NZ527873A - Vaccine - Google Patents
VaccineInfo
- Publication number
- NZ527873A NZ527873A NZ527873A NZ52787302A NZ527873A NZ 527873 A NZ527873 A NZ 527873A NZ 527873 A NZ527873 A NZ 527873A NZ 52787302 A NZ52787302 A NZ 52787302A NZ 527873 A NZ527873 A NZ 527873A
- Authority
- NZ
- New Zealand
- Prior art keywords
- protein
- human
- mouse
- sequence
- vaccine
- Prior art date
Links
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- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
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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
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/54—Interleukins [IL]
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- C07—ORGANIC CHEMISTRY
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- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
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- C07—ORGANIC CHEMISTRY
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Landscapes
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- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
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Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
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| GBGB0105360.2A GB0105360D0 (en) | 2001-03-03 | 2001-03-03 | Chimaeric immunogens |
| PCT/GB2002/000900 WO2002070711A1 (en) | 2001-03-03 | 2002-03-01 | Vaccine |
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| NZ527873A true NZ527873A (en) | 2005-12-23 |
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| NZ527873A NZ527873A (en) | 2001-03-03 | 2002-03-01 | Vaccine |
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| EP (1) | EP1368477A1 (https=) |
| JP (1) | JP4238031B2 (https=) |
| KR (1) | KR20030081490A (https=) |
| CN (1) | CN1543504A (https=) |
| AU (1) | AU2002233560B2 (https=) |
| BR (1) | BR0207819A (https=) |
| CA (1) | CA2439628A1 (https=) |
| CZ (1) | CZ20032373A3 (https=) |
| GB (1) | GB0105360D0 (https=) |
| HU (1) | HUP0303372A3 (https=) |
| IL (1) | IL157498A0 (https=) |
| MX (1) | MXPA03007915A (https=) |
| NO (1) | NO20033882L (https=) |
| NZ (1) | NZ527873A (https=) |
| PL (1) | PL365066A1 (https=) |
| WO (1) | WO2002070711A1 (https=) |
| ZA (1) | ZA200306647B (https=) |
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| US7560534B2 (en) | 2000-05-08 | 2009-07-14 | Celldex Research Corporation | Molecular conjugates comprising human monoclonal antibodies to dendritic cells |
| JP2006503017A (ja) * | 2002-08-30 | 2006-01-26 | グラクソ グループ リミテッド | Ｉｌ−１３要素及びｔ細胞エピトープを含む免疫原組成物並びにその治療上の使用 |
| JP2006503018A (ja) * | 2002-08-30 | 2006-01-26 | グラクソ グループ リミテッド | ワクチン |
| EP1539232A1 (en) * | 2002-09-12 | 2005-06-15 | Pharmexa A/S | Immunization against autologous ghrelin |
| US9259459B2 (en) * | 2003-01-31 | 2016-02-16 | Celldex Therapeutics Inc. | Antibody vaccine conjugates and uses therefor |
| CA2514979A1 (en) * | 2003-01-31 | 2004-09-02 | Celldex Therapeutics, Inc. | Antibody vaccine conjugates and uses therefor |
| EP1608316A4 (en) * | 2003-03-24 | 2007-08-15 | Mercia Pharma Inc | METHOD AND COMPOSITIONS FOR THE TREATMENT AND PREVENTION OF INFLAMMATORY CONDITIONS |
