CA2769822C - Methods of modulating immune function - Google Patents
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- CA2769822C CA2769822C CA2769822A CA2769822A CA2769822C CA 2769822 C CA2769822 C CA 2769822C CA 2769822 A CA2769822 A CA 2769822A CA 2769822 A CA2769822 A CA 2769822A CA 2769822 C CA2769822 C CA 2769822C
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Landscapes
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| US61/289,951 | 2009-12-23 | ||
| PCT/US2010/045479 WO2011020024A2 (en) | 2009-08-13 | 2010-08-13 | Methods of modulating immune function |
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| CA (1) | CA2769822C (enExample) |
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Families Citing this family (70)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20100266495A1 (en) * | 2004-05-21 | 2010-10-21 | Brigham Young University | Anti-Cancer Activity of an Anti-Thymidine Kinase Monoclonal Antibody |
| US7520860B2 (en) | 2005-04-13 | 2009-04-21 | Marie G. Johnson | Detection of coronary artery disease using an electronic stethoscope |
| ES2537580T3 (es) | 2007-09-04 | 2015-06-09 | Compugen Ltd. | Polipéptidos y polinucleótidos, y usos de los mismos como una diana farmacológica para producir fármacos y agentes biológicos |
| JP5883384B2 (ja) * | 2009-08-13 | 2016-03-15 | ザ ジョンズ ホプキンス ユニバーシティー | 免疫機能を調節する方法 |
| WO2011146313A1 (en) | 2010-05-19 | 2011-11-24 | The University Of North Carolina At Chapel Hill | Pyrazolopyrimidine compounds for the treatment of cancer |
| EP2726503B1 (en) | 2011-06-30 | 2019-09-04 | Compugen Ltd. | Polypeptides and uses thereof for treatment of autoimmune disorders and infection |
| BR112014007788A2 (pt) | 2011-10-03 | 2017-04-18 | Univ North Carolina Chapel Hill | compostos de pirrolopirimidina para tratamento do câncer |
| KR20140126357A (ko) | 2012-02-01 | 2014-10-30 | 컴퓨젠 엘티디. | C1orf32 항체 및 이의 암 치료를 위한 용도 |
| WO2013148147A1 (en) | 2012-03-26 | 2013-10-03 | The U.S.A., As Represented By The Secretary Dept. Of Health And Human Services | Dna methylation analysis for the diagnosis, prognosis and treatment of adrenal neoplasms |
| MX2014013632A (es) | 2012-05-22 | 2015-02-05 | Univ North Carolina | Compuestos de pirimidina para el tratamiento de cancer. |
| TWI556194B (zh) * | 2012-06-29 | 2016-11-01 | 希科母股份有限公司 | 對象檢出裝置、對象檢出方法及對象檢出用電腦程式 |
| US9562047B2 (en) | 2012-10-17 | 2017-02-07 | The University Of North Carolina At Chapel Hill | Pyrazolopyrimidine compounds for the treatment of cancer |
| WO2014085225A1 (en) | 2012-11-27 | 2014-06-05 | The University Of North Carolina At Chapel Hill | Pyrimidine compounds for the treatment of cancer |
| MX2015008117A (es) | 2012-12-21 | 2016-03-31 | Amplimmune Inc | Anticuerpos anti-h7cr. |
| US20140205609A1 (en) * | 2013-01-24 | 2014-07-24 | Fred T. Valentine | Methods for inducing systemic immune responses to cancer |
| US10093737B2 (en) | 2013-03-01 | 2018-10-09 | Albert Einstein College Of Medicine, Inc. | HHLA2 as a novel inhibitor of human immune system and uses thereof |
| JP2016519108A (ja) | 2013-04-18 | 2016-06-30 | アルモ・バイオサイエンシーズ・インコーポレイテッド | インターロイキン−10を疾病及び疾患の治療に用いる方法 |
