EA031715B1 - ПРОТИВОВОСПАЛИТЕЛЬНЫЙ НЕСИАЛИРОВАННЫЙ ПОЛИПЕПТИД МОДИФИЦИРОВАННОГО Fc-УЧАСТКА hIgG1, СПОСОБ ЕГО ПОЛУЧЕНИЯ И ПРИМЕНЕНИЕ - Google Patents
ПРОТИВОВОСПАЛИТЕЛЬНЫЙ НЕСИАЛИРОВАННЫЙ ПОЛИПЕПТИД МОДИФИЦИРОВАННОГО Fc-УЧАСТКА hIgG1, СПОСОБ ЕГО ПОЛУЧЕНИЯ И ПРИМЕНЕНИЕ Download PDFInfo
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- EA031715B1 EA031715B1 EA201491215A EA201491215A EA031715B1 EA 031715 B1 EA031715 B1 EA 031715B1 EA 201491215 A EA201491215 A EA 201491215A EA 201491215 A EA201491215 A EA 201491215A EA 031715 B1 EA031715 B1 EA 031715B1
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- polypeptide
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- nucleic acid
- inflammatory
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| US12384848B2 (en) | 2011-12-19 | 2025-08-12 | The Rockefeller University | Anti-inflammatory polypeptides |
| CN104010659A (zh) | 2011-12-19 | 2014-08-27 | 洛克菲勒大学 | 非唾液酸化的抗炎多肽 |
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| US9512214B2 (en) | 2012-09-02 | 2016-12-06 | Abbvie, Inc. | Methods to control protein heterogeneity |
| CA2905010A1 (en) | 2013-03-12 | 2014-09-18 | Abbvie Inc. | Human antibodies that bind human tnf-alpha and methods of preparing the same |
| WO2014151878A2 (en) | 2013-03-14 | 2014-09-25 | Abbvie Inc. | Methods for modulating protein glycosylation profiles of recombinant protein therapeutics using monosaccharides and oligosacharides |
| US9017687B1 (en) | 2013-10-18 | 2015-04-28 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same using displacement chromatography |
| US9598667B2 (en) | 2013-10-04 | 2017-03-21 | Abbvie Inc. | Use of metal ions for modulation of protein glycosylation profiles of recombinant proteins |
| US20160215061A1 (en) * | 2013-10-08 | 2016-07-28 | Merck Sharp & Dohme Corp. | Fc CONTAINING POLYPEPTIDES HAVING INCREASED BINDING TO FcGammaRIIB |
| US9085618B2 (en) | 2013-10-18 | 2015-07-21 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same |
| US9181337B2 (en) | 2013-10-18 | 2015-11-10 | Abbvie, Inc. | Modulated lysine variant species compositions and methods for producing and using the same |
| US20150139988A1 (en) | 2013-11-15 | 2015-05-21 | Abbvie, Inc. | Glycoengineered binding protein compositions |
| DK3221363T3 (da) | 2014-11-21 | 2020-08-10 | Bristol Myers Squibb Co | Antistoffer mod cd73 og anvendelser deraf |
| HRP20201756T8 (hr) | 2014-11-21 | 2021-08-20 | Bristol-Myers Squibb Company | Antitijela koja sadrže modificirane regije teškog lanca |
| SG10202006538TA (en) | 2014-12-23 | 2020-08-28 | Bristol Myers Squibb Co | Antibodies to tigit |
| EA202191471A1 (ru) * | 2015-03-04 | 2022-01-31 | Зе Рокфеллер Юниверсити | Противовоспалительные полипептиды |
| US10300127B2 (en) | 2015-03-20 | 2019-05-28 | The Rockefeller University | Immune complex |
| LT3303396T (lt) | 2015-05-29 | 2023-01-10 | Bristol-Myers Squibb Company | Antikūnai prieš ox40 ir jų panaudojimo būdai |
| MX2017016502A (es) | 2015-06-29 | 2018-03-12 | Univ Rockefeller | Anticuerpos contra cd40 con actividad agonista mejorada. |
| FR3038517B1 (fr) * | 2015-07-06 | 2020-02-28 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Utilisation de fragments fc modifies en immunotherapie |
| CA3016534A1 (en) | 2016-03-04 | 2017-09-08 | The Rockefeller University | Antibodies to cd40 with enhanced agonist activity |
| KR20180118725A (ko) | 2016-03-04 | 2018-10-31 | 브리스톨-마이어스 스큅 컴퍼니 | 항-cd73 항체와의 조합 요법 |
| EP3551749B1 (en) | 2016-12-07 | 2023-09-27 | East Carolina University | Compositions and methods for in vitro cultivation and/or expansion of regulatory t cells |
