CH669395A5 - - Google Patents
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- CH669395A5 CH669395A5 CH5667/83A CH566783A CH669395A5 CH 669395 A5 CH669395 A5 CH 669395A5 CH 5667/83 A CH5667/83 A CH 5667/83A CH 566783 A CH566783 A CH 566783A CH 669395 A5 CH669395 A5 CH 669395A5
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- CH
- Switzerland
- Prior art keywords
- mutein
- ifn
- synthetic
- dna
- serine
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Classifications
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- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- 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
-
- 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
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/54—Interleukins [IL]
- C07K14/55—IL-2
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
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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
-
- 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
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/555—Interferons [IFN]
- C07K14/565—IFN-beta
-
- 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
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/102—Mutagenizing nucleic acids
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/808—Materials and products related to genetic engineering or hybrid or fused cell technology, e.g. hybridoma, monoclonal products
- Y10S530/809—Fused cells, e.g. hybridoma
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S930/00—Peptide or protein sequence
- Y10S930/01—Peptide or protein sequence
- Y10S930/14—Lymphokine; related peptides
- Y10S930/141—Interleukin
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S930/00—Peptide or protein sequence
- Y10S930/01—Peptide or protein sequence
- Y10S930/14—Lymphokine; related peptides
- Y10S930/142—Interferon
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Medicinal Chemistry (AREA)
- Wood Science & Technology (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Biophysics (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
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- Veterinary Medicine (AREA)
- Toxicology (AREA)
- Plant Pathology (AREA)
- Microbiology (AREA)
- Physics & Mathematics (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Virology (AREA)
- Communicable Diseases (AREA)
- Crystallography & Structural Chemistry (AREA)
- Immunology (AREA)
- Oncology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US43515482A | 1982-10-19 | 1982-10-19 | |
| US48616283A | 1983-04-15 | 1983-04-15 |
Publications (1)
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|---|---|
| CH669395A5 true CH669395A5 (enExample) | 1989-03-15 |
Family
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| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CH5667/83A CH669395A5 (enExample) | 1982-10-19 | 1983-10-18 |
Country Status (23)
| Country | Link |
|---|---|
| EP (4) | EP0192811B1 (enExample) |
| JP (2) | JPS6128392A (enExample) |
| KR (1) | KR910009900B1 (enExample) |
| AT (4) | ATE33503T1 (enExample) |
| AU (1) | AU563962B2 (enExample) |
| BE (1) | BE898016A (enExample) |
| CA (1) | CA1340861C (enExample) |
| CH (1) | CH669395A5 (enExample) |
| DE (4) | DE3382528D1 (enExample) |
| DK (2) | DK168767B1 (enExample) |
| ES (4) | ES526541A0 (enExample) |
| FI (1) | FI82266C (enExample) |
| FR (1) | FR2534594B1 (enExample) |
| GB (1) | GB2130219B (enExample) |
| GR (1) | GR79408B (enExample) |
| IE (1) | IE56026B1 (enExample) |
| IL (1) | IL69970A (enExample) |
