DK173262B1 - Syntetisk polypeptid og dets anvendelse til diagnosticering af Epstein-Barr-virus, syntetisk polypeptidoligomer og syntetis - Google Patents
Syntetisk polypeptid og dets anvendelse til diagnosticering af Epstein-Barr-virus, syntetisk polypeptidoligomer og syntetis Download PDFInfo
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- DK173262B1 DK173262B1 DK198706388A DK638887A DK173262B1 DK 173262 B1 DK173262 B1 DK 173262B1 DK 198706388 A DK198706388 A DK 198706388A DK 638887 A DK638887 A DK 638887A DK 173262 B1 DK173262 B1 DK 173262B1
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- polypeptide
- amino acid
- antibodies
- synthetic polypeptide
- immunoreactant
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- C12N2710/00011—Details
- C12N2710/16011—Herpesviridae
- C12N2710/16211—Lymphocryptovirus, e.g. human herpesvirus 4, Epstein-Barr Virus
- C12N2710/16222—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
-
- 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
- Y10S435/81—Packaged device or kit
-
- 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
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- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Virology (AREA)
- Tropical Medicine & Parasitology (AREA)
- Gastroenterology & Hepatology (AREA)
- Immunology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Polyamides (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US06/938,643 US4879213A (en) | 1986-12-05 | 1986-12-05 | Synthetic polypeptides and antibodies related to Epstein-Barr virus early antigen-diffuse |
| US93864386 | 1986-12-05 |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| DK638887D0 DK638887D0 (da) | 1987-12-04 |
| DK638887A DK638887A (da) | 1988-06-06 |
| DK173262B1 true DK173262B1 (da) | 2000-05-29 |
Family
ID=25471727
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DK198706388A DK173262B1 (da) | 1986-12-05 | 1987-12-04 | Syntetisk polypeptid og dets anvendelse til diagnosticering af Epstein-Barr-virus, syntetisk polypeptidoligomer og syntetis |
Country Status (13)
| Country | Link |
|---|---|
| US (1) | US4879213A (xx) |
| EP (1) | EP0280813B1 (xx) |
| JP (2) | JP2624973B2 (xx) |
| AT (1) | ATE107316T1 (xx) |
| AU (1) | AU610099B2 (xx) |
| CA (1) | CA1315481C (xx) |
| DE (1) | DE3750088T2 (xx) |
| DK (1) | DK173262B1 (xx) |
| ES (1) | ES2054692T3 (xx) |
| IE (1) | IE63368B1 (xx) |
| IL (1) | IL84690A (xx) |
| NZ (1) | NZ222794A (xx) |
| ZA (1) | ZA879025B (xx) |
Families Citing this family (164)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7351412B1 (en) * | 1983-12-05 | 2008-04-01 | Institut Pasteur | Cloned DNA sequences related to the genomic RNA of lymphadenopathy-associated-virus (LAV) and proteins encoded by said LAV genomic RNA |
| US5116725A (en) * | 1984-08-08 | 1992-05-26 | Scripps Clinic And Research Foundation | Assay for Epstein-Barr virus infection with solid phase bound synthetic polypeptides |
| US5256768A (en) * | 1985-12-13 | 1993-10-26 | The Johns Hopkins University | Expression of antigenic Epstein-Barr virus polypeptides in bacteria and their use in diagnostics |
| US6255078B1 (en) * | 1986-03-26 | 2001-07-03 | Pharmacia & Upjohn Company | Pseudorabies virus protein cross reference to related applications |
| US6172186B1 (en) * | 1986-03-26 | 2001-01-09 | Pharmacia & Upjohn Company | Pseudorabies virus protein |
