JP3368902B2 - ワクチンおよび診断に有用なＨｅｌｉｃｏｂａｃｔｅｒｐｙｌｏｒｉタンパク質 - Google Patents
ワクチンおよび診断に有用なＨｅｌｉｃｏｂａｃｔｅｒｐｙｌｏｒｉタンパク質Info
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- JP3368902B2 JP3368902B2 JP51530993A JP51530993A JP3368902B2 JP 3368902 B2 JP3368902 B2 JP 3368902B2 JP 51530993 A JP51530993 A JP 51530993A JP 51530993 A JP51530993 A JP 51530993A JP 3368902 B2 JP3368902 B2 JP 3368902B2
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- polynucleotide
- sequence
- contiguous sequence
- helicobacter pylori
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- 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
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Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
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- 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
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- 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
- A61P31/04—Antibacterial agents
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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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/205—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Campylobacter (G)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/68—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving nucleic acids
- C12Q1/6876—Nucleic acid products used in the analysis of nucleic acids, e.g. primers or probes
- C12Q1/6888—Nucleic acid products used in the analysis of nucleic acids, e.g. primers or probes for detection or identification of organisms
- C12Q1/689—Nucleic acid products used in the analysis of nucleic acids, e.g. primers or probes for detection or identification of organisms for bacteria
-
- 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
- C07K2319/00—Fusion polypeptide
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/40—Fusion polypeptide containing a tag for immunodetection, or an epitope for immunisation
-
- 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
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/975—Kit
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Biochemistry (AREA)
- Analytical Chemistry (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Engineering & Computer Science (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- General Chemical & Material Sciences (AREA)
- Veterinary Medicine (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Physics & Mathematics (AREA)
- Microbiology (AREA)
- Immunology (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Communicable Diseases (AREA)
- Oncology (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Enzymes And Modification Thereof (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| IT92A000052 | 1992-03-02 | ||
| ITFI920052A IT1262895B (it) | 1992-03-02 | 1992-03-02 | Proteina estratta da ceppi citotossici di helicobacter pylori, gene che la esprime, uso della proteina come vaccino o diagnostico. |
| EPPCT/EP93/00158 | 1993-01-25 | ||
| GB93/00158 | 1993-01-25 | ||
| PCT/EP1993/000472 WO1993018150A1 (en) | 1992-03-02 | 1993-03-02 | Helicobacter pylori proteins useful for vaccines and diagnostics |
Related Child Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2000126696A Division JP2000333686A (ja) | 1992-03-02 | 2000-04-26 | ワクチンおよび診断に有用なＨｅｌｉｃｏｂａｃｔｅｒｐｙｌｏｒｉタンパク質 |
| JP2000126695A Division JP3408494B2 (ja) | 1992-03-02 | 2000-04-26 | ワクチンおよび診断に有用なＨｅｌｉｃｏｂａｃｔｅｒｐｙｌｏｒｉタンパク質 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH07504565A JPH07504565A (ja) | 1995-05-25 |
| JP3368902B2 true JP3368902B2 (ja) | 2003-01-20 |
