JP6613312B2 - 膵臓癌を処置するためのペプチドをベースとする方法 - Google Patents
膵臓癌を処置するためのペプチドをベースとする方法 Download PDFInfo
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- JP6613312B2 JP6613312B2 JP2017540549A JP2017540549A JP6613312B2 JP 6613312 B2 JP6613312 B2 JP 6613312B2 JP 2017540549 A JP2017540549 A JP 2017540549A JP 2017540549 A JP2017540549 A JP 2017540549A JP 6613312 B2 JP6613312 B2 JP 6613312B2
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| ES3010559T3 (en) | 2017-02-28 | 2025-04-03 | Endocyte Inc | Compositions and methods for car t cell therapy |
| JP2020517259A (ja) | 2017-04-19 | 2020-06-18 | ボード・オブ・リージエンツ，ザ・ユニバーシテイ・オブ・テキサス・システム | 操作された抗原受容体を発現する免疫細胞 |
| JP7051898B2 (ja) | 2017-04-24 | 2022-04-11 | ナントセル，インコーポレイテッド | 標的型ネオエピトープベクター及びそのための方法 |
| US20190224275A1 (en) | 2017-05-12 | 2019-07-25 | Aurinia Pharmaceuticals Inc. | Protocol for treatment of lupus nephritis |
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| TW202000229A (zh) | 2018-02-23 | 2020-01-01 | 美商安德賽特公司 | Car t細胞療法之順序方法 |
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| US20220143130A1 (en) * | 2018-08-29 | 2022-05-12 | Riptide Bioscience, Inc. | Peptides Having Immunomodulatory Properties |
| US10413584B1 (en) | 2018-08-29 | 2019-09-17 | Riptide Bioscience, Inc. | Peptides having immunomodulatory properties |
| WO2020046297A2 (en) * | 2018-08-29 | 2020-03-05 | Riptide Bioscience, Inc. | Peptides having immunomodulatory properties |
| CN110960679A (zh) * | 2018-09-28 | 2020-04-07 | 江苏康缘药业股份有限公司 | 一种抗肿瘤的药物组合物及其应用 |
| US20220053773A1 (en) * | 2018-10-01 | 2022-02-24 | Innate Immunity LLC | Compositions and methods for the treatment of pathogenic infections in plants |
| US20200102356A1 (en) * | 2018-10-01 | 2020-04-02 | NMC Inc. | Compositions and Methods for the Treatment of Huanglongbing (HLB) aka Citrus Greening in Citrus Plants |
| US12331320B2 (en) | 2018-10-10 | 2025-06-17 | The Research Foundation For The State University Of New York | Genome edited cancer cell vaccines |
| US10548944B1 (en) | 2018-10-19 | 2020-02-04 | Riptide Bioscience, Inc. | Antimicrobial peptides and methods of using the same |
| WO2020176478A1 (en) | 2019-02-25 | 2020-09-03 | The University Of Chicago | Methods and compositions for treating inflammatory and autoimmune conditions with ecm-affinity peptides linked to anti-inflammatory agents |
| CA3134420A1 (en) * | 2019-04-12 | 2020-10-15 | Riptide Bioscience, Inc. | Methods for modulating macrophage activity |
| JP7606471B2 (ja) | 2019-05-22 | 2024-12-25 | レイドス， インコーポレイテッド | Ｌａｇ３結合ペプチド |
| US20220125866A1 (en) * | 2019-06-28 | 2022-04-28 | Nantcell, Inc | Pharmaceutical compositions to enhance phagocytosis without inflammation |
| CN115768757B (zh) | 2019-12-19 | 2025-07-11 | 美利坚合众国,由健康及人类服务部部长代表 | Cd206调节剂及其用途和制备方法 |
| CN111116713B (zh) * | 2020-01-07 | 2023-06-23 | 郑州大学 | Sirpa蛋白亲和环肽及其应用 |
| EP4100428A4 (en) | 2020-02-04 | 2024-03-06 | Seattle Children's Hospital (DBA Seattle Children's Research Institute) | CHIMERIC ANTI-DINITROPHENOL ANTIGEN RECEPTORS |
| AU2021246017A1 (en) * | 2020-03-31 | 2022-11-10 | Innate Immunity LLC | Recombinant peptide to treat fire blight |
| US11338040B2 (en) | 2020-06-04 | 2022-05-24 | Leidos, Inc. | Immunomodulatory compounds |
| WO2022034523A1 (en) | 2020-08-13 | 2022-02-17 | Immunitybio, Inc. | Phagocytosis-inducing compounds and methods of use |
| WO2022081426A1 (en) | 2020-10-12 | 2022-04-21 | Leidos, Inc. | Immunomodulatory peptides |
| EP4365187A4 (en) * | 2021-06-28 | 2025-11-19 | Univ Korea Res & Bus Found | Peptide with anticancer activity and its use |
| CN115607674B (zh) * | 2021-07-15 | 2023-09-19 | 深圳开悦生命科技有限公司 | Rna解旋酶dhx33抑制剂在制备用于治疗胰腺癌的药物中的应用 |
| WO2023080578A1 (ko) * | 2021-11-05 | 2023-05-11 | 주식회사 레메디 | 상처 치료 및 항염증 활성을 가지는 펩타이드 및 이의 용도 |
| WO2023097111A2 (en) * | 2021-11-29 | 2023-06-01 | Riptide Bioscience, Inc. | Methods and compositions for treating calcinosis associated conditions |
| WO2023111695A1 (en) * | 2021-12-16 | 2023-06-22 | Ramakrishna Reddy Isanaka | A stable anti-angiogenic and anti-inflammatory pharmaceutical formulation and pharmaceutical combination for treatment and prevention of psoriasis |
| KR102920640B1 (ko) | 2022-03-11 | 2026-01-29 | 국립순천대학교산학협력단 | 항진균 활성을 나타내는 펩타이드 및 이를 유효성분으로 포함하는 항진균용 조성물 |
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| CN115838395A (zh) * | 2022-11-15 | 2023-03-24 | 西北农林科技大学 | 具有可溶性环氧化物水解酶抑制作用的活性肽及其应用 |
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Family Cites Families (27)
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