ES2251831T3 - Inhibidores de la activacion de nf-kb. - Google Patents
Inhibidores de la activacion de nf-kb.Info
- Publication number
- ES2251831T3 ES2251831T3 ES99924594T ES99924594T ES2251831T3 ES 2251831 T3 ES2251831 T3 ES 2251831T3 ES 99924594 T ES99924594 T ES 99924594T ES 99924594 T ES99924594 T ES 99924594T ES 2251831 T3 ES2251831 T3 ES 2251831T3
- Authority
- ES
- Spain
- Prior art keywords
- protein
- baselineskip
- activation
- kappab
- seq
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
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- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
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Landscapes
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Applications Claiming Priority (2)
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| EP98201472 | 1998-05-06 | ||
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| ES99924594T Expired - Lifetime ES2251831T3 (es) | 1998-05-06 | 1999-05-05 | Inhibidores de la activacion de nf-kb. |
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| EP1075519B1 (en) | 1998-05-06 | 2005-11-09 | Vlaams Interuniversitair Instituut voor Biotechnologie vzw. | Inhibitors of nf-kb activation |
| GB9930616D0 (en) * | 1999-12-24 | 2000-02-16 | Mathilda & Terence Kennedy Ins | Activation and inhibition of the immune system |
| AU2002350412B2 (en) * | 2001-06-22 | 2006-06-15 | Vlaams Interuniversitair Instituut Voor Biotechnologie Vzw | Abin-mediated hepatitis protection |
| US7700553B2 (en) | 2003-09-24 | 2010-04-20 | Institut Pasteur | Selective inhibition of NF-κB activation by peptides designed to disrupt nemo oligomerization |
| WO2006029981A1 (en) * | 2004-09-13 | 2006-03-23 | Vib Vzw | Abin-mediated protection against lung inflammatory disease |
| CN1304418C (zh) * | 2005-02-22 | 2007-03-14 | 中国人民解放军第三军医大学第三附属医院 | 核因子－κB p65亚基拮抗肽及其应用 |
| WO2006108844A1 (en) * | 2005-04-14 | 2006-10-19 | Vib Vzw | Treatment of egfr dependent tumors by abin (a20-binding inhibitor of nf kappab) |
| CA2667972A1 (en) * | 2006-10-30 | 2008-05-08 | Michael Tovey | Gene reporter assay, kit and cells with improved sensitivity and/or specificity for determining the level of an extracellular signal |
| CN101307094B (zh) * | 2008-03-21 | 2011-09-28 | 中国人民解放军第三军医大学第三附属医院 | 一种核因子-κB p65亚基拮抗多肽 |
| CN101798336B (zh) * | 2009-02-06 | 2012-02-29 | 中国人民解放军第三军医大学第三附属医院 | 一种具有示踪功能的抗肿瘤化合物 |
| CN111606976A (zh) * | 2020-05-26 | 2020-09-01 | 中国人民解放军军事科学院军事医学研究院 | 一种小肽及其在抑制阿片成瘾性和耐受性上的应用 |
Family Cites Families (18)
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|---|---|---|---|---|
| US4217344A (en) * | 1976-06-23 | 1980-08-12 | L'oreal | Compositions containing aqueous dispersions of lipid spheres |
| US4235871A (en) * | 1978-02-24 | 1980-11-25 | Papahadjopoulos Demetrios P | Method of encapsulating biologically active materials in lipid vesicles |
| US4186183A (en) * | 1978-03-29 | 1980-01-29 | The United States Of America As Represented By The Secretary Of The Army | Liposome carriers in chemotherapy of leishmaniasis |
| US4261975A (en) * | 1979-09-19 | 1981-04-14 | Merck & Co., Inc. | Viral liposome particle |
| US4485054A (en) * | 1982-10-04 | 1984-11-27 | Lipoderm Pharmaceuticals Limited | Method of encapsulating biologically active materials in multilamellar lipid vesicles (MLV) |