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| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP51530993A Expired - Lifetime JP3368902B2 (ja) | 1992-03-02 | 1993-03-02 | ワクチンおよび診断に有用なＨｅｌｉｃｏｂａｃｔｅｒｐｙｌｏｒｉタンパク質 |
| JP2000126696A Pending JP2000333686A (ja) | 1992-03-02 | 2000-04-26 | ワクチンおよび診断に有用なＨｅｌｉｃｏｂａｃｔｅｒｐｙｌｏｒｉタンパク質 |
| JP2000126695A Expired - Lifetime JP3408494B2 (ja) | 1992-03-02 | 2000-04-26 | ワクチンおよび診断に有用なＨｅｌｉｃｏｂａｃｔｅｒｐｙｌｏｒｉタンパク質 |
| JP2005263068A Withdrawn JP2006055168A (ja) | 1992-03-02 | 2005-09-09 | ワクチンおよび診断に有用なＨｅｌｉｃｏｂａｃｔｅｒｐｙｌｏｒｉタンパク質 |
Family Applications After (3)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2000126696A Pending JP2000333686A (ja) | 1992-03-02 | 2000-04-26 | ワクチンおよび診断に有用なＨｅｌｉｃｏｂａｃｔｅｒｐｙｌｏｒｉタンパク質 |
| JP2000126695A Expired - Lifetime JP3408494B2 (ja) | 1992-03-02 | 2000-04-26 | ワクチンおよび診断に有用なＨｅｌｉｃｏｂａｃｔｅｒｐｙｌｏｒｉタンパク質 |
| JP2005263068A Withdrawn JP2006055168A (ja) | 1992-03-02 | 2005-09-09 | ワクチンおよび診断に有用なＨｅｌｉｃｏｂａｃｔｅｒｐｙｌｏｒｉタンパク質 |
Country Status (7)
| Country | Link |
|---|---|
| US (3) | US6077706A (cg-RX-API-DMAC7.html) |
| EP (1) | EP0967279B1 (cg-RX-API-DMAC7.html) |
| JP (4) | JP3368902B2 (cg-RX-API-DMAC7.html) |
| AU (1) | AU3630093A (cg-RX-API-DMAC7.html) |
| CA (2) | CA2383007A1 (cg-RX-API-DMAC7.html) |
| DE (2) | DE69334197T2 (cg-RX-API-DMAC7.html) |
| WO (1) | WO1993018150A1 (cg-RX-API-DMAC7.html) |
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| US5866375A (en) * | 1991-10-31 | 1999-02-02 | Chiron S.P.A. | Method for the culture of microorganisms of the genera helicobacter, campylobacter and arcobacter employing culture media comprising cyclodextrins |
| US5721349A (en) * | 1992-02-26 | 1998-02-24 | Vanderbilt University | Vacuolating toxin-deficient H. pylori |
| AU3728293A (en) * | 1992-02-26 | 1993-09-13 | Vanderbilt University | Purified vacuolating toxin from (helicobacter) pylori and methods to use same |
| US5928865A (en) * | 1992-03-02 | 1999-07-27 | Chiron S.P.A. | Compositions comprising isolated Helicobacter pylori CagI polynucleotides and method of preparation thereof |
| IT1262896B (it) * | 1992-03-06 | 1996-07-22 | Composti coniugati formati da proteine heat shock (hsp) e oligo-poli- saccaridi, loro uso per la produzione di vaccini. | |
| MX9301706A (es) * | 1992-04-13 | 1994-05-31 | Oravax Inc | Composicion de vacuna para el tratamiento de la infeccion por helicobacter. |
| US5733740A (en) * | 1992-10-13 | 1998-03-31 | Vanderbilt University | Taga gene and methods for detecting predisposition to peptic ulceration and gastric carcinoma |
| US5403924A (en) * | 1992-10-13 | 1995-04-04 | Vanderbilt University | Taga gene and methods for detecting predisposition to peptic ulceration |
| US5972336A (en) * | 1992-11-03 | 1999-10-26 | Oravax Merieux Co. | Urease-based vaccine against helicobacter infection |
| US6290962B1 (en) * | 1992-11-03 | 2001-09-18 | Oravax, Inc. | Urease-based vaccine and treatment for helicobacter infection |
| US6258359B1 (en) | 1993-05-19 | 2001-07-10 | Institut Pasteur | Immunogenic compositions against helicobacter infection, polypeptides for use in the compositions, and nucleic acid sequences encoding said polypeptides |
| WO1995014093A1 (en) | 1993-05-19 | 1995-05-26 | Institut Pasteur | Immunogenic compositions against helicobacter infection, polypeptides for use in the compositions and nucleic acid sequences encoding said polypeptides |
| GB9313279D0 (en) * | 1993-06-28 | 1993-08-11 | Medical Res Council | Protection against infection with helicobacter pylori |
