biological response modifiers involved in dendritic and/or lymphoid progenitor cell proliferation and/or differentiation |
| US5639642A (en) * | 1994-06-16 | 1997-06-17 | Novo Nordisk A/S | Synthetic leader peptide sequences |
| US5623054A (en) | 1994-06-23 | 1997-04-22 | The General Hospital Corporation | Crucifer AFT proteins and uses thereof |
| US5574008A (en) * | 1994-08-30 | 1996-11-12 | Eli Lilly And Company | Biologically active fragments of glucagon-like insulinotropic peptide |
| US5512549A (en) * | 1994-10-18 | 1996-04-30 | Eli Lilly And Company | Glucagon-like insulinotropic peptide analogs, compositions, and methods of use |
| JP4312259B2 (ja) | 1995-04-27 | 2009-08-12 | アムジェン フレモント インク． | 免疫したゼノマウス（ＸｅｎｏＭｏｕｓｅ）に由来するヒト抗体 |
| EP0823941A4 (en) | 1995-04-28 | 2001-09-19 | Abgenix Inc | HUMAN ANTIBODIES DERIVED FROM IMMUNIZED XENO MOUSES |
| US5804162A (en) | 1995-06-07 | 1998-09-08 | Alliance Pharmaceutical Corp. | Gas emulsions stabilized with fluorinated ethers having low Ostwald coefficients |
| US5811097A (en) | 1995-07-25 | 1998-09-22 | The Regents Of The University Of California | Blockade of T lymphocyte down-regulation associated with CTLA-4 signaling |
| GB9526733D0 (en) * | 1995-12-30 | 1996-02-28 | Delta Biotechnology Ltd | Fusion proteins |
| US6110707A (en) * | 1996-01-19 | 2000-08-29 | Board Of Regents, The University Of Texas System | Recombinant expression of proteins from secretory cell lines |
| US6087129A (en) * | 1996-01-19 | 2000-07-11 | Betagene, Inc. | Recombinant expression of proteins from secretory cell lines |
| EP0910578A2 (en) | 1996-01-19 | 1999-04-28 | The Board Of Regents, The University Of Texas System | Recombinant expression of proteins from secretory cell lines |
| JP2978435B2 (ja) | 1996-01-24 | 1999-11-15 | チッソ株式会社 | アクリロキシプロピルシランの製造方法 |
| US5912229A (en) * | 1996-03-01 | 1999-06-15 | Novo Nordisk Als | Use of a pharmaceutical composition comprising an appetite-suppressing peptide |
| JP4064460B2 (ja) | 1996-03-01 | 2008-03-19 | ノボ ノルディスク アクティーゼルスカブ | 食欲抑制性ペプチドを含む医薬組成物の用途 |
| WO1997033899A1 (en) | 1996-03-14 | 1997-09-18 | Human Genome Sciences, Inc. | Apoptosis inducing molecule i |
| EP0904278A4 (en) | 1996-03-22 | 1999-09-15 | Human Genome Sciences Inc | MOLECULE II INDUCER OF APOPTOSIS |
| US6300065B1 (en) * | 1996-05-31 | 2001-10-09 | Board Of Trustees Of The University Of Illinois | Yeast cell surface display of proteins and uses thereof |
| US6110703A (en) * | 1996-07-05 | 2000-08-29 | Novo Nordisk A/S | Method for the production of polypeptides |
| WO1998005782A1 (en) * | 1996-08-02 | 1998-02-12 | Zymogenetics, Inc. | Testis-specific insulin homolog polypeptides |
| US6006753A (en) * | 1996-08-30 | 1999-12-28 | Eli Lilly And Company | Use of GLP-1 or analogs to abolish catabolic changes after surgery |
| US6458924B2 (en) * | 1996-08-30 | 2002-10-01 | Novo Nordisk A/S | Derivatives of GLP-1 analogs |
| US6277819B1 (en) | 1996-08-30 | 2001-08-21 | Eli Lilly And Company | Use of GLP-1 or analogs in treatment of myocardial infarction |
| WO1998011136A1 (en) | 1996-09-09 | 1998-03-19 | Novo Nordisk A/S | A cDNA AND PEPTIDE WITH RELATION TO CANCER AND WEIGHT LOSS |
| EP0961832A4 (en) | 1996-09-18 | 2003-02-26 | Human Genome Sciences Inc | HUMAN TUMOR NECROSIS FACTOR-TYPE RECEPTOR GENES |
| US5916771A (en) | 1996-10-11 | 1999-06-29 | Abgenix, Inc. | Production of a multimeric protein by cell fusion method |
| UA65549C2 (uk) * | 1996-11-05 | 2004-04-15 | Елі Ліллі Енд Компані | Спосіб регулювання ожиріння шляхом периферійного введення аналогів та похідних glp-1 (варіанти) та фармацевтична композиція |
