CA2469477A1 - Phenotypic screen of chimeric proteins - Google Patents
Phenotypic screen of chimeric proteins Download PDFInfo
- Publication number
- CA2469477A1 CA2469477A1 CA002469477A CA2469477A CA2469477A1 CA 2469477 A1 CA2469477 A1 CA 2469477A1 CA 002469477 A CA002469477 A CA 002469477A CA 2469477 A CA2469477 A CA 2469477A CA 2469477 A1 CA2469477 A1 CA 2469477A1
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- cell
- nucleic acid
- protein
- transcription factor
- zinc finger
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| US20070212703A1 (en) * | 2005-09-27 | 2007-09-13 | Stemmer Willem P | Proteinaceous pharmaceuticals and uses thereof |
| US7846445B2 (en) * | 2005-09-27 | 2010-12-07 | Amunix Operating, Inc. | Methods for production of unstructured recombinant polymers and uses thereof |
| WO2007058833A2 (en) | 2005-11-10 | 2007-05-24 | Pioneer Hi-Bred International, Inc. | Dof (dna binding with one finger) sequences and methods of use |
| AR060523A1 (es) | 2006-04-19 | 2008-06-25 | Pioneer Hi Bred Int | Moleculas de polinucleotidos aislados que corresponden a alelos mutantes y tipo salvaje del gen de maiz d9 y metodos para usarlas |
| WO2007137114A2 (en) | 2006-05-17 | 2007-11-29 | Pioneer Hi-Bred International, Inc. | Artificial plant minichromosomes |
| EP2032149A4 (en) * | 2006-06-13 | 2010-09-01 | Fmc Biopolymer As | METHOD AND SYSTEMS FOR THE USE OF BIOPOLYMER-BASED BEADS AND HYDROGELS |
| BRPI0715393A2 (pt) * | 2006-08-07 | 2013-06-25 | Genzyme Corp | terapia de combinaÇço |
| KR100812110B1 (ko) | 2006-10-24 | 2008-03-12 | 한국과학기술원 | 징크 핑거 단백질과 원핵 생물의 전사 인자를 포함하는인공 전사 인자의 제조 및 이의 이용 |
| US7642436B2 (en) | 2007-04-13 | 2010-01-05 | Ball Horticultural Company | Petunia mutant allele |
| CA2687211A1 (en) | 2007-05-25 | 2008-12-04 | Cropdesign N.V. | Yield enhancement in plants by modulation of maize alfins |
| EP2164863A4 (en) | 2007-06-15 | 2010-07-28 | Univ Arkansas | METHOD FOR THE ADMINISTRATION OF MOLECULES IN CELLS USING A RICIN SUB-UNIT AND RELATED COMPOSITIONS THEREOF |
| BRPI0815416A2 (pt) * | 2007-08-15 | 2014-10-21 | Amunix Inc | Composições e métodos para modificar propriedades de polipeptídeos biologicamente ativos |
| US8829282B2 (en) | 2008-05-14 | 2014-09-09 | Monsanto Technology, Llc | Plants and seeds of spring canola variety SCV425044 |
| US7964774B2 (en) | 2008-05-14 | 2011-06-21 | Monsanto Technology Llc | Plants and seeds of spring canola variety SCV384196 |
| US7935870B2 (en) | 2008-05-14 | 2011-05-03 | Monsanto Technology Llc | Plants and seeds of spring canola variety SCV354718 |
| US7947877B2 (en) | 2008-05-14 | 2011-05-24 | Monosanto Technology LLC | Plants and seeds of spring canola variety SCV328921 |
| AU2009329893A1 (en) * | 2008-12-23 | 2011-06-30 | Vivoscript, Inc. | Compositions and methods for re-programming cells without genetic modification |
| EP2387567B1 (en) | 2009-01-14 | 2014-06-11 | The Salk Institute for Biological Studies | Compounds that protect against amyloid diseases |
| WO2010091122A1 (en) * | 2009-02-03 | 2010-08-12 | Amunix, Inc. | Extended recombinant polypeptides and compositions comprising same |
| WO2010118477A1 (en) | 2009-04-17 | 2010-10-21 | Molecular Plant Breeding Nominees Ltd | Plant promoter operable in endosperm and uses thereof |
| CN102439032B (zh) | 2009-05-04 | 2015-07-22 | 先锋国际良种公司 | 通过调节ap2转录因子增加植物中的产量 |
| US8071848B2 (en) | 2009-06-17 | 2011-12-06 | Monsanto Technology Llc | Plants and seeds of spring canola variety SCV218328 |
| BR112012004094A2 (pt) | 2009-08-24 | 2016-03-08 | Amunix Operating Inc | composições de fator vii de coagulação e métodos para fazer e usar as mesmas |