| JP6682426B2 (ja) * | 2013-05-24 | 2020-04-15 | メディミューン,エルエルシー | 抗b7−h5抗体およびその使用 |
| CN105848674A (zh) * | 2013-11-11 | 2016-08-10 | 阿尔莫生物科技股份有限公司 | 将白细胞介素-10用于治疗疾病和病症的方法 |
| GB201403775D0 (en) | 2014-03-04 | 2014-04-16 | Kymab Ltd | Antibodies, uses & methods |
| US9603850B2 (en) | 2014-04-11 | 2017-03-28 | The University Of North Carolina At Chapel Hill | MerTK-specific pyrazolopyrimidine compounds |
| WO2015167948A1 (en) * | 2014-04-30 | 2015-11-05 | Albert Einstein College Of Medicine Of Yeshiva University | Tmigd2 and its derivatives as blockers or binders of cancer-expressed hhla2 for immunotherapies |
| SMT202100116T1 (it) | 2014-05-28 | 2021-05-07 | Agenus Inc | Anticorpi anti-gitr e metodi di utilizzo degli stessi |
| AU2015271126A1 (en) * | 2014-06-04 | 2016-12-08 | Ngm Biopharmaceuticals, Inc. | Compositions and methods for targeting a pathway |
| WO2016109546A2 (en) | 2014-12-30 | 2016-07-07 | Genentech, Inc. | Methods and compositions for prognosis and treatment of cancers |
| MA41414A (fr) | 2015-01-28 | 2017-12-05 | Centre Nat Rech Scient | Protéines de liaison agonistes d' icos |
| SG11201705844SA (en) * | 2015-02-06 | 2017-08-30 | Heat Biologics Inc | Vector co-expressing vaccine and costimulatory molecules |
| RS60614B1 (sr) * | 2015-03-23 | 2020-08-31 | Jounce Therapeutics Inc | Antitela za icos |
| SG10202103445QA (en) * | 2015-04-13 | 2021-05-28 | Regeneron Pharma | Humanized sirpa-il15 knockin mice and methods of use thereof |
| EP3283508B1 (en) | 2015-04-17 | 2021-03-17 | Alpine Immune Sciences, Inc. | Immunomodulatory proteins with tunable affinities |
| ITUB20151014A1 (it) * | 2015-05-27 | 2016-11-27 | Univ Degli Studi Del Piemonte Orientale Amedeo Avogadro | Ligandi del recettore b7h nel trattamento di osteopenia e osteoporosi |
| CN107849144B (zh) | 2015-05-29 | 2021-09-17 | 艾吉纳斯公司 | 抗-ctla-4抗体及其使用方法 |
| US10968277B2 (en) | 2015-10-22 | 2021-04-06 | Jounce Therapeutics, Inc. | Gene signatures for determining ICOS expression |
| EP3383430A4 (en) | 2015-12-02 | 2019-12-18 | Agenus Inc. | ANTIBODIES AND METHOD FOR USE THEREOF |
| US11547739B2 (en) * | 2015-12-16 | 2023-01-10 | La Jolla Institute For Allergy And Immunology | Peptides and methods related to ICOS signaling |
| US10709708B2 (en) | 2016-03-17 | 2020-07-14 | The University Of North Carolina At Chapel Hill | Method of treating cancer with a combination of MER tyrosine kinase inhibitor and an epidermal growth factor receptor (EGFR) inhibitor |
| KR102824067B1 (ko) | 2016-04-15 | 2025-06-23 | 알파인 이뮨 사이언시즈, 인코포레이티드 | Icos 리간드 변이체 면역조절 단백질 및 그의 용도 |
| EP3443000B1 (en) | 2016-04-15 | 2025-11-12 | Alpine Immune Sciences, Inc. | Cd80 variant immunomodulatory proteins and uses thereof |
| WO2018029474A2 (en) | 2016-08-09 | 2018-02-15 | Kymab Limited | Anti-icos antibodies |
| BR112018076260A2 (pt) | 2016-06-20 | 2019-03-26 | Kymab Limited | anticorpo ou fragmento do mesmo que se liga especificamente a hpd-l1, anticorpo biespecífico ou proteína de fusão, uso de um anticorpo ou fragmento, método, composição farmacêutica, método de modulação, método de inibição, método de tratamento, ácido nucleico, vetor, hospedeiro e imunocitocina |