| EP1306092A3 (en) | 1996-11-05 | 2003-05-07 | Eli Lilly & Company | Use of GLP-1 and analogs administered peripherally, in regulation of obesity |
| EP0941114B1 (en) | 1996-11-12 | 2005-02-23 | Novo Nordisk A/S | Use of glp-1 peptides |
| DE69738539T2 (de) | 1996-12-03 | 2009-03-26 | Amgen Fremont Inc. | Vollkommen humane Antikörper die EGFR binden |
| JP2001527387A (ja) | 1997-01-24 | 2001-12-25 | ノボ ノルディスク アクティーゼルスカブ | 合成リーダーペプチド配列 |
| EP0921817B1 (en) | 1997-01-29 | 2001-03-28 | PolyMASC Pharmaceuticals plc | Pegylation process |
| US20030175858A1 (en) * | 1997-03-07 | 2003-09-18 | Ruben Steven M. | 186 human secreted proteins |
| US20030065139A1 (en) * | 1998-03-19 | 2003-04-03 | Craig A. Rosen | Secreted protein hmmbd35 |
| US20030049618A1 (en) * | 1997-03-07 | 2003-03-13 | Ruben Steven M. | 186 human secreted proteins |
| US6420526B1 (en) * | 1997-03-07 | 2002-07-16 | Human Genome Sciences, Inc. | 186 human secreted proteins |
| US20060084082A1 (en) * | 1997-03-07 | 2006-04-20 | Human Genome Sciences, Inc. | 186 human secreted proteins |
| US5981488A (en) * | 1997-03-31 | 1999-11-09 | Eli Lillly And Company | Glucagon-like peptide-1 analogs |
| BRPI9809391B8 (pt) | 1997-04-14 | 2021-05-25 | Amgen Res Munich Gmbh | processo para a produção de um receptor de antígeno anti-humano, anticorpo humano e composição farmacêutica |
| US6235883B1 (en) | 1997-05-05 | 2001-05-22 | Abgenix, Inc. | Human monoclonal antibodies to epidermal growth factor receptor |
| GB9713412D0 (en) | 1997-06-26 | 1997-08-27 | Delta Biotechnology Ltd | Improved protein expression strains |
| JP2001516580A (ja) | 1997-09-17 | 2001-10-02 | ジェネンテック・インコーポレーテッド | 分泌性の、および膜貫通性のポリぺプチド、およびそれをコードする核酸 |
| ES2303358T3 (es) | 1997-11-03 | 2008-08-01 | Human Genome Sciences, Inc. | Vegi, un inhibidor de la angiogenesis y el crecimiento tumoral. |
| ATE466027T1 (de) | 1998-02-27 | 2010-05-15 | Novo Nordisk As | Abkömmlinge von glp-1 analogen |
| US7205280B2 (en) * | 1998-03-11 | 2007-04-17 | Cognosci, Inc. | Methods of suppressing microglial activation |
| AU775422B2 (en) * | 1998-06-15 | 2004-07-29 | Gtc Biotherapeutics, Inc. | Erythropoietin analog-human serum albumin fusion |
| MY155270A (en) | 1998-09-24 | 2015-09-30 | Lilly Co Eli | Use of glp-1 or analogs in treatment of stroke |
| US7259136B2 (en) | 1999-04-30 | 2007-08-21 | Amylin Pharmaceuticals, Inc. | Compositions and methods for treating peripheral vascular disease |
| US6514500B1 (en) * | 1999-10-15 | 2003-02-04 | Conjuchem, Inc. | Long lasting synthetic glucagon like peptide {GLP-!} |
| US6329336B1 (en) | 1999-05-17 | 2001-12-11 | Conjuchem, Inc. | Long lasting insulinotropic peptides |
| US20020048571A1 (en) | 1999-07-19 | 2002-04-25 | Jeno Gyuris | Chimeric polypeptides of serum albumin and uses related thereto |
| IL147714A0 (en) | 1999-07-19 | 2002-08-14 | Gpc Biotech Inc | Chimeric polypeptides of serum albumin and uses related thereto |
| CA2405550A1 (en) * | 2000-04-12 | 2001-10-25 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| WO2001089554A2 (en) | 2000-05-19 | 2001-11-29 | Bionebraska, Inc. | Treatment of acute coronary syndrome with glp-1 |
| NZ519752A (en) | 2000-10-20 | 2005-04-29 | Amylin Pharmaceuticals Inc | Treatment of hibernating myocardium and diabetic cardiomyopathy with a GLP-1 peptide |
| US7101561B2 (en) * | 2000-12-01 | 2006-09-05 | Innogenetics N.V. | Purified hepatitis C virus envelope proteins for diagnostic and therapeutic use |
| DK1355942T3 (da) * | 2000-12-07 | 2008-11-17 | Lilly Co Eli | GLP-1-fusionsproteiner |
