CA2488218C - Therapeutic epitopes and uses thereof - Google Patents
Therapeutic epitopes and uses thereof Download PDFInfo
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- CA2488218C CA2488218C CA2488218A CA2488218A CA2488218C CA 2488218 C CA2488218 C CA 2488218C CA 2488218 A CA2488218 A CA 2488218A CA 2488218 A CA2488218 A CA 2488218A CA 2488218 C CA2488218 C CA 2488218C
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- WCPAKWJPBJAGKN-UHFFFAOYSA-N oxadiazole Chemical compound C1=CON=N1 WCPAKWJPBJAGKN-UHFFFAOYSA-N 0.000 description 1
- 101800002712 p27 Proteins 0.000 description 1
- 230000008506 pathogenesis Effects 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- LWTDZKXXJRRKDG-UHFFFAOYSA-N phaseollin Natural products C1OC2=CC(O)=CC=C2C2C1C1=CC=C3OC(C)(C)C=CC3=C1O2 LWTDZKXXJRRKDG-UHFFFAOYSA-N 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 230000008121 plant development Effects 0.000 description 1
- 230000008635 plant growth Effects 0.000 description 1
- 108010040003 polyglutamine Proteins 0.000 description 1
- 229920000155 polyglutamine Polymers 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 230000001902 propagating effect Effects 0.000 description 1
- 230000000069 prophylactic effect Effects 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000003252 repetitive effect Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 235000009566 rice Nutrition 0.000 description 1
- 239000004248 saffron Substances 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
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- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 210000000813 small intestine Anatomy 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- YEENEYXBHNNNGV-XEHWZWQGSA-M sodium;3-acetamido-5-[acetyl(methyl)amino]-2,4,6-triiodobenzoate;(2r,3r,4s,5s,6r)-2-[(2r,3s,4s,5r)-3,4-dihydroxy-2,5-bis(hydroxymethyl)oxolan-2-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol Chemical compound [Na+].CC(=O)N(C)C1=C(I)C(NC(C)=O)=C(I)C(C([O-])=O)=C1I.O[C@H]1[C@H](O)[C@@H](CO)O[C@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 YEENEYXBHNNNGV-XEHWZWQGSA-M 0.000 description 1
- 230000030118 somatic embryogenesis Effects 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 238000007619 statistical method Methods 0.000 description 1
- 239000008174 sterile solution Substances 0.000 description 1
- 235000020790 strict gluten-free diet Nutrition 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- YROXIXLRRCOBKF-UHFFFAOYSA-N sulfonylurea Chemical compound OC(=N)N=S(=O)=O YROXIXLRRCOBKF-UHFFFAOYSA-N 0.000 description 1
- 230000002123 temporal effect Effects 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 229940104230 thymidine Drugs 0.000 description 1
- 239000004408 titanium dioxide Substances 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
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- 238000013519 translation Methods 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
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- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 239000003981 vehicle Substances 0.000 description 1
- 238000011179 visual inspection Methods 0.000 description 1
- 239000011534 wash buffer Substances 0.000 description 1
- 239000008215 water for injection Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/415—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
- A61P1/04—Drugs for disorders of the alimentary tract or the digestive system for ulcers, gastritis or reflux esophagitis, e.g. antacids, inhibitors of acid secretion, mucosal protectants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
