CN109803679A - 在基因组重新编码生物体中生产硒代生物制剂 - Google Patents
在基因组重新编码生物体中生产硒代生物制剂 Download PDFInfo
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- C—CHEMISTRY; METALLURGY
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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- C—CHEMISTRY; METALLURGY
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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- C07K16/243—Colony Stimulating Factors
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- C—CHEMISTRY; METALLURGY
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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- C07K16/2863—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against receptors for growth factors, growth regulators
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- C—CHEMISTRY; METALLURGY
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
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- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
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- C07K—PEPTIDES
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- C07K2317/60—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments
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- C07K2317/622—Single chain antibody (scFv)
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- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
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- C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
Landscapes
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| US62/537,986 | 2017-07-28 | ||
| PCT/US2017/049354 WO2018045018A1 (en) | 2016-08-30 | 2017-08-30 | Production of seleno-biologics in genomically recoded organisms |
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Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2021203861A1 (zh) * | 2020-04-10 | 2021-10-14 | 苏州普乐康医药科技有限公司 | 一种抗igf-1r抗体及其应用 |
| CN114144426A (zh) * | 2019-04-19 | 2022-03-04 | 印地安纳大学理事会 | 餐时或基础胰岛素类似物通过内部二硒桥的稳定化 |
| WO2023051680A1 (zh) * | 2021-09-30 | 2023-04-06 | 正大天晴药业集团股份有限公司 | 针对免疫检查点的双特异性抗体 |
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| US9840553B2 (en) | 2014-06-28 | 2017-12-12 | Kodiak Sciences Inc. | Dual PDGF/VEGF antagonists |
| WO2017117464A1 (en) | 2015-12-30 | 2017-07-06 | Kodiak Sciences Inc. | Antibodies and conjugates thereof |
| US11542332B2 (en) | 2016-03-26 | 2023-01-03 | Bioatla, Inc. | Anti-CTLA4 antibodies, antibody fragments, their immunoconjugates and uses thereof |
| CN109844105A (zh) | 2016-07-11 | 2019-06-04 | 得克萨斯州大学系统董事会 | 包含硒代半胱氨酸的重组多肽及其产生方法 |
| BR112020017872A2 (pt) | 2018-03-02 | 2020-12-22 | Kodiak Sciences Inc. | Anticorpos de il-6 e construtos de fusão e conjugados dos mesmos |
| JP7384906B2 (ja) * | 2018-07-09 | 2023-11-21 | ジーアールオー・バイオサイエンシズ・インコーポレイテッド | 非標準アミノ酸含有組成物とその使用 |
| WO2021072265A1 (en) | 2019-10-10 | 2021-04-15 | Kodiak Sciences Inc. | Methods of treating an eye disorder |
| AU2020398327A1 (en) | 2019-12-03 | 2022-07-14 | Evotec International Gmbh | Interferon-associated antigen binding proteins and uses thereof |
| US11179473B2 (en) | 2020-02-21 | 2021-11-23 | Silverback Therapeutics, Inc. | Nectin-4 antibody conjugates and uses thereof |
| JP2023545520A (ja) | 2020-10-14 | 2023-10-30 | ビリジアン セラピューティクス, インコーポレイテッド | 甲状腺眼疾患を治療するための組成物及び方法 |
| WO2023019171A1 (en) | 2021-08-10 | 2023-02-16 | Viridian Therapeutics, Inc. | Compositions, doses, and methods for treatment of thyroid eye disease |
Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20100298212A1 (en) * | 2007-11-20 | 2010-11-25 | Ambrx, Inc. | Modified Insulin Polypeptides and Their Uses |
| AU2012216723A1 (en) * | 2007-11-20 | 2012-09-27 | Ambrx, Inc. | Modified insulin polypeptides and their uses |
| US20140024592A1 (en) * | 2010-09-08 | 2014-01-23 | Howard Florey Institute Of Experimental Physiology And Medicine | Modified Relaxin Polypeptides |
| CN103619875A (zh) * | 2011-01-28 | 2014-03-05 | 加拿大国家研究委员会 | 免疫球蛋白结构域的工程改造 |
| US20140154744A1 (en) * | 2011-07-11 | 2014-06-05 | Yale University | Compositions and Methods for Making Selenocysteine Containing Polypeptides |
| CN105111304A (zh) * | 2015-09-30 | 2015-12-02 | 山东阿华生物药业有限公司 | 重组人胰岛素前体的纯化和酶切转换方法 |
Family Cites Families (18)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6849417B1 (en) * | 1998-04-06 | 2005-02-01 | The United States Of America As Represented By The Department Of Health And Human Services | Mammalian selenoprotein differentially expressed in tumor cells |
| AU6987200A (en) | 1999-08-16 | 2001-03-13 | Karolinska Innovations Ab | Methods and means for selenoprotein expression |
