NO333213B1 - Survivin-avledet peptid, farmasoytisk blanding, multi-epitop vaksine og anvendelse av peptidet for fremstilling av et medikament for behandling av kreft - Google Patents
Survivin-avledet peptid, farmasoytisk blanding, multi-epitop vaksine og anvendelse av peptidet for fremstilling av et medikament for behandling av kreft Download PDFInfo
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- NO333213B1 NO333213B1 NO20053999A NO20053999A NO333213B1 NO 333213 B1 NO333213 B1 NO 333213B1 NO 20053999 A NO20053999 A NO 20053999A NO 20053999 A NO20053999 A NO 20053999A NO 333213 B1 NO333213 B1 NO 333213B1
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Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US10/354,090 US20040210035A1 (en) | 2002-01-30 | 2003-01-30 | Survivin-derived peptides and use thereof |
| US10/715,417 US7892559B2 (en) | 2002-01-30 | 2003-11-19 | Survivin-derived peptides and use thereof |
| PCT/DK2004/000062 WO2004067023A2 (en) | 2003-01-30 | 2004-01-30 | Survivin-derived peptides and use thereof |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| NO20053999D0 NO20053999D0 (no) | 2005-08-29 |
| NO20053999L NO20053999L (no) | 2005-10-28 |
| NO333213B1 true NO333213B1 (no) | 2013-04-08 |
Family
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Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO20053999A NO333213B1 (no) | 2003-01-30 | 2005-08-29 | Survivin-avledet peptid, farmasoytisk blanding, multi-epitop vaksine og anvendelse av peptidet for fremstilling av et medikament for behandling av kreft |
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| EP (5) | EP2857034B1 (ru) |
| JP (1) | JP5121143B2 (ru) |
| CN (2) | CN101906148B (ru) |
| AT (3) | ATE454159T1 (ru) |
| AU (1) | AU2004208469B2 (ru) |
| CA (1) | CA2513104C (ru) |
| DE (3) | DE602004016287D1 (ru) |
| EA (1) | EA008026B1 (ru) |
| ES (2) | ES2312956T3 (ru) |
| HK (2) | HK1087335A1 (ru) |
| MX (1) | MXPA05008128A (ru) |
| NO (1) | NO333213B1 (ru) |
| NZ (1) | NZ541510A (ru) |
| PT (3) | PT2092938E (ru) |
| WO (1) | WO2004067023A2 (ru) |
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| US7892559B2 (en) * | 2002-01-30 | 2011-02-22 | Survac Aps | Survivin-derived peptides and use thereof |
| US20040210035A1 (en) * | 2002-01-30 | 2004-10-21 | Straten Eivind Per Thor | Survivin-derived peptides and use thereof |
| PL2087904T3 (pl) * | 2003-11-19 | 2014-01-31 | Survac Aps | Zastosowanie terapeutyczne peptydów pochodzących z białek BcL-XL u pacjentów z rakiem |
| JP4602006B2 (ja) * | 2004-06-29 | 2010-12-22 | 独立行政法人科学技術振興機構 | サバイビン由来のｈｌａ−ａ２４結合性癌抗原ペプチド |
| WO2012079878A2 (en) | 2010-12-14 | 2012-06-21 | Immatics Biotechnologies Gmbh | Hla-binding peptides derived from prostate-associated antigenic molecules and methods of use thereof |
| US8487076B1 (en) | 2005-01-25 | 2013-07-16 | Nec Corporation | HLA-binding peptide, and DNA fragment and recombinant vector coding for said HLA-binding peptide |
| AU2011203536B2 (en) * | 2005-02-04 | 2012-11-15 | Survac Aps | Survivin peptide vaccine |
| DK1853305T3 (en) | 2005-02-04 | 2014-12-01 | Survac Aps | Survivin-peptide vaccine |
| AU2011203535B2 (en) * | 2005-02-04 | 2012-10-11 | Survac Aps | Survivin peptide vaccine |
| US20060276423A1 (en) * | 2005-04-18 | 2006-12-07 | Rachel Altura | Survivin-directed RNA interference-compositions and methods |
| US20070104689A1 (en) * | 2005-09-27 | 2007-05-10 | Merck Patent Gmbh | Compositions and methods for treating tumors presenting survivin antigens |
| FR2891462B1 (fr) | 2005-09-30 | 2009-10-16 | Commissariat Energie Atomique | Epitopes t cd4+ de la survivine et leurs applications |