-
- 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
-
- 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
- A61P37/02—Immunomodulators
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- General Chemical & Material Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Animal Behavior & Ethology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Botany (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Hematology (AREA)
- Obesity (AREA)
- Diabetes (AREA)
- Transplantation (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Breeding Of Plants And Reproduction By Means Of Culturing (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Medicines Containing Plant Substances (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB0212885.8 | 2002-06-05 | ||
| GBGB0212885.8A GB0212885D0 (en) | 2002-06-05 | 2002-06-05 | Therapeutic epitopes and uses thereof |
| PCT/GB2003/002450 WO2003104273A2 (en) | 2002-06-05 | 2003-06-05 | Therapeutic epitopes and uses thereof |
Publications (2)
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|---|---|
| CA2488218A1 CA2488218A1 (en) | 2003-12-18 |
| CA2488218C true CA2488218C (en) | 2020-11-10 |
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| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2488218A Expired - Lifetime CA2488218C (en) | 2002-06-05 | 2003-06-05 | Therapeutic epitopes and uses thereof |
Country Status (15)
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|---|---|
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| EP (3) | EP1513873B1 (cg-RX-API-DMAC7.html) |
| JP (6) | JP2006512893A (cg-RX-API-DMAC7.html) |
| AU (1) | AU2003244771B2 (cg-RX-API-DMAC7.html) |
| CA (1) | CA2488218C (cg-RX-API-DMAC7.html) |
| CY (1) | CY1115730T1 (cg-RX-API-DMAC7.html) |
| DK (1) | DK1513873T3 (cg-RX-API-DMAC7.html) |
| ES (1) | ES2510440T3 (cg-RX-API-DMAC7.html) |
| GB (1) | GB0212885D0 (cg-RX-API-DMAC7.html) |
| MX (2) | MXPA04012117A (cg-RX-API-DMAC7.html) |
| NZ (1) | NZ537226A (cg-RX-API-DMAC7.html) |
| PT (1) | PT1513873E (cg-RX-API-DMAC7.html) |
| SI (1) | SI1513873T1 (cg-RX-API-DMAC7.html) |
| WO (1) | WO2003104273A2 (cg-RX-API-DMAC7.html) |
| ZA (1) | ZA200409740B (cg-RX-API-DMAC7.html) |
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| GB9923306D0 (en) | 1999-10-01 | 1999-12-08 | Isis Innovation | Diagnostic and therapeutic epitope, and transgenic plant |
| EP2409711B1 (en) | 2002-02-14 | 2018-11-21 | The Board of Trustees of the Leland Stanford Junior University | Enzyme treatment of foodstuffs for celiac sprue |
| US8143210B2 (en) | 2002-02-14 | 2012-03-27 | The Board Of Trustees Of The Leland Stanford Junior University | Enzyme treatment of foodstuffs for celiac sprue |
| US7462688B2 (en) * | 2002-05-14 | 2008-12-09 | The Board Of Trustees Of The Leland Stanford Junior University | Peptides for diagnostic and therapeutic methods for celiac sprue |
| AU2003234634A1 (en) * | 2002-05-14 | 2003-12-02 | Felix Hausch | Drug therapy for celiac sprue |
| WO2004045392A2 (en) * | 2002-11-20 | 2004-06-03 | The Board Of Trustees Of The Leland Stanford Junior University | Diagnostic method for celiac sprue |
| US7202216B2 (en) * | 2002-05-14 | 2007-04-10 | The Board Of Trustees Of The Leland Stanford Junior University | Drug therapy for celiac sprue |
| US7265093B2 (en) * | 2002-05-14 | 2007-09-04 | The Board Of Trustees Of The Leland Stanford Junior University | Drug therapy for Celiac Sprue |
| GB0212885D0 (en) | 2002-06-05 | 2002-07-17 | Isis Innovation | Therapeutic epitopes and uses thereof |