| TWI788340B (zh) | 2017-04-07 | 2023-01-01 | 美商必治妥美雅史谷比公司 | 抗icos促效劑抗體及其用途 |
| IL270596B1 (en) | 2017-05-25 | 2025-09-01 | Bristol Myers Squibb Co | Antibodies comprising modified heavy constant region for use in treating cancer |
| CN111032688A (zh) * | 2017-08-11 | 2020-04-17 | 研究发展基金会 | 用于延长的血清半衰期的工程化抗体fc变体 |
| CA3085472A1 (en) | 2017-12-19 | 2019-06-27 | The Rockefeller University | Human igg fc domain variants with improved effector function |
| KR102813744B1 (ko) | 2017-12-27 | 2025-05-28 | 브리스톨-마이어스 스큅 컴퍼니 | 항-cd40 항체 및 그의 용도 |
| WO2020089811A1 (en) | 2018-10-31 | 2020-05-07 | Novartis Ag | Dc-sign antibody drug conjugates |
| TW202033555A (zh) | 2018-11-16 | 2020-09-16 | 美商必治妥美雅史谷比公司 | 抗nkg2a抗體及其用途 |
| KR20210096167A (ko) | 2018-11-28 | 2021-08-04 | 브리스톨-마이어스 스큅 컴퍼니 | 변형된 중쇄 불변 영역을 포함하는 항체 |
| US20230192867A1 (en) | 2020-05-15 | 2023-06-22 | Bristol-Myers Squibb Company | Antibodies to garp |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2008076487A2 (en) * | 2006-12-20 | 2008-06-26 | Verenium Corporation | Antibodies and methods for making and using them |
| US20100286067A1 (en) * | 2008-01-08 | 2010-11-11 | Biogenerix Ag | Glycoconjugation of polypeptides using oligosaccharyltransferases |
| WO2011059684A1 (en) * | 2009-10-29 | 2011-05-19 | Centocor Ortho Biotech Inc. | Antibody glycosylation variants |
Family Cites Families (21)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7064191B2 (en) | 2000-10-06 | 2006-06-20 | Kyowa Hakko Kogyo Co., Ltd. | Process for purifying antibody |
| US20040002587A1 (en) * | 2002-02-20 | 2004-01-01 | Watkins Jeffry D. | Fc region variants |
| US8188231B2 (en) | 2002-09-27 | 2012-05-29 | Xencor, Inc. | Optimized FC variants |
| US20040110930A1 (en) | 2002-10-03 | 2004-06-10 | Reinl Stephen J. | Multimeric protein engineering |
| WO2006076594A2 (en) * | 2005-01-12 | 2006-07-20 | Xencor, Inc. | Antibodies and fc fusion proteins with altered immunogenicity |
| MX2007013924A (es) | 2005-05-09 | 2008-01-28 | Glycart Biotechnology Ag | Moleculas que unen antigeno que tienen regiones fc modificadas y union alterada a receptores fc. |
| WO2007005786A2 (en) | 2005-06-30 | 2007-01-11 | Centocor, Inc. | Methods and compositions with enhanced therapeutic activity |
| US20080206246A1 (en) | 2006-04-05 | 2008-08-28 | Ravetch Jeffrey V | Polypeptides with enhanced anti-inflammatory and decreased cytotoxic properties and relating methods |
| CA2627981A1 (en) | 2005-11-07 | 2007-05-18 | The Rockefeller University | Reagents, methods and systems for selecting a cytotoxic antibody or variant thereof |
| US8470318B2 (en) | 2005-11-07 | 2013-06-25 | The Rockefeller University | Polypeptides with enhanced anti-inflammatory and decreased cytotoxic properties and relating methods |
| EP3456351A1 (en) | 2006-04-05 | 2019-03-20 | The Rockefeller University | Polypeptides with enhanced anti-inflammatory and decreased cytotoxic properties and relating methods |
| NZ597651A (en) | 2006-10-26 | 2012-07-27 | Univ Rockefeller | Polypeptides with enhanced anti-inflammatory and decreased cytotoxic properties and relating methods |
| CN101646775B (zh) * | 2006-12-28 | 2016-08-24 | 森托科尔奥索生物科技公司 | 用于产生脱唾液酸化免疫球蛋白的方法和载体 |
| US20110020269A1 (en) | 2007-05-08 | 2011-01-27 | Beth Israel Deaconess Medical Center, Inc. | Methods and compositions for modifying t cell immune responses and inflammation |
| EP3176264B1 (en) * | 2007-05-30 | 2018-09-26 | Postech Academy-Industry- Foundation | Immunoglobulin fusion proteins |