| US4501728A (en) * | 1983-01-06 | 1985-02-26 | Technology Unlimited, Inc. | Masking of liposomes from RES recognition |
| US4946787A (en) * | 1985-01-07 | 1990-08-07 | Syntex (U.S.A.) Inc. | N-(ω,(ω-1)-dialkyloxy)- and N-(ω,(ω-1)-dialkenyloxy)-alk-1-yl-N,N,N-tetrasubstituted ammonium lipids and uses therefor |
| US5049386A (en) * | 1985-01-07 | 1991-09-17 | Syntex (U.S.A.) Inc. | N-ω,(ω-1)-dialkyloxy)- and N-(ω,(ω-1)-dialkenyloxy)Alk-1-YL-N,N,N-tetrasubstituted ammonium lipids and uses therefor |
| US4897355A (en) * | 1985-01-07 | 1990-01-30 | Syntex (U.S.A.) Inc. | N[ω,(ω-1)-dialkyloxy]- and N-[ω,(ω-1)-dialkenyloxy]-alk-1-yl-N,N,N-tetrasubstituted ammonium lipids and uses therefor |
| US4797368A (en) * | 1985-03-15 | 1989-01-10 | The United States Of America As Represented By The Department Of Health And Human Services | Adeno-associated virus as eukaryotic expression vector |
| US4774085A (en) * | 1985-07-09 | 1988-09-27 | 501 Board of Regents, Univ. of Texas | Pharmaceutical administration systems containing a mixture of immunomodulators |
| US4837028A (en) * | 1986-12-24 | 1989-06-06 | Liposome Technology, Inc. | Liposomes with enhanced circulation time |
| US5264618A (en) | 1990-04-19 | 1993-11-23 | Vical, Inc. | Cationic lipids for intracellular delivery of biologically active molecules |
| WO1991017424A1 (en) | 1990-05-03 | 1991-11-14 | Vical, Inc. | Intracellular delivery of biologically active substances by means of self-assembling lipid complexes |
| US5173414A (en) * | 1990-10-30 | 1992-12-22 | Applied Immune Sciences, Inc. | Production of recombinant adeno-associated virus vectors |
| US5587308A (en) | 1992-06-02 | 1996-12-24 | The United States Of America As Represented By The Department Of Health & Human Services | Modified adeno-associated virus vector capable of expression from a novel promoter |
| UA71889C2 (uk) * | 1996-04-02 | 2005-01-17 | Йєда Рісерч Енд Дівелопмент Ко. Лтд. | Модулятори зв'язаного з рецептором tnf фактора (traf), їх одержання та застосування |
| EP1075519B1 (en) | 1998-05-06 | 2005-11-09 | Vlaams Interuniversitair Instituut voor Biotechnologie vzw. | Inhibitors of nf-kb activation |
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1999
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- 1999-05-05 ES ES99924594T patent/ES2251831T3/es not_active Expired - Lifetime
- 1999-05-05 WO PCT/BE1999/000055 patent/WO1999057133A2/en not_active Ceased
- 1999-05-05 CA CA002328483A patent/CA2328483A1/en not_active Abandoned
- 1999-05-05 AU AU41244/99A patent/AU754434B2/en not_active Ceased
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- 1999-05-05 JP JP2000547102A patent/JP2002513552A/ja active Pending
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2003
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| WO1999057133A3 (en) | 2000-02-24 |
| DE69928244D1 (de) | 2005-12-15 |
| DE69928244T2 (de) | 2006-08-10 |
| AU754434B2 (en) | 2002-11-14 |
| WO1999057133A2 (en) | 1999-11-11 |
| JP2002513552A (ja) | 2002-05-14 |
| CA2328483A1 (en) | 1999-11-11 |
| US7414026B2 (en) | 2008-08-19 |
| US6673897B1 (en) | 2004-01-06 |
| ATE309352T1 (de) | 2005-11-15 |
| AU4124499A (en) | 1999-11-23 |
| EP1075519A2 (en) | 2001-02-14 |
| EP1075519B1 (en) | 2005-11-09 |
| US20040092430A1 (en) | 2004-05-13 |
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