| LU (3) | LU88761I2 (enExample) |
| NL (2) | NL930119I2 (enExample) |
| NO (1) | NO173740C (enExample) |
| NZ (1) | NZ205922A (enExample) |
| PH (2) | PH20343A (enExample) |
| PT (1) | PT77512B (enExample) |
Families Citing this family (125)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| IE56026B1 (en) * | 1982-10-19 | 1991-03-27 | Cetus Corp | Cysteine-depleted muteins of biologically active proteins |
| IL71951A0 (en) * | 1983-06-01 | 1984-09-30 | Hoffmann La Roche | Polypeptides having interferon activity,their preparation and pharmaceutical compositions containing them |
| WO1985000817A1 (en) * | 1983-08-10 | 1985-02-28 | Amgen | Microbial expression of interleukin ii |
| GB8334102D0 (en) * | 1983-12-21 | 1984-02-01 | Searle & Co | Interferons with cysteine pattern |
| US4530787A (en) * | 1984-03-28 | 1985-07-23 | Cetus Corporation | Controlled oxidation of microbially produced cysteine-containing proteins |
| DE3575072D1 (de) | 1984-03-28 | 1990-02-08 | Cetus Corp | Pharmazeutische zusammensetzungen von mikrobenerzeugtem interleukin-2. |
| DE3574731D1 (de) * | 1984-05-08 | 1990-01-18 | Genetics Inst | Ein menschlicher t-zellwachstumsfaktor. |
| GB8412564D0 (en) * | 1984-05-17 | 1984-06-20 | Searle & Co | Structure and properties |
| IL75318A (en) * | 1984-05-31 | 1994-08-26 | Genentech Inc | Recombinant human memotoxin and methods for its recombinant production |
| US5683688A (en) * | 1984-05-31 | 1997-11-04 | Genentech, Inc. | Unglycosylated recombinant human lymphotoxin polypeptides and compositions |
| US5672347A (en) * | 1984-07-05 | 1997-09-30 | Genentech, Inc. | Tumor necrosis factor antagonists and their use |
| CA1275954C (en) | 1984-08-31 | 1990-11-06 | Hing Cheug Wong | 3'-expression enhancing fragments and method |
| WO1986002068A1 (fr) * | 1984-09-26 | 1986-04-10 | Takeda Chemical Industries, Ltd. | Separation mutuelle de proteines |
| IL76360A0 (en) | 1984-09-26 | 1986-01-31 | Takeda Chemical Industries Ltd | Mutual separation of proteins |
| US4606917A (en) * | 1984-10-03 | 1986-08-19 | Syntex (U.S.A) Inc. | Synergistic antiviral composition |
| US4857316A (en) * | 1984-10-03 | 1989-08-15 | Syntex (U.S.A.) Inc. | Synergistic antiviral composition |
| US4959314A (en) | 1984-11-09 | 1990-09-25 | Cetus Corporation | Cysteine-depleted muteins of biologically active proteins |
| US4572798A (en) * | 1984-12-06 | 1986-02-25 | Cetus Corporation | Method for promoting disulfide bond formation in recombinant proteins |
| US5342614A (en) * | 1984-12-21 | 1994-08-30 | Otsuka Pharmaceutical Co., Ltd. | Method of treating arthritus or inflammation with IL-1β or derivatives thereof |
| US6107465A (en) * | 1984-12-21 | 2000-08-22 | Otsuka Pharmaceutical Co., Ltd. | IL-1β and derivatives thereof and drugs |
| DK172052B1 (da) * | 1984-12-21 | 1997-09-29 | Otsuka Pharma Co Ltd | Antitumor-aktivt stof, fremgangsmåde til dets fremstilling, lægemiddel indeholdende stoffet, gen kodende for stoffet, vektor indeholdende genet samt rekombinant mikroorganisme transformet med en sådan vektor |
| DE3500681A1 (de) * | 1985-01-11 | 1986-07-17 | Hoechst Ag, 6230 Frankfurt | Verfahren zur isolierung und reinigung von lymphokinen |
| US4863849A (en) * | 1985-07-18 | 1989-09-05 | New York Medical College | Automatable process for sequencing nucleotide |
| US4810643A (en) * | 1985-08-23 | 1989-03-07 | Kirin- Amgen Inc. | Production of pluripotent granulocyte colony-stimulating factor |
| US6004548A (en) | 1985-08-23 | 1999-12-21 | Amgen, Inc. | Analogs of pluripotent granulocyte colony-stimulating factor |
