BRPI1010666B1 - Composição farmacêutica, métodos para indução de célula apresentadora de antígeno com indutibilidade de linfócito t citotóxico e para indução de linfócito t citotóxico, bem como usos de peptídeos - Google Patents
Composição farmacêutica, métodos para indução de célula apresentadora de antígeno com indutibilidade de linfócito t citotóxico e para indução de linfócito t citotóxico, bem como usos de peptídeos Download PDFInfo
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| KR102740924B1 (ko) | 2017-09-20 | 2024-12-13 | 더 유니버시티 오브 브리티쉬 콜롬비아 | 신규한 항-ｈｌａ-ａ2 항체 및 이의 용도 |
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4722848A (en) | 1982-12-08 | 1988-02-02 | Health Research, Incorporated | Method for immunizing animals with synthetically modified vaccinia virus |
| EP0239102A3 (en) | 1986-03-28 | 1989-07-12 | Tsuji, Kimiyoshi | Process for the formation of human-human hybridoma |
| GB8823869D0 (en) | 1988-10-12 | 1988-11-16 | Medical Res Council | Production of antibodies |
| US5703055A (en) | 1989-03-21 | 1997-12-30 | Wisconsin Alumni Research Foundation | Generation of antibodies through lipid mediated DNA delivery |
| US5108921A (en) | 1989-04-03 | 1992-04-28 | Purdue Research Foundation | Method for enhanced transmembrane transport of exogenous molecules |
| US6150584A (en) | 1990-01-12 | 2000-11-21 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| AU8507191A (en) | 1990-08-29 | 1992-03-30 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5625126A (en) | 1990-08-29 | 1997-04-29 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5661016A (en) | 1990-08-29 | 1997-08-26 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
| US5679647A (en) | 1993-08-26 | 1997-10-21 | The Regents Of The University Of California | Methods and devices for immunizing a host against tumor-associated antigens through administration of naked polynucleotides which encode tumor-associated antigenic peptides |
| US5804566A (en) | 1993-08-26 | 1998-09-08 | The Regents Of The University Of California | Methods and devices for immunizing a host through administration of naked polynucleotides with encode allergenic peptides |
| US5739118A (en) | 1994-04-01 | 1998-04-14 | Apollon, Inc. | Compositions and methods for delivery of genetic material |
| US5736524A (en) | 1994-11-14 | 1998-04-07 | Merck & Co.,. Inc. | Polynucleotide tuberculosis vaccine |
| US5922687A (en) | 1995-05-04 | 1999-07-13 | Board Of Trustees Of The Leland Stanford Junior University | Intracellular delivery of nucleic acids using pressure |
| AU6632496A (en) | 1995-08-03 | 1997-03-05 | Rijksuniversiteit Te Leiden | Cell derived antigen presenting vesicles |
| US5853719A (en) | 1996-04-30 | 1998-12-29 | Duke University | Methods for treating cancers and pathogen infections using antigen-presenting cells loaded with RNA |
| JP2000516090A (ja) | 1996-07-26 | 2000-12-05 | スローン―ケッタリング インスティチュート フォー キャンサー リサーチ | 遺伝子的免疫化のための方法と試薬 |
| US20030068623A1 (en) * | 1997-06-16 | 2003-04-10 | Genentech, Inc. | Secreted and transmembrane polypeptides and nucleic acids encoding the same |
| FR2766205B1 (fr) | 1997-07-16 | 2002-08-30 | Inst Nat Sante Rech Med | Nouveau procede de sensibilisation de cellules presentatrices d'antigene et nouveaux moyens pour la mise en oeuvre du procede |
| ATE375362T1 (de) | 1998-06-25 | 2007-10-15 | Kyogo Itoh | Von cyclophilin b abstammende tumorantigen- peptide |
| ES2747357T3 (es) | 2001-03-14 | 2020-03-10 | Dako Denmark As | Construcciones de moléculas MHC y sus usos para el diagnóstico y terapia |
| CA2399569A1 (en) | 2001-09-25 | 2003-03-25 | Yusuke Nakamura | Diagnostic markers and drug targets for treatment of cancer |
| GB2392158B (en) | 2002-08-21 | 2005-02-16 | Proimmune Ltd | Chimeric MHC protein and oligomer thereof |
| EP1548032B9 (en) | 2002-09-12 | 2009-10-28 | Oncotherapy Science, Inc. | Kdr peptides and vaccines comprising the same |
| CA2580412A1 (en) | 2004-09-13 | 2006-03-23 | Government Of The United States Of America, Represented By The Secretary , Department Of Health And Human Services | Compositions comprising t cell receptors and methods of use thereof |
| JP4370409B2 (ja) | 2005-06-22 | 2009-11-25 | 国立大学法人東北大学 | がんの予後予測方法 |
| WO2007013665A2 (en) | 2005-07-27 | 2007-02-01 | Oncotherapy Science, Inc. | Method of diagnosing small cell lung cancer |
| CN101273144B (zh) * | 2005-07-27 | 2011-12-28 | 肿瘤疗法科学股份有限公司 | 诊断食道癌的方法 |
| KR101130597B1 (ko) | 2005-09-13 | 2012-04-02 | 다카라 바이오 가부시키가이샤 | Ｔ 세포 리셉터 및 그 리셉터를 코드하는 핵산 |
| ES2365077T3 (es) * | 2006-06-16 | 2011-09-21 | Onco Therapy Science, Inc. | Péptido antígeno anticáncer derivado de sparc y composición farmacéutica que comprende el mismo. |
| US8470534B2 (en) | 2006-12-01 | 2013-06-25 | Erik S. Knudsen | Methods of predicting resistance or sensitivity to therapies for cancer |
| TWI441648B (zh) | 2007-01-03 | 2014-06-21 | Oncotherapy Science Inc | Ｆｏｘｐ３胜肽疫苗 |
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