SK284856B6 - Imunogénna molekula, farmaceutická kompozícia, ligand, spôsob prípravy imunogénnej molekuly a jej použitie - Google Patents
Imunogénna molekula, farmaceutická kompozícia, ligand, spôsob prípravy imunogénnej molekuly a jej použitie Download PDFInfo
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- SK284856B6 SK284856B6 SK1181-98A SK118198A SK284856B6 SK 284856 B6 SK284856 B6 SK 284856B6 SK 118198 A SK118198 A SK 118198A SK 284856 B6 SK284856 B6 SK 284856B6
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/42—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against immunoglobulins
- C07K16/4283—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against immunoglobulins against an allotypic or isotypic determinant on Ig
- C07K16/4291—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against immunoglobulins against an allotypic or isotypic determinant on Ig against IgE
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
-
- 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
- A61P37/08—Antiallergic agents
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/34—Identification of a linear epitope shorter than 20 amino acid residues or of a conformational epitope defined by amino acid residues
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/52—Constant or Fc region; Isotype
- C07K2317/528—CH4 domain
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Immunology (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pulmonology (AREA)
- Microbiology (AREA)
- Mycology (AREA)
- Epidemiology (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GBGB9604412.8A GB9604412D0 (en) | 1996-03-01 | 1996-03-01 | Organic compounds |
| GBGB9617702.7A GB9617702D0 (en) | 1996-08-22 | 1996-08-22 | Organic compounds |
| PCT/EP1997/001013 WO1997031948A1 (en) | 1996-03-01 | 1997-02-28 | Peptide immunogens for vaccination against and treatment of allergy |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| SK118198A3 SK118198A3 (en) | 1999-03-12 |
| SK284856B6 true SK284856B6 (sk) | 2006-01-05 |
Family
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Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| SK1181-98A SK284856B6 (sk) | 1996-03-01 | 1997-02-28 | Imunogénna molekula, farmaceutická kompozícia, ligand, spôsob prípravy imunogénnej molekuly a jej použitie |
Country Status (25)
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|---|---|
| US (1) | US6610297B1 (da) |
| EP (1) | EP0885244B2 (da) |
| JP (2) | JP3421970B2 (da) |
| KR (2) | KR100584051B1 (da) |
| CN (1) | CN1174998C (da) |
| AT (1) | ATE230417T1 (da) |
| AU (1) | AU719609B2 (da) |
| BR (1) | BR9707819A (da) |
| CA (1) | CA2245497C (da) |
| CY (1) | CY2457B1 (da) |
| CZ (1) | CZ299551B6 (da) |
| DE (1) | DE69718150T3 (da) |
| DK (1) | DK0885244T4 (da) |
| ES (1) | ES2190799T5 (da) |
| HK (1) | HK1014962A1 (da) |
| HU (1) | HUP9901109A3 (da) |
| IL (1) | IL125590A (da) |
| NO (1) | NO321043B1 (da) |
| NZ (1) | NZ331651A (da) |
| PL (1) | PL187209B1 (da) |
| RU (1) | RU2193413C2 (da) |
| SI (1) | SI0885244T2 (da) |
| SK (1) | SK284856B6 (da) |
| TR (1) | TR199801722T2 (da) |
| WO (1) | WO1997031948A1 (da) |
Families Citing this family (32)
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| US6913749B2 (en) | 1998-11-02 | 2005-07-05 | Resistentia Pharmaceuticals Ab | Immunogenic polypeptides for inducing anti-self IgE responses |
| EP1621209A3 (en) * | 1998-11-02 | 2006-04-19 | Resistentia Pharmaceuticals AB | Vaccines based on domains of chimeric immunoglobulin E peptides |
| ATE412434T1 (de) | 1998-11-30 | 2008-11-15 | Cytos Biotechnology Ag | Molekulare anordnung von allergenen, verfahren zur deren herstellung und deren verwendung |
| EP1156825A2 (en) * | 1999-02-25 | 2001-11-28 | SMITHKLINE BEECHAM BIOLOGICALS s.a. | Immunogens comprising a peptide and a carrier derived from h.influenzae protein d |