| US9567399B1 (en) | 2016-06-20 | 2017-02-14 | Kymab Limited | Antibodies and immunocytokines |
| US11834490B2 (en) | 2016-07-28 | 2023-12-05 | Alpine Immune Sciences, Inc. | CD112 variant immunomodulatory proteins and uses thereof |
| US11471488B2 (en) | 2016-07-28 | 2022-10-18 | Alpine Immune Sciences, Inc. | CD155 variant immunomodulatory proteins and uses thereof |
| CN116640214A (zh) | 2016-08-09 | 2023-08-25 | 科马布有限公司 | 分离抗体及其应用 |
| US11779604B2 (en) | 2016-11-03 | 2023-10-10 | Kymab Limited | Antibodies, combinations comprising antibodies, biomarkers, uses and methods |
| FI3551660T3 (fi) | 2016-12-07 | 2023-12-11 | Agenus Inc | Anti-ctla-4-vasta-aineita ja niiden käyttömenetelmiä |
| CN106755372B (zh) * | 2016-12-12 | 2020-03-31 | 青岛泱深生物医药有限公司 | 一种分子标志物在口腔鳞状细胞癌诊断和治疗中的应用 |
| US11192933B2 (en) * | 2017-02-27 | 2021-12-07 | Shattuck Labs, Inc. | VSIG8-based chimeric proteins |
| CN110809581A (zh) | 2017-03-16 | 2020-02-18 | 高山免疫科学股份有限公司 | Pd-l2变体免疫调节蛋白及其用途 |
| GB201709808D0 (en) | 2017-06-20 | 2017-08-02 | Kymab Ltd | Antibodies |
| US10752689B2 (en) * | 2017-06-26 | 2020-08-25 | Bio-Techne Corporation | Hybridoma clones, monoclonal antibodies to VSIG-4, and methods of making and using |
| UA128472C2 (uk) | 2017-08-25 | 2024-07-24 | Файв Прайм Терапеутікс Інк. | B7-h4 антитіла і методи їх використання |
| KR102813968B1 (ko) | 2017-10-10 | 2025-05-29 | 알파인 이뮨 사이언시즈, 인코포레이티드 | Ctla-4 변이체 면역조절 단백질 및 이의 용도 |
| MX2020004540A (es) * | 2017-10-18 | 2020-08-03 | Alpine Immune Sciences Inc | Proteinas inmunomoduladoras de ligando icos variante y composiciones y metodos relacionados. |
| EP3728314A1 (en) | 2017-12-19 | 2020-10-28 | Kymab Limited | Bispecific antibody for icos and pd-l1 |
| GB201721338D0 (en) | 2017-12-19 | 2018-01-31 | Kymab Ltd | Anti-icos Antibodies |
| EP3735417A1 (en) | 2018-01-03 | 2020-11-11 | Alpine Immune Sciences, Inc. | Multi-domain immunomodulatory proteins and methods of use thereof |
| JP7054955B2 (ja) * | 2018-01-12 | 2022-04-15 | ゲノム アンド カンパニー | Kirrel2及びkirrel2抑制剤の新規用途 |
| BR112020016986A2 (pt) | 2018-02-21 | 2021-03-02 | Five Prime Therapeutics, Inc. | formulações de anticorpo contra b7-h4 |
| CA3091801A1 (en) | 2018-03-02 | 2019-09-06 | Five Prime Therapeutics, Inc. | B7-h4 antibodies and methods of use thereof |
| BR112020015999A2 (pt) * | 2018-04-06 | 2020-12-15 | Dana-Farber Cancer Institute, Inc. | Kir3dl3 como um receptor de hhla2, anticorpos anti-hhla2 e usos dos mesmos |
| CN108872588B (zh) * | 2018-06-14 | 2021-05-28 | 华南农业大学 | 一种与种公猪繁殖性能密切相关的精子蛋白标记spaca4及其应用 |
| WO2019241758A1 (en) | 2018-06-15 | 2019-12-19 | Alpine Immune Sciences, Inc. | Pd-1 variant immunomodulatory proteins and uses thereof |
| JP2021533796A (ja) * | 2018-08-21 | 2021-12-09 | エヌジーエム バイオファーマシューティカルス,インコーポレーテッド | B7−h7結合剤及びその使用方法 |
| US12331320B2 (en) | 2018-10-10 | 2025-06-17 | The Research Foundation For The State University Of New York | Genome edited cancer cell vaccines |
| JP2022527761A (ja) * | 2019-03-26 | 2022-06-06 | フォーティ セブン, インコーポレイテッド | がん治療のための多重特異性作用物質 |
| GB202007099D0 (en) | 2020-05-14 | 2020-07-01 | Kymab Ltd | Tumour biomarkers for immunotherapy |
| WO2022243378A1 (en) | 2021-05-18 | 2022-11-24 | Kymab Limited | Uses of anti-icos antibodies |