| DE3706233A1 (de) * | 1987-02-26 | 1988-09-08 | Behringwerke Ag | Immunogene fusionsproteine, die epstein-barr-virusproteine enthalten |
| NZ225295A (en) * | 1987-07-07 | 1991-07-26 | Biotech Australia Pty Ltd | Nematode antigen, its production and vaccines containing it |
| US5948644A (en) * | 1988-09-26 | 1999-09-07 | Biotechnology Australia Pty Ltd. | Polynucleotides encoding excretory/secretory proteins of parasitic nematodes, host cells transformed therewith |
| US5079172A (en) * | 1988-11-04 | 1992-01-07 | Board Of Trustees Operating Michigan State University | Method for detecting the presence of antibodies using gold-labeled antibodies and test kit |
| US6572862B1 (en) * | 1989-11-08 | 2003-06-03 | Baylor College Of Medicine | Methods and reagents to detect and characterize Norwalk and related viruses |
| AU640430B2 (en) * | 1989-11-24 | 1993-08-26 | Council Of The Queensland Institute Of Medical Research, The | Im peptides |
| WO1991008224A1 (en) * | 1989-11-24 | 1991-06-13 | The Council Of The Queensland Institute Of Medical Research | Im peptides |
| US5106726A (en) * | 1990-02-16 | 1992-04-21 | United Biomedical, Inc. | Synthetic peptides specific for the detection of antibodies to HCV |
| JP2596466B2 (ja) * | 1990-03-03 | 1997-04-02 | アサヒビール株式会社 | ダニの主要アレルゲンの還伝情報を有するｄｎａおよび該アレルゲンの製造方法 |
| US6197548B1 (en) | 1990-04-02 | 2001-03-06 | Medeva Pharma Limited | Transformed Pichia expressing the pertactin antigen |
| US5798105A (en) * | 1990-06-06 | 1998-08-25 | University Of Nijmegan | DNA encoding a plasmodium 16kD protein |
| US5674735A (en) * | 1990-07-06 | 1997-10-07 | University Court Of The University Of Glasgow | DNA encoding the EHV-4 gH or gC glycoprotein |
| GB9014950D0 (en) * | 1990-07-06 | 1990-08-29 | Univ Glasgow | Ehv-4 glycoprotein vaccine |
| US6730305B1 (en) | 2000-05-08 | 2004-05-04 | The Uab Research Foundation | Nucleotide sequences encoding bovine respiratory syncytial virus immunogenic proteins |
| AU650040B2 (en) * | 1990-07-24 | 1994-06-09 | Uab Research Foundation, The | Methods of use of bovine respiratory syncytial virus recombinant DNA, proteins vaccines, antibodies, and transformed cells |
| GB9016315D0 (en) * | 1990-07-25 | 1990-09-12 | Burnie James P | Medicaments |
| US5736362A (en) * | 1990-10-26 | 1998-04-07 | The University Of Melbourne | Ryegrass pollen allergen |
| US5972337A (en) * | 1990-11-01 | 1999-10-26 | Cancer Research Fund Of Contra Costa | 46 kilodalton human milk fat globule (HMFG) antigen, fragments and fusion protein |
| US5200344A (en) * | 1990-11-13 | 1993-04-06 | Blaser Martin J | Diagnostic testing for campylobacter jejuni or campylobacter coli infections using novel antigens |
| JP3015969B2 (ja) * | 1990-11-30 | 2000-03-06 | ダイナボット株式会社 | 扁平上皮癌関連抗原蛋白質及び該蛋白質をコードするｄｎａ |
| GB9027728D0 (en) * | 1990-12-20 | 1991-02-13 | Smithkline Beecham Biolog | Novel protein |
| US5741493A (en) * | 1991-01-24 | 1998-04-21 | Pasteur Merieux Serums Et Vaccins | Vaccine composition against influenza, with synergic effects, containing influenza virus core as an additive |
| US5525508A (en) * | 1991-02-06 | 1996-06-11 | Biotech Australia Pty Limited | Haemonchus contortus vaccine |
| AU663863B2 (en) * | 1991-02-06 | 1995-10-26 | Biotech Australia Pty Limited | Nematode vaccine |
| US6673916B1 (en) | 1991-02-12 | 2004-01-06 | Colorado State University Research Foundation | Compositions of parasitic helminth PLA2 nucleic acid molecules and uses thereof |