| IL172896A0 (en) * | 2005-12-29 | 2006-06-11 | Yeda Res & Dev | Cxcr4 inhibition |
| ES2529193T3 (es) * | 2007-07-19 | 2015-02-17 | Health Research, Inc. | Péptidos de survivina como vacunas contra el cáncer |
| US8580269B2 (en) | 2007-07-19 | 2013-11-12 | Health Research, Inc. | Survivin peptides for autoimmune therapies |
| AU2009232774B2 (en) | 2008-03-31 | 2014-05-29 | Tella Inc. | Partial peptide of Survivin presented on MHC class II molecule and use thereof |
| HUE024541T2 (hu) | 2008-05-14 | 2016-01-28 | Immatics Biotechnologies Gmbh | Szurvivinbõl és neurocanból származó új és hatásos II-es osztályú MHC peptidek |
| TWI526219B (zh) * | 2008-06-19 | 2016-03-21 | 腫瘤療法 科學股份有限公司 | Ｃｄｃａ１抗原決定位胜肽及含此胜肽的疫苗 |
| ES2536465T3 (es) | 2008-10-01 | 2015-05-25 | Immatics Biotechnologies Gmbh | Composición de péptidos tumor-asociados y relacionados con la vacuna contra el cáncer para el tratamiento de glioblastoma (GBM) y otros cánceres |
| US9023802B2 (en) | 2009-12-14 | 2015-05-05 | Immatics Biotechnologies Gmbh | HLA-binding peptides derived from prostate-associated antigenic molecules and methods of use thereof |
| GB201004575D0 (en) | 2010-03-19 | 2010-05-05 | Immatics Biotechnologies Gmbh | Composition of tumor associated peptides and related anti cancer vaccine for the treatment of gastric cancer and other cancers |
| WO2012126118A1 (en) * | 2011-03-21 | 2012-09-27 | Atlantic Cancer Research Institute | Polypeptides with affinity for heat shock proteins (hsps) and hsp associated complexes (hacs) and their use in diagnosis and therapy |
| AU2013266066A1 (en) | 2012-05-25 | 2014-12-11 | Agenus Inc. | Identification of MHC class I phospho-peptide antigens from breast cancer utilizing sHLA technology and complementary enrichment strategies |
| WO2014010229A1 (en) | 2012-07-10 | 2014-01-16 | Oncotherapy Science, Inc. | Cdca1 epitope peptides for th1 cells and vaccines containing the same |
| WO2014153636A1 (en) * | 2013-03-27 | 2014-10-02 | Immunovaccine Technologies Inc. | Method for improving the efficacy of a survivin vaccine in the treatment of cancer |
| WO2015077607A1 (en) | 2013-11-22 | 2015-05-28 | The Board Of Trustees Of The University Of Illinois | Engineered high-affinity human t cell receptors |
| WO2016011210A2 (en) | 2014-07-15 | 2016-01-21 | Juno Therapeutics, Inc. | Engineered cells for adoptive cell therapy |
| WO2016109880A1 (en) | 2015-01-06 | 2016-07-14 | Immunovaccine Technologies Inc. | Lipid a mimics, methods of preparation, and uses thereof |
| GB201507030D0 (en) | 2015-04-24 | 2015-06-10 | Immatics Biotechnologies Gmbh | Immunotherapy against lung cancers, in particular NSCLC |
| WO2016176761A1 (en) * | 2015-05-01 | 2016-11-10 | Immunovaccine Technologies Inc., | Methods for potentiating an immune response using depot-forming and non-depot-forming vaccines |
| MA42895A (fr) | 2015-07-15 | 2018-05-23 | Juno Therapeutics Inc | Cellules modifiées pour thérapie cellulaire adoptive |
| WO2017083963A1 (en) | 2015-11-18 | 2017-05-26 | Immunovaccine Technologies Inc. | Adjuvanting systems and water-free vaccine compositions comprising a polyi:c polynucleotide adjuvant and a lipid-based adjuvant |
| GB201604755D0 (en) * | 2016-03-21 | 2016-05-04 | Vaxeal Res Sas | Immunogenic compositions |
| CA3031170A1 (en) | 2016-09-21 | 2018-03-29 | Amal Therapeutics Sa | Fusion comprising a cell penetrating peptide, a multi epitope and a tlr peptide agonist for treatment of cancer |
| EP3522917A2 (en) | 2016-10-07 | 2019-08-14 | Enterome S.A. | Microbiota sequence variants of tumor-related antigenic epitopes |