| GB202107994D0 (en) | 2021-06-04 | 2021-07-21 | Kymab Ltd | Treatment of cancer |
| CN119040454A (zh) * | 2024-09-27 | 2024-11-29 | 华南农业大学 | Slc26a2基因作为肉鸡胫骨软骨发育不良标志物的应用 |
Family Cites Families (118)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US4675187A (en) | 1983-05-16 | 1987-06-23 | Bristol-Myers Company | BBM-1675, a new antibiotic complex |
| US6054561A (en) | 1984-02-08 | 2000-04-25 | Chiron Corporation | Antigen-binding sites of antibody molecules specific for cancer antigens |
| IL71691A (en) | 1984-04-27 | 1991-04-15 | Yeda Res & Dev | Production of interferon-ypsilon |
| US5807715A (en) | 1984-08-27 | 1998-09-15 | The Board Of Trustees Of The Leland Stanford Junior University | Methods and transformed mammalian lymphocyte cells for producing functional antigen-binding protein including chimeric immunoglobulin |
| US4676980A (en) | 1985-09-23 | 1987-06-30 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Target specific cross-linked heteroantibodies |
| GB8607679D0 (en) | 1986-03-27 | 1986-04-30 | Winter G P | Recombinant dna product |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| US4987071A (en) | 1986-12-03 | 1991-01-22 | University Patents, Inc. | RNA ribozyme polymerases, dephosphorylases, restriction endoribonucleases and methods |
| US5116742A (en) | 1986-12-03 | 1992-05-26 | University Patents, Inc. | RNA ribozyme restriction endoribonucleases and methods |
| AU600575B2 (en) | 1987-03-18 | 1990-08-16 | Sb2, Inc. | Altered antibodies |
| US5336603A (en) | 1987-10-02 | 1994-08-09 | Genentech, Inc. | CD4 adheson variants |
| US5190929A (en) | 1988-05-25 | 1993-03-02 | Research Corporation Technologies, Inc. | Cyclophosphamide analogs useful as anti-tumor agents |
| KR900005995A (ko) | 1988-10-31 | 1990-05-07 | 우메모또 요시마사 | 변형 인터류킨-2 및 그의 제조방법 |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| EP0394827A1 (en) | 1989-04-26 | 1990-10-31 | F. Hoffmann-La Roche Ag | Chimaeric CD4-immunoglobulin polypeptides |
| US5112946A (en) | 1989-07-06 | 1992-05-12 | Repligen Corporation | Modified pf4 compositions and methods of use |
| FR2650598B1 (fr) | 1989-08-03 | 1994-06-03 | Rhone Poulenc Sante | Derives de l'albumine a fonction therapeutique |
| WO1991006570A1 (en) | 1989-10-25 | 1991-05-16 | The University Of Melbourne | HYBRID Fc RECEPTOR MOLECULES |
| GB8928874D0 (en) | 1989-12-21 | 1990-02-28 | Celltech Ltd | Humanised antibodies |
| US5552391A (en) | 1990-01-16 | 1996-09-03 | La Jolla Pharmaceutical Company | Chemically-defined non-polymeric valency platform molecules and conjugates thereof |
| US5580756A (en) * | 1990-03-26 | 1996-12-03 | Bristol-Myers Squibb Co. | B7Ig fusion protein |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| US5349053A (en) | 1990-06-01 | 1994-09-20 | Protein Design Labs, Inc. | Chimeric ligand/immunoglobulin molecules and their uses |
| AU643109B2 (en) | 1990-12-14 | 1993-11-04 | Cell Genesys, Inc. | Chimeric chains for receptor-associated signal transduction pathways |
| DE69233482T2 (de) | 1991-05-17 | 2006-01-12 | Merck & Co., Inc. | Verfahren zur Verminderung der Immunogenität der variablen Antikörperdomänen |