| US6419923B1 (en) * | 1991-02-12 | 2002-07-16 | Heska Corporation | Filariid nematode cysteine protease proteins, and uses thereof |
| US6099843A (en) * | 1991-02-12 | 2000-08-08 | Heska Corporation | Parasitic helminth PLA2 proteins |
| CA2067031C (en) * | 1991-04-26 | 2003-02-18 | Shigekazu Nagata | Dna coding for human cell surface antigen |
| US5670362A (en) * | 1991-06-18 | 1997-09-23 | Akzo Nobel N.V. | DNA encoding an Eimeria 100kD antigen |
| ZA924203B (en) * | 1991-06-18 | 1993-03-31 | Akzo Nv | Coccidiosis poultry vaccine |
| US6146870A (en) * | 1991-12-13 | 2000-11-14 | Heska Corporation | Flea protease proteins |
| GB9200117D0 (en) | 1992-01-06 | 1992-02-26 | Connaught Lab | Production of recombinant chimeric proteins for vaccine use |
| US7141244B1 (en) * | 1992-03-02 | 2006-11-28 | Chiron Srl | Helicobacter pylori proteins useful for vaccines and diagnostics |
| GB9209993D0 (en) * | 1992-05-08 | 1992-06-24 | Munn Edward A | Vaccines |
| USRE37224E1 (en) * | 1992-06-05 | 2001-06-12 | Dalhousie University | Method to prevent fertilization in mammals by administering a single dose of zona pellucida derived antigens, liposome and adjuvant |
| US5736141A (en) * | 1992-06-05 | 1998-04-07 | Dalhousie University | Method to prevent fertilization in mammals by administering a single dose of zona pellucida derived antigens, liposome and Freund's adjuvant |
| US5980899A (en) * | 1992-06-10 | 1999-11-09 | The United States Of America As Represented By The Department Of Health And Human Services | Identification of peptides that stimulate hepatitis C virus specific cytotoxic T cells |
| US7060283B1 (en) | 1992-09-15 | 2006-06-13 | Ortho Diagnostic Systems, Inc. | Immunoreactive peptides from Epstein-Barr virus |
| US7326535B2 (en) | 1993-09-15 | 2008-02-05 | Ortho Diagnostic Systems Inc. | Immunoreactive peptides from Epstein-Barr virus |
| DE69329347T2 (de) * | 1992-09-15 | 2001-10-31 | Georgetown University, Washington | Immunreaktive peptide des epstein-barrvirus |
| US5962316A (en) | 1992-10-16 | 1999-10-05 | Cold Spring Harbor Laboratory | Cell-cycle regulatory proteins, and uses related thereto |
| US6290962B1 (en) * | 1992-11-03 | 2001-09-18 | Oravax, Inc. | Urease-based vaccine and treatment for helicobacter infection |
| US5972336A (en) * | 1992-11-03 | 1999-10-26 | Oravax Merieux Co. | Urease-based vaccine against helicobacter infection |
| JP3852945B2 (ja) * | 1993-01-22 | 2006-12-06 | スローン − ケタリング・インスティテュート・フォー・キャンサー・リサーチ | Ｑｓ−２１を伴う、ガングリオシド‐ｋｌｈ複合体 |
| JPH08507207A (ja) * | 1993-02-26 | 1996-08-06 | ザ フィニッシュ ナショナル パブリック ヘルス インスティチュート | グラム陽性菌中の商業的に重要な菌体外タンパク質の高められた生産のための方法及び系 |
| US6849427B1 (en) * | 1993-03-12 | 2005-02-01 | Immulogic Pharmaceutical Corp. | Nucleic acids encoding a house dust mite allergen, Der p VII, and uses therefor |
| CA2116640A1 (en) * | 1993-03-25 | 1994-09-26 | Alexey Terskikh | Carcinoembryonic antigen derivatives |
| US6632613B1 (en) * | 1993-06-02 | 2003-10-14 | University Of Utah Research Foundation | Compositions and kits for fluorescence polarization assay of large molecules |
| GB9312324D0 (en) * | 1993-06-15 | 1993-07-28 | Pitman Moore Inc | Vaccine |
| US5571711A (en) | 1993-06-17 | 1996-11-05 | Ludwig Institute For Cancer Research | Isolated nucleic acid molecules coding for BAGE tumor rejection antigen precursors |
| JPH09502604A (ja) * | 1993-08-27 | 1997-03-18 | エンテリック リサーチ ラボラトリーズ インコーポレイテッド | Ｃａｍｐｙｌｏｂａｃｔｅｒｊｅｊｕｎｉ抗原、並びにそれらの製造及び利用 |