| WO2007075438A2 (en) * | 2005-12-15 | 2007-07-05 | Codon Devices, Inc. | Polypeptides comprising unnatural amino acids, methods for their production and uses therefor |
| WO2009043051A2 (en) | 2007-09-27 | 2009-04-02 | Biogen Idec Ma Inc. | Cd23 binding molecules and methods of use thereof |
| JP5572972B2 (ja) * | 2009-03-16 | 2014-08-20 | Jnc株式会社 | インスリン分泌促進剤などの薬物のスクリーニング方法 |
| DK2717898T3 (en) | 2011-06-10 | 2019-03-25 | Bioverativ Therapeutics Inc | COAGULATING COMPOUNDS AND PROCEDURES FOR USE THEREOF |
| US10240158B2 (en) | 2011-07-11 | 2019-03-26 | Yale University | Compositions and methods for making selenocysteine containing polypeptides |
| US10876142B2 (en) | 2011-07-11 | 2020-12-29 | Yale University | Compositions and methods for making selenocysteine containing polypeptides |
| EP2968552B1 (en) | 2013-03-14 | 2020-03-11 | The Scripps Research Institute | Targeting agent antibody conjugates and uses thereof |
| US20150050682A1 (en) | 2013-08-15 | 2015-02-19 | University Of Vermont And State Agricultural College | Direct assay of thioredoxin reductase activity |
| WO2015066543A1 (en) * | 2013-11-01 | 2015-05-07 | Board Of Regents, The University Of Texas System | Targeting her2 and her3 with bispecific antibodies in cancerous cells |
| US10118950B2 (en) | 2014-08-30 | 2018-11-06 | Northwestern University | Platforms for cell-free protein synthesis comprising extracts from genomically recoded E. coli strains having genetic knock-out mutations in release factor 1 (RF-1) and endA |
| WO2016172269A2 (en) * | 2015-04-20 | 2016-10-27 | University Of Utah Research Foundation | Insulin analogs having shortened b chain peptides and associated methods |
| US10557160B2 (en) | 2015-12-15 | 2020-02-11 | Board Of Regents, The University Of Texas System | Transgenic bacteria with expanded amino acid usage and nucleic acid molecules for use in the same |
| CN109844105A (zh) * | 2016-07-11 | 2019-06-04 | 得克萨斯州大学系统董事会 | 包含硒代半胱氨酸的重组多肽及其产生方法 |
| AU2017298565B2 (en) | 2016-07-22 | 2021-08-19 | The Walter And Eliza Hall Institute Of Medical Research | Insulin analogs |
| IL264330B2 (en) * | 2016-07-22 | 2024-05-01 | Univ Utah Res Found | An insulin analog, pharmaceutical composition comprising it and its uses |
| CN114144426A (zh) | 2019-04-19 | 2022-03-04 | 印地安纳大学理事会 | 餐时或基础胰岛素类似物通过内部二硒桥的稳定化 |
-
2017
- 2017-08-30 CA CA3034701A patent/CA3034701A1/en active Pending
- 2017-08-30 US US16/329,761 patent/US11492650B2/en active Active
- 2017-08-30 CN CN201780053385.XA patent/CN109803679A/zh active Pending
- 2017-08-30 JP JP2019531589A patent/JP7186400B2/ja active Active
- 2017-08-30 WO PCT/US2017/049354 patent/WO2018045018A1/en not_active Ceased
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-
2022
- 2022-11-18 JP JP2022184852A patent/JP7378106B2/ja active Active
Patent Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20100298212A1 (en) * | 2007-11-20 | 2010-11-25 | Ambrx, Inc. | Modified Insulin Polypeptides and Their Uses |
| AU2012216723A1 (en) * | 2007-11-20 | 2012-09-27 | Ambrx, Inc. | Modified insulin polypeptides and their uses |
| US20140024592A1 (en) * | 2010-09-08 | 2014-01-23 | Howard Florey Institute Of Experimental Physiology And Medicine | Modified Relaxin Polypeptides |
| CN103619875A (zh) * | 2011-01-28 | 2014-03-05 | 加拿大国家研究委员会 | 免疫球蛋白结构域的工程改造 |
| US20140154744A1 (en) * | 2011-07-11 | 2014-06-05 | Yale University | Compositions and Methods for Making Selenocysteine Containing Polypeptides |
| CN105111304A (zh) * | 2015-09-30 | 2015-12-02 | 山东阿华生物药业有限公司 | 重组人胰岛素前体的纯化和酶切转换方法 |
Non-Patent Citations (2)
| Title |
|---|
| LUIS MORODER: "Isosteric replacement of sulfur with other chalcogens in peptides and proteins", JOURNAL OF PEPTIDE SCIENCE, vol. 11, pages 205 * |
| QING-XIN HUA等: "Structure of a protein in a kinetic trap", NATURE STRUCTURAL BIOLOGY, vol. 2, pages 130 * |
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN114144426A (zh) * | 2019-04-19 | 2022-03-04 | 印地安纳大学理事会 | 餐时或基础胰岛素类似物通过内部二硒桥的稳定化 |
| WO2021203861A1 (zh) * | 2020-04-10 | 2021-10-14 | 苏州普乐康医药科技有限公司 | 一种抗igf-1r抗体及其应用 |
| WO2023051680A1 (zh) * | 2021-09-30 | 2023-04-06 | 正大天晴药业集团股份有限公司 | 针对免疫检查点的双特异性抗体 |
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| JP7378106B2 (ja) | 2023-11-13 |
| EP3506945A1 (en) | 2019-07-10 |
| JP2023015347A (ja) | 2023-01-31 |
| EP3506945A4 (en) | 2020-07-15 |
| WO2018045018A1 (en) | 2018-03-08 |
| WO2018045018A8 (en) | 2018-05-11 |
| CA3034701A1 (en) | 2018-03-08 |
| US11492650B2 (en) | 2022-11-08 |
| JP7186400B2 (ja) | 2022-12-09 |
| US20190194713A1 (en) | 2019-06-27 |
| JP2020502104A (ja) | 2020-01-23 |
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