| EP0590058B1 (en) | 1991-06-14 | 2003-11-26 | Genentech, Inc. | HUMANIZED Heregulin ANTIBODy |
| WO1994004679A1 (en) | 1991-06-14 | 1994-03-03 | Genentech, Inc. | Method for making humanized antibodies |
| DK0606217T4 (da) * | 1991-06-27 | 2009-03-30 | Bristol Myers Squibb Co | CTL4-receptor, fusionsproteiner indeholdende den samt anvendelse deraf |
| US5844095A (en) | 1991-06-27 | 1998-12-01 | Bristol-Myers Squibb Company | CTLA4 Ig fusion proteins |
| GB9115364D0 (en) | 1991-07-16 | 1991-08-28 | Wellcome Found | Antibody |
| AU669124B2 (en) | 1991-09-18 | 1996-05-30 | Kyowa Hakko Kirin Co., Ltd. | Process for producing humanized chimera antibody |
| US5565332A (en) | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| US6162432A (en) | 1991-10-07 | 2000-12-19 | Biogen, Inc. | Method of prophylaxis or treatment of antigen presenting cell driven skin conditions using inhibitors of the CD2/LFA-3 interaction |
| DE4135070C1 (enExample) | 1991-10-24 | 1993-05-19 | Institut Fuer Rundfunktechnik Gmbh, 8000 Muenchen, De | |
| DE69233204T2 (de) | 1991-12-13 | 2004-07-15 | Xoma Corp., Berkeley | Verfahren und materialien zur herstellung von modifizierten variablen antikörperdomänen und ihre therapeutische verwendung |
| US5824307A (en) | 1991-12-23 | 1998-10-20 | Medimmune, Inc. | Human-murine chimeric antibodies against respiratory syncytial virus |
| US5622929A (en) | 1992-01-23 | 1997-04-22 | Bristol-Myers Squibb Company | Thioether conjugates |
| FR2686899B1 (fr) | 1992-01-31 | 1995-09-01 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides biologiquement actifs, leur preparation et compositions pharmaceutiques les contenant. |
| FR2686901A1 (fr) | 1992-01-31 | 1993-08-06 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides antithrombotiques, leur preparation et compositions pharmaceutiques les contenant. |
| GB9203459D0 (en) | 1992-02-19 | 1992-04-08 | Scotgen Ltd | Antibodies with germ-line variable regions |
| US5733743A (en) | 1992-03-24 | 1998-03-31 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| US5447851B1 (en) | 1992-04-02 | 1999-07-06 | Univ Texas System Board Of | Dna encoding a chimeric polypeptide comprising the extracellular domain of tnf receptor fused to igg vectors and host cells |
| US5639641A (en) | 1992-09-09 | 1997-06-17 | Immunogen Inc. | Resurfacing of rodent antibodies |
| TW402639B (en) | 1992-12-03 | 2000-08-21 | Transkaryotic Therapies Inc | Protein production and protein delivery |
| US6180377B1 (en) | 1993-06-16 | 2001-01-30 | Celltech Therapeutics Limited | Humanized antibodies |
| US5834252A (en) | 1995-04-18 | 1998-11-10 | Glaxo Group Limited | End-complementary polymerase reaction |
| US5605793A (en) | 1994-02-17 | 1997-02-25 | Affymax Technologies N.V. | Methods for in vitro recombination |
| US5837458A (en) | 1994-02-17 | 1998-11-17 | Maxygen, Inc. | Methods and compositions for cellular and metabolic engineering |
| US5532159A (en) | 1994-04-01 | 1996-07-02 | The Ohio State University | Monoclonal antibody to canine placental oncofetal protein for detecting cancer |
| AU3382595A (en) | 1994-07-29 | 1996-03-04 | Smithkline Beecham Corporation | Novel compounds |
