JP2014503198A - 組換え酵素および他のタンパク質のタンパク質発現および分泌を改善する新規シグナル配列 - Google Patents
組換え酵素および他のタンパク質のタンパク質発現および分泌を改善する新規シグナル配列 Download PDFInfo
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| JP2021505135A (ja) * | 2017-11-30 | 2021-02-18 | アミカス セラピューティックス インコーポレイテッド | Ｃｄｋｌ５発現変異体及びｃｄｋｌ５融合タンパク質 |
| JP2021521851A (ja) * | 2018-04-30 | 2021-08-30 | アミカス セラピューティックス インコーポレイテッド | 遺伝子治療構築物及び使用方法 |
| JP2022530833A (ja) * | 2019-04-30 | 2022-07-01 | ザ・トラステイーズ・オブ・ザ・ユニバーシテイ・オブ・ペンシルベニア | ポンペ病の治療のために有用な組成物 |
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SI3164492T1 (sl) * | 2014-07-03 | 2020-02-28 | F. Hoffmann-La Roche Ag | Sistem polipeptidne ekspresije |
| WO2017180587A2 (en) | 2016-04-11 | 2017-10-19 | Obsidian Therapeutics, Inc. | Regulated biocircuit systems |
| JP7341900B2 (ja) | 2017-03-03 | 2023-09-11 | オブシディアン セラピューティクス， インコーポレイテッド | 免疫療法のためのｃｄ１９組成物及び方法 |
| EP3635009B1 (en) | 2017-06-07 | 2026-02-25 | Regeneron Pharmaceuticals, Inc. | Compositions and methods for internalizing enzymes |
| IL276464B2 (en) | 2018-02-07 | 2026-01-01 | Regeneron Pharma | Methods and compositions for administering therapeutic protein |
| MA52626A (fr) | 2018-05-17 | 2021-03-24 | Regeneron Pharma | Anticorps anti-cd63, conjugués et leurs utilisations |
| US20220403001A1 (en) | 2018-06-12 | 2022-12-22 | Obsidian Therapeutics, Inc. | Pde5 derived regulatory constructs and methods of use in immunotherapy |
| WO2020077114A2 (en) | 2018-10-10 | 2020-04-16 | Amicus Therapeutics, Inc. | Disulfide bond stabilized polypeptide compositions and methods of use |
| EP3870600A1 (en) | 2018-10-24 | 2021-09-01 | Obsidian Therapeutics, Inc. | Er tunable protein regulation |
| CN113454227B (zh) * | 2018-12-19 | 2025-05-23 | 维萨梅布有限公司 | 编码蛋白质的rna |
| MX2021010840A (es) | 2019-03-08 | 2022-01-19 | Obsidian Therapeutics Inc | Composiciones de anhidrasa carbónica 2 (ca2) humana y métodos de regulación ajustable. |
| US20220267398A1 (en) | 2019-06-12 | 2022-08-25 | Obsidian Therapeutics, Inc. | Ca2 compositions and methods for tunable regulation |
| KR20220044266A (ko) | 2019-06-12 | 2022-04-07 | 옵시디안 테라퓨틱스, 인크. | 조정 가능한 조절을 위한 ca2 조성물 및 방법 |
| WO2021046451A1 (en) | 2019-09-06 | 2021-03-11 | Obsidian Therapeutics, Inc. | Compositions and methods for dhfr tunable protein regulation |
| CN112342247B (zh) * | 2020-11-10 | 2022-03-11 | 江苏科技大学 | 一种提高家蚕细胞表达外源蛋白分泌率的方法 |
| KR20230128001A (ko) | 2020-12-01 | 2023-09-01 | 더 트러스티스 오브 더 유니버시티 오브 펜실베니아 | 엔젤만 증후군의 치료를 위한 조성물 및 이의 용도 |
| WO2023086939A1 (en) | 2021-11-12 | 2023-05-19 | Amicus Therapeutics, Inc. | Compositions and methods for treating mucopolysaccharidosis iiia |
| WO2025264978A2 (en) | 2024-06-20 | 2025-12-26 | Amicus Therapeutics, Inc. | Recombinant alpha-galactosidase a proteins and gene therapy |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2002530426A (ja) * | 1998-11-24 | 2002-09-17 | ブリストル−マイヤーズ スクイブ カンパニー | ７０ｋＤ熱ショック蛋白による化合物の細胞内標的輸送 |