| WO2000050461A1 (en) * | 1999-02-25 | 2000-08-31 | Smithkline Beecham Biologicals S.A. | Epitopes or mimotopes derived from the c-epsilon-3 or c-epsilon-4 domains of ige, antagonists thereof, and their therapeutic uses |
| GB9908533D0 (en) * | 1999-04-14 | 1999-06-09 | Novartis Ag | Organic compounds |
| IL152054A0 (en) * | 2000-04-13 | 2003-05-29 | Bio Life Science Forschungs & Entwicklungsgesellschaft Mbh | Vaccine against cancerous diseases which is based on mimotopes of antigens expressed on tumor cells |
| AU2001252458A1 (en) | 2000-05-05 | 2001-11-20 | Martin Bachmann | Molecular antigen arrays and vaccines |
| EP1967205B1 (en) | 2000-08-30 | 2012-10-10 | Pfizer Products Inc. | Anti-IgE vaccines |
| US7264810B2 (en) | 2001-01-19 | 2007-09-04 | Cytos Biotechnology Ag | Molecular antigen array |
| US7094409B2 (en) | 2001-01-19 | 2006-08-22 | Cytos Biotechnology Ag | Antigen arrays for treatment of allergic eosinophilic diseases |
| US7128911B2 (en) | 2001-01-19 | 2006-10-31 | Cytos Biotechnology Ag | Antigen arrays for treatment of bone disease |
| EP1236740B1 (de) * | 2001-02-28 | 2012-07-18 | Bio Life Science Forschungs- und Entwicklungsges.m.b.H. | Vakzine gegen Krebserkrankungen, die mit dem HER-2/neu Onkogen assoziiert sind |
| EP1239032A1 (en) | 2001-03-02 | 2002-09-11 | Société des Produits Nestlé S.A. | Lactic acid bacteria as agents for treating and preventing allergy |
| JP2003047482A (ja) | 2001-05-22 | 2003-02-18 | Pfizer Prod Inc | 非アナフィラキシー誘発性ＩｇＥワクチン |
| US7604955B2 (en) | 2001-08-13 | 2009-10-20 | Swey-Shen Alex Chen | Immunoglobulin E vaccines and methods of use thereof |
| US7115266B2 (en) | 2001-10-05 | 2006-10-03 | Cytos Biotechnology Ag | Angiotensin peptide-carrier conjugates and uses thereof |
| ATE361097T1 (de) * | 2002-01-15 | 2007-05-15 | Bio Life Science Forschungs & Entwicklungsgesellschaft Mbh | Orale vakzinierung mit dem tumor-antigen-mimotop gln-met-trp-ala-pro-gln-trp-gly-pro-asp |
| BR0312935A (pt) | 2002-07-17 | 2005-06-21 | Cytos Biotechnology Ag | Partìcula semelhante a vìrus, muteìna, vetores para produzir a referida partìcula e proteìna recombinante, composição, processo para produção de fileira ordena e repetitva de antìgeno, molécula de ácido nucléico, célula hospedeira, método para produção da referida partìcula e uso da composição de vacina |
| RU2326693C2 (ru) | 2002-07-18 | 2008-06-20 | Цитос Байотекнолоджи Аг | Конъюгаты гаптен-носитель и их применение |
| MXPA05000819A (es) | 2002-07-19 | 2005-08-29 | Cytos Biotechnology Ag | Composiciones de vacunas que contienen arreglos de antigeno amiloide beta 1-6. |
| EP1534335B9 (en) | 2002-08-14 | 2016-01-13 | Macrogenics, Inc. | Fcgammariib-specific antibodies and methods of use thereof |
| US20050065136A1 (en) * | 2003-08-13 | 2005-03-24 | Roby Russell R. | Methods and compositions for the treatment of infertility using dilute hormone solutions |
| WO2005105106A2 (en) * | 2004-04-21 | 2005-11-10 | Roby Russell R | Hormone treatment of macular degeneration |
| US20060025390A1 (en) * | 2004-07-28 | 2006-02-02 | Roby Russell R | Treatment of hormone allergy and related symptoms and disorders |
| ITMI20052517A1 (it) * | 2005-12-29 | 2007-06-30 | Lofarma Spa | Varianbtio ipoallergeniche dell'allergene maggiore bet v 1 di polline di betula verrucosa |
| LT2029173T (lt) | 2006-06-26 | 2016-11-10 | Macrogenics, Inc. | Fc riib specifiniai antikūnai ir jų panaudojimo būdai |
| EP2012122A1 (en) * | 2007-07-06 | 2009-01-07 | Medigene AG | Mutated parvovirus structural proteins as vaccines |
| US8865179B2 (en) * | 2008-01-26 | 2014-10-21 | Swey-Shen Alexchen | Aptameric IgE peptides in a protein scaffold as an allergy vaccine |