| GB9415379D0 (en) | 1994-07-29 | 1994-09-21 | Smithkline Beecham Plc | Novel compounds |
| ATE238668T1 (de) | 1995-01-17 | 2003-05-15 | Brigham & Womens Hospital | Rezeptorspezifischer transepithelialer transport von immunogenen |
| US6030613A (en) | 1995-01-17 | 2000-02-29 | The Brigham And Women's Hospital, Inc. | Receptor specific transepithelial transport of therapeutics |
| US6265150B1 (en) | 1995-06-07 | 2001-07-24 | Becton Dickinson & Company | Phage antibodies |
| US5723125A (en) | 1995-12-28 | 1998-03-03 | Tanox Biosystems, Inc. | Hybrid with interferon-alpha and an immunoglobulin Fc linked through a non-immunogenic peptide |
| WO1997034631A1 (en) | 1996-03-18 | 1997-09-25 | Board Of Regents, The University Of Texas System | Immunoglobin-like domains with increased half lives |
| WO1998023289A1 (en) | 1996-11-27 | 1998-06-04 | The General Hospital Corporation | MODULATION OF IgG BINDING TO FcRn |
| US6277375B1 (en) | 1997-03-03 | 2001-08-21 | Board Of Regents, The University Of Texas System | Immunoglobulin-like domains with increased half-lives |
| US7411051B2 (en) * | 1997-03-07 | 2008-08-12 | Human Genome Sciences, Inc. | Antibodies to HDPPA04 polypeptide |
| TWI239847B (en) | 1997-12-02 | 2005-09-21 | Elan Pharm Inc | N-terminal fragment of Abeta peptide and an adjuvant for preventing and treating amyloidogenic disease |
| DK1490386T3 (da) | 1998-03-10 | 2008-12-15 | Genentech Inc | Nyt polypeptid og nukleinsyrer kodende for dette |
| AU4640600A (en) | 1999-05-11 | 2000-11-21 | Eli Lilly And Company | Amyloid precursor protein protease and related nucleic acid compounds |
| EP1514933A1 (en) | 1999-07-08 | 2005-03-16 | Research Association for Biotechnology | Secretory protein or membrane protein |
| EP1210428B1 (en) | 1999-08-23 | 2015-03-18 | Dana-Farber Cancer Institute, Inc. | Pd-1, a receptor for b7-4, and uses therefor |
| US6429303B1 (en) | 1999-09-03 | 2002-08-06 | Curagen Corporation | Nucleic acids encoding members of the human B lymphocyte activation antigen B7 family and methods of using the same |
| EP1212344A4 (en) | 1999-09-03 | 2004-08-04 | Human Genome Sciences Inc | POLYNUCLEOTIDES, POLYPEPTIDES AND ANTIBODIES OF THE TYPE B7 |
| ATE366814T1 (de) * | 1999-09-21 | 2007-08-15 | Genetics Inst Llc | Gl50 moleküle, sowie verwendungen derselben |
| EP2341074A1 (en) | 2000-03-01 | 2011-07-06 | MedImmune, LLC | Antibodies binding to the f protein of a respiratory syncytial virus (rsv) |
| US6569681B1 (en) | 2000-03-14 | 2003-05-27 | Transkaryotic Therapies, Inc. | Methods of improving homologous recombination |
| US6416999B1 (en) | 2000-04-07 | 2002-07-09 | Raven Biotechnologies, Inc. | Human Müllerian duct-derived epithelial cells and methods of isolation and uses thereof |
| US6987024B1 (en) | 2000-04-10 | 2006-01-17 | Raven Biotechnologies, Inc. | Human ovarian mesothelial cells and methods of isolation and uses thereof |
| US6436704B1 (en) | 2000-04-10 | 2002-08-20 | Raven Biotechnologies, Inc. | Human pancreatic epithelial progenitor cells and methods of isolation and use thereof |
| CA2405550A1 (en) | 2000-04-12 | 2001-10-25 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| US20060154313A1 (en) | 2000-04-13 | 2006-07-13 | Immunex Corporation | Human B7 polypeptide B7-H3A |