| EP0716697B1 (en) * | 1993-09-03 | 2003-04-02 | McGILL UNIVERSITY | DIFFERENTIALLY EXPRESSED $i(LEISHMANIA) GENES AND PROTEINS |
| GB9322702D0 (en) * | 1993-11-03 | 1993-12-22 | Agricultural & Food Res | Vaccines |
| US7691632B2 (en) * | 1993-11-18 | 2010-04-06 | Cold Spring Harbor Laboratory | Kit for detecting the level of cyclin-dependent kinase inhibitor P16 gene expression |
| SE9400088D0 (sv) * | 1994-01-14 | 1994-01-14 | Kabi Pharmacia Ab | Bacterial receptor structures |
| US6740734B1 (en) | 1994-01-14 | 2004-05-25 | Biovitrum Ab | Bacterial receptor structures |
| AUPM368994A0 (en) * | 1994-02-04 | 1994-02-24 | Saramane Pty Ltd | Malaria merozoite antigen subunit vaccine |
| EP0746622B1 (en) * | 1994-02-09 | 2002-10-16 | Syngenta Mogen B.V. | Antifungal proteins, dna coding therefor, and hosts incorporating same |
| DE69503038T2 (de) | 1994-02-14 | 1999-03-25 | Amgen Inc., Thousand Oaks, Calif. | Zellzyklusprotein in Säugetieren |
| US20030129204A1 (en) * | 1994-03-25 | 2003-07-10 | Moredun Scientific Limited | Vaccines against helminthic parasites |
| US5693496A (en) * | 1994-06-20 | 1997-12-02 | Merck & Co., Inc. | DNA encoding the mouse and human PH30 beta chain protein |
| DE69529219T2 (de) * | 1994-07-01 | 2003-11-06 | Chiron Corp. (N.D.Ges.D. Staates Delaware), Emeryville | Helicobacter proteine und impstoffe |
| ZA958366B (en) * | 1994-10-06 | 1996-04-24 | Akzo Nobel Nv | New toxoplasma gondii antigens |
| US6051237A (en) * | 1994-11-08 | 2000-04-18 | The Trustees Of The University Of Pennsylvania | Specific immunotherapy of cancer using a live recombinant bacterial vaccine vector |
| US8956621B2 (en) | 1994-11-08 | 2015-02-17 | The Trustees Of The University Of Pennsylvania | Compositions and methods for treatment of cervical dysplasia |
| US7635479B2 (en) * | 2000-03-29 | 2009-12-22 | The Trustees Of The University Of Pennsylvania | Composition and methods for enhancing immunogenecity of antigens |
| US8114414B2 (en) * | 1994-11-08 | 2012-02-14 | The Trustees Of The University Of Pennsylvania | Compositions and methods for treatment of cervical cancer |
| US8791237B2 (en) * | 1994-11-08 | 2014-07-29 | The Trustees Of The University Of Pennsylvania | Compositions and methods for treatment of non-hodgkins lymphoma |
| US5976543A (en) * | 1994-12-04 | 1999-11-02 | Yeda Research And Development Co., Ltd. | 12-kDa protein derived from M. Tuberculosis useful for treatment of autoimmune diseases |
| FR2728904B1 (fr) * | 1995-01-04 | 1997-03-14 | Pasteur Institut | Reactif peptidique permettant de detecter une infection primaire a virus d'epstein-barr par recherche des anticorps correspondants, et procede d'utilisation de ce reactif |
| US6287574B1 (en) * | 1995-03-17 | 2001-09-11 | Biochem Pharma Inc. | Proteinase K resistant surface protein of neisseria meningitidis |
| US6506553B1 (en) * | 1995-03-30 | 2003-01-14 | Ortho Diagnostics Systems, Inc. | Method for diagnosis of Epstein-Barr virus associated disease |
| DE69618080T2 (de) * | 1995-06-06 | 2002-06-13 | Organon Teknika B.V., Boxtel | Epstein-Barr Viruspeptide, und Antikörper gegen diese Peptide |
| ZA964896B (en) * | 1995-06-07 | 1997-01-08 | Connaught Lab | Expression of lipoproteins |
| US6251405B1 (en) * | 1995-06-07 | 2001-06-26 | Connaught Laboratories, Inc. | Immunological combination compositions and methods |
