RU2499053C2 - Способ синтеза белка с модифицированным профилем n-гликозилирования в растениях - Google Patents
Способ синтеза белка с модифицированным профилем n-гликозилирования в растениях Download PDFInfo
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- RU2499053C2 RU2499053C2 RU2010101024/10A RU2010101024A RU2499053C2 RU 2499053 C2 RU2499053 C2 RU 2499053C2 RU 2010101024/10 A RU2010101024/10 A RU 2010101024/10A RU 2010101024 A RU2010101024 A RU 2010101024A RU 2499053 C2 RU2499053 C2 RU 2499053C2
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| US94434407P | 2007-06-15 | 2007-06-15 | |
| US60/944,344 | 2007-06-15 | ||
| PCT/CA2008/001139 WO2008151440A1 (en) | 2007-06-15 | 2008-06-13 | Modifying glycoprotein production in plants |
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| RU2013137208/10A Division RU2013137208A (ru) | 2007-06-15 | 2013-08-08 | Способ синтеза белка с модифицированным профилем n-гликозилирования в растениях |
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| RU2010101024A RU2010101024A (ru) | 2011-07-20 |
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| RU2010101024/10A RU2499053C2 (ru) | 2007-06-15 | 2008-06-13 | Способ синтеза белка с модифицированным профилем n-гликозилирования в растениях |
| RU2013137208/10A RU2013137208A (ru) | 2007-06-15 | 2013-08-08 | Способ синтеза белка с модифицированным профилем n-гликозилирования в растениях |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
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| RU2013137208/10A RU2013137208A (ru) | 2007-06-15 | 2013-08-08 | Способ синтеза белка с модифицированным профилем n-гликозилирования в растениях |
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| EP (1) | EP2155880B1 (https=) |
| JP (1) | JP5783720B2 (https=) |
| KR (2) | KR101385050B1 (https=) |
| CN (3) | CN104962579A (https=) |
| AU (1) | AU2008261527C1 (https=) |
| BR (1) | BRPI0812538B1 (https=) |
| CA (2) | CA2795379A1 (https=) |
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| ES (1) | ES2624776T3 (https=) |
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| MA (1) | MA31516B1 (https=) |
| MX (1) | MX2009013665A (https=) |
| NZ (2) | NZ598417A (https=) |
| PL (1) | PL2155880T3 (https=) |
| PT (1) | PT2155880T (https=) |
| RU (2) | RU2499053C2 (https=) |
| SG (1) | SG185249A1 (https=) |
| SI (1) | SI2155880T1 (https=) |
| TN (1) | TN2009000512A1 (https=) |
| WO (1) | WO2008151440A1 (https=) |
| ZA (1) | ZA201000207B (https=) |
Families Citing this family (18)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA2615372A1 (en) | 2007-07-13 | 2009-01-13 | Marc-Andre D'aoust | Influenza virus-like particles (vlps) comprising hemagglutinin |
| WO2009076778A1 (en) | 2007-11-27 | 2009-06-25 | Medicago Inc. | Recombinant influenza virus-like particles (vlps) produced in transgenic plants expressing hemagglutinin |
| AU2009267769B2 (en) | 2008-07-08 | 2015-07-16 | Medicago Inc. | Soluble recombinant influenza antigens |
| NZ590351A (en) | 2008-07-18 | 2012-11-30 | Medicago Inc | HA1 domain totally or partially free of N-linked glycosylation operatively linked to a regulatory region |
| HUE039100T2 (hu) | 2009-06-24 | 2018-12-28 | Medicago Inc | Hemagglutinint tartalmazó kimer influenzavírus-jellegû részecskék |
| KR101773431B1 (ko) | 2009-09-22 | 2017-09-12 | 메디카고 인코포레이티드 | 식물-유래 ｖｌｐ의 제조방법 |
| TWI620816B (zh) | 2011-03-23 | 2018-04-11 | 苜蓿股份有限公司 | 植物衍生蛋白回收方法 |
| WO2012170678A1 (en) * | 2011-06-07 | 2012-12-13 | Fraunhofer Usa, Inc. | In vivo de-glycosylation of recombinant proteins by co-expression with pngase f |