| JP2007528212A (ja) * | 2003-11-06 | 2007-10-11 | ジェネンコー・インターナショナル・インク | 糸状菌におけるプロテアーゼ抑制剤及びその変異体の発現 |
| JP2009533364A (ja) * | 2006-04-11 | 2009-09-17 | ツェー・エス・エル・ベーリング・ゲー・エム・ベー・ハー | 治療用ポリペプチドのインビボでの回収を増大させる方法 |
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Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2002530426A (ja) * | 1998-11-24 | 2002-09-17 | ブリストル−マイヤーズ スクイブ カンパニー | ７０ｋＤ熱ショック蛋白による化合物の細胞内標的輸送 |
| JP2007528212A (ja) * | 2003-11-06 | 2007-10-11 | ジェネンコー・インターナショナル・インク | 糸状菌におけるプロテアーゼ抑制剤及びその変異体の発現 |
| JP2009533364A (ja) * | 2006-04-11 | 2009-09-17 | ツェー・エス・エル・ベーリング・ゲー・エム・ベー・ハー | 治療用ポリペプチドのインビボでの回収を増大させる方法 |
Non-Patent Citations (3)
| Title |
|---|
| JPN6015035069; 'Ｄｅｆｉｎｉｔｉｏｎ： Ｆｕｌｌ＝７８ ｋＤａ ｇｌｕｃｏｓｅ-ｒｅｇｕｌａｔｅｄ ｐｒｏｔｅｉｎ， ０５-ＯＣＴ-２０１０ ｕｐｌｏａｄｅｄ， ［ｒｅｔｒｉｅｖｅｄ ｏｎ ２０１５-０８-１９］' Ｄａｔａｂａｓｅ ＵｎｉＰｒｏｔ ［ｏｎｌｉｎｅ］， Ａｃｃｅｓｓｉｎ Ｎｏ．Ｑ３Ｓ４Ｔ７ * |
| JPN6015035071; Ｐｒｏｔｅｉｎ Ｅｘｐｒ． Ｐｕｒｉｆ． Ｖｏｌ．５６， Ｎｏ．１, 2007, ｐｐ．８-１９ * |
| JPN6015035073; Ａｐｐｌ． Ｍｉｃｒｏｂｉｏｌ． Ｂｉｏｔｅｃｈｎｏｌ． Ｖｏｌ．５０, 1998, ｐｐ．４４７-４５４ * |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2021505135A (ja) * | 2017-11-30 | 2021-02-18 | アミカス セラピューティックス インコーポレイテッド | Ｃｄｋｌ５発現変異体及びｃｄｋｌ５融合タンパク質 |
| JP2021521851A (ja) * | 2018-04-30 | 2021-08-30 | アミカス セラピューティックス インコーポレイテッド | 遺伝子治療構築物及び使用方法 |
| JP7749322B2 (ja) | 2018-04-30 | 2025-10-06 | アミカス セラピューティックス インコーポレイテッド | 遺伝子治療構築物及び使用方法 |
| JP2022530833A (ja) * | 2019-04-30 | 2022-07-01 | ザ・トラステイーズ・オブ・ザ・ユニバーシテイ・オブ・ペンシルベニア | ポンペ病の治療のために有用な組成物 |
| JP7585233B2 (ja) | 2019-04-30 | 2024-11-18 | ザ・トラステイーズ・オブ・ザ・ユニバーシテイ・オブ・ペンシルベニア | ポンペ病の治療のために有用な組成物 |
Also Published As
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| EP3461905A1 (en) | 2019-04-03 |
| PT2643468T (pt) | 2018-10-11 |
| US20140045216A1 (en) | 2014-02-13 |
| SMT201800466T1 (it) | 2018-11-09 |
| KR20190060888A (ko) | 2019-06-03 |
| RS57601B1 (sr) | 2018-11-30 |
| BR112013012671A2 (pt) | 2016-10-11 |
| EP2643468A4 (en) | 2014-12-24 |
| LT2643468T (lt) | 2018-09-10 |
| WO2012071422A2 (en) | 2012-05-31 |
| DK3461905T3 (da) | 2020-11-02 |
| KR20130121878A (ko) | 2013-11-06 |
| SI2643468T1 (sl) | 2018-10-30 |
| ES2687415T3 (es) | 2018-10-25 |
| EP2643468B1 (en) | 2018-07-04 |
| HUE039070T2 (hu) | 2018-12-28 |
| PL2643468T3 (pl) | 2018-11-30 |
| CA2818689A1 (en) | 2012-05-31 |
| DK2643468T3 (en) | 2018-09-24 |
| EP2643468A2 (en) | 2013-10-02 |
| HRP20181315T1 (hr) | 2018-10-19 |
| US9279007B2 (en) | 2016-03-08 |
| KR101984318B1 (ko) | 2019-05-31 |
| CN103328649A (zh) | 2013-09-25 |
| EP3461905B1 (en) | 2020-08-05 |
| CN103328649B (zh) | 2016-06-22 |
| CA2818689C (en) | 2021-09-21 |
| WO2012071422A3 (en) | 2012-08-02 |
| BR112013012671B1 (pt) | 2022-03-03 |
| ES2829199T3 (es) | 2021-05-31 |
| CY1121049T1 (el) | 2019-12-11 |
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