| DE69432929T2 (de) * | 1993-07-27 | 2004-04-15 | Csl Ltd., Parkville | Behandlung eines durch helicobakter verursachten gastroduodenalen krankheit |
| US6406703B1 (en) | 1993-07-27 | 2002-06-18 | Csl Limited | Treatment of H. pylori associated gastroduodenal disease |
| US5750119A (en) * | 1994-01-13 | 1998-05-12 | Mount Sinai School Of Medicine Of The City University Of New York | Immunotherapeutic stress protein-peptide complexes against cancer |
| US5997873A (en) | 1994-01-13 | 1999-12-07 | Mount Sinai School Of Medicine Of The City University Of New York | Method of preparation of heat shock protein 70-peptide complexes |
| US5961979A (en) * | 1994-03-16 | 1999-10-05 | Mount Sinai School Of Medicine Of The City University Of New York | Stress protein-peptide complexes as prophylactic and therapeutic vaccines against intracellular pathogens |
| GB2290710B (en) * | 1994-06-29 | 1998-03-25 | Reckitt & Colmann Prod Ltd | Protease from helicobacter pylori for use in vaccines/therapeutic compositions |
| AU695769B2 (en) * | 1994-07-01 | 1998-08-20 | Provost Fellows And Scholars Of The College Of The Holy And Undivided Trinity Of Queen Elizabeth Near Dublin, The | Helicobacter proteins and vaccines |
| GB9505438D0 (en) * | 1995-03-17 | 1995-05-03 | Sod Conseils Rech Applic | Antisense oligonucleotides |
| AU6343696A (en) * | 1995-07-07 | 1997-02-10 | Oravax, Inc | Helicobacter clpb |
| US5985270A (en) * | 1995-09-13 | 1999-11-16 | Fordham University | Adoptive immunotherapy using macrophages sensitized with heat shock protein-epitope complexes |
| US5837251A (en) * | 1995-09-13 | 1998-11-17 | Fordham University | Compositions and methods using complexes of heat shock proteins and antigenic molecules for the treatment and prevention of neoplastic diseases |
| US5935576A (en) * | 1995-09-13 | 1999-08-10 | Fordham University | Compositions and methods for the treatment and prevention of neoplastic diseases using heat shock proteins complexed with exogenous antigens |
| EP0797585A1 (fr) * | 1995-10-09 | 1997-10-01 | Pasteur Merieux Serums Et Vaccins | Recepteur lactoferrine d'helicobacter |
| DK0909323T3 (da) | 1996-01-04 | 2007-05-21 | Novartis Vaccines & Diagnostic | Helicobacter pylori-bakterioferritin |
| JPH1033179A (ja) * | 1996-07-24 | 1998-02-10 | Fuso Yakuhin Kogyo Kk | 感染症診断用プローブ |
| WO1998012562A1 (en) * | 1996-09-20 | 1998-03-26 | Cortecs International Limited | Adhesins from heliobacter pylori and their diagnostic and therapeutic uses |
| ATE218709T1 (de) * | 1996-12-19 | 2002-06-15 | Chiron Corp | Helicobacter pylori diagnostika |
| US6017540A (en) | 1997-02-07 | 2000-01-25 | Fordham University | Prevention and treatment of primary and metastatic neoplastic diseases and infectious diseases with heat shock/stress protein-peptide complexes |
| US5830464A (en) * | 1997-02-07 | 1998-11-03 | Fordham University | Compositions and methods for the treatment and growth inhibition of cancer using heat shock/stress protein-peptide complexes in combination with adoptive immunotherapy |
| CA2289253A1 (en) * | 1997-04-30 | 1998-11-05 | Merieux Oravax | Anti-helicobacter vaccine composition for use by the subdiaphragmatic systemic route, and combined mucosal/parenteral immunization method |
| FR2748477B1 (fr) * | 1997-07-01 | 2001-07-13 | Pasteur Merieux Serums Vacc | Nouvelle proteine membranaire d'helicobacter pylori |
| US6914131B1 (en) | 1998-10-09 | 2005-07-05 | Chiron S.R.L. | Neisserial antigens |
| CA2315880A1 (en) * | 1997-12-31 | 1999-07-15 | Stressgen Biotechnologies Corporation | Streptococcal heat shock proteins of the hsp60 family |