| MX337723B (es) | 2008-12-09 | 2016-03-15 | Pfizer Vaccines Llc | Vacuna de peptido ch3 de ige. |
| CA2800774A1 (en) * | 2010-06-07 | 2011-12-15 | Pfizer Vaccines Llc | Ige ch3 peptide vaccine |
| RU2761431C9 (ru) * | 2020-10-26 | 2022-04-18 | Федеральное государственное бюджетное учреждение "Государственный научный центр "Институт иммунологии" Федерального медико-биологического агентства России (ФГБУ "ГНЦ Институт иммунологии" ФМБА России) | Рекомбинантный полипептид на основе аллергена пыльцы березы и аллергена яблока в качестве вакцины от аллергии |
Family Cites Families (36)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE2602443A1 (de) | 1975-04-04 | 1976-10-21 | Univ California | Biologisch aktive polypeptide |
| US4171299A (en) | 1975-04-04 | 1979-10-16 | The Regents Of The University Of California | Polypeptide agents for blocking the human allergic response |
| DE2861593D1 (en) | 1977-06-29 | 1982-03-11 | Beecham Group Plc | Peptides, pharmaceutical compositions containing the peptides and a process for the preparation of the peptides |
| JPS5944399A (ja) | 1982-09-07 | 1984-03-12 | Takeda Chem Ind Ltd | 新規ｄｎａ |
| GB8616166D0 (en) * | 1986-07-02 | 1986-08-06 | Research Corp Ltd | Polypeptide competitor |
| US4892827A (en) | 1986-09-24 | 1990-01-09 | The United States Of America As Represented By The Department Of Health And Human Services | Recombinant pseudomonas exotoxins: construction of an active immunotoxin with low side effects |
| EP0269455A3 (en) | 1986-11-28 | 1989-09-06 | Takeda Chemical Industries, Ltd. | Highly purified fused protein comprising human ige fc fragment and production thereof |
| JPH02502183A (ja) | 1987-02-20 | 1990-07-19 | インクローン システムズ、インコーポレーテッド | ワクチン処方におけるモノクローナル抗体 |
| CA1336818C (en) | 1987-04-16 | 1995-08-29 | International Institute Of Cellular And Molecular Pathology | Treatment of allergy and composition thereof |
| NZ226552A (en) | 1987-10-13 | 1991-04-26 | Terrapin Tech Inc | Method of selection of antibodies for use as immunodiagnostic reagents |
| GB8727045D0 (en) | 1987-11-19 | 1987-12-23 | Research Corp Ltd | Immunoglobulin e competitor |
| US5342924A (en) | 1987-12-31 | 1994-08-30 | Tanox Biosystems, Inc. | Extracellular segments of human ε immunoglobulin anchoring peptides and antibodies specific therefor |
| US5449760A (en) | 1987-12-31 | 1995-09-12 | Tanox Biosystems, Inc. | Monoclonal antibodies that bind to soluble IGE but do not bind IGE on IGE expressing B lymphocytes or basophils |
| GB8910263D0 (en) | 1989-05-04 | 1989-06-21 | Ciba Geigy Ag | Monoclonal antibodies specific for an immunoglobulin isotype |
| GB8913737D0 (en) | 1989-06-15 | 1989-08-02 | Univ Birmingham | A novel anti-allergy treatment |
| SG70982A1 (en) | 1990-01-23 | 2000-03-21 | Tanox Biosystems Inc | Extracellular segments of human and immunoglobulin anchoring peptides and antibodies specific therefor |
| EP0605410B1 (en) | 1990-05-25 | 1995-08-16 | Peptide Therapeutics Limited | Immunodiagnostic assay for rheumatoid arthritis |
| US5258289A (en) | 1990-09-05 | 1993-11-02 | Davis Claude G | Method for the selecting of genes encoding catalytic antibodies |
| GB9101550D0 (en) | 1991-01-24 | 1991-03-06 | Mastico Robert A | Antigen-presenting chimaeric protein |
| US5965709A (en) * | 1991-08-14 | 1999-10-12 | Genentech, Inc. | IgE antagonists |
| EP0602126B1 (en) * | 1991-08-14 | 2003-03-05 | Genentech, Inc. | Immunoglobulin variants for specific fc epsilon receptors |
| SE9102808L (sv) * | 1991-09-26 | 1993-03-27 | Lars T Hellman Inst F Immunolo | Vaccin, foer humant bruk, vars avsedda effekt aer att lindra symptomen eller foerhindra uppkomsten av ige-medierade allergiska reaktioner |
| GB9125024D0 (en) | 1991-11-25 | 1992-01-22 | Kirby Julian | Rheumatoid arthritus treatment |