| US9181532B2 (en) | 2011-07-29 | 2015-11-10 | Icon Genetics Gmbh | Production of galactosylated N-glycans in plants |
| NZ622731A (en) | 2011-09-30 | 2016-04-29 | Medicago Inc | Increasing virus-like particle yield in plants |
| KR20130125337A (ko) * | 2012-05-08 | 2013-11-18 | 경상대학교산학협력단 | 고-만노오스형 n-글라이칸을 생산하는 식물체 및 이를 이용한 고-만노오스형 n-글라이칸의 생산방법 |
| US12467058B2 (en) | 2013-03-28 | 2025-11-11 | Aramis Biotechnologies Inc. | Influenza virus-like particle production in plants |
| ES2803508T3 (es) | 2013-03-28 | 2021-01-27 | Medicago Inc | Producción de partículas similares al virus de la gripe en plantas |
| RU2731295C2 (ru) | 2014-07-11 | 2020-09-01 | Медикаго Инк. | Модификация продуцирования белков в растениях |
| WO2016079739A2 (en) * | 2014-11-20 | 2016-05-26 | Yissum Research Development Company Of The Hebrew University Of Jerusalem Ltd. | Compositions and methods for producing polypeptides with a modified glycosylation pattern in plant cells |
| US11499160B2 (en) | 2016-12-01 | 2022-11-15 | Plantform Corporation | Transgenic plant with reduced fucosyltransferase and xylosyltransferase activity |
| US11649465B2 (en) * | 2017-09-11 | 2023-05-16 | R.J. Reynolds Tobacco Company | Methods and compositions for increasing expression of genes of interest in a plant by co-expression with p21 |
| WO2022153973A1 (ja) * | 2021-01-15 | 2022-07-21 | デンカ株式会社 | 栽培条件を決定する方法、及び目的タンパク質又は目的ペプチドの製造方法 |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2003078637A2 (en) * | 2002-03-19 | 2003-09-25 | Plant Research International B.V. | Optimizing glycan processing in plants |
| WO2004065540A2 (en) * | 2003-01-22 | 2004-08-05 | Glycart Biotechnology Ag | Fusion constructs and use of same to produce antibodies with increased fc receptor binding affinity and effector function |
| RU2004106559A (ru) * | 2001-08-03 | 2005-05-10 | Гликарт Биотекнолоджи АГ (CH) | Гликозилированные антитела (варианты), обладающие повышенной антителозависимой клеточной цитотоксичностью |
| US6998267B1 (en) * | 1998-12-09 | 2006-02-14 | The Dow Chemical Company | Method for manufacturing glycoproteins having human-type glycosylation |
Family Cites Families (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5312746A (en) * | 1993-01-08 | 1994-05-17 | Life Technologies, Inc. | Cloning and expressing restriction endonucleases and modification methylases from caryophanon |
| GB9524350D0 (en) * | 1995-11-29 | 1996-01-31 | Lynxvale Ltd | Enhancer-increased gene expression in plants |
| US5945326A (en) * | 1997-03-20 | 1999-08-31 | New England Biolabs, Inc. | Method for cloning and producing the Spel restriction endonuclease |
| US7125978B1 (en) | 1999-10-04 | 2006-10-24 | Medicago Inc. | Promoter for regulating expression of foreign genes |
| KR100817660B1 (ko) * | 1999-10-04 | 2008-03-27 | 메디카고 인코포레이티드 | 외래 유전자의 발현을 조절하는 프로모터 |
| BR0014945A (pt) * | 1999-10-21 | 2004-08-31 | Monsanto Co | Modificação pós-traducional de proteìnas recombinantes produzidas em plantas |
| ES2349427T3 (es) * | 1999-10-26 | 2011-01-03 | Stichting Dienst Landbouwkundig Onderzoek | Glicosilación de tipo mamífero en plantas. |
| DE60044858D1 (de) * | 1999-10-26 | 2010-09-30 | Stichting Dienst Landbouwkundi | Säugetierartige Glykosylierung in Pflanzen |
| DK1356068T3 (en) * | 2001-01-19 | 2015-02-16 | Phyton Holdings Llc | PROCESS FOR THE PRODUCTION OF secretory glycoprotein with HUMAN TYPE SUGAR CHAIN FOR USING A PLANT CELL |
| US20030035774A1 (en) | 2001-07-18 | 2003-02-20 | Adjei Akwete L. | Salt/ion pair medicinal aerosol formulation |