| WO2004096849A2 (en) * | 2003-04-25 | 2004-11-11 | University Of Manitoba | Peptide-based cytokine/chemokine vaccines against allergy |
| US20090098142A1 (en) * | 2004-06-09 | 2009-04-16 | Kasaian Marion T | Methods and compositions for treating and monitoring treatment of IL-13-associated disorders |
| AR049390A1 (es) * | 2004-06-09 | 2006-07-26 | Wyeth Corp | Anticuerpos contra la interleuquina-13 humana y usos de los mismos |
| US7501121B2 (en) * | 2004-06-17 | 2009-03-10 | Wyeth | IL-13 binding agents |
| ES2389080T3 (es) * | 2004-06-11 | 2012-10-23 | Riken | Fármaco que presenta un ligando de células reguladoras contenido en el liposoma |
| TWI307630B (en) | 2004-07-01 | 2009-03-21 | Glaxo Group Ltd | Immunoglobulins |
| US20090181078A1 (en) * | 2006-09-26 | 2009-07-16 | Infectious Disease Research Institute | Vaccine composition containing synthetic adjuvant |
| PT2468300T (pt) | 2006-09-26 | 2018-01-30 | Infectious Disease Res Inst | Composição para vacina contendo adjuvante sintético |
| BRPI0810561A2 (pt) * | 2007-04-23 | 2019-09-24 | Wyeth Corp | métodos e composições para tratar e monitorar tratamento de desordens associadas à il-13. |
| EP2155889A4 (en) * | 2007-05-25 | 2010-06-16 | Centocor Ortho Biotech Inc | TOLL RECEPTOR 3 MODULATORS AND USES THEREOF |
| NZ599777A (en) * | 2007-11-07 | 2013-09-27 | Celldex Therapeutics Inc | Antibodies that bind human dendritic and epithelial cell 205 (DEC-205) |
| KR102136433B1 (ko) | 2012-05-16 | 2020-07-22 | 이뮨 디자인 코포레이션 | Hsv-2 백신 |
| EP2986303B1 (en) | 2013-04-18 | 2020-02-26 | Immune Design Corp. | Gla monotherapy for use in cancer treatment |
| US9463198B2 (en) | 2013-06-04 | 2016-10-11 | Infectious Disease Research Institute | Compositions and methods for reducing or preventing metastasis |
| CN117222664A (zh) * | 2021-01-29 | 2023-12-12 | 拜耳动物保健有限责任公司 | 用于破坏自身耐受的疫苗组合物 |
Family Cites Families (27)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4554101A (en) * | 1981-01-09 | 1985-11-19 | New York Blood Center, Inc. | Identification and preparation of epitopes on antigens and allergens on the basis of hydrophilicity |
| US4866034A (en) * | 1982-05-26 | 1989-09-12 | Ribi Immunochem Research Inc. | Refined detoxified endotoxin |
| US4436727A (en) * | 1982-05-26 | 1984-03-13 | Ribi Immunochem Research, Inc. | Refined detoxified endotoxin product |
| US4945050A (en) * | 1984-11-13 | 1990-07-31 | Cornell Research Foundation, Inc. | Method for transporting substances into living cells and tissues and apparatus therefor |
| US4877611A (en) * | 1986-04-15 | 1989-10-31 | Ribi Immunochem Research Inc. | Vaccine containing tumor antigens and adjuvants |
| US5278302A (en) * | 1988-05-26 | 1994-01-11 | University Patents, Inc. | Polynucleotide phosphorodithioates |
| US4912094B1 (en) * | 1988-06-29 | 1994-02-15 | Ribi Immunochem Research Inc. | Modified lipopolysaccharides and process of preparation |
| US5697901A (en) * | 1989-12-14 | 1997-12-16 | Elof Eriksson | Gene delivery by microneedle injection |
| AU661684B2 (en) * | 1991-06-18 | 1995-08-03 | Regents Of The University Of California, The | Cloned glutamic acid decarboxylase |
| DE4137333A1 (de) * | 1991-11-13 | 1993-05-19 | W Prof Dr Sebald | Therapeutische mittel, die antagonisten oder partielle agonisten des humanen interleukin 4 sind oder diese enthalten, hil-4-mutantenproteine sowie vefahren zu deren herstellung |