| US6936259B2 (en) | 1995-06-08 | 2005-08-30 | University Of Saskatchewan | CAMP factor of Streptococcus uberis |
| US5863543A (en) * | 1996-06-05 | 1999-01-26 | University Of Saskatchewan | Camp factor of streptococcus uberis |
| FR2736360B1 (fr) * | 1995-07-04 | 1997-09-05 | Pasteur Institut | Clonage et caracterisation du gene fiba de h.pylori, production de souches aflagellees |
| US6338852B1 (en) | 1995-09-01 | 2002-01-15 | Corixa Corporation | Compounds and methods for diagnosis of tuberculosis |
| US6458366B1 (en) * | 1995-09-01 | 2002-10-01 | Corixa Corporation | Compounds and methods for diagnosis of tuberculosis |
| US6592877B1 (en) * | 1995-09-01 | 2003-07-15 | Corixa Corporation | Compounds and methods for immunotherapy and diagnosis of tuberculosis |
| US6290969B1 (en) * | 1995-09-01 | 2001-09-18 | Corixa Corporation | Compounds and methods for immunotherapy and diagnosis of tuberculosis |
| CN1214080A (zh) * | 1995-09-26 | 1999-04-14 | 华盛顿州大学 | Rfhv/kshv亚族疱疹病毒的糖蛋白b |
| US6610506B1 (en) * | 1995-12-01 | 2003-08-26 | University Technologies International, Inc. | Transferrin binding proteins of Pasteurella haemolytica and vaccines containing same |
| US6001600A (en) * | 1996-12-20 | 1999-12-14 | Smithkline Beecham Plc | DNA encoding tests polypeptides |
| GB9526356D0 (en) * | 1995-12-22 | 1996-02-21 | Smithkline Beecham Plc | Novel compounds |
| GB9526359D0 (en) * | 1995-12-22 | 1996-02-21 | Smithkline Beecham Plc | Novel compounds |
| WO1997025429A1 (en) * | 1996-01-04 | 1997-07-17 | Rican Limited | Helicobacter pylori bacterioferritin |
| US5910568A (en) * | 1996-01-11 | 1999-06-08 | The Penn State Research Foundation | Molecule involved in binding of sperm to egg surfaces and procedures for use of this molecule to enhance or decrease potential fertility |
| GB9600955D0 (en) * | 1996-01-17 | 1996-03-20 | Smithkline Beecham Plc | Novel compounds |
| DE19601754A1 (de) * | 1996-01-19 | 1997-07-24 | Hoechst Ag | Dictyocaulus viviparus Antigen zur Diagnose des Lungenwurmbefalls und zur Vakzinierung |
| US6087163A (en) * | 1997-02-06 | 2000-07-11 | The Public Health Research Institute Of The City Of New York, Inc. | Mycobacterium tuberculosis specific proteins and genes, mixtures of anitgens and uses thereof |
| US7341727B1 (en) * | 1996-05-03 | 2008-03-11 | Emergent Product Development Gaithersburg Inc. | M. catarrhalis outer membrane protein-106 polypeptide, methods of eliciting an immune response comprising same |
| NZ330050A (en) * | 1996-08-01 | 2000-01-28 | James L Wallis | Detection, prevention and treatment of papillomatus digital dermatitis in ruminants using biologically pure Serpens spp |
| US5952194A (en) * | 1996-08-01 | 1999-09-14 | Heska Corporation | Flea nucleic acid sequences and uses thereof |
| US6284255B1 (en) * | 1996-08-29 | 2001-09-04 | Genesis Research & Development Corporation Limited | Compounds and methods for treatment and diagnosis of mycobacterial infections |
| US6190659B1 (en) * | 1996-09-17 | 2001-02-20 | The Rockefeller University | Bacterial plasmin binding protein and methods of use thereof |
| US5976542A (en) * | 1996-09-23 | 1999-11-02 | New England Medical Center | Compositions and methods for treatment of streptococcus pneumoniae infection |
| US6183976B1 (en) | 1996-10-01 | 2001-02-06 | Corixa Corporation | Compounds and methods for the diagnosis and treatment of B. microti infection |