| CA1297003C (en) * | 1985-09-20 | 1992-03-10 | Jack H. Nunberg | Composition and method for treating animals |
| US5359035A (en) * | 1985-12-21 | 1994-10-25 | Hoechst Aktiengesellschaft | Bifunctional proteins including interleukin-2 (IL-2) and granuloctyte macrophage colony stimulating factor (GM-CSF) |
| AU595864B2 (en) * | 1986-03-14 | 1990-04-12 | Otsuka Pharmaceutical Co., Ltd. | Il-1 alpha derivatives and drugs |
| US5008374A (en) * | 1986-03-14 | 1991-04-16 | Otsuka Pharmaceutical Co., Ltd. | IL-1α derivatives and drugs |
| DE3683910D1 (de) * | 1986-09-05 | 1992-03-26 | Cetus Corp | Oxidationsresistente muteine von beta-interferon, deren herstellung und diese muteine enthaltende praeparate. |
| JP2526965B2 (ja) * | 1987-02-24 | 1996-08-21 | 武田薬品工業株式会社 | ムテイン,dnaおよびその用途 |
| US4987070A (en) * | 1987-03-04 | 1991-01-22 | Suntory Limited | Use of a 97 amino acid leader sequence from the E. coli B-galactosidase gene for the production of hanp and hptc as fusion proteins |
| EP0377579A1 (en) * | 1987-07-07 | 1990-07-18 | California Biotechnology, Inc. | Recombinant fibroblast growth factors |
| WO1989004326A1 (en) * | 1987-11-04 | 1989-05-18 | California Biotechnology Inc. | Alveolar surfactant proteins |
| ATE198353T1 (de) * | 1988-08-24 | 2001-01-15 | American Cyanamid Co | Stabilisierung von somatotropinen durch modifikation von cystein-resten durch orts- spezifische mutagenese oder chemische derivatisierung |
| US5079230A (en) * | 1988-09-12 | 1992-01-07 | Pitman-Moore, Inc. | Stable bioactive somatotropins |
| CA2003886A1 (en) * | 1988-12-16 | 1990-06-16 | Anthony F. Purchio | Cloning and expression of simian transforming growth factor-beta 1 |
| WO1990008823A1 (en) * | 1989-01-31 | 1990-08-09 | The Upjohn Company | Somatotropin analogs |
| DE69025211T2 (de) * | 1989-02-17 | 1996-09-19 | Merck & Co Inc | Protein-Antikrebsmittel |
| US5621078A (en) * | 1989-03-22 | 1997-04-15 | Merck & Co., Inc. | Modified pseudomonas exotoxin PE40 |
| AU5355790A (en) * | 1989-04-19 | 1990-11-16 | Cetus Corporation | Multifunctional m-csf proteins and genes encoding therefor |
| US6207798B1 (en) | 1989-08-03 | 2001-03-27 | Merck & Co., Inc. | Modified PE40 toxin fusion proteins |
| US5173297A (en) * | 1991-07-01 | 1992-12-22 | Quest International Flavors & Food Ingredients Company Division Of Indopco, Inc. | Bacteriocin from lactococcus lactis subspecies lactis |
| IL98528A0 (en) * | 1990-06-21 | 1992-07-15 | Merck & Co Inc | Pharmaceutical compositions containing hybrid for killing bladder cancer cells |
| FR2671554A1 (fr) * | 1991-01-11 | 1992-07-17 | Clonatec Sa | Peptides synthetiques derivant de l'antigene hbc du virus de l'hepatite b, leurs applications a la detection d'une infection par ce virus et a la vaccination contre l'hepatite b. |
| FR2686899B1 (fr) | 1992-01-31 | 1995-09-01 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides biologiquement actifs, leur preparation et compositions pharmaceutiques les contenant. |
| US5545723A (en) * | 1994-03-15 | 1996-08-13 | Biogen Inc. | Muteins of IFN-β |
| US5814485A (en) * | 1995-06-06 | 1998-09-29 | Chiron Corporation | Production of interferon-β (IFN-β) in E. coli |
| DE19544167A1 (de) * | 1995-11-17 | 1997-05-22 | Schering Ag | Verwendung von Interferon-ß zur Behandlung von Bronchialkarzinom bei Bestrahlungstherapie |
| WO1997048808A1 (en) * | 1996-06-19 | 1997-12-24 | Chiron Corporation | Bacterial production of interferon-beta using low levels of sodium and potassium ions |
| CN1100875C (zh) * | 1998-03-06 | 2003-02-05 | 上海华晨生物技术研究所 | 新型重组人白细胞介素2的制备方法及其表达载体和工程菌 |