| ATE509102T1 (de) * | 1994-07-15 | 2011-05-15 | Univ Iowa Res Found | Immunomodulatorische oligonukleotide |
| JPH10503371A (ja) * | 1994-07-29 | 1998-03-31 | スミスクライン・ビーチャム・パブリック・リミテッド・カンパニー | 新規化合物 |
| US5696234A (en) * | 1994-08-01 | 1997-12-09 | Schering Corporation | Muteins of mammalian cytokine interleukin-13 |
| CA2213301C (en) * | 1995-02-20 | 2010-01-26 | Amrad Operations Pty. Ltd. | Immunoreactive and immunotherapeutic molecules which interact in subjects with insulin-dependent diabetes mellitus (iddm) |
| US5614191A (en) * | 1995-03-15 | 1997-03-25 | The United States Of America As Represented By The Department Of Health And Human Services | IL-13 receptor specific chimeric proteins and uses thereof |
| US6518061B1 (en) * | 1995-03-15 | 2003-02-11 | The United States Of America As Represented By The Department Of Health And Human Services | IL-13 receptor specific chimeric proteins and uses thereof |
| EP0759468A1 (en) * | 1995-08-10 | 1997-02-26 | Laboratoires Virbac | Feline interleukin-4 |
| US5666153A (en) * | 1995-10-03 | 1997-09-09 | Virtual Shopping, Inc. | Retractable teleconferencing apparatus |
| US6664227B1 (en) * | 1996-03-01 | 2003-12-16 | Genetics Institute, Llc | Treatment of fibrosis by antagonism of IL-13 and IL-13 receptor chains |
| US5843449A (en) * | 1996-03-25 | 1998-12-01 | Akzo Nobel N.V. | Proteins and novel peptides derived from autoantigen for use in immunotherapy of autoimmune diseases |
| US5856462A (en) * | 1996-09-10 | 1999-01-05 | Hybridon Incorporated | Oligonucleotides having modified CpG dinucleosides |
| ATE375363T1 (de) * | 1997-07-14 | 2007-10-15 | Bolder Biotechnology Inc | Derivate des wachstumshormons und verwandte proteine |
| EP0911401A1 (en) * | 1997-10-21 | 1999-04-28 | Bayer Ag | Muteins of interleukin 4 showing low-affinity and short-term interaction with the common gamma chain |
| CA2322624A1 (en) * | 1998-03-20 | 1999-09-23 | Genzyme Corporation | Induction of immunity against tumor self-antigens |
| US6576232B1 (en) * | 1998-04-03 | 2003-06-10 | The Penn State Research Foundation | IL13 mutants |
| AU5617900A (en) * | 1999-06-17 | 2001-01-09 | Robert C. Gallo | Chimeric chemokine-antigen polypeptides and uses therefor |
| CA2404763A1 (en) * | 1999-11-11 | 2001-05-17 | Raj K. Puri | Mutated il-13 molecules and their uses |
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| HUP0303372A3 (en) | 2008-06-30 |
| US20050260216A1 (en) | 2005-11-24 |
| EP1368477A1 (en) | 2003-12-10 |
| ZA200306647B (en) | 2004-11-26 |
| NO20033882D0 (no) | 2003-09-02 |
| CZ20032373A3 (cs) | 2004-01-14 |
| CN1543504A (zh) | 2004-11-03 |
| JP4238031B2 (ja) | 2009-03-11 |
| WO2002070711A1 (en) | 2002-09-12 |
| US20030194391A1 (en) | 2003-10-16 |
| PL365066A1 (en) | 2004-12-27 |
| BR0207819A (pt) | 2004-03-02 |
| CA2439628A1 (en) | 2002-09-12 |
| IL157498A0 (en) | 2004-03-28 |
| AU2002233560B2 (en) | 2006-09-07 |
| GB0105360D0 (en) | 2001-04-18 |
| NO20033882L (no) | 2003-10-31 |
| HUP0303372A2 (hu) | 2004-01-28 |
| JP2005502314A (ja) | 2005-01-27 |
| KR20030081490A (ko) | 2003-10-17 |
| MXPA03007915A (es) | 2003-12-04 |
| US20050186209A1 (en) | 2005-08-25 |
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