| US6306396B1 (en) * | 1996-10-01 | 2001-10-23 | Corixa Corporation | Compounds and methods for the diagnosis and treatment of B. microti infection |
| US6451315B1 (en) | 1996-10-01 | 2002-09-17 | Corixa Corporation | Compounds and methods for the diagnosis and treatment of B. microti infection |
| US20040023865A1 (en) * | 1996-10-01 | 2004-02-05 | Corixa Corporation | Compounds and methods for the diagnosis and treatment of B. microti infection |
| US6214971B1 (en) | 1996-10-01 | 2001-04-10 | Corixa Corporation | Compounds and methods for the diagnosis and treatment of Babesia microti infection |
| US6569433B1 (en) | 1996-10-01 | 2003-05-27 | Corixa Corporation | Compounds and methods for the diagnosis and treatment of B. microti infection |
| US6593147B1 (en) | 1996-10-17 | 2003-07-15 | University Of Florida Research Foundation, Inc. | Nucleic acid vaccines against rickettsial diseases and methods of use |
| US6025338A (en) | 1996-10-17 | 2000-02-15 | University Of Florida | Nucleic acid vaccines against rickettsial diseases and methods of use |
| US6653128B2 (en) | 1996-10-17 | 2003-11-25 | University Of Florida | Nucleic acid vaccines against rickettsial diseases and methods of use |
| US6372887B1 (en) * | 1996-11-07 | 2002-04-16 | Heska Corporation | Flea serine protease inhibitor proteins |
| US5869290A (en) * | 1996-11-21 | 1999-02-09 | Smithkline Beecham Corporation | Cayae1 polynucleotides |
| US6403093B1 (en) * | 1997-03-21 | 2002-06-11 | Mayo Foundation For Medical Education And Research | Methods to detect granulocytic ehrlichiosis |
| US6555653B2 (en) | 1997-05-20 | 2003-04-29 | Corixa Corporation | Compounds for diagnosis of tuberculosis and methods for their use |
| US6613881B1 (en) | 1997-05-20 | 2003-09-02 | Corixa Corporation | Compounds for immunotherapy and diagnosis of tuberculosis and methods of their use |
| US7087713B2 (en) * | 2000-02-25 | 2006-08-08 | Corixa Corporation | Compounds and methods for diagnosis and immunotherapy of tuberculosis |
| AUPO784197A0 (en) * | 1997-07-10 | 1997-08-07 | Csl Limited | Treatment of nasopharyngeal carcinoma |
| US7964192B1 (en) | 1997-12-02 | 2011-06-21 | Janssen Alzheimer Immunotherapy | Prevention and treatment of amyloidgenic disease |
| US7790856B2 (en) | 1998-04-07 | 2010-09-07 | Janssen Alzheimer Immunotherapy | Humanized antibodies that recognize beta amyloid peptide |
| US7588766B1 (en) * | 2000-05-26 | 2009-09-15 | Elan Pharma International Limited | Treatment of amyloidogenic disease |
| TWI239847B (en) | 1997-12-02 | 2005-09-21 | Elan Pharm Inc | N-terminal fragment of Abeta peptide and an adjuvant for preventing and treating amyloidogenic disease |
| US20080050367A1 (en) | 1998-04-07 | 2008-02-28 | Guriq Basi | Humanized antibodies that recognize beta amyloid peptide |
| US6761888B1 (en) | 2000-05-26 | 2004-07-13 | Neuralab Limited | Passive immunization treatment of Alzheimer's disease |
| JP2002529705A (ja) * | 1998-10-29 | 2002-09-10 | コンネクス・ゲーエムベーハー | 糞便中の耐酸性微生物を検出するための新規方法 |
| US6465633B1 (en) | 1998-12-24 | 2002-10-15 | Corixa Corporation | Compositions and methods of their use in the treatment, prevention and diagnosis of tuberculosis |
| MXPA01009256A (es) * | 1999-03-12 | 2003-07-14 | Aventis Pasteur | Antigenos de chlamydia y fragmentos de acido desoxirribonucleico correspondientes y usos de los mismos. |
| US8143386B2 (en) * | 1999-04-07 | 2012-03-27 | Corixa Corporation | Fusion proteins of mycobacterium tuberculosis antigens and their uses |