| CA2405550A1 (en) | 2000-04-12 | 2001-10-25 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| EP1935431A3 (en) | 2000-05-15 | 2008-08-13 | Health Research, Inc. | Cancer treatments by using a combination of an antibody against her2 and interleukin-2 |
| DE10112825A1 (de) | 2001-03-16 | 2002-10-02 | Fresenius Kabi De Gmbh | HESylierung von Wirkstoffen in wässriger Lösung |
| US6887462B2 (en) | 2001-04-09 | 2005-05-03 | Chiron Corporation | HSA-free formulations of interferon-beta |
| US20030082138A1 (en) * | 2001-09-18 | 2003-05-01 | Chiron Corporation | Methods for treating multiple sclerosis |
| KR100511749B1 (ko) * | 2001-11-06 | 2005-09-02 | 선바이오(주) | 변형된 인터페론-베타, 및 이의 화학적으로 변형된 배합체 |
| AU2002364586A1 (en) | 2001-12-21 | 2003-07-30 | Delta Biotechnology Limited | Albumin fusion proteins |
| DE10209821A1 (de) | 2002-03-06 | 2003-09-25 | Biotechnologie Ges Mittelhesse | Kopplung von Proteinen an ein modifiziertes Polysaccharid |
| DE10209822A1 (de) | 2002-03-06 | 2003-09-25 | Biotechnologie Ges Mittelhesse | Kopplung niedermolekularer Substanzen an ein modifiziertes Polysaccharid |
| AU2003255406B2 (en) | 2002-09-11 | 2009-09-10 | Fresenius Kabi Deutschland Gmbh | Hydroxyalkyl starch derivatives |
| US7538092B2 (en) | 2002-10-08 | 2009-05-26 | Fresenius Kabi Deutschland Gmbh | Pharmaceutically active oligosaccharide conjugates |
| CA2513213C (en) | 2003-01-22 | 2013-07-30 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| WO2005014655A2 (en) | 2003-08-08 | 2005-02-17 | Fresenius Kabi Deutschland Gmbh | Conjugates of hydroxyalkyl starch and a protein |
| RS53073B (sr) | 2003-11-04 | 2014-04-30 | Novartis Vaccines And Diagnostics Inc. | Upotreba antagonističkih anti-cd40 monoklonska antitela |
| AU2005227263A1 (en) * | 2004-03-05 | 2005-10-06 | Novartis Vaccines And Diagnostics, Inc. | In vitro test system for predicting patient tolerability of therapeutic agents |
| DE202005021885U1 (de) | 2004-03-11 | 2011-03-03 | Fresenius Kabi Deutschland Gmbh | Hydroxyalkylstärke-Protein-Konjugate, durch reduktive Aminierung hergestellt |
| US7642072B2 (en) * | 2004-07-26 | 2010-01-05 | Enzon Pharmaceuticals, Inc. | Optimized interferon-beta gene |
| GB0523282D0 (en) | 2005-11-15 | 2005-12-21 | Isis Innovation | Methods using pores |
| GB2453377A (en) | 2007-10-05 | 2009-04-08 | Isis Innovation | Transmembrane protein pores and molecular adapters therefore. |
| EP2070950A1 (en) | 2007-12-14 | 2009-06-17 | Fresenius Kabi Deutschland GmbH | Hydroxyalkyl starch derivatives and process for their preparation |
| EP2085095B1 (en) | 2008-01-17 | 2012-03-07 | Philogen S.p.A. | Combination of an anti-EDb fibronectin antibody-IL-2 fusion protein, and a molecule binding to B cells, B cell progenitors and/or their cancerous counterpart |
| US20110229877A1 (en) | 2008-07-07 | 2011-09-22 | Oxford Nanopore Technologies Limited | Enzyme-pore constructs |
| US9447152B2 (en) | 2008-07-07 | 2016-09-20 | Oxford Nanopore Technologies Limited | Base-detecting pore |
| US9077937B2 (en) * | 2008-11-06 | 2015-07-07 | Alcatel Lucent | Method and apparatus for fast channel change |
| GB0820927D0 (en) | 2008-11-14 | 2008-12-24 | Isis Innovation | Method |
| CA2750874A1 (en) | 2009-01-30 | 2010-08-05 | Oxford Nanopore Technologies Limited | Hybridization linkers |
| JP5843614B2 (ja) | 2009-01-30 | 2016-01-13 | オックスフォード ナノポア テクノロジーズ リミテッド | 膜貫通配列決定における核酸構築物のためのアダプター |
| GB0905140D0 (en) | 2009-03-25 | 2009-05-06 | Isis Innovation | Method |
| KR101939420B1 (ko) | 2011-02-11 | 2019-01-16 | 옥스포드 나노포어 테크놀로지즈 리미티드 | 돌연변이체 세공 |