| EP2279410B1 (en) | 2008-04-22 | 2015-11-11 | The Rockefeller University | Methods of identifying anti-inflammatory compounds |
| LT2647707T (lt) * | 2010-11-30 | 2018-11-12 | Chugai Seiyaku Kabushiki Kaisha | Citotoksiškumą indukuojantis terapinis agentas |
| CA3167037A1 (en) * | 2010-12-20 | 2012-06-28 | The Rockefeller University | Modulating agonistic tnfr antibodies |
| EP2694109A4 (en) * | 2011-04-07 | 2015-02-18 | Neotope Biosciences Ltd | COMPOSITIONS AND METHODS FOR THE TREATMENT OF PROTEIN AGGREGATION DISEASES WITH IC3B DEPOSITION |
| US20130273089A1 (en) * | 2011-11-03 | 2013-10-17 | Tolera Therapeutics, Inc. | Antibody and methods for selective inhibition of t-cell responses |
| CN104010659A (zh) * | 2011-12-19 | 2014-08-27 | 洛克菲勒大学 | 非唾液酸化的抗炎多肽 |
-
2012
- 2012-12-10 CN CN201280062837.8A patent/CN104010659A/zh active Pending
- 2012-12-10 PT PT12860516T patent/PT2793943T/pt unknown
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- 2012-12-10 CA CA2859022A patent/CA2859022A1/en active Pending
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- 2012-12-10 EP EP18196115.2A patent/EP3485909A1/en active Pending
- 2012-12-10 ES ES12860516.9T patent/ES2692539T3/es active Active
- 2012-12-10 US US14/368,701 patent/US9587025B2/en active Active
- 2012-12-10 WO PCT/US2012/068718 patent/WO2013095966A1/en not_active Ceased
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- 2014-06-12 IL IL233082A patent/IL233082B/en active IP Right Grant
- 2014-07-15 ZA ZA2014/05185A patent/ZA201405185B/en unknown
-
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- 2015-03-04 US US14/638,905 patent/US9845358B2/en active Active
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- 2017-12-18 US US15/845,487 patent/US10894832B2/en active Active
- 2017-12-27 JP JP2017251227A patent/JP2018093874A/ja active Pending
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- 2019-08-19 IL IL268787A patent/IL268787B/en unknown
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- 2020-11-20 US US16/953,639 patent/US11608379B2/en active Active
- 2020-11-25 US US17/104,125 patent/US11613579B2/en active Active
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- 2021-01-07 JP JP2021001368A patent/JP2021063117A/ja active Pending
-
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- 2022-03-04 JP JP2022033240A patent/JP2022091768A/ja active Pending
-
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- 2024-06-26 JP JP2024102976A patent/JP2024125369A/ja active Pending
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2008076487A2 (en) * | 2006-12-20 | 2008-06-26 | Verenium Corporation | Antibodies and methods for making and using them |
| US20100286067A1 (en) * | 2008-01-08 | 2010-11-11 | Biogenerix Ag | Glycoconjugation of polypeptides using oligosaccharyltransferases |
| WO2011059684A1 (en) * | 2009-10-29 | 2011-05-19 | Centocor Ortho Biotech Inc. | Antibody glycosylation variants |
Non-Patent Citations (2)
| Title |
|---|
| BURTON, DR. et al. Sugar Determines Antibody Activity. Science. August 4, 2006; Vol. 313, pages 627-628, DOI: 10.1126/science.1131712; page 627, column 2, paragraph 2 to page 627, column 3, paragraph 1; figure 1 * |
| RAMAKRISHNA, C. et al. Passively Administered Pooled Human Immunoglobulins Exert IL-10 Dependent Anti-Inflammatory Effects That Protect Against Fatal HSV Encephalitis. PLoS Pathog. June 2, 2011; Vol. 7, No. 6, pages 1-17: e1002071. doi:10.1371/journal.ppat,1002071; abstract; page 2, column 1, paragraph 1; page 14, column 1, paragraph 4; figures 1d, 6 * |
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