| US7579313B2 (en) | 2003-11-18 | 2009-08-25 | The Board Of Trustees Of The Leland Stanford Junior University | Transglutaminase inhibitors and methods of use thereof |
| EP1765395B1 (en) * | 2004-04-16 | 2011-02-09 | The Governors of the University of Alberta | Anti-gluten egg yolk antibodies for the treatment of celiac disease |
| US7628985B2 (en) * | 2004-04-26 | 2009-12-08 | The Board Of Regents Of The Leland Stanford Junior University | Therapeutic enzyme formulations and uses thereof in celiac sprue and/or dermatitis herpetoformis |
| US7534426B2 (en) * | 2004-04-26 | 2009-05-19 | The Board Of Trustees Of The Leland Stanford Junior University | Glutenase enzyme assays |
| US7563864B2 (en) * | 2004-04-26 | 2009-07-21 | Celiac Sprue Research Foundation | Prolyl endopeptidase mediated destruction of T cell epitopes in whole gluten |
| AU2011247868B2 (en) * | 2004-04-28 | 2014-05-22 | Btg International Limited | Epitopes related to coeliac disease |
| EP2412380B1 (en) * | 2004-04-28 | 2021-01-06 | BTG International Limited | Epitopes related to coeliac disease |
| US10105437B2 (en) | 2004-04-28 | 2018-10-23 | Btg International Limited | Epitopes related to coeliac disease |
| EP2136833B1 (en) | 2007-03-16 | 2019-05-01 | The Board of Trustees of the Leland Stanford Junior University | Combination enzyme therapy for digestion of dietary gluten |
| US8282928B2 (en) | 2007-05-30 | 2012-10-09 | The Governors Of The University Of Alberta | Anti-gluten egg yolk antibodies for the treatment of celiac disease |
| DE102007044673A1 (de) * | 2007-09-18 | 2009-03-19 | Zimmer, Klaus-Peter, Prof. Dr. med. | Impfstoff zur Behandlung von Zöliakie und Verfahren zur Herstellung des Impfstoffes, Verwendung einer mit einem bakteriellen Toxin konjugierten Peptidsequenz zur Aktivierung des Immunsystems gegen Prolamine sowie Designerpeptid |
| AU2013204429B9 (en) * | 2008-11-30 | 2017-01-05 | Immusant, Inc. | Compositions and methods for treatment of celiac disease |
| MX346450B (es) | 2008-11-30 | 2017-03-17 | Immusant Inc * | Composiciones y métodos para el tratamiento de la enfermedad celíaca. |
| US9518087B2 (en) | 2010-08-10 | 2016-12-13 | Ecole Polytechnique Federale De Lausanne (Epfl) | Erythrocyte-binding therapeutics |
| US9517257B2 (en) | 2010-08-10 | 2016-12-13 | Ecole Polytechnique Federale De Lausanne (Epfl) | Erythrocyte-binding therapeutics |
| US9850296B2 (en) | 2010-08-10 | 2017-12-26 | Ecole Polytechnique Federale De Lausanne (Epfl) | Erythrocyte-binding therapeutics |
| US20140037661A1 (en) * | 2011-02-08 | 2014-02-06 | Phadia Ab | Wheat Antigens and Peptides for Diagnosis of Wheat Induced Hypersensitivity |
| ES2402286B1 (es) * | 2011-09-29 | 2014-03-04 | Universidad De Valladolid | Péptido inmunogénico del gluten y sus aplicaciones. |
| CA3191015A1 (en) | 2012-02-07 | 2013-08-15 | Vibrant Holdings, Llc | Substrates, peptide arrays, and methods |
| US10006909B2 (en) | 2012-09-28 | 2018-06-26 | Vibrant Holdings, Llc | Methods, systems, and arrays for biomolecular analysis |
| US10286376B2 (en) | 2012-11-14 | 2019-05-14 | Vibrant Holdings, Llc | Substrates, systems, and methods for array synthesis and biomolecular analysis |
| CA2923379C (en) | 2013-02-15 | 2023-01-03 | Vibrant Holdings, Llc | Methods and compositions for amplified electrochemiluminescence detection |
| EP3043812A1 (en) | 2013-09-10 | 2016-07-20 | Immusant Inc. | Dosage of a gluten peptide composition |
| US10946079B2 (en) | 2014-02-21 | 2021-03-16 | Ecole Polytechnique Federale De Lausanne | Glycotargeting therapeutics |