| US6602977B1 (en) | 1999-04-19 | 2003-08-05 | Biovitrum Ab | Receptor structures |
| WO2001024820A1 (en) | 1999-10-07 | 2001-04-12 | Corixa Corporation | Fusion proteins of mycobacterium tuberculosis |
| WO2001098460A2 (en) * | 2000-06-20 | 2001-12-27 | Corixa Corporation | Fusion proteins of mycobacterium tuberculosis |
| US6821739B2 (en) * | 2000-10-13 | 2004-11-23 | The Regents Of The University Of California | Methods of diagnosing and treating Crohn's disease using Pseudomonas antigens |
| US7700751B2 (en) | 2000-12-06 | 2010-04-20 | Janssen Alzheimer Immunotherapy | Humanized antibodies that recognize β-amyloid peptide |
| US7700344B2 (en) * | 2001-03-26 | 2010-04-20 | The Trustees Of The University Of Pennsylvania | Compositions and methods for enhancing the immunogenicity of antigens |
| US8771702B2 (en) | 2001-03-26 | 2014-07-08 | The Trustees Of The University Of Pennsylvania | Non-hemolytic LLO fusion proteins and methods of utilizing same |
| CA2458854A1 (en) * | 2001-08-31 | 2003-03-06 | Chiron Srl | Helicobacter pylori vaccination |
| NO318426B1 (no) | 2001-10-02 | 2005-04-18 | Neurozym Biotech As | Et materiale for a senke konsentrasjonen av patogene tarmpeptider |
| WO2003070187A2 (en) * | 2002-02-15 | 2003-08-28 | Corixa Corporation | Fusion proteins of mycobacterium tuberculosis |
| MY139983A (en) | 2002-03-12 | 2009-11-30 | Janssen Alzheimer Immunotherap | Humanized antibodies that recognize beta amyloid peptide |
| US7344718B2 (en) * | 2003-01-31 | 2008-03-18 | University Of North Dakota | Yersinia species compositions |
| NZ567324A (en) * | 2003-02-01 | 2009-08-28 | Wyeth Corp | Active immunization to generate antibodies to soluble A-beta |
| PE20050627A1 (es) | 2003-05-30 | 2005-08-10 | Wyeth Corp | Anticuerpos humanizados que reconocen el peptido beta amiloideo |
| EP1670506B1 (en) * | 2003-10-02 | 2012-11-21 | Novartis AG | Liquid vaccines for multiple meningococcal serogroups |
| AR052051A1 (es) | 2004-12-15 | 2007-02-28 | Neuralab Ltd | Anticuerpos ab humanizados usados en mejorar la cognicion |
| ES2396555T3 (es) | 2004-12-15 | 2013-02-22 | Janssen Alzheimer Immunotherapy | Anticuerpos que reconocen péptido beta amiloide |
| GB0507632D0 (en) * | 2005-04-15 | 2005-05-25 | Secr Defence | Vaccine |
| GB0519871D0 (en) * | 2005-09-30 | 2005-11-09 | Secr Defence | Immunogenic agents |
| US8784810B2 (en) | 2006-04-18 | 2014-07-22 | Janssen Alzheimer Immunotherapy | Treatment of amyloidogenic diseases |
| US8268326B2 (en) * | 2006-08-15 | 2012-09-18 | The Trustees Of The University Of Pennsylvania | Compositions comprising HMW-MAA and fragments thereof, and methods of use thereof |
| DK2977456T3 (en) * | 2006-08-15 | 2018-01-22 | Univ Pennsylvania | Compositions comprising HMW-MAA and fragments thereof for the treatment of cancer |
| LT2144924T (lt) * | 2007-04-16 | 2016-10-10 | Minervax Aps | Sulieto baltymo vakcina |
| US8003097B2 (en) | 2007-04-18 | 2011-08-23 | Janssen Alzheimer Immunotherapy | Treatment of cerebral amyloid angiopathy |
| JP5889529B2 (ja) | 2007-07-27 | 2016-03-22 | ヤンセン・サイエンシズ・アイルランド・ユーシー | アミロイド原性疾患の処置 |
| JO3076B1 (ar) | 2007-10-17 | 2017-03-15 | Janssen Alzheimer Immunotherap | نظم العلاج المناعي المعتمد على حالة apoe |
| US8758765B2 (en) * | 2008-07-29 | 2014-06-24 | The University Of Chicago | Compositions and methods related to Staphylococcal bacterium proteins |