| US8440891B2 (en) | 2009-09-22 | 2013-05-14 | Board of Trustees of the University of Akransas, N.A. | Rice cultivar CL 142-AR |
| US8440892B2 (en) | 2009-10-15 | 2013-05-14 | Board Of Trustees Of The University Of Arkansas, N.A. | Rice cultivar CL 181-AR |
| EP2529018B1 (en) | 2009-12-30 | 2016-06-22 | Pioneer Hi-Bred International, Inc. | Methods and compositions for the introduction and regulated expression of genes in plants |
| AU2010339481B2 (en) | 2009-12-30 | 2016-02-04 | Pioneer Hi-Bred International, Inc. | Methods and compositions for targeted polynucleotide modification |
| US20130189780A1 (en) * | 2009-12-31 | 2013-07-25 | Fate Therapeutics, Inc. | Reprogramming compositions |
| US8148611B2 (en) | 2010-02-26 | 2012-04-03 | Monsanto Technology Llc | Plants and seeds of spring canola variety SCV453784 |
| US8143488B2 (en) | 2010-02-26 | 2012-03-27 | Monsanto Technoloy LLC | Plants and seeds of spring canola variety SCV470336 |
| US8138394B2 (en) | 2010-02-26 | 2012-03-20 | Monsanto Technology Llc | Plants and seeds of spring canola variety SCV431158 |
| US8581048B2 (en) | 2010-03-09 | 2013-11-12 | Monsanto Technology, Llc | Plants and seeds of spring canola variety SCV119103 |
| US8153865B2 (en) | 2010-03-11 | 2012-04-10 | Monsanto Technology Llc | Plants and seeds of spring canola variety SCV152154 |
| BR112012028052A2 (pt) | 2010-05-06 | 2019-09-24 | Du Pont | polipeptídeo, polinucleotídeo, cassete de expressão,planta e método de melhoramento de tolerância a seca em uma planta. |
| US8513487B2 (en) | 2011-04-07 | 2013-08-20 | Zenon LISIECZKO | Plants and seeds of spring canola variety ND-662c |
| US8513494B2 (en) | 2011-04-08 | 2013-08-20 | Chunren Wu | Plants and seeds of spring canola variety SCV695971 |
| US8507761B2 (en) | 2011-05-05 | 2013-08-13 | Teresa Huskowska | Plants and seeds of spring canola variety SCV372145 |
| US8513495B2 (en) | 2011-05-10 | 2013-08-20 | Dale Burns | Plants and seeds of spring canola variety SCV291489 |
| US8785729B2 (en) | 2011-08-09 | 2014-07-22 | Nunhems, B.V. | Lettuce variety redglace |
| US8754293B2 (en) | 2011-09-09 | 2014-06-17 | Nunhems B.V. | Lettuce variety intred |
| WO2013096810A1 (en) | 2011-12-21 | 2013-06-27 | The Curators Of The University Of Missouri | Soybean variety s05-11482 |
| WO2013096818A1 (en) | 2011-12-21 | 2013-06-27 | The Curators Of The University Of Missouri | Soybean variety s05-11268 |
| US9380756B2 (en) | 2012-01-04 | 2016-07-05 | Nunhems B.V. | Lettuce variety multigreen 50 |
| LT2822577T (lt) | 2012-02-15 | 2019-03-25 | Bioverativ Therapeutics Inc. | Rekombinantiniai faktoriaus viii baltymai |
| HRP20221531T1 (hr) | 2012-02-15 | 2023-02-17 | Bioverativ Therapeutics Inc. | Pripravci faktora viii i postupci dobivanja i korištenja istih |
| US8859857B2 (en) | 2012-04-26 | 2014-10-14 | Monsanto Technology Llc | Plants and seeds of spring canola variety SCV259778 |
| US8835720B2 (en) | 2012-04-26 | 2014-09-16 | Monsanto Technology Llc | Plants and seeds of spring canola variety SCV967592 |
| US8878009B2 (en) | 2012-04-26 | 2014-11-04 | Monsanto Technology, LLP | Plants and seeds of spring canola variety SCV318181 |
| US8802935B2 (en) | 2012-04-26 | 2014-08-12 | Monsanto Technology Llc | Plants and seeds of spring canola variety SCV942568 |
| CN102816214B (zh) * | 2012-07-27 | 2014-08-13 | 中国人民解放军军事医学科学院生物工程研究所 | 乙型肝炎病毒HBx基因的人工转录因子及其应用 |
| CN102994437B (zh) * | 2012-11-06 | 2014-04-02 | 大连理工大学 | 高产木质纤维素降解酶的链霉菌人工锌指蛋白突变菌株及其获得方法 |