| AU2002310122A1 (en) | 2001-05-25 | 2002-12-09 | Human Genome Sciences, Inc. | Chemokine beta-1 fusion proteins |
| US7101843B2 (en) | 2001-08-23 | 2006-09-05 | Eli Lilly And Company | Glucagon-like peptide-1 analogs |
| US20030228298A1 (en) * | 2001-09-04 | 2003-12-11 | Mark Nesbit | Abrogen polypeptides, nucleic acids encoding them and methods for using them to inhibit angiogenesis |
| WO2003030821A2 (en) * | 2001-10-05 | 2003-04-17 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| ES2561985T3 (es) * | 2001-10-10 | 2016-03-01 | Ratiopharm Gmbh | Remodelación y glicoconjugación de anticuerpos |
| KR101271635B1 (ko) * | 2001-12-21 | 2013-06-12 | 휴먼 게놈 사이언시즈, 인코포레이티드 | 알부민 융합 단백질 |
| CA2484556A1 (en) * | 2001-12-21 | 2003-07-24 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| AU2002364586A1 (en) * | 2001-12-21 | 2003-07-30 | Delta Biotechnology Limited | Albumin fusion proteins |
| AU2002353374A1 (en) * | 2001-12-21 | 2003-07-09 | Nexia Biotechnologies, Inc. | Production of butyrylcholinesterases in transgenic mammals |
| US20080167238A1 (en) * | 2001-12-21 | 2008-07-10 | Human Genome Sciences, Inc. | Albumin Fusion Proteins |
| JP2005535569A (ja) | 2002-04-04 | 2005-11-24 | ノボ・ノルデイスク・エー／エス | Ｇｌｐ−１アゴニスト及び心臓血管合併症 |
| CN1241946C (zh) * | 2002-07-01 | 2006-02-15 | 美国福源集团 | 对多种细胞具刺激增生作用的人血清白蛋白重组融合蛋白 |
| CA2513213C (en) * | 2003-01-22 | 2013-07-30 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| CA2528591C (en) | 2003-06-12 | 2013-01-08 | Eli Lilly And Company | Glp-1 analog fusion proteins |
| SI1729795T1 (sl) * | 2004-02-09 | 2016-04-29 | Human Genome Sciences, Inc. | Albuminski fuzijski proteini |
| US20070270339A1 (en) * | 2004-04-23 | 2007-11-22 | Serono, Inc. | Use of GPCR54 Ligands for the Treatment of Infertility |
| US20070021336A1 (en) | 2004-12-24 | 2007-01-25 | Christen Anderson | Use of GLP-1 and agonists thereof to prevent cardiac myocyte apoptosis |
| WO2006110887A2 (en) | 2005-04-11 | 2006-10-19 | Amylin Pharmaceuticals, Inc | Use of glp-1, exendin and agonists thereof to delay or prevent cardiac remodeling |
| KR20080071119A (ko) | 2005-08-12 | 2008-08-01 | 휴먼 게놈 사이언시즈, 인코포레이티드 | 알부민 융합 단백질 |
| AU2007267833B2 (en) | 2006-05-26 | 2012-07-26 | Amylin Pharmaceuticals, Llc | Composition and methods for treatment of congestive heart failure |
| EP2046367A4 (en) | 2006-06-07 | 2009-11-11 | Human Genome Sciences Inc | ALBUM INFUSION PROTEINS |
| US20090209469A1 (en) | 2006-08-04 | 2009-08-20 | Dennis Kim | Use of Exendins and GLP-1 Receptor Agonists for Altering Lipoprotein Particle Size and Subclass Composition |
| JP5005450B2 (ja) * | 2007-07-13 | 2012-08-22 | 本田技研工業株式会社 | 燃料給油管の口元内部構造 |
-
2005
- 2005-02-09 SI SI200532048T patent/SI1729795T1/sl unknown
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- 2006-08-08 US US11/500,314 patent/US20070048282A1/en not_active Abandoned
- 2006-09-08 MA MA29305A patent/MA28565B1/fr unknown
- 2006-09-08 NO NO20064059A patent/NO20064059L/no not_active Application Discontinuation
-
2009
- 2009-08-03 US US12/534,585 patent/US8143026B2/en not_active Expired - Fee Related
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2010
- 2010-10-07 AU AU2010227035A patent/AU2010227035A1/en not_active Abandoned
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2012
- 2012-02-28 JP JP2012041914A patent/JP5568582B2/ja not_active Expired - Fee Related
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2016
- 2016-04-18 CY CY20161100318T patent/CY1117401T1/el unknown
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