| DK3443979T3 (da) | 2011-03-11 | 2020-08-24 | Assist Publique - Hôpitaux De Paris | Il-2-doseringsplan til behandling af systemisk lupus erythematosus |
| JP6298404B2 (ja) | 2011-07-25 | 2018-03-20 | オックスフォード ナノポール テクノロジーズ リミテッド | 膜貫通ポアを用いる二重鎖ポリヌクレオチド配列決定のためのヘアピンループ方法 |
| GB201119244D0 (en) | 2011-11-08 | 2011-12-21 | British American Tobacco Co | Smoking article |
| CN112646019B (zh) | 2012-04-10 | 2022-08-16 | 牛津纳米孔科技公开有限公司 | 突变胞溶素孔 |
| EP2875154B1 (en) | 2012-07-19 | 2017-08-23 | Oxford Nanopore Technologies Limited | SSB method for characterising a nucleic acid |
| GB201314695D0 (en) | 2013-08-16 | 2013-10-02 | Oxford Nanopore Tech Ltd | Method |
| AU2014224432B2 (en) | 2013-03-08 | 2019-10-24 | Oxford Nanopore Technologies Limited | Enzyme stalling method |
| GB201313477D0 (en) | 2013-07-29 | 2013-09-11 | Univ Leuven Kath | Nanopore biosensors for detection of proteins and nucleic acids |
| EP3013355B1 (en) | 2013-06-25 | 2019-08-07 | ICM - Institut du Cerveau et da la Moelle Epinière | Il-2 for use in treating alzheimer disease and related disorders |
| GB201403096D0 (en) | 2014-02-21 | 2014-04-09 | Oxford Nanopore Tech Ltd | Sample preparation method |
| EP2918285A1 (en) | 2014-03-11 | 2015-09-16 | Université Pierre et Marie Curie (Paris 6) | Interleukin-2 for treating food allergy |
| EP3137490B1 (en) | 2014-05-02 | 2021-01-27 | Oxford Nanopore Technologies Limited | Mutant pores |
| US10400014B2 (en) | 2014-09-01 | 2019-09-03 | Oxford Nanopore Technologies Ltd. | Mutant CsgG pores |
| US10266885B2 (en) | 2014-10-07 | 2019-04-23 | Oxford Nanopore Technologies Ltd. | Mutant pores |
| GB201418159D0 (en) | 2014-10-14 | 2014-11-26 | Oxford Nanopore Tech Ltd | Method |
| WO2016172445A2 (en) * | 2015-04-24 | 2016-10-27 | The University Of Florida Research Foundation, Inc. | Methods of identifying biologically active random peptides in plants and libraries of plants expressing candidate biologically active random peptides |
| US10876109B2 (en) | 2015-04-24 | 2020-12-29 | University Of Florida Research Foundation, Inc. | Methods of identifying biologically active random peptides in prokaryotic cells and libraries of prokaryotic cells expressing candidate biologically active random peptides |
| US10801023B2 (en) * | 2015-04-24 | 2020-10-13 | University Of Florida Research Foundation, Inc. | Methods of identifying biologically active random peptides in plants and libraries of plants expressing candidate biologically active random peptides |
| JP7038655B2 (ja) | 2015-10-22 | 2022-03-18 | イルトゥー・ファルマ | Il-2医薬組成物 |
| GB201609220D0 (en) | 2016-05-25 | 2016-07-06 | Oxford Nanopore Tech Ltd | Method |
| EP3475413B1 (en) | 2016-06-22 | 2024-02-14 | David Klatzmann | Genetically modified t lymphocytes |
| JP7165717B2 (ja) | 2017-03-15 | 2022-11-04 | パンディオン・オペレーションズ・インコーポレイテッド | 標的免疫寛容 |
| MX2019013517A (es) | 2017-05-24 | 2020-08-17 | Pandion Operations Inc | Inmunotolerancia dirigida. |
| USRE50550E1 (en) | 2017-12-06 | 2025-08-26 | Pandion Operations, Inc. | IL-2 muteins and uses thereof |
| US10174091B1 (en) | 2017-12-06 | 2019-01-08 | Pandion Therapeutics, Inc. | IL-2 muteins |
| US10946068B2 (en) | 2017-12-06 | 2021-03-16 | Pandion Operations, Inc. | IL-2 muteins and uses thereof |
| EP3752178A1 (en) | 2018-02-16 | 2020-12-23 | Iltoo Pharma | Use of interleukin 2 for treating sjögren's syndrome |
| GB201807793D0 (en) | 2018-05-14 | 2018-06-27 | Oxford Nanopore Tech Ltd | Method |
| WO2019241315A1 (en) | 2018-06-12 | 2019-12-19 | Obsidian Therapeutics, Inc. | Pde5 derived regulatory constructs and methods of use in immunotherapy |
