JP5916613B2 - 多発性骨髄腫細胞からの抗原ペプチドの同定 - Google Patents
多発性骨髄腫細胞からの抗原ペプチドの同定 Download PDFInfo
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| US12/564,501 US8075895B2 (en) | 2009-09-22 | 2009-09-22 | Identification of antigenic peptides from multiple myeloma cells |
| US12/564,501 | 2009-09-22 | ||
| PCT/US2010/049466 WO2011037859A2 (en) | 2009-09-22 | 2010-09-20 | Identification of antigenic peptides from multiple myeloma cells |
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| KR102508166B1 (ko) | 2014-04-10 | 2023-03-13 | 시애틀 칠드런즈 호스피탈 디/비/에이 시애틀 칠드런즈 리서치 인스티튜트 | 세포 면역요법을 위한 방법 및 조성물 |
| US11458167B2 (en) | 2015-08-07 | 2022-10-04 | Seattle Children's Hospital | Bispecific CAR T-cells for solid tumor targeting |
| US11116784B2 (en) | 2016-02-26 | 2021-09-14 | Beth Israel Deaconess Medical Center, Inc. | Niacinamide (NAM) in ischemic tissue injury |
| AU2017283480A1 (en) | 2016-06-13 | 2019-01-24 | Torque Therapeutics, Inc. | Methods and compositions for promoting immune cell function |
| CN110291200B (zh) | 2016-12-12 | 2024-05-14 | 西雅图儿童医院（Dba西雅图儿童研究所） | 对哺乳动物细胞中转基因表达的药剂配体诱导具有增大的灵敏度的嵌合转录因子变异体 |
| JP7136454B2 (ja) * | 2017-01-20 | 2022-09-13 | 国立大学法人京都大学 | ＣＤ８α＋β＋細胞傷害性Ｔ細胞の製造方法 |
| PT3515465T (pt) | 2017-08-18 | 2024-03-04 | Regeneron Pharma | Métodos para o tratamento de uma dermatite atópica grave mediante a administração de um inibidor de il-4r |
| EP3678701A4 (en) | 2017-09-05 | 2021-12-01 | Torque Therapeutics, Inc. | THERAPEUTIC PROTEIN COMPOSITIONS AND METHODS FOR PREPARING AND USING THE SAME |
| SG11202104611YA (en) * | 2018-11-08 | 2021-06-29 | Neximmune Inc | T cell compositions with improved phenotypic properties |
Family Cites Families (35)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5766920A (en) * | 1982-08-11 | 1998-06-16 | Cellcor, Inc. | Ex vivo activation of immune cells |
| US4690915A (en) * | 1985-08-08 | 1987-09-01 | The United States Of America As Represented By The Department Of Health And Human Services | Adoptive immunotherapy as a treatment modality in humans |
| AU7873187A (en) * | 1986-08-08 | 1988-02-24 | University Of Minnesota | Method of culturing leukocytes |
| US4844893A (en) * | 1986-10-07 | 1989-07-04 | Scripps Clinic And Research Foundation | EX vivo effector cell activation for target cell killing |
| US5126132A (en) * | 1989-08-21 | 1992-06-30 | The United States Of America As Represented By The Department Of Health And Human Services | Tumor infiltrating lymphocytes as a treatment modality for human cancer |
| US5728388A (en) * | 1989-10-03 | 1998-03-17 | Terman; David S. | Method of cancer treatment |
| DE69430315T2 (de) * | 1993-08-06 | 2002-11-21 | Epimmune, Inc. | Methoden zur (ex vivo) therapie mittels peptid - bestueckten antigen - praesentierenden zellen zur aktivierung von ctl |
| IL109540A0 (en) * | 1994-05-03 | 1994-08-26 | Yeda Res & Dev | Synthetic peptides and their use in tumor diagnosis and therapy |
| US5827642A (en) * | 1994-08-31 | 1998-10-27 | Fred Hutchinson Cancer Research Center | Rapid expansion method ("REM") for in vitro propagation of T lymphocytes |
| CA2207736A1 (en) * | 1994-12-14 | 1996-06-20 | The Scripps Research Institute | In vivo activation of tumor-specific cytotoxic t cells |
| EP0814838B1 (en) * | 1995-03-08 | 2003-05-14 | The Scripps Research Institute | Antigen presenting system and activation of t-cells |
| ATE347588T1 (de) * | 1996-05-23 | 2006-12-15 | Scripps Research Inst | Systeme zur präsentation von mhc-antigenen der klasse ii und verfahren zur aktivierung von cd4?+-t-lymphozyten |
| CA2278847A1 (en) * | 1997-01-31 | 1998-08-06 | Hemosol Inc. | Method for the production of selected lymphocytes |
| US6790662B1 (en) * | 1999-03-12 | 2004-09-14 | Ortho-Mcneil Pharmaceutical, Inc. | Method of isolating CD8+ cells, and related hybridoma cells antibodies and polypeptides |
| US20020048763A1 (en) * | 2000-02-04 | 2002-04-25 | Penn Sharron Gaynor | Human genome-derived single exon nucleic acid probes useful for gene expression analysis |