| US10953101B2 (en) | 2014-02-21 | 2021-03-23 | École Polytechnique Fédérale De Lausanne (Epfl) | Glycotargeting therapeutics |
| US10046056B2 (en) | 2014-02-21 | 2018-08-14 | École Polytechnique Fédérale De Lausanne (Epfl) | Glycotargeting therapeutics |
| CN106456743A (zh) | 2014-02-21 | 2017-02-22 | 洛桑聚合联合学院 | 糖靶向性治疗剂 |
| WO2015164747A1 (en) | 2014-04-24 | 2015-10-29 | Immusant, Inc. | Methods for diagnosing celiac disease using circulating cytokines/chemokines |
| JP6887945B2 (ja) * | 2014-09-10 | 2021-06-16 | ヴィブラント ホールディングス リミテッド ライアビリティ カンパニー | セリアック病に関するペプチドマイクロアレイおよび新規バイオマーカー |
| CA2962933A1 (en) | 2014-09-29 | 2016-04-07 | Immusant, Inc. | Use of hla genetic status to assess or select treatment of celiac disease |
| US10473647B1 (en) | 2014-11-21 | 2019-11-12 | Immusant, Inc. | Peptides for use in treatment and diagnosis of type 1 diabetes |
| EP3109255A1 (en) * | 2015-06-26 | 2016-12-28 | Institut National De La Recherche Agronomique | Immunogenic composition |
| EP3313868A1 (en) * | 2015-06-26 | 2018-05-02 | Institut National De La Recherche Agronomique (INRA) | Immunogenic composition |
| WO2017146118A1 (ja) * | 2016-02-23 | 2017-08-31 | 田中貴金属工業株式会社 | グリアジン検出用免疫クロマト分析装置、免疫クロマト分析キットおよび免疫クロマト分析方法 |
| WO2018218250A2 (en) | 2017-05-26 | 2018-11-29 | Vibrant Holdings, Llc | Photoactive compounds and methods for biomolecule detection and sequencing |
| EP3638296A1 (en) | 2017-06-16 | 2020-04-22 | The University Of Chicago | Compositions and methods for inducing immune tolerance |
| JP6568193B2 (ja) * | 2017-12-19 | 2019-08-28 | ホーユー株式会社 | エピトープ |
| KR20210010879A (ko) | 2018-05-09 | 2021-01-28 | 더 유니버서티 오브 시카고 | 면역 관용 관여 조성물 및 방법 |
| AU2019266303B2 (en) | 2018-05-09 | 2025-12-18 | Vibrant Holdings, Llc | Methods of synthesizing a polynucleotide array using photactivated agents |
| CA3145972A1 (en) * | 2019-07-04 | 2021-01-07 | Ukko Inc. | De-epitoped alpha gliadin and use of same for the management of celiac disease and gluten sensitivity |
| CN114761028A (zh) | 2019-09-27 | 2022-07-15 | 英特瑞克斯顿阿克图比奥帝克斯有限公司 | 乳糜泻的治疗 |
| GB202113858D0 (en) * | 2021-09-28 | 2021-11-10 | Nextera As | Peptides |
| CN115124606B (zh) * | 2022-06-27 | 2025-03-28 | 上海理工大学 | 含有氨基酸结构pqqp的寡肽及其制备方法和应用 |
Family Cites Families (86)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4459355A (en) | 1982-07-12 | 1984-07-10 | International Paper Company | Method for transforming plant cells |
| US4536475A (en) | 1982-10-05 | 1985-08-20 | Phytogen | Plant vector |
| NL8300698A (nl) | 1983-02-24 | 1984-09-17 | Univ Leiden | Werkwijze voor het inbouwen van vreemd dna in het genoom van tweezaadlobbige planten; agrobacterium tumefaciens bacterien en werkwijze voor het produceren daarvan; planten en plantecellen met gewijzigde genetische eigenschappen; werkwijze voor het bereiden van chemische en/of farmaceutische produkten. |
| JPS6047683A (ja) | 1983-08-24 | 1985-03-15 | Kirin Brewery Co Ltd | プロモ−タ− |
| US5036006A (en) | 1984-11-13 | 1991-07-30 | Cornell Research Foundation, Inc. | Method for transporting substances into living cells and tissues and apparatus therefor |
| US5100792A (en) | 1984-11-13 | 1992-03-31 | Cornell Research Foundation, Inc. | Method for transporting substances into living cells and tissues |
| US4945050A (en) | 1984-11-13 | 1990-07-31 | Cornell Research Foundation, Inc. | Method for transporting substances into living cells and tissues and apparatus therefor |
| US4943674A (en) | 1987-05-26 | 1990-07-24 | Calgene, Inc. | Fruit specific transcriptional factors |
| DK162399C (da) | 1986-01-28 | 1992-03-23 | Danisco | Fremgangsmaade til ekspression af gener i baelgplanteceller, dna-fragment, rekombineret dna-fragment samt plasmid til brug ved udoevelsen af fremgangsmaaden |
