ZA200306647B - Vaccine. - Google Patents
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- ZA200306647B ZA200306647B ZA200306647A ZA200306647A ZA200306647B ZA 200306647 B ZA200306647 B ZA 200306647B ZA 200306647 A ZA200306647 A ZA 200306647A ZA 200306647 A ZA200306647 A ZA 200306647A ZA 200306647 B ZA200306647 B ZA 200306647B
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- 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
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- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
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Landscapes
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| AU (1) | AU2002233560B2 (hu) |
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| WO (1) | WO2002070711A1 (hu) |
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| DE60022665T2 (de) * | 1999-09-25 | 2006-06-22 | Coley Pharmaceutical Gmbh | Immunstimulierende nukeinsäuren |
| US7560534B2 (en) | 2000-05-08 | 2009-07-14 | Celldex Research Corporation | Molecular conjugates comprising human monoclonal antibodies to dendritic cells |
| JP2006501249A (ja) * | 2002-08-30 | 2006-01-12 | グラクソ グループ リミテッド | ワクチン |
| US20060147417A1 (en) * | 2002-08-30 | 2006-07-06 | Claire Ashman | Immunogenic composition comprising an il-13 element and t cell epitopes, and its therapeutic use |
| JP2006504413A (ja) * | 2002-09-12 | 2006-02-09 | ファーメクサ エイ／エス | 自家グレリンに対する免疫化 |
| CN1767852B (zh) * | 2003-01-31 | 2010-04-14 | 塞尔德克斯医疗公司 | 抗体疫苗缀合物及其用途 |
| US9259459B2 (en) * | 2003-01-31 | 2016-02-16 | Celldex Therapeutics Inc. | Antibody vaccine conjugates and uses therefor |
| MXPA05010222A (es) * | 2003-03-24 | 2006-05-22 | Mercia Pharma Llc | Metodos y composiciones para tratar y prevenir condiciones inflamatorias. |
| WO2004096849A2 (en) * | 2003-04-25 | 2004-11-11 | University Of Manitoba | Peptide-based cytokine/chemokine vaccines against allergy |
| US7501121B2 (en) * | 2004-06-17 | 2009-03-10 | Wyeth | IL-13 binding agents |
| 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 |
| DK1767216T3 (da) * | 2004-06-11 | 2012-09-03 | Riken | Lægemiddel med regulatorisk celleligand indeholdt i liposom |
| TWI307630B (en) | 2004-07-01 | 2009-03-21 | Glaxo Group Ltd | Immunoglobulins |
| SI2068918T1 (sl) | 2006-09-26 | 2012-09-28 | Infectious Disease Res Inst | Si - ep sestavek za cepljenje, ki vsebuje sintetiäśna pomagala |
| US20090181078A1 (en) * | 2006-09-26 | 2009-07-16 | Infectious Disease Research Institute | Vaccine composition containing synthetic adjuvant |
| CA2685123A1 (en) * | 2007-04-23 | 2008-10-30 | Wyeth | Methods and compositions for treating and monitoring treatment of il-13-associated disorders |
| US20080299138A1 (en) * | 2007-05-25 | 2008-12-04 | Duffy Karen E | Toll-Like Receptor 3 Modulators and Uses Thereof |
| EA201692127A1 (ru) | 2007-11-07 | 2017-08-31 | Селлдекс Терапьютикс Инк. | Антитела, связывающиеся с человеческим dec-205 |
| PT2850431T (pt) | 2012-05-16 | 2018-07-23 | Immune Design Corp | Vacinas para hsv-2 |
| JP6426706B2 (ja) | 2013-04-18 | 2018-11-21 | イミューン デザイン コーポレイション | がん処置で使用するためのｇｌａ単剤療法 |
| US9463198B2 (en) | 2013-06-04 | 2016-10-11 | Infectious Disease Research Institute | Compositions and methods for reducing or preventing metastasis |
| AU2022212600A1 (en) * | 2021-01-29 | 2023-08-17 | Bayer Animal Health Gmbh | Vaccine composition for breaking self-tolerance |
