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Titlebook: Amyloid Proteins; Einar M. Sigurdsson Book 20051st edition Humana Press 2005 ELISA.Termination.Vivo.biology.electron microscopy.molecular

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發(fā)表于 2025-3-21 17:32:14 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
期刊全稱Amyloid Proteins
影響因子2023Einar M. Sigurdsson
視頻videohttp://file.papertrans.cn/155/154779/154779.mp4
發(fā)行地址Includes supplementary material:
學(xué)科分類Methods in Molecular Biology
圖書(shū)封面Titlebook: Amyloid Proteins;  Einar M. Sigurdsson Book 20051st edition Humana Press 2005 ELISA.Termination.Vivo.biology.electron microscopy.molecular
影響因子A proven collection of readily reproducible techniques for studying amyloid proteins andtheir involvement in the etiology, pathogenesis, diagnosis, and therapy of amyloid diseases. The contributors provide methods for the preparation of amyloid and its precursors (oligomers and protofibrils), in vitro assays and analytical techniques for their study, and cell culture models and assays for the production of amyloid proteins. Additional chapters present readily reproducible techniques for amyloid extraction from tissue, its detection in vitro and in vivo, as well as nontransgenic methods for developing amyloid mouse models. The protocols follow the successful Methods in Molecular Biology? series format, each offering step-by-step laboratory instructions, an introduction outlining the principle behind the technique, lists of the necessary equipment and reagents, and tips on troubleshooting and avoiding known pitfalls.
Pindex Book 20051st edition
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書(shū)目名稱Amyloid Proteins影響因子(影響力)




書(shū)目名稱Amyloid Proteins影響因子(影響力)學(xué)科排名




書(shū)目名稱Amyloid Proteins網(wǎng)絡(luò)公開(kāi)度




書(shū)目名稱Amyloid Proteins網(wǎng)絡(luò)公開(kāi)度學(xué)科排名




書(shū)目名稱Amyloid Proteins被引頻次




書(shū)目名稱Amyloid Proteins被引頻次學(xué)科排名




書(shū)目名稱Amyloid Proteins年度引用




書(shū)目名稱Amyloid Proteins年度引用學(xué)科排名




書(shū)目名稱Amyloid Proteins讀者反饋




書(shū)目名稱Amyloid Proteins讀者反饋學(xué)科排名




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,Wie man über ein Problem nachdenken soll,tly produces covalent bonds among unmodified polypeptide chains through . generation of peptide free radicals. PICUP provides a snapshot of the native oligomerization state of proteins and can be used for assembly state analysis of a wide variety of peptides and proteins.
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Wie unterscheiden sich Bildungskonzepte? to PHFs. These include: a purification protocol for recombinantly expressed tau; a general method for the polyanion induced polymerization of tau to PHFs; the quantitation of PHFs by a fluorescence-based assay; the imaging and verification of PHFs by negative stain transmission electron microscopy.
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https://doi.org/10.1007/3-540-44903-5 easy source of robust cells, and secondly, using brain tissue that provides the proper cerebral VSMCs, but is more problematic to work with. Finally the maintenance, preservation, and characterization of the isolated VSMCs are described.
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