| US20020081590A1 (en) * | 2000-02-04 | 2002-06-27 | Aeomica, Inc. | Methods and apparatus for predicting, confirming, and displaying functional information derived from genomic sequence |
| EP1326961B1 (en) | 2000-09-15 | 2007-08-22 | Ortho-McNeil Pharmaceutical, Inc. | Compositions and methods for inducing specific cytolytic t cell responses |
| US20090062512A1 (en) * | 2000-10-10 | 2009-03-05 | Hildebrand William H | Comparative ligand mapping from MHC class I positive cells |
| US7919467B2 (en) * | 2000-12-04 | 2011-04-05 | Immunotope, Inc. | Cytotoxic T-lymphocyte-inducing immunogens for prevention, treatment, and diagnosis of cancer |
| US20040071671A1 (en) * | 2001-02-20 | 2004-04-15 | Leturcq Didier J. | Cell therapy method for the treatment of tumors |
| EP1407004B1 (en) * | 2001-05-15 | 2009-08-05 | Ortho-McNeil-Janssen Pharmaceuticals, Inc. | Ex-vivo priming for generating cd40-ligand specific cytotoxic t lymphocytes to treat autoimmune and allergic disease |
| US20050053918A1 (en) * | 2001-05-16 | 2005-03-10 | Technion Research & Development Foundation Ltd. | Method of identifying peptides capable of binding to MHC molecules, peptides identified thereby and their uses |
| JP2004527263A (ja) * | 2001-05-30 | 2004-09-09 | フォンダツィオーネ テレソン | 免疫抑制活性を有するエクスビボ単離ｃｄ２５＋ｃｄ４＋ｔ細胞とその使用 |
| DE10148236A1 (de) * | 2001-09-29 | 2003-04-24 | Immugenics Ag | Tumor-Peptidantigene aus humanem PRDI-BF1-Protein |
| WO2003033667A2 (en) * | 2001-10-18 | 2003-04-24 | The Government Of The United States Of America, Represented By The Secretary, Department Of Health And Human Services | Use of mx gtpases in the prognosis and treatment of cancer |
| US7371736B2 (en) * | 2001-11-07 | 2008-05-13 | The Board Of Trustees Of The University Of Arkansas | Gene expression profiling based identification of DKK1 as a potential therapeutic targets for controlling bone loss |
| DE10225144A1 (de) * | 2002-05-29 | 2003-12-18 | Immatics Biotechnologies Gmbh | An MHC-Moleküle bindende Tumor-assoziierte Peptide |
| US8222033B2 (en) * | 2002-08-12 | 2012-07-17 | Argos Therapeutics, Inc. | CD4+CD25− T cells and Tr1-like regulatory T cells |
| DE102004026135A1 (de) * | 2004-05-25 | 2006-01-05 | Immatics Biotechnologies Gmbh | An MHC-Moleküle bindende Tumor-assoziierte Peptide |
| US20090075832A1 (en) * | 2005-02-24 | 2009-03-19 | Cemines, Inc | Compositions and Methods for Classifying Biological Samples |
| WO2007035717A2 (en) * | 2005-09-19 | 2007-03-29 | The Rockefeller University | Glycolipids and analogues thereof as antigents for nk t cells |
| WO2007071390A1 (en) * | 2005-12-21 | 2007-06-28 | Sentoclone Ab | Method for treating malignant melanoma |
| MX2008011302A (es) | 2006-03-01 | 2008-11-04 | Janssen Pharmaceutica Nv | Tratamiento de cancer que combina agente de linfodeplecion con linfocitos t citotoxicos y citocinas. |
| US8124408B2 (en) * | 2006-10-04 | 2012-02-28 | Janssen Pharmaceutica N.V. | Preparation of inactivated artificial antigen presenting cells and their use in cell therapies |
| US20090028847A1 (en) * | 2007-04-12 | 2009-01-29 | Trustees Of Boston University | Multiple myeloma and al amyloid immunotherapy targeting immunoglobulin light chains and uses thereof |
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| WO2011037859A2 (en) | 2011-03-31 |
| AU2010298519A1 (en) | 2012-04-12 |
| WO2011037859A3 (en) | 2011-05-19 |
| EP2480562A4 (en) | 2013-03-13 |
| JP2013505296A (ja) | 2013-02-14 |
| EP2480562A2 (en) | 2012-08-01 |
| US20120045466A1 (en) | 2012-02-23 |
| EP2480562B1 (en) | 2015-10-21 |
| US8075895B2 (en) | 2011-12-13 |
| AU2010298519B2 (en) | 2015-11-05 |
| CA2774946A1 (en) | 2011-03-31 |
| US20120046645A1 (en) | 2012-02-23 |
| US8323655B2 (en) | 2012-12-04 |
| US20110070185A1 (en) | 2011-03-24 |
| US8323965B2 (en) | 2012-12-04 |
| US8232101B2 (en) | 2012-07-31 |
| US20120045829A1 (en) | 2012-02-23 |
| IL218720A0 (en) | 2012-06-28 |
| NZ598932A (en) | 2014-10-31 |
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