| KR101113432B1 (ko) * | 2002-02-13 | 2012-02-29 | 위스콘신 얼럼나이 리서어치 화운데이션 | 인플루엔자 바이러스 벡터의 패키징을 위한 신호 |
| CN1665934B (zh) * | 2002-03-19 | 2010-05-26 | 国际植物研究所 | GNTIII(UDP-N乙酰葡萄糖胺:β-D-甘露糖苷β(1,4)-N-乙酰葡萄糖胺基-转移酶III)在植物中的表达 |
| ES2349777T3 (es) * | 2003-01-22 | 2011-01-11 | Glycart Biotechnology Ag | Constructos de fusión y uso de los mismos para producir anticuerpos con mayor afinidad de unión al receptor de fc y función efectora. |
| KR20060035596A (ko) * | 2003-05-05 | 2006-04-26 | 보이스 톰슨 인스터튜트 포 플랜트 리서치 | 외래유전자도입 식물로부터 유래된 면역보호성 조성물을제조하기 위한 벡터와 세포 |
| JP2006212019A (ja) * | 2004-04-30 | 2006-08-17 | National Institute Of Agrobiological Sciences | 植物を用いたユビキノン−１０の製造方法 |
-
2008
- 2008-06-13 DK DK08772802.8T patent/DK2155880T3/en active
- 2008-06-13 JP JP2010511461A patent/JP5783720B2/ja not_active Expired - Fee Related
- 2008-06-13 RU RU2010101024/10A patent/RU2499053C2/ru active
- 2008-06-13 CN CN201510364867.XA patent/CN104962579A/zh active Pending
- 2008-06-13 BR BRPI0812538-4A patent/BRPI0812538B1/pt not_active IP Right Cessation
- 2008-06-13 WO PCT/CA2008/001139 patent/WO2008151440A1/en not_active Ceased
- 2008-06-13 EP EP08772802.8A patent/EP2155880B1/en active Active
- 2008-06-13 CN CN2008801031743A patent/CN101918559A/zh active Pending
- 2008-06-13 ES ES08772802.8T patent/ES2624776T3/es active Active
- 2008-06-13 SG SG2012066486A patent/SG185249A1/en unknown
- 2008-06-13 US US12/664,567 patent/US20110008837A1/en not_active Abandoned
- 2008-06-13 CA CA2795379A patent/CA2795379A1/en not_active Abandoned
- 2008-06-13 PT PT87728028T patent/PT2155880T/pt unknown
- 2008-06-13 SI SI200831699A patent/SI2155880T1/sl unknown
- 2008-06-13 PL PL08772802T patent/PL2155880T3/pl unknown
- 2008-06-13 MX MX2009013665A patent/MX2009013665A/es active IP Right Grant
- 2008-06-13 HU HUE08772802A patent/HUE031698T2/en unknown
- 2008-06-13 KR KR1020107000811A patent/KR101385050B1/ko not_active Expired - Fee Related
- 2008-06-13 CA CA2700180A patent/CA2700180C/en active Active
- 2008-06-13 KR KR1020137014893A patent/KR20130075787A/ko not_active Ceased
- 2008-06-13 AU AU2008261527A patent/AU2008261527C1/en not_active Ceased
- 2008-06-13 NZ NZ598417A patent/NZ598417A/xx not_active IP Right Cessation
- 2008-06-13 CN CN2013101091944A patent/CN103382487A/zh active Pending
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-
2009
- 2009-12-07 IL IL202568A patent/IL202568A/en active IP Right Grant
- 2009-12-10 TN TNP2009000512A patent/TN2009000512A1/fr unknown
- 2009-12-14 EG EG2009121826A patent/EG26600A/en active
-
2010
- 2010-01-12 MA MA32504A patent/MA31516B1/fr unknown
- 2010-01-12 ZA ZA2010/00207A patent/ZA201000207B/en unknown
-
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- 2013-08-08 RU RU2013137208/10A patent/RU2013137208A/ru not_active Application Discontinuation
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6998267B1 (en) * | 1998-12-09 | 2006-02-14 | The Dow Chemical Company | Method for manufacturing glycoproteins having human-type glycosylation |
| RU2004106559A (ru) * | 2001-08-03 | 2005-05-10 | Гликарт Биотекнолоджи АГ (CH) | Гликозилированные антитела (варианты), обладающие повышенной антителозависимой клеточной цитотоксичностью |
| WO2003078637A2 (en) * | 2002-03-19 | 2003-09-25 | Plant Research International B.V. | Optimizing glycan processing in plants |
| WO2004065540A2 (en) * | 2003-01-22 | 2004-08-05 | Glycart Biotechnology Ag | Fusion constructs and use of same to produce antibodies with increased fc receptor binding affinity and effector function |
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