| EP0242236B2 (en) | 1986-03-11 | 1996-08-21 | Plant Genetic Systems N.V. | Plant cells resistant to glutamine synthetase inhibitors, made by genetic engineering |
| US5107065A (en) | 1986-03-28 | 1992-04-21 | Calgene, Inc. | Anti-sense regulation of gene expression in plant cells |
| US5177010A (en) | 1986-06-30 | 1993-01-05 | University Of Toledo | Process for transforming corn and the products thereof |
| US5187073A (en) | 1986-06-30 | 1993-02-16 | The University Of Toledo | Process for transforming gramineae and the products thereof |
| NZ221259A (en) | 1986-07-31 | 1990-05-28 | Calgene Inc | Seed specific transcriptional regulation |
| EP0267159A3 (de) | 1986-11-07 | 1990-05-02 | Ciba-Geigy Ag | Verfahren zur genetischen Modifikation monokotyler Pflanzen |
| US4866247A (en) | 1986-12-11 | 1989-09-12 | The Lincoln Electric Company | Apparatus and method of short circuiting arc welding |
| US4971908A (en) | 1987-05-26 | 1990-11-20 | Monsanto Company | Glyphosate-tolerant 5-enolpyruvyl-3-phosphoshikimate synthase |
| US5356799A (en) | 1988-02-03 | 1994-10-18 | Pioneer Hi-Bred International, Inc. | Antisense gene systems of pollination control for hybrid seed production |
| US5371014A (en) | 1988-02-12 | 1994-12-06 | Daicel Chemical Industries, Ltd. | Process for the production of optically active 2-hydroxy acid esters using microbes to reduce the 2-oxo precursor |
| US5179022A (en) | 1988-02-29 | 1993-01-12 | E. I. Du Pont De Nemours & Co. | Biolistic apparatus for delivering substances into cells and tissues in a non-lethal manner |
| US5614395A (en) | 1988-03-08 | 1997-03-25 | Ciba-Geigy Corporation | Chemically regulatable and anti-pathogenic DNA sequences and uses thereof |
| US5250515A (en) | 1988-04-11 | 1993-10-05 | Monsanto Company | Method for improving the efficacy of insect toxins |
| US5565346A (en) | 1988-07-27 | 1996-10-15 | Calgene, Inc. | Transformation and regeneration system for legumes |
| US5428146A (en) | 1988-11-07 | 1995-06-27 | Max-Planck-Gesellschaft Zur Forderung | Wound-stimulated DNA-sequence from solanum tuberosum and its use |
| US5110732A (en) | 1989-03-14 | 1992-05-05 | The Rockefeller University | Selective gene expression in plants |
| US5086169A (en) | 1989-04-20 | 1992-02-04 | The Research Foundation Of State University Of New York | Isolated pollen-specific promoter of corn |
| US5629183A (en) | 1989-05-08 | 1997-05-13 | The United States Of America As Represented By The Secretary Of Agriculture | Plant transformation by gene transfer into pollen |
| US5097025A (en) | 1989-08-01 | 1992-03-17 | The Rockefeller University | Plant promoters |
| US5550318A (en) | 1990-04-17 | 1996-08-27 | Dekalb Genetics Corporation | Methods and compositions for the production of stably transformed, fertile monocot plants and cells thereof |
| US7705215B1 (en) | 1990-04-17 | 2010-04-27 | Dekalb Genetics Corporation | Methods and compositions for the production of stably transformed, fertile monocot plants and cells thereof |
| HU218465B (hu) | 1989-08-09 | 2000-09-28 | Dekalb Genetics Corporation | Eljárások és kompozíciók stabilan transzformált, termő egyszikű növények és sejtjeik előállítására |
| US4919813A (en) | 1989-08-25 | 1990-04-24 | The United States Of America As Represented By The Department Of Energy | Photoenhanced anaerobic digestion of organic acids |
| DE69034138T2 (de) | 1989-10-27 | 2005-05-12 | The Salk Institute For Biological Studies, La Jolla | Rezeptorverbindungen von glutamin und herstellung |