| EP3033097B1 (en) | 2013-08-14 | 2021-03-10 | Bioverativ Therapeutics Inc. | Factor viii-xten fusions and uses thereof |
| WO2016007640A1 (en) | 2014-07-10 | 2016-01-14 | Benson Hill Biosystems, Inc. | Compositions and methods for increasing plant growth and yield |
| MX2018001497A (es) | 2015-08-03 | 2018-05-15 | Bioverativ Therapeutics Inc | Proteinas de fusion de factor ix y metodos para producirlas y usarlas. |
| IL293963A (en) | 2015-09-01 | 2022-08-01 | Univ California | Modular polypeptide libraries and methods of making and using same |
| US10947554B2 (en) | 2015-10-23 | 2021-03-16 | Donald Danforth Plant Science Center | Expression of dicarboxylate transporter from setaria italica in transgenic plants to increase yield |
| EP3372985B1 (en) | 2015-10-28 | 2025-06-25 | The University Of Tokyo | Analysis device |
| US11330776B2 (en) | 2015-10-30 | 2022-05-17 | Pioneer Hi-Bred International, Inc. | Methods and compositions for rapid plant transformation |
| WO2017078836A1 (en) | 2015-11-06 | 2017-05-11 | Pioneer Hi-Bred International, Inc. | Methods and compositions of improved plant transformation |
| WO2018102743A1 (en) | 2016-12-02 | 2018-06-07 | Bioverativ Therapeutics Inc. | Methods of treating hemophilic arthropathy using chimeric clotting factors |
| AU2019234474B2 (en) | 2018-03-12 | 2025-05-15 | Pioneer Hi-Bred International, Inc. | Methods for plant transformation |
| RS66972B1 (sr) | 2018-05-18 | 2025-07-31 | Bioverativ Therapeutics Inc | Metode lečenja hemofilije a |
| WO2019241443A1 (en) | 2018-06-13 | 2019-12-19 | Thinkcyte Inc. | Methods and systems for cytometry |
| US20210277409A1 (en) | 2018-06-28 | 2021-09-09 | Pioneer Hi-Bred International, Inc. | Methods for selecting transformed plants |
| CN113226333A (zh) | 2018-10-02 | 2021-08-06 | 桑格摩生物治疗股份有限公司 | 用于调控Tau蛋白的方法和组合物 |
| WO2020081819A1 (en) * | 2018-10-18 | 2020-04-23 | Thinkcyte Inc. | Methods and systems for target screening |
| JP2022512817A (ja) | 2018-10-31 | 2022-02-07 | パイオニア ハイ-ブレッド インターナショナル, インコーポレイテッド | オクロバクテリウム(Ochrobactrum)媒介植物形質転換のための組成物及び方法 |
| EP4083603A4 (en) | 2019-12-27 | 2024-04-03 | ThinkCyte, Inc. | FLOW CYTOMETER PERFORMANCE EVALUATION METHODS AND STANDARD PARTICLE SUSPENSION |
| WO2021138560A2 (en) | 2020-01-02 | 2021-07-08 | The Trustees Of Columbia University In The City Of New York | Programmable and portable crispr-cas transcriptional activation in bacteria |
| WO2021200911A1 (ja) | 2020-04-01 | 2021-10-07 | シンクサイト株式会社 | フローサイトメーター |
| WO2021200960A1 (ja) | 2020-04-01 | 2021-10-07 | シンクサイト株式会社 | 観察装置 |
| CN113077849B (zh) * | 2021-03-16 | 2023-03-31 | 华南农业大学 | 一种大肠杆菌β-内酰胺类获得性耐药表型预测复合方法 |
| CN113643758B (zh) * | 2021-09-22 | 2023-04-07 | 华南农业大学 | 面向肠杆科细菌获得抗β-内酰胺类耐药性基因的预测方法 |
| CN115873900A (zh) * | 2021-12-28 | 2023-03-31 | 武汉爱博泰克生物科技有限公司 | 胞外表达人源Ly6d蛋白的重组表达质粒、重组细胞及构建方法 |
| CN114360652B (zh) * | 2022-01-28 | 2023-04-28 | 深圳太力生物技术有限责任公司 | 细胞株相似性评价方法及相似细胞株培养基配方推荐方法 |
Family Cites Families (29)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5763209A (en) * | 1988-09-26 | 1998-06-09 | Arch Development Corporation | Methods and materials relating to the functional domains of DNA binding proteins |
| US6107059A (en) * | 1992-04-29 | 2000-08-22 | Affymax Technologies N.V. | Peptide library and screening method |
| US6242568B1 (en) * | 1994-01-18 | 2001-06-05 | The Scripps Research Institute | Zinc finger protein derivatives and methods therefor |
| US6140466A (en) * | 1994-01-18 | 2000-10-31 | The Scripps Research Institute | Zinc finger protein derivatives and methods therefor |
