JP6014805B2 - テイラードマルチサイトコンビナトリアルアセンブリー - Google Patents
テイラードマルチサイトコンビナトリアルアセンブリー Download PDFInfo
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| US20030194807A1 (en) | 1992-11-02 | 2003-10-16 | Roberto Crea | Walk-through mutagenesis |
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| US6165793A (en) | 1996-03-25 | 2000-12-26 | Maxygen, Inc. | Methods for generating polynucleotides having desired characteristics by iterative selection and recombination |
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| US20020028443A1 (en) | 1999-09-27 | 2002-03-07 | Jay M. Short | Method of dna shuffling with polynucleotides produced by blocking or interrupting a synthesis or amplification process |
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| US6713279B1 (en) | 1995-12-07 | 2004-03-30 | Diversa Corporation | Non-stochastic generation of genetic vaccines and enzymes |
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| US6562594B1 (en) | 1999-09-29 | 2003-05-13 | Diversa Corporation | Saturation mutagenesis in directed evolution |
| US5789166A (en) | 1995-12-08 | 1998-08-04 | Stratagene | Circular site-directed mutagenesis |
| GB9701425D0 (en) | 1997-01-24 | 1997-03-12 | Bioinvent Int Ab | A method for in vitro molecular evolution of protein function |
| DE69940879D1 (de) | 1998-11-11 | 2009-06-25 | Japan Science & Tech Agency | Verfahren zur mutagenese |
| US6376191B1 (en) * | 2000-03-22 | 2002-04-23 | Mergen, Ltd. | Microarray-based analysis of polynucleotide sequence variations |
| JP3859947B2 (ja) | 2000-08-04 | 2006-12-20 | 独立行政法人理化学研究所 | 突然変異導入方法 |
| EP1309677B2 (en) | 2000-08-11 | 2012-04-11 | Genencor International, Inc. | Bacillus transformation, transformants and mutant libraries |
| FR2813314B1 (fr) | 2000-08-25 | 2004-05-07 | Biomethodes | Procede de mutagenese dirigee massive |
| USPP13969P3 (en) | 2001-04-05 | 2003-07-15 | Her Majesty The Queen In Right Of Canada As Represented By The Minister Of Agriculture | Shrub rose plant named ‘Morden Sunrise’ |
| US8067556B2 (en) | 2001-07-26 | 2011-11-29 | Agilent Technologies, Inc. | Multi-site mutagenesis |
| DE10148607A1 (de) | 2001-10-02 | 2003-04-10 | Max Planck Gesellschaft | Methoden zur DNA-Manipulation |
| US20030129709A1 (en) | 2001-11-02 | 2003-07-10 | Olga Makarova | Method for site-directed mutagenesis of nucleic acid molecules using a single primer |
| CA2468710A1 (en) | 2001-12-03 | 2003-06-12 | Diversa Corporation | Chromosomal saturation mutagenesis |
| AUPS263402A0 (en) | 2002-05-29 | 2002-06-20 | Young, Lei | Targeted amplification of template strand (TATS) technology, and its use in DNA mutagenesis, deletion & insertion |
| US20060134624A1 (en) | 2003-02-06 | 2006-06-22 | Salerno John C | Polymerase-based protocols for the introductions of deletions and insertions |
| US20060228786A1 (en) | 2003-02-06 | 2006-10-12 | Salerno John C | Polymerase-based protocols for the introduction of deletions and insertions |
| US6878531B1 (en) | 2003-11-10 | 2005-04-12 | Medical College Of Georgia Research Institute | Method for multiple site-directed mutagenesis |
| US20060288786A1 (en) * | 2005-03-18 | 2006-12-28 | Flores Andres H L | Ultrasonically coupled scanning probe microscope |
| US20060223066A1 (en) * | 2005-03-29 | 2006-10-05 | Applera Corporation | Methods for normalizing and for identifying small nucleic acids |
| JP2008546424A (ja) * | 2005-06-28 | 2008-12-25 | アジェンコート パーソナル ジェノミクス コーポレイション | 修飾ポリヌクレオチドを作製する方法および配列決定する方法 |
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| Publication number | Publication date |
|---|---|
| EA201070206A1 (ru) | 2010-06-30 |
| NZ582876A (en) | 2012-07-27 |
| WO2009018449A1 (en) | 2009-02-05 |
| US9476078B2 (en) | 2016-10-25 |
| EP2183378A4 (en) | 2010-09-22 |
| EP2183378A1 (en) | 2010-05-12 |
| ZA201000152B (en) | 2011-06-29 |
| CN101821402A (zh) | 2010-09-01 |
| CA2693102A1 (en) | 2009-02-05 |
| CN104673784A (zh) | 2015-06-03 |
| DK3031919T3 (en) | 2019-01-07 |
| KR101685712B1 (ko) | 2016-12-12 |
| ES2701883T3 (es) | 2019-02-26 |
| US20100216192A1 (en) | 2010-08-26 |
| EP3031919B1 (en) | 2018-09-19 |
| KR20100045494A (ko) | 2010-05-03 |
| MX2010001182A (es) | 2010-04-21 |
| EP3031919A1 (en) | 2016-06-15 |
| CN101821402B (zh) | 2015-03-04 |
| JP2010535034A (ja) | 2010-11-18 |
| CA2693102C (en) | 2020-03-10 |
| IL202839A0 (en) | 2010-06-30 |
| EA020657B1 (ru) | 2014-12-30 |
| MX353478B (es) | 2018-01-15 |
| BRPI0815046A2 (pt) | 2014-10-14 |
| AU2008282101A1 (en) | 2009-02-05 |
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