| US5589583A (en) | 1990-01-11 | 1996-12-31 | Monsanto Company | Plant promoter |
| US5484956A (en) | 1990-01-22 | 1996-01-16 | Dekalb Genetics Corporation | Fertile transgenic Zea mays plant comprising heterologous DNA encoding Bacillus thuringiensis endotoxin |
| HU220773B1 (hu) | 1990-01-22 | 2002-05-28 | Dekalb Genetics Corporation | Eljárás termő transzgenikus kukoricanövények előállítására |
| EP0442174A1 (en) | 1990-02-13 | 1991-08-21 | Pioneer Hi-Bred International, Inc. | Stable transformation of plant cells |
| US5618988A (en) | 1990-03-02 | 1997-04-08 | Amoco Corporation | Enhanced carotenoid accumulation in storage organs of genetically engineered plants |
| US5204253A (en) | 1990-05-29 | 1993-04-20 | E. I. Du Pont De Nemours And Company | Method and apparatus for introducing biological substances into living cells |
| US5187267A (en) | 1990-06-19 | 1993-02-16 | Calgene, Inc. | Plant proteins, promoters, coding sequences and use |
| ES2173077T3 (es) | 1990-06-25 | 2002-10-16 | Monsanto Technology Llc | Plantas que toleran glifosato. |
| NZ239977A (en) | 1990-11-14 | 1993-08-26 | Pioneer Hi Bred Int | Transforming plants by the use of agrobacterium |
| US5932782A (en) | 1990-11-14 | 1999-08-03 | Pioneer Hi-Bred International, Inc. | Plant transformation method using agrobacterium species adhered to microprojectiles |
| AU9054291A (en) | 1990-11-26 | 1992-06-25 | E.I. Du Pont De Nemours And Company | Herbicidal oxazine ethers |
| US5459252A (en) | 1991-01-31 | 1995-10-17 | North Carolina State University | Root specific gene promoter |
| AU1202192A (en) | 1991-02-07 | 1992-09-07 | Plant Genetic Systems N.V. | Stamen-specific promoters from corn |
| IL101508A0 (en) | 1991-04-08 | 1992-12-30 | Rhone Poulenc Agrochimie | Chimeric plant genes based on upstream regulatory elements of helianthinin |
| ES2163400T3 (es) | 1991-05-15 | 2002-02-01 | Monsanto Technology Llc | Metodo de creacion de una planta de arroz transformada. |
| AU2515592A (en) | 1991-08-23 | 1993-03-16 | University Of Florida | A novel method for the production of transgenic plants |
| EP1983056A1 (en) | 1992-07-07 | 2008-10-22 | Japan Tobacco Inc. | Method for transforming monocotyledons |
| CA2148258A1 (en) | 1992-10-29 | 1994-05-11 | Nicholas Barrie La Thangue | Transcription factor dp-1 |
| US5389226A (en) | 1992-12-17 | 1995-02-14 | Amorphous Technologies International, Inc. | Electrodeposition of nickel-tungsten amorphous and microcrystalline coatings |
| TW404844B (en) | 1993-04-08 | 2000-09-11 | Oxford Biosciences Ltd | Needleless syringe |
| AU6819194A (en) | 1993-05-03 | 1994-11-21 | Cornell Research Foundation Inc. | Isolated dna elements that direct pistil-specific and anther-specific gene expression and methods of using same |
| US5670349A (en) | 1993-08-02 | 1997-09-23 | Virginia Tech Intellectual Properties, Inc. | HMG2 promoter expression system and post-harvest production of gene products in plants and plant cell cultures |
| AU687863B2 (en) | 1993-09-03 | 1998-03-05 | Japan Tobacco Inc. | Method of transforming monocotyledon by using scutellum of immature embryo |
| US5495007A (en) | 1994-04-29 | 1996-02-27 | Thompson; Gary A. | Phloem-specific promoter |
| US5633363A (en) | 1994-06-03 | 1997-05-27 | Iowa State University, Research Foundation In | Root preferential promoter |
| US5646333A (en) | 1994-09-02 | 1997-07-08 | Drexel University | Plant promoter useful for directing the expression of foreign proteins to the plant epidermis |
| HUT76355A (en) | 1995-11-24 | 1997-08-28 | Bay Zoltan Alkalmazott Kutatas | Plant gene-expression vector family based on dna fragments regulating alfalfa h3 histon gene variant (ms h3g1) |