| WO1999057278A2 (en) * | 1998-04-30 | 1999-11-11 | Chiron S.P.A. | IMMUNIZATION AGAINST AND TREATMENT FOR INFECTION BY $i(H.PYLORI) |
| US6585975B1 (en) * | 1998-04-30 | 2003-07-01 | Acambis, Inc. | Use of Salmonella vectors for vaccination against helicobacter infection |
| US6838553B1 (en) * | 1999-10-05 | 2005-01-04 | Academia Sinica | Peptide repeat immunogens |
| GB9924060D0 (en) * | 1999-10-11 | 1999-12-15 | Chiron Spa | VIP54 protein |
| PT2275551E (pt) | 1999-10-29 | 2015-06-29 | Novartis Vaccines & Diagnostic | Péptidos antigénicos de neisseria |
| US8273360B2 (en) | 2000-01-17 | 2012-09-25 | Novartis Ag | Outer membrane vesicle (OMV) vaccine comprising N. meningitidis serogroup B outer membrane proteins |
| JP2004505894A (ja) | 2000-06-02 | 2004-02-26 | ユニバーシティー オブ コネティカット ヘルス センター | 免疫療法のためのα（２）マクログロブリンと抗原分子との複合体 |
| US20020107368A1 (en) * | 2000-12-07 | 2002-08-08 | Jing-Hui Tian | Helicobacter proteins, gene sequences and uses thereof |
| EP2332573A1 (en) | 2001-05-31 | 2011-06-15 | Novartis Vaccines and Diagnostics, Inc. | Chimeric alphavirus replicon particles |
| GB0115176D0 (en) | 2001-06-20 | 2001-08-15 | Chiron Spa | Capular polysaccharide solubilisation and combination vaccines |
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| GB0121591D0 (en) | 2001-09-06 | 2001-10-24 | Chiron Spa | Hybrid and tandem expression of neisserial proteins |
| WO2003015712A2 (en) | 2001-08-20 | 2003-02-27 | University Of Connecticut Health Center | Methods for preparing compositions comprising heat shock proteins or alpha-2-macroglobulin |
| CA2476626A1 (en) | 2002-02-20 | 2003-08-28 | Chiron Corporation | Microparticles with adsorbed polypeptide-containing molecules |
| US20050250175A1 (en) * | 2002-08-02 | 2005-11-10 | Takehiko Nomura | Bacterial cell wall skeleton component preparaion |
| GB0220194D0 (en) | 2002-08-30 | 2002-10-09 | Chiron Spa | Improved vesicles |
| ATE352316T1 (de) | 2002-11-01 | 2007-02-15 | Glaxosmithkline Biolog Sa | Immunogene zusammensetzung |
| US20070059329A1 (en) | 2002-11-15 | 2007-03-15 | Nathalie Norais | Unexpected surface proteins in meningococcus |
| GB0227346D0 (en) | 2002-11-22 | 2002-12-31 | Chiron Spa | 741 |
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| WO2004087153A2 (en) | 2003-03-28 | 2004-10-14 | Chiron Corporation | Use of organic compounds for immunopotentiation |
| GB0308198D0 (en) | 2003-04-09 | 2003-05-14 | Chiron Srl | ADP-ribosylating bacterial toxin |
| US7731967B2 (en) | 2003-04-30 | 2010-06-08 | Novartis Vaccines And Diagnostics, Inc. | Compositions for inducing immune responses |
| PL1631264T5 (pl) | 2003-06-02 | 2018-09-28 | Glaxosmithkline Biologicals Sa | Kompozycje immunogenne oparte na biodegradowalnych mikrocząstkach zawierających toksoid błonicy i tężca |
| ATE516306T1 (de) | 2003-08-13 | 2011-07-15 | Novartis Vaccines & Diagnostic | Verbessertes verfahren zur reinigung von tfpi und tfpi-analogen |
| EP1730171A1 (en) | 2004-02-19 | 2006-12-13 | Ramot at Tel Aviv University Ltd. | Peptide mimotopes of mycobacterial mannosylated lipoglycans and uses thereof |
| JP5041279B2 (ja) * | 2004-04-22 | 2012-10-03 | 株式会社 Ｍｂｒ | 細菌細胞壁骨格成分を含有する製剤 |
| JP2008504292A (ja) | 2004-06-24 | 2008-02-14 | ノバルティス ヴァクシンズ アンド ダイアグノスティクス， インコーポレイテッド | 免疫増強用の化合物 |
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| US8147837B2 (en) | 2004-06-24 | 2012-04-03 | Yissum Research Development Company Of The Hebrew University Of Jerusalem | Use of mycobacterial mannosylated lipoglycans peptide mimotopes for treating inflammation |
