Interact的問題，透過圖書和論文來找解法和答案更準確安心。 我們找到下列包括價格和評價等資訊懶人包

Medical Humanities and Disability Studies: Beyond Disciplines

為了解決Interact的問題，作者Murray, Stuart 這樣論述：

Medical Humanities and Disability Studies are two critical fields at the cutting edge of innovative interdisciplinary work in the Arts and Humanities, but to date there has been no book length study of the (occasionally vexed) relationship between the two. This book addresses that and presents a

series of provocative arguments about how the two disciplines interact, the forms their critical practice take, and what each can learn from the other. Although the two disciplines have emerged from different critical heritages they share many features, from identifying processes of exclusion and ch

ampioning user participation to a commitment to inter- and cross-disciplinary methodologies. But the subjects differ in other ways: medical humanities has evolved from considerations of the place of humanities in the development of medical education, while disability studies has its origins in right

s- and identity-based discourses. While both are part of the ’critical turn’ that has marked new interdisciplinary work in the last 15 years, each has developed through different theoretical contexts and often brings different perspectives to its subject material. Written in an accessible manner and

aimed at a wide audience in both fields and the new humanities more widely, it asserts that both subject areas need to evaluate their recent successes and challenge core assumptions if they are to remain critically relevant in the evolving study of social and cultural experiences of health.

Interact進入發燒排行的影片

研究 Cep170 不同的分布位置以及其對神經型態發生之影響

為了解決Interact的問題，作者陳芃慈 這樣論述：

微管是神經細胞中不可缺少的結構，會參與神經細胞發育過程中的每一步驟，與微管有相互作用的蛋白質稱為微管相關蛋白 (MAP)，許多 MAP 會藉由調節微管影響神經細胞的發育。運用質譜儀定量且定序比較分化為神經細胞前後的MAP，發現 Cep170 富含於神經細胞的微管。 Cep170 為一具有 Forkhead associated (FHA) 功能域的中心體相關蛋白，位於具有絲分裂能力細胞的中心體遠端附屬物 (subdistal appendage)， Cep170 被發現和人腦發育異常相關疾病有關，例如小頭畸形和平腦症，如此證明 Cep170 在中樞神經系統的發育中有著至關重要的作用。實驗室發

現 Cep170 大量表達會促進神經纖維生長，然而由於先前抑制 Cep170 的效率較差，無法觀察到抑制 Cep170 後對於神經細胞的影響；另外還觀察到 Cep170 在神經細胞中有多種不同的定位：細胞本體中形成一個點、沿著神經纖維的點狀分布、在最長的神經纖維的尾端含量上升，但是這些不同位置在神經細胞中的作用仍然未知。在此研究中，我們成功抑制神經細胞內的 Cep170 ；此外，我們依照功能域設計不同的 Cep170 截斷行突變來破壞神經細胞中特定的 Cep170 分布。我們發現沿著神經纖維的點狀分佈需要微管結合功能域和 FHA 功能域，而 Cep170 聚集於神經纖維尾端需要 FHA 功能域

；且微管穩定性會影響 Cep170 沿著神經纖維的點狀分佈，不穩定的微管會導致 Cep170 於近端神經纖維的點狀分布消失。

From Scientific Progress to Economic Growth: The Economics and the Economy of Science

為了解決Interact的問題，作者Witte, Frank 這樣論述：

The past few centuries have seen an enormous increase in living standards in many parts of the world and these economies have become more complex than ever before. At the same time, progress in science and technology has reached unprecedented heights, taking us far beyond the wildest dreams of a

few generations ago. Questions as to how science, technology and the economy interact are pertinent and important ones, whose partial answers require a view "from across the fence" between disciplines.This book provides an introduction to the vast and varied field of the economics of science. It is

a unique blend of an economic perspective on the way science works, what makes scientists tick, and a study of the impact of scientific and technological progress on economies and their growth. Whether it is about the speculative market of ideas or science and technology as engines of the economy, t

here is something here for economists, engineers and scientists alike.

潛藏危機：Musashi-1固有無序區域介導與神經退行性疾病相關蛋白之異常聚集

為了解決Interact的問題，作者杜岱芸 這樣論述：

蛋白質病變(proteopathy)是退行性疾病的常見原因，通過錯誤折疊的蛋白質異常聚集形成類澱粉沉積症(amyloidogenesis)，從而導致破壞組織內的穩態。尤其是，近期研究表明細胞內具有固有無序區域 (intrinsically disordered regions)的蛋白容易進行液-液相分離(liquid-liquid phase separation)，從而在細胞中組裝蛋白質凝聚層(coacervates)。在本研究中，我們假設具有固有無序區域的蛋白質受環境壓力影響，促進異常折疊甚至形成聚集體，這將進一步形成澱粉樣斑塊(amyloid plaques)並在組織內堆積，導致蛋白質

病變。我們主要探討不僅是RNA結合蛋白、也是幹性基因的Musashi-1，是否與具有豐富IDR的Musashi-1 C-末端區域相互作用以進行液-液相分離，最終形成澱粉樣原纖維(amyloid fibrils)。為了