| WO2020007937A1 (en) | 2018-07-03 | 2020-01-09 | Iltoo Pharma | Use of interleukin-2 for treating systemic sclerosis |
| US12403181B2 (en) | 2018-08-13 | 2025-09-02 | Iltoo Pharma | Combination of interleukin-2 with an interleukin 1 inhibitor, conjugates and therapeutic uses thereof |
| US12352765B2 (en) | 2018-11-15 | 2025-07-08 | The Board Of Trustees Of The Leland Stanford Junior University | Compositions and methods of prognosis and classification for preeclampsia |
| EP3972992A4 (en) | 2019-05-20 | 2023-07-19 | Pandion Operations, Inc. | MADCAM TARGETED IMMUNOTLERANCE |
| KR20220139293A (ko) | 2019-12-12 | 2022-10-14 | 일투 파마 | 인터류킨 2 키메라 구축물 |
| WO2021168079A1 (en) | 2020-02-21 | 2021-08-26 | Pandion Operations, Inc. | Tissue targeted immunotolerance with a cd39 effector |
| CA3166887A1 (en) | 2020-03-06 | 2021-09-10 | Gilbert BENSIMON | Low dose human interleukin-2 for the treatment of amyotrophic lateral sclerosis |
| WO2021221485A1 (ko) * | 2020-04-29 | 2021-11-04 | 에이비온 주식회사 | 이중 돌연변이를 가지는 인간 인터페론-베타 변이체 및 인간 인터페론-베타 변이체의 안정성을 향상시키는 방법 |
| CN116075523A (zh) * | 2020-04-29 | 2023-05-05 | 基因制药株式会社 | 具有融合的干扰素-β突变蛋白和抗体的重组蛋白以及包含其的药物组合物 |
| WO2022045935A1 (en) * | 2020-08-28 | 2022-03-03 | Joint Stock Company "Biocad" | Aav5-based vaccine against sars-cov-2 |
| MX2024004291A (es) | 2021-10-06 | 2024-06-28 | Iltoo Pharma | Construcciones quiméricas de interleucina 2 con especificidad de direccionamiento a tejidos inflamados. |
| KR20240038789A (ko) * | 2022-05-24 | 2024-03-25 | 제이에이치엠 바이오파마슈티컬 (항저우) 씨오., 엘티디. | 재조합 보툴리눔 신경독소 a형 및 이의 제조 방법 |
| KR20250039519A (ko) | 2022-06-16 | 2025-03-20 | 세파론 엘엘씨 | 항-pd-1 항체-약화된 il-2 면역접합체 및 그의 용도 |
| CA3265946A1 (en) | 2022-09-12 | 2024-03-21 | Univ Sorbonne | INTERLEUKIN-2 FOR THE TREATMENT OF AUTISM SPECTRUM DISORDERS |
| WO2024121173A1 (en) | 2022-12-05 | 2024-06-13 | Centre Hospitalier Universitaire De Nimes | Low dose human interleukin-2 for the treatment of amyotrophic lateral sclerosis in a subgroup of patients |
| WO2025032158A1 (en) | 2023-08-08 | 2025-02-13 | Institut National de la Santé et de la Recherche Médicale | Method to treat tauopathies |
Family Cites Families (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5359688A (en) * | 1976-11-11 | 1978-05-29 | Tanpakushitsu Kenkiyuu Shiyour | Production of novel polypeptide |
| US4399216A (en) * | 1980-02-25 | 1983-08-16 | The Trustees Of Columbia University | Processes for inserting DNA into eucaryotic cells and for producing proteinaceous materials |
| FI88175C (fi) * | 1980-04-03 | 1993-04-13 | Biogen Inc | Rekombinant-dna-molekyler och foerfaranden foer framstaellning av polypeptider liknande humant -interferon |
| JPS58110548A (ja) * | 1981-12-24 | 1983-07-01 | Asahi Chem Ind Co Ltd | 新規な生理活性ペプチド |
| US6936694B1 (en) * | 1982-05-06 | 2005-08-30 | Intermune, Inc. | Manufacture and expression of large structural genes |
| IE56026B1 (en) * | 1982-10-19 | 1991-03-27 | Cetus Corp | Cysteine-depleted muteins of biologically active proteins |
| IL71951A0 (en) * | 1983-06-01 | 1984-09-30 | Hoffmann La Roche | Polypeptides having interferon activity,their preparation and pharmaceutical compositions containing them |
| WO1985000817A1 (en) * | 1983-08-10 | 1985-02-28 | Amgen | Microbial expression of interleukin ii |
| US4959314A (en) * | 1984-11-09 | 1990-09-25 | Cetus Corporation | Cysteine-depleted muteins of biologically active proteins |
-
1983
- 1983-10-10 IE IE2380/83A patent/IE56026B1/en active Protection Beyond IP Right Term
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