| US20090317420A1 (en) | 2004-07-29 | 2009-12-24 | Chiron Corporation | Immunogenic compositions for gram positive bacteria such as streptococcus agalactiae |
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| JP5215865B2 (ja) | 2005-11-22 | 2013-06-19 | ノバルティス ヴァクシンズ アンド ダイアグノスティクス インコーポレイテッド | ノロウイルス抗原およびサポウイルス抗原 |
| ES2536426T3 (es) | 2006-03-23 | 2015-05-25 | Novartis Ag | Compuestos de imidazoquinoxalina como inmunomoduladores |
| KR100846494B1 (ko) * | 2006-09-26 | 2008-07-17 | 삼성전자주식회사 | 헬리코박터 파일로리의 표적 서열을 증폭하기 위한프라이머 세트, 상기 프라이머 세트를 이용하여 헬리코박터파일로리를 검출하는 방법 및 상기 프라이머 세트를포함하는 헬리코박터 파일로리를 검출하는 키트 |
| GB0700562D0 (en) | 2007-01-11 | 2007-02-21 | Novartis Vaccines & Diagnostic | Modified Saccharides |
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| ES2412237T3 (es) | 2008-08-01 | 2013-07-10 | Cleveland Biolabs, Inc. | Métodos para tratar lesiones por reperfusión |
| WO2010032138A2 (en) | 2008-09-18 | 2010-03-25 | Novartis Ag | Vaccine adjuvant combinations |
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| JP2013503148A (ja) | 2009-08-27 | 2013-01-31 | ノバルティス アーゲー | アルミニウム、オリゴヌクレオチドおよびポリカチオンを含むアジュバント |
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| ES2458355T3 (es) | 2010-09-01 | 2014-05-05 | Novartis Ag | Adsorción de inmunopotenciadores sobre sales metálicas insolubles |
| US9618508B2 (en) | 2010-12-14 | 2017-04-11 | Glaxosmithkline Biologicals Sa | Flow cytometry analysis of materials adsorbed to metal salts |
| CN103476458B (zh) | 2011-01-10 | 2017-02-15 | 克利夫兰生物实验室公司 | Toll样受体激动剂治疗癌症的用途 |
| BR112013022397A2 (pt) | 2011-03-02 | 2017-09-26 | Derek OHagan | vacinas combinadas com doses menores de antígeno e/ou adjuvante |
| RU2014140336A (ru) | 2012-03-07 | 2016-04-27 | Новартис Аг | Иммунологически полезные соли аргинина |
| JP2015510872A (ja) | 2012-03-07 | 2015-04-13 | ノバルティス アーゲー | Ｓｔｒｅｐｔｏｃｏｃｃｕｓｐｎｅｕｍｏｎｉａｅ抗原の増強された製剤 |
| RU2014140521A (ru) | 2012-03-08 | 2016-04-27 | Новартис Аг | Адъювантные составы бустерных вакцин |
| EP2877852B1 (en) * | 2012-07-23 | 2022-05-25 | Hermouet, Sylvie | A protein microarray for characterizing the specificity of the monoclonal immunoglobulins of mgus or myeloma patients |
| KR20170031251A (ko) | 2014-07-30 | 2017-03-20 | 클리브랜드 바이오랩스, 아이엔씨. | 플라젤린 조성물 및 용도 |
| WO2016109002A2 (en) | 2014-10-16 | 2016-07-07 | Cleveland Biolabs, Inc. | Methods and compositions for the treatment of radiation-related disorders |
| SE541618C2 (en) * | 2017-02-24 | 2019-11-12 | Biotome Pty Ltd | Novel peptides and their use in diagnosis |
Family Cites Families (17)
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|---|---|---|---|---|
| DE3751307T2 (de) | 1986-03-28 | 1995-09-21 | The Board Of Trustees Of The University Of Illinois, Urbana, Ill. | Zubereitungen und verfahren für klone, die, mit mehrfacharzneimittelresistenz assoziierte, dna-sequenzen in menschlichen zellen enthalten. |
| US5554372A (en) | 1986-09-22 | 1996-09-10 | Emory University | Methods and vaccines comprising surface-active copolymers |
| US5459041A (en) * | 1988-02-18 | 1995-10-17 | Enteric Research Laboratories, Inc. | Campylobacter pylori antigens and uses thereof for detection of Campylobacter pylori infection |
| US4882271A (en) * | 1988-03-10 | 1989-11-21 | Baylor College Of Medicine | Process for preparation of high molecular weight cell-associated protein of campylobacter pylori and use for serological detection of campylobacter pylori infection |
| FR2637612B1 (fr) * | 1988-10-06 | 1993-09-10 | Pasteur Institut | Sequences de nucleotides codant pour une proteine a activite ureasique |
| JP3436756B2 (ja) | 1988-12-19 | 2003-08-18 | アメリカン・サイアナミド・カンパニー | 髄膜炎菌のクラスｉの外膜タンパク質のワクチン |