| US6036983A (en) | 1996-05-20 | 2000-03-14 | Novo Nordisk A/S | Method of obtaining protein hydrolysates |
| WO1997047647A1 (es) | 1996-06-13 | 1997-12-18 | Consejo Superior De Investigaciones Cientificas | Proteinas vegetales |
| GB9624456D0 (en) | 1996-11-25 | 1997-01-15 | Isis Innovation | Assay method |
| US5977436A (en) | 1997-04-09 | 1999-11-02 | Rhone Poulenc Agrochimie | Oleosin 5' regulatory region for the modification of plant seed lipid composition |
| US5959175A (en) | 1997-04-09 | 1999-09-28 | Thomas; Terry L. | Sunflower albumin 5' regulatory region for the modification of plant seed lipid composition |
| ES2132025B1 (es) | 1997-06-12 | 2000-12-01 | Consejo Superior Investigacion | Proteinas urag de las plantas. |
| EP0905518A1 (en) * | 1997-09-23 | 1999-03-31 | Academisch Ziekenhuis Leiden | Peptides specific for gluten-sensitive T-cells and use thereof |
| US6100450A (en) | 1997-10-22 | 2000-08-08 | Rhone-Poulenc Agrochimie | Seed specific promoters based on arabidopsis genes |
| US6232445B1 (en) | 1997-10-29 | 2001-05-15 | Sunol Molecular Corporation | Soluble MHC complexes and methods of use thereof |
| AU3478599A (en) | 1998-04-09 | 1999-11-01 | E.I. Du Pont De Nemours And Company | Cell cycle regulatory proteins |
| JP2002514423A (ja) | 1998-05-08 | 2002-05-21 | コンセホ・スペリオル・デ・インヴェスティガシオンス・シエンティフィカス | 組換え植物ｅ２ｆペプチドを発現するトランスジェニック植物細胞 |
| EP1108031A2 (en) * | 1998-09-03 | 2001-06-20 | Pia Vaag | 17 kDa FOAM PROTEIN |
| AU3230200A (en) | 1999-02-12 | 2000-08-29 | Pioneer Hi-Bred International, Inc. | Transgenic plants with modified expression of the dp protein |
| GB9923306D0 (en) | 1999-10-01 | 1999-12-08 | Isis Innovation | Diagnostic and therapeutic epitope, and transgenic plant |
| EP1377604B1 (en) * | 2001-04-12 | 2014-12-31 | Academisch Ziekenhuis Leiden | Methods and means for use of hla-dq restricted t-cell receptors and hla-dq-binding prolamine-derived peptides |
| EP1332760A1 (en) * | 2002-02-04 | 2003-08-06 | Academisch Ziekenhuis Leiden | Novel epitopes for celiac disease and autoimmune diseases, methods for detecting those and novel non-antigenic food compounds |
| EP2409711B1 (en) * | 2002-02-14 | 2018-11-21 | The Board of Trustees of the Leland Stanford Junior University | Enzyme treatment of foodstuffs for celiac sprue |
| US7320788B2 (en) * | 2002-02-14 | 2008-01-22 | The Board Of Trustees Of The Leland Stanford Junior University | Enzyme treatment of foodstuffs for Celiac Sprue |
| WO2004045392A2 (en) | 2002-11-20 | 2004-06-03 | The Board Of Trustees Of The Leland Stanford Junior University | Diagnostic method for celiac sprue |
| US7202216B2 (en) | 2002-05-14 | 2007-04-10 | The Board Of Trustees Of The Leland Stanford Junior University | Drug therapy for celiac sprue |
| AU2003234634A1 (en) | 2002-05-14 | 2003-12-02 | Felix Hausch | Drug therapy for celiac sprue |
| GB0212885D0 (en) * | 2002-06-05 | 2002-07-17 | Isis Innovation | Therapeutic epitopes and uses thereof |
| US6992916B2 (en) | 2003-06-13 | 2006-01-31 | Taiwan Semiconductor Manufacturing Co., Ltd. | SRAM cell design with high resistor CMOS gate structure for soft error rate improvement |
| EP2412380B1 (en) | 2004-04-28 | 2021-01-06 | BTG International Limited | Epitopes related to coeliac disease |
| MX346450B (es) * | 2008-11-30 | 2017-03-17 | Immusant Inc * | Composiciones y métodos para el tratamiento de la enfermedad celíaca. |
| JP6520175B2 (ja) | 2015-02-10 | 2019-05-29 | 富士通株式会社 | 無線通信装置、基地局システム及び無線通信装置制御方法 |
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