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 |
| US4436727A (en) * | 1982-05-26 | 1984-03-13 | Ribi Immunochem Research, Inc. | Refined detoxified endotoxin product |
| US4866034A (en) * | 1982-05-26 | 1989-09-12 | Ribi Immunochem Research Inc. | Refined detoxified endotoxin |
| 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 |
| EP1167379A3 (en) * | 1994-07-15 | 2004-09-08 | University Of Iowa Research Foundation | Immunomodulatory oligonucleotides |
| EP0770135A1 (en) * | 1994-07-29 | 1997-05-02 | Smithkline Beecham Plc | Novel compounds |
| US5696234A (en) * | 1994-08-01 | 1997-12-09 | Schering Corporation | Muteins of mammalian cytokine interleukin-13 |
| US6818217B1 (en) * | 1995-02-20 | 2004-11-16 | Amrad Corporation Limited | Immunoreactive peptides |
| 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 |
| 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 |
| 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 |
| WO1999003887A1 (en) * | 1997-07-14 | 1999-01-28 | Bolder Biotechnology, Inc. | Derivatives of growth hormone and related proteins |
| 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 |
| JP2002506618A (ja) * | 1998-03-20 | 2002-03-05 | ジェンザイム・コーポレーション | 腫瘍自己抗原に対する免疫誘導 |
| 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 |
| AU1599301A (en) * | 1999-11-11 | 2001-06-06 | Government Of The United States Of America, As Represented By The Secretary Of The Department Of Health And Human Services, The | Modulating IL-13 activity using mutated IL-13 molecules that are antagonists or agonists of IL-13 |
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2002
- 2002-03-01 MX MXPA03007915A patent/MXPA03007915A/es not_active Application Discontinuation
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- 2002-03-01 HU HU0303372A patent/HUP0303372A3/hu unknown
- 2002-03-01 CZ CZ20032373A patent/CZ20032373A3/cs unknown
- 2002-03-01 US US10/469,561 patent/US20050260216A1/en not_active Abandoned
- 2002-03-01 KR KR10-2003-7011573A patent/KR20030081490A/ko not_active Application Discontinuation
- 2002-03-01 WO PCT/GB2002/000900 patent/WO2002070711A1/en not_active Application Discontinuation
- 2002-03-01 IL IL15749802A patent/IL157498A0/xx unknown
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- 2002-03-01 BR BR0207819-8A patent/BR0207819A/pt not_active IP Right Cessation
- 2002-03-01 EP EP02700490A patent/EP1368477A1/en not_active Withdrawn
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- 2002-03-01 JP JP2002570736A patent/JP4238031B2/ja not_active Expired - Fee Related
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| CZ20032373A3 (cs) | 2004-01-14 |
| US20030194391A1 (en) | 2003-10-16 |
| NO20033882L (no) | 2003-10-31 |
| AU2002233560B2 (en) | 2006-09-07 |
| NO20033882D0 (no) | 2003-09-02 |
| KR20030081490A (ko) | 2003-10-17 |
| GB0105360D0 (en) | 2001-04-18 |
| HUP0303372A3 (en) | 2008-06-30 |
| EP1368477A1 (en) | 2003-12-10 |
| IL157498A0 (en) | 2004-03-28 |
| JP2005502314A (ja) | 2005-01-27 |
| NZ527873A (en) | 2005-12-23 |
| CN1543504A (zh) | 2004-11-03 |
| BR0207819A (pt) | 2004-03-02 |
| US20050260216A1 (en) | 2005-11-24 |
| WO2002070711A1 (en) | 2002-09-12 |
| PL365066A1 (en) | 2004-12-27 |
| US20050186209A1 (en) | 2005-08-25 |
| HUP0303372A2 (hu) | 2004-01-28 |
| MXPA03007915A (es) | 2003-12-04 |
| JP4238031B2 (ja) | 2009-03-11 |
| CA2439628A1 (en) | 2002-09-12 |
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