| GB8928625D0 (en) * | 1989-12-19 | 1990-02-21 | 3I Res Expl Ltd | H.pylori dna probes |
| US5292658A (en) | 1989-12-29 | 1994-03-08 | University Of Georgia Research Foundation, Inc. Boyd Graduate Studies Research Center | Cloning and expressions of Renilla luciferase |
| ES2198514T3 (es) | 1991-08-27 | 2004-02-01 | F. Hoffmann-La Roche Ag | Cebadores y sondas para la deteccion de la hepatitis c. |
| US5354854A (en) | 1991-11-07 | 1994-10-11 | The Curators Of The University Of Missouri | Expression system for use in plants to suppress foreign expression and method |
| US5721349A (en) * | 1992-02-26 | 1998-02-24 | Vanderbilt University | Vacuolating toxin-deficient H. pylori |
| IT1262895B (it) | 1992-03-02 | 1996-07-22 | Proteina estratta da ceppi citotossici di helicobacter pylori, gene che la esprime, uso della proteina come vaccino o diagnostico. | |
| US5733740A (en) | 1992-10-13 | 1998-03-31 | Vanderbilt University | Taga gene and methods for detecting predisposition to peptic ulceration and gastric carcinoma |
| US5403924A (en) * | 1992-10-13 | 1995-04-04 | Vanderbilt University | Taga gene and methods for detecting predisposition to peptic ulceration |
| US6019982A (en) * | 1994-08-26 | 2000-02-01 | The Administrators Of The Tulane Educational Fund | Mutant enterotoxin effective as a non-toxic oral adjuvant |
| US6902903B1 (en) | 1996-12-19 | 2005-06-07 | Chiron Corporation | Helicobacter pylori diagnostics |
| CA2408328C (en) | 2000-05-10 | 2012-04-17 | Aventis Pasteur Limited | Immunogenic polypeptides encoded by mage minigenes and uses thereof |
-
1993
- 1993-03-02 DE DE69334197T patent/DE69334197T2/de not_active Expired - Lifetime
- 1993-03-02 CA CA002383007A patent/CA2383007A1/en active Pending
- 1993-03-02 CA CA002131729A patent/CA2131729C/en not_active Expired - Lifetime
- 1993-03-02 AU AU36300/93A patent/AU3630093A/en not_active Abandoned
- 1993-03-02 JP JP51530993A patent/JP3368902B2/ja not_active Expired - Lifetime
- 1993-03-02 DE DE69333110T patent/DE69333110T2/de not_active Expired - Lifetime
- 1993-03-02 WO PCT/EP1993/000472 patent/WO1993018150A1/en not_active Ceased
- 1993-03-02 EP EP99202698A patent/EP0967279B1/en not_active Expired - Lifetime
-
1995
- 1995-06-06 US US08/470,260 patent/US6077706A/en not_active Expired - Lifetime
-
2000
- 2000-04-26 JP JP2000126696A patent/JP2000333686A/ja active Pending
- 2000-04-26 JP JP2000126695A patent/JP3408494B2/ja not_active Expired - Lifetime
-
2001
- 2001-08-02 US US09/921,157 patent/US20040048353A1/en not_active Abandoned
-
2003
- 2003-07-08 US US10/615,668 patent/US7700755B2/en not_active Expired - Fee Related
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2005
- 2005-09-09 JP JP2005263068A patent/JP2006055168A/ja not_active Withdrawn
Also Published As
| Publication number | Publication date |
|---|---|
| CA2131729C (en) | 2008-02-12 |
| CA2383007A1 (en) | 1993-09-16 |
| EP0967279B1 (en) | 2008-01-02 |
| DE69333110T2 (de) | 2004-05-06 |
| US7700755B2 (en) | 2010-04-20 |
| US20040048353A1 (en) | 2004-03-11 |
| JPH07504565A (ja) | 1995-05-25 |
| AU3630093A (en) | 1993-10-05 |
| US6077706A (en) | 2000-06-20 |
| DE69334197T2 (de) | 2008-12-11 |
| JP2000350591A (ja) | 2000-12-19 |
| US20050276819A1 (en) | 2005-12-15 |
| CA2131729A1 (en) | 1993-09-16 |
| WO1993018150A1 (en) | 1993-09-16 |
| DE69334197D1 (de) | 2008-02-14 |
| JP2000333686A (ja) | 2000-12-05 |
| JP3408494B2 (ja) | 2003-05-19 |
| DE69333110D1 (de) | 2003-08-28 |
| JP2006055168A (ja) | 2006-03-02 |
| EP0967279A1 (en) | 1999-12-29 |
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