| JPH06113881A (ja) | 1992-10-07 | 1994-04-26 | Snow Brand Milk Prod Co Ltd | ヒト型モノクローナル抗ペプチド抗体及びこれをコードするｄｎａ |
| US5759551A (en) | 1993-04-27 | 1998-06-02 | United Biomedical, Inc. | Immunogenic LHRH peptide constructs and synthetic universal immune stimulators for vaccines |
| DK0708656T3 (da) | 1993-04-27 | 2002-12-02 | United Biomedical Inc | Antigene LHRH peptidkonstruktioner og universelle syntetiske immunstimulatorer til vacciner |
| JPH09500615A (ja) | 1993-05-14 | 1997-01-21 | ジェネンテク，インコーポレイテッド | Ｒａｓ−ファルネシル転移酵素阻害剤 |
| GB9320897D0 (en) | 1993-10-11 | 1993-12-01 | Peptide Therapeutics Ltd | Compounds useful in anti-allergy treatment |
| GB9324013D0 (en) * | 1993-11-22 | 1994-01-12 | 3I Res Expl Ltd | Polypeptides |
| FR2715304B1 (fr) * | 1994-01-26 | 1996-04-26 | Merieux Serums Vaccins Pasteur | Vaccin anti-allergique. |
| WO1995026365A1 (en) * | 1994-03-28 | 1995-10-05 | United Biomedical, Inc. | Synthetic peptide based immunogens for the treatment of allergy |
| WO1996001643A1 (en) | 1994-07-08 | 1996-01-25 | Thomas Jefferson University | IgE ANTAGONISTS |
| EP0787150A1 (en) | 1994-10-25 | 1997-08-06 | United Biomedical, Inc. | SYNTHETIC IgE MEMBRANE ANCHOR PEPTIDE IMMUNOGENS FOR THE TREATMENT OF ALLERGY |
| WO1998024808A2 (en) | 1996-12-06 | 1998-06-11 | THE UNITED STATES OF AMERICA represented by THE SECRETARY DEPARTMENT OF HEALTH & HUMAN SERVICES, THE NATIONAL INSTITUTES OF HEALTH | INHIBITION OF IgE-MEDIATED ALLERGIES BY A HUMAN IgE-DERIVED OLIGOPEPTIDE |
| EP0955311A3 (en) | 1998-04-09 | 2000-08-16 | Idexx Laboratories, Inc. | Peptide vaccine for canine allergy |
| TWI229679B (en) | 1998-06-20 | 2005-03-21 | United Biomedical Inc | Artificial T helper cell epitopes as immune stimulators for synthetic peptide immunogens |
-
1997
- 1997-02-28 BR BR9707819A patent/BR9707819A/pt not_active Application Discontinuation
- 1997-02-28 JP JP53063297A patent/JP3421970B2/ja not_active Expired - Fee Related
- 1997-02-28 US US09/125,641 patent/US6610297B1/en not_active Expired - Fee Related
- 1997-02-28 CN CNB971926719A patent/CN1174998C/zh not_active Expired - Fee Related
- 1997-02-28 WO PCT/EP1997/001013 patent/WO1997031948A1/en active IP Right Grant
- 1997-02-28 KR KR1020057005577A patent/KR100584051B1/ko not_active IP Right Cessation
- 1997-02-28 KR KR10-1998-0706845A patent/KR100498198B1/ko not_active IP Right Cessation
- 1997-02-28 SK SK1181-98A patent/SK284856B6/sk unknown
- 1997-02-28 AU AU18796/97A patent/AU719609B2/en not_active Ceased
- 1997-02-28 CA CA002245497A patent/CA2245497C/en not_active Expired - Fee Related
- 1997-02-28 HU HU9901109A patent/HUP9901109A3/hu unknown
- 1997-02-28 NZ NZ331651A patent/NZ331651A/xx unknown
- 1997-02-28 AT AT97905136T patent/ATE230417T1/de not_active IP Right Cessation
- 1997-02-28 DK DK97905136T patent/DK0885244T4/da active
- 1997-02-28 IL IL12559097A patent/IL125590A/xx not_active IP Right Cessation
- 1997-02-28 DE DE69718150T patent/DE69718150T3/de not_active Expired - Lifetime
- 1997-02-28 RU RU98118184/14A patent/RU2193413C2/ru not_active IP Right Cessation
- 1997-02-28 EP EP97905136A patent/EP0885244B2/en not_active Expired - Lifetime
- 1997-02-28 CZ CZ0277198A patent/CZ299551B6/cs not_active IP Right Cessation
- 1997-02-28 PL PL97328858A patent/PL187209B1/pl not_active IP Right Cessation
- 1997-02-28 SI SI9730490T patent/SI0885244T2/sl unknown
- 1997-02-28 TR TR1998/01722T patent/TR199801722T2/xx unknown
- 1997-02-28 ES ES97905136T patent/ES2190799T5/es not_active Expired - Lifetime
-
1998
- 1998-08-31 NO NO19983999A patent/NO321043B1/no unknown
- 1998-12-31 HK HK98119259A patent/HK1014962A1/xx not_active IP Right Cessation
-
2002
- 2002-12-26 JP JP2002377664A patent/JP2003231696A/ja active Pending
-
2004
- 2004-06-04 CY CY0400044A patent/CY2457B1/xx unknown
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