| US11478538B2 (en) | 2016-10-07 | 2022-10-25 | Enterome S.A. | Immunogenic compounds for cancer therapy |
| KR102622188B1 (ko) | 2016-10-07 | 2024-01-05 | 엔터롬 에스.에이. | 암 치료를 위한 면역원성 화합물 |
| US20180264095A1 (en) | 2017-03-03 | 2018-09-20 | Treos Bio Zrt | Population-based immunogenic peptide identification platform |
| JP6993677B2 (ja) * | 2017-11-08 | 2022-01-13 | 学校法人日本医科大学 | 犬におけるがんの予防、がんの治療またはがんの転移の予防のためのがんペプチドワクチン |
| FI3773689T3 (fi) * | 2018-04-11 | 2023-01-31 | Antigeenisiä peptidejä syövän ehkäisyyn ja hoitoon | |
| MA53543A (fr) | 2018-09-04 | 2021-07-14 | Treos Bio Ltd | Vaccins peptidiques |
| FR3087448B1 (fr) | 2018-10-23 | 2023-10-13 | Pdc Line Pharma | Lignee pdc modifiee pour secreter une cytokine |
| JP2022513072A (ja) * | 2018-11-19 | 2022-02-07 | イムノバクシーン・テクノロジーズ・インコーポレイテッド | 腫瘍の処置におけるサバイビン治療薬の効能を改善するための方法 |
| CN111440246B (zh) * | 2020-04-16 | 2022-03-18 | 成都仕康美生物科技有限公司 | 靶向HLA-B的嵌合抗原受体、编码基因、CAR-Tregs细胞及其制备方法、用途 |
| KR20230044133A (ko) * | 2021-09-24 | 2023-04-03 | 주식회사 차백신연구소 | 종양 연관 항원으로부터 유래된 펩타이드 및 리포펩타이드와 면역활성물질로 구성되는 아쥬번트를 포함하는 항암 백신 조성물 및 이의 용도 |
| CN115477686B (zh) * | 2022-09-22 | 2024-01-30 | 北海黑珍珠海洋生物科技有限公司 | 一种具有美白功效的珍珠贝活性肽及其应用 |
Family Cites Families (14)
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| US5342774A (en) | 1991-05-23 | 1994-08-30 | Ludwig Institute For Cancer Research | Nucleotide sequence encoding the tumor rejection antigen precursor, MAGE-1 |
| US6037135A (en) * | 1992-08-07 | 2000-03-14 | Epimmune Inc. | Methods for making HLA binding peptides and their uses |
| EP0658113B1 (en) | 1992-08-31 | 2004-10-20 | Ludwig Institute For Cancer Research | Isolated nonapeptide derived from mage-3 gene and presented by hla-a1, and uses thereof |
| US5514539A (en) * | 1993-06-29 | 1996-05-07 | The United States Of America As Represented By The Department Of Health And Human Services | Nucleotide and deduced amino acid sequences of the envelope 1 gene of 51 isolates of hepatitis C virus and the use of reagents derived from these sequences in diagnostic methods and vaccines |
| US6096313A (en) | 1996-02-09 | 2000-08-01 | Ludwig Institute For Cancer Research | Compositions containing immunogenic molecules and granulocyte-macrophage colony stimulating factor, as an adjuvant |
| DE69739105D1 (de) * | 1996-11-20 | 2008-12-24 | Univ Yale | Survivin, ein protein das zelluläre apoptosis hemmt, und dessen modulation |
| WO1999050637A2 (en) * | 1998-03-27 | 1999-10-07 | Ludwig Institute For Cancer Research | Isolated multimeric complexes useful in analysis of t cells, peptides useful in making the complexes, and uses thereof |
| WO1999050440A2 (en) * | 1998-04-01 | 1999-10-07 | Yale University | Method to identify modulators of survivin - tubulin interaction |
| AU4990999A (en) | 1998-07-14 | 2000-02-07 | Jenner Biotherapies, Inc. | Survivin, and peptides thereof, as an anti-cancer vaccine |
| AU2002240818C1 (en) * | 2001-03-14 | 2008-11-06 | Agilent Technologies, Inc. | MHC molecule constructs and their uses for diagnosis and therapy |
| US20040210035A1 (en) * | 2002-01-30 | 2004-10-21 | Straten Eivind Per Thor | Survivin-derived peptides and use thereof |
| US7892559B2 (en) | 2002-01-30 | 2011-02-22 | Survac Aps | Survivin-derived peptides and use thereof |
| DE10225144A1 (de) | 2002-05-29 | 2003-12-18 | Immatics Biotechnologies Gmbh | An MHC-Moleküle bindende Tumor-assoziierte Peptide |
| PL2087904T3 (pl) | 2003-11-19 | 2014-01-31 | Survac Aps | Zastosowanie terapeutyczne peptydów pochodzących z białek BcL-XL u pacjentów z rakiem |
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