| JP3597140B2 (ja) * | 2000-05-18 | 2004-12-02 | 日本たばこ産業株式会社 | 副刺激伝達分子ailimに対するヒトモノクローナル抗体及びその医薬用途 |
| AU2001264747A1 (en) | 2000-05-22 | 2001-12-03 | Idec Pharmaceuticals Corporation | Identification of unique binding interactions between certain antibodies and thehuman b7.1 and b7.2 co-stimulatory antigens |
| EP1892251A3 (en) | 2000-06-06 | 2008-12-31 | Brystol-Myers Squibb Company | B7-related nucleic acids and polypeptides and their uses for immunomodulation |
| US20030031675A1 (en) | 2000-06-06 | 2003-02-13 | Mikesell Glen E. | B7-related nucleic acids and polypeptides useful for immunomodulation |
| US6965018B2 (en) | 2000-06-06 | 2005-11-15 | Bristol-Myers Squibb Company | Antibodies directed to B7-related polypeptide, BSL-2 |
| AU7298201A (en) * | 2000-06-23 | 2002-01-08 | Biogen Inc | Gp286 nucleic acids and polypeptides |
| EP1301524A1 (en) * | 2000-06-30 | 2003-04-16 | Human Genome Sciences, Inc. | B7-like polynucleotides, polypeptides, and antibodies |
| US6635750B1 (en) | 2000-07-20 | 2003-10-21 | Millennium Pharmaceuticals, Inc. | B7-H2 nucleic acids, members of the B7 family |
| WO2002010187A1 (en) | 2000-07-27 | 2002-02-07 | Mayo Foundation For Medical Education And Research | B7-h3 and b7-h4, novel immunoregulatory molecules |
| EP1327638A4 (en) | 2000-09-12 | 2004-09-29 | Kirin Brewery | NEW WALL MEMBRANE OF DENDRITIC CELLS AND THEIR USE |
| US20030134283A1 (en) | 2000-10-03 | 2003-07-17 | Peterson David P. | Genes regulated in dendritic cell differentiation |
| WO2002032375A2 (en) | 2000-10-18 | 2002-04-25 | Sloan-Kettering Institute For Cancer Research | Uses of monoclonal antibody 8h9 |
| US6818216B2 (en) | 2000-11-28 | 2004-11-16 | Medimmune, Inc. | Anti-RSV antibodies |
| RU2322500C2 (ru) | 2000-12-01 | 2008-04-20 | Макс-Планк-Гезелльшафт Цур Фердерунг Дер Виссеншафтен Е.Ф. | Малые молекулы рнк, опосредующие интерференцию рнк |
| PE20020574A1 (es) | 2000-12-06 | 2002-07-02 | Wyeth Corp | Anticuerpos humanizados que reconocen el peptido amiloideo beta |
| PT1355919E (pt) | 2000-12-12 | 2011-03-02 | Medimmune Llc | Moléculas com semivida longa, composições que as contêm e suas utilizações |
| US7651541B2 (en) | 2001-01-10 | 2010-01-26 | State Line Holdings, LLC | Chemical change agent |
| AU2002250236A1 (en) | 2001-03-02 | 2002-09-19 | Medimmune, Inc. | Cd2 antagonists for treatment of autoimmune or inflammatory disease |
| WO2002097046A2 (en) | 2001-05-25 | 2002-12-05 | Amgen, Inc. | B7 related protein-2 molecules and uses thereof |
| US20070015144A9 (en) | 2001-05-25 | 2007-01-18 | Genset, S.A. | Human cDNAs and proteins and uses thereof |
| AU2001286171B2 (en) | 2001-05-25 | 2008-01-10 | Serono Genetics Institute S.A. | Human CDNAs and proteins and uses thereof |
| US6441163B1 (en) | 2001-05-31 | 2002-08-27 | Immunogen, Inc. | Methods for preparation of cytotoxic conjugates of maytansinoids and cell binding agents |
| AU2002347761A1 (en) | 2001-08-02 | 2003-02-24 | Eli Lilly And Company | Novel polypeptide analogs and fusions and their methods of use |