| US5882941A (en) * | 1994-05-04 | 1999-03-16 | Massachusette Institute Of Technology | Programmable genotoxic agents and uses therefor |
| EP0781331B1 (en) * | 1994-08-20 | 2008-09-03 | Gendaq Limited | Improvements in or relating to binding proteins for recognition of dna |
| US6326166B1 (en) * | 1995-12-29 | 2001-12-04 | Massachusetts Institute Of Technology | Chimeric DNA-binding proteins |
| US5789538A (en) * | 1995-02-03 | 1998-08-04 | Massachusetts Institute Of Technology | Zinc finger proteins with high affinity new DNA binding specificities |
| US5866941A (en) * | 1995-02-23 | 1999-02-02 | Silicon Systems, Inc. | Ultra thin, leadless and molded surface mount integrated circuit package |
| GB9710809D0 (en) * | 1997-05-23 | 1997-07-23 | Medical Res Council | Nucleic acid binding proteins |
| US20030166107A1 (en) * | 1997-09-18 | 2003-09-04 | Genentech, Inc. | Secreted and transmembrane polypeptides and nucleic acids encoding the same |
| WO1999045132A1 (en) * | 1998-03-02 | 1999-09-10 | Massachusetts Institute Of Technology | Poly zinc finger proteins with improved linkers |
| US7013219B2 (en) * | 1999-01-12 | 2006-03-14 | Sangamo Biosciences, Inc. | Regulation of endogenous gene expression in cells using zinc finger proteins |
| US6534261B1 (en) * | 1999-01-12 | 2003-03-18 | Sangamo Biosciences, Inc. | Regulation of endogenous gene expression in cells using zinc finger proteins |
| US6453242B1 (en) * | 1999-01-12 | 2002-09-17 | Sangamo Biosciences, Inc. | Selection of sites for targeting by zinc finger proteins and methods of designing zinc finger proteins to bind to preselected sites |
| US6599692B1 (en) * | 1999-09-14 | 2003-07-29 | Sangamo Bioscience, Inc. | Functional genomics using zinc finger proteins |
| US20020164575A1 (en) * | 1999-09-14 | 2002-11-07 | Sangamo Biosciences, Inc., A Delaware Corporation | Gene identification |
| AU776576B2 (en) * | 1999-12-06 | 2004-09-16 | Sangamo Biosciences, Inc. | Methods of using randomized libraries of zinc finger proteins for the identification of gene function |
| ATE355368T1 (de) * | 2000-01-24 | 2006-03-15 | Gendaq Ltd | Nucleinsäure bindende polypeptide gekennzeichnet durch flexible linker verbundene nucleinsäuredomäne |
| JP5047437B2 (ja) * | 2000-02-08 | 2012-10-10 | サンガモ バイオサイエンシーズ, インコーポレイテッド | 薬物の発見のための細胞 |
| US20020061512A1 (en) * | 2000-02-18 | 2002-05-23 | Kim Jin-Soo | Zinc finger domains and methods of identifying same |
| AU2001257331A1 (en) * | 2000-04-28 | 2001-11-12 | Sangamo Biosciences, Inc. | Methods for designing exogenous regulatory molecules |
| WO2001088197A2 (en) * | 2000-05-16 | 2001-11-22 | Massachusetts Institute Of Technology | Methods and compositions for interaction trap assays |
| US6492117B1 (en) * | 2000-07-12 | 2002-12-10 | Gendaq Limited | Zinc finger polypeptides capable of binding DNA quadruplexes |
| US7067317B2 (en) * | 2000-12-07 | 2006-06-27 | Sangamo Biosciences, Inc. | Regulation of angiogenesis with zinc finger proteins |
| US7026462B2 (en) * | 2000-12-07 | 2006-04-11 | Sangamo Biosciences, Inc. | Regulation of angiogenesis with zinc finger proteins |
| EP1417344B1 (en) * | 2001-08-17 | 2011-06-15 | Toolgen, Inc. | Zinc finger domain libraries |
| US20040214766A1 (en) * | 2001-10-01 | 2004-10-28 | Kari Alitalo | VEGF-C or VEGF-D materials and methods for treatment of neuropathologies |
| EP1451297A4 (en) * | 2001-12-07 | 2006-06-28 | Toolgen Inc | PHENOTYPIC SCANNING OF CHIMERIC PROTEINS |
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| EP1451297A4 (en) | 2006-06-28 |
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