| US9067981B1 (en) | 2008-10-30 | 2015-06-30 | Janssen Sciences Ireland Uc | Hybrid amyloid-beta antibodies |
| GB0900455D0 (en) | 2009-01-13 | 2009-02-11 | Secr Defence | Vaccine |
| EP2403935B1 (en) | 2009-03-04 | 2017-05-10 | The Trustees Of The University Of Pennsylvania | Compositions comprising angiogenic factors and methods of use thereof |
| ES2444693T3 (es) * | 2009-05-05 | 2014-02-26 | Universitätsklinikum Freiburg | Polipéptido derivado de enterococo y su uso para vacunación |
| EP2717909B1 (en) * | 2011-06-04 | 2017-12-06 | Rochester General Hospital Research Institute | Compositions and methods related to p6 of haemophilus influenzae |
| WO2012178078A2 (en) | 2011-06-22 | 2012-12-27 | University Of North Dakota | Use of yscf, truncated yscf and yscf homologs as adjuvants |
| WO2013113000A2 (en) | 2012-01-26 | 2013-08-01 | Luc Montagnier | Detection of dna sequences as risk factors for hiv infection |
| WO2014025254A1 (en) | 2012-08-10 | 2014-02-13 | Stichting Vu-Vumc | Ebv markers and systemic lupus erythematosus |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4707358A (en) * | 1984-01-30 | 1987-11-17 | The University Of Chicago | Vaccine against Epstein-Barr Virus |
| US4654419A (en) * | 1984-08-08 | 1987-03-31 | Scripps Clinic And Research Foundation | Synthetic polypeptides and antibodies related to epstein-barr virus nuclear antigen |
-
1986
- 1986-12-05 US US06/938,643 patent/US4879213A/en not_active Expired - Lifetime
-
1987
- 1987-12-01 ZA ZA879025A patent/ZA879025B/xx unknown
- 1987-12-02 ES ES87310609T patent/ES2054692T3/es not_active Expired - Lifetime
- 1987-12-02 IL IL84690A patent/IL84690A/xx not_active IP Right Cessation
- 1987-12-02 EP EP87310609A patent/EP0280813B1/en not_active Expired - Lifetime
- 1987-12-02 AT AT87310609T patent/ATE107316T1/de not_active IP Right Cessation
- 1987-12-02 DE DE3750088T patent/DE3750088T2/de not_active Expired - Lifetime
- 1987-12-03 NZ NZ222794A patent/NZ222794A/xx unknown
- 1987-12-03 AU AU82073/87A patent/AU610099B2/en not_active Expired
- 1987-12-04 CA CA000553508A patent/CA1315481C/en not_active Expired - Fee Related
- 1987-12-04 DK DK198706388A patent/DK173262B1/da not_active IP Right Cessation
- 1987-12-04 JP JP62307353A patent/JP2624973B2/ja not_active Expired - Lifetime
- 1987-12-04 IE IE330387A patent/IE63368B1/en not_active IP Right Cessation
-
1994
- 1994-11-16 JP JP6281648A patent/JP2682959B2/ja not_active Expired - Lifetime
Also Published As
| Publication number | Publication date |
|---|---|
| ATE107316T1 (de) | 1994-07-15 |
| EP0280813B1 (en) | 1994-06-15 |
| JP2624973B2 (ja) | 1997-06-25 |
| AU8207387A (en) | 1988-06-09 |
| DE3750088T2 (de) | 1994-12-01 |
| NZ222794A (en) | 1991-01-29 |
| EP0280813A3 (en) | 1990-06-06 |
| JPH07233200A (ja) | 1995-09-05 |
| AU610099B2 (en) | 1991-05-16 |
| IE63368B1 (en) | 1995-04-19 |
| DE3750088D1 (de) | 1994-07-21 |
| EP0280813A2 (en) | 1988-09-07 |
| DK638887A (da) | 1988-06-06 |
| IL84690A0 (en) | 1988-05-31 |
| DK638887D0 (da) | 1987-12-04 |
| ES2054692T3 (es) | 1994-08-16 |
| US4879213A (en) | 1989-11-07 |
| CA1315481C (en) | 1993-03-30 |
| ZA879025B (en) | 1988-05-27 |
| JPS63225398A (ja) | 1988-09-20 |
| IL84690A (en) | 1992-11-15 |
| JP2682959B2 (ja) | 1997-11-26 |
| IE873303L (en) | 1988-06-05 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| B1 | Patent granted (law 1993) | ||
| PUP | Patent expired |