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Titlebook: Biobetters; Protein Engineering Amy Rosenberg,Barthélemy Demeule Book 2015 American Association of Pharmaceutical Scientists 2015 drug tar

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發(fā)表于 2025-3-21 18:15:35 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
期刊全稱Biobetters
期刊簡(jiǎn)稱Protein Engineering
影響因子2023Amy Rosenberg,Barthélemy Demeule
視頻videohttp://file.papertrans.cn/187/186527/186527.mp4
發(fā)行地址Essential reading for companies and research institutions working on the development of biopharmaceuticals.Examines two product classes - therapeutic enzymes and monoclonal antibodies - as examples of
學(xué)科分類AAPS Advances in the Pharmaceutical Sciences Series
圖書(shū)封面Titlebook: Biobetters; Protein Engineering  Amy Rosenberg,Barthélemy Demeule Book 2015 American Association of Pharmaceutical Scientists 2015 drug tar
影響因子“Biobetters: Protein Engineering to Approach the Curative” discusses the optimization of protein therapeutic products for treatment of human diseases. It is based on the fact that though numerous important therapeutic protein products have been developed for life threatening and chronic diseases that possess acceptable safety and efficacy profiles, these products have generally not been reexamined and modified for an improved clinical performance, with enhancements both to safety and efficacy profiles. Advances in protein engineering, coupled with greatly enhanced understanding of critical product quality attributes for efficacy and safety, make it possible to optimize predecessor products for clinical performance, thereby enhancing patient quality of life and with the potential for great savings in health care costs. Yet despite such knowledge, there is little movement towards such modifications. This book examines engineering protein therapeutic products such that they exhibit an optimal, not just an adequate, clinical performance profile.?Two product classes, therapeutic enzymes for lysosomal storage diseases (enzyme replacement therapies, ERT) and monoclonal antibodies (mAbs),
Pindex Book 2015
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https://doi.org/10.1007/978-94-009-2007-1ure that can mediate biological response upon specifically binding to an antigen. This chapter introduces readers to the chemical structure of antibodies, with specific focus on the structure of immunoglobulin G (IgG). The chapter also highlights functionally important IgG domains and their susceptibility to chemical degradation.
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978-1-4939-4994-6American Association of Pharmaceutical Scientists 2015
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Studies in History and Philosophy of Sciencessibility that the health of patients might be improved by the administration of purified exogenous enzyme. Glucocerebrosidase for this investigation was originally obtained from human placental tissue. Intravenous administration of this enzyme to patients with Gaucher disease reduced the amount of
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https://doi.org/10.1007/978-3-031-51258-2 MPS IV, MPS VI, Gaucher disease, Fabry disease, and Pompe disease. The therapeutic enzyme replacement effectively lowers substrate accumulation and has dramatically improved lifespan, increased overall quality of life, and diminished the extent of organ involvement in these conditions. Despite this
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