| WO2003068938A2 (en) | 2002-02-12 | 2003-08-21 | Raven Biotechnologies, Inc | Human fetal bladder-derived epithelial cells |
| US20040162236A1 (en) | 2002-04-01 | 2004-08-19 | John Alsobrook | Therapeutic polypeptides, nucleic acids encoding same, and methods of use |
| EP1575509B1 (en) | 2002-05-10 | 2011-10-26 | Purdue Research Foundation | Epha2 agonistic monoclonal antibodies and methods of use thereof |
| CA2485373A1 (en) | 2002-05-10 | 2003-11-20 | Medimmune, Inc. | Epha2 monoclonal antibodies and methods of use thereof |
| EP1565489B1 (en) | 2002-06-19 | 2010-11-17 | Raven Biotechnologies, Inc. | Internalizing antibodies specific for the RAAG10 cell surface target |
| EP1539218A4 (en) * | 2002-06-20 | 2007-08-22 | Univ California | COMPOSITIONS AND METHODS FOR MODULATING LYMPHOCYTE ACTIVITY |
| US20060275287A1 (en) | 2002-06-21 | 2006-12-07 | Brad St Croix | Scroll compressor |
| CA2494485A1 (en) | 2002-07-25 | 2004-02-05 | Medimmune, Inc. | Methods of treating and preventing rsv, hmpv, and piv using anti-rsv, anti-hmpv, and anti-piv antibodies |
| DK2284266T3 (da) | 2002-11-14 | 2014-01-13 | Thermo Fisher Scient Biosciences Inc | sIRNA-MOLEKYLE MOD TP53 |
| US9068234B2 (en) | 2003-01-21 | 2015-06-30 | Ptc Therapeutics, Inc. | Methods and agents for screening for compounds capable of modulating gene expression |
| AU2004280333A1 (en) | 2003-08-22 | 2005-04-21 | Medimmune, Llc | Humanization of antibodies |
| JP2008518936A (ja) | 2004-10-29 | 2008-06-05 | メディミューン,インコーポレーテッド | Rsv感染症および関連状態を予防および治療する方法 |
| JP2008546426A (ja) * | 2005-05-12 | 2008-12-25 | ザイモジェネティクス, インコーポレイテッド | T細胞を共刺激するためにpHHLA2を使用する方法 |
| ATE552837T1 (de) | 2005-12-02 | 2012-04-15 | Univ Johns Hopkins | Verwendung von hochdosierten oxazaphosphorin- arzneimitteln zur behandlung von immunstörungen |
| WO2007070488A2 (en) | 2005-12-12 | 2007-06-21 | The Cbr Institute For Biomedical Research, Inc. | Integrin alpha l i domain mutants with increased binding affinity |
| CA2673659A1 (en) * | 2006-12-27 | 2008-07-10 | The Johns Hopkins University | Methods of detecting and diagnosing inflamatory responses and disorders by determining the level of soluble b7-h4 |
| US20100285039A1 (en) | 2008-01-03 | 2010-11-11 | The Johns Hopkins University | B7-H1 (CD274) Antagonists Induce Apoptosis of Tumor Cells |
| JP5883384B2 (ja) * | 2009-08-13 | 2016-03-15 | ザ ジョンズ ホプキンス ユニバーシティー | 免疫機能を調節する方法 |
| MX2015008117A (es) * | 2012-12-21 | 2016-03-31 | Amplimmune Inc | Anticuerpos anti-h7cr. |
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| ES2666152T3 (es) | 2018-05-03 |
| EP3381937A3 (en) | 2018-10-31 |
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| JP2013501814A (ja) | 2013-01-17 |
| WO2011020024A2 (en) | 2011-02-17 |
| US20160024211A1 (en) | 2016-01-28 |
| WO2011020024A3 (en) | 2011-06-23 |
| EP3381937A2 (en) | 2018-10-03 |
| US20160002336A1 (en) | 2016-01-07 |
| US20120219559A1 (en) | 2012-08-30 |
| AU2010282340B2 (en) | 2016-12-22 |
| US9676856B2 (en) | 2017-06-13 |
| CA2769822A1 (en) | 2011-02-17 |
| EP2464661A2 (en) | 2012-06-20 |
| JP5883384B2 (ja) | 2016-03-15 |
| US8840889B2 (en) | 2014-09-23 |
| AU2016266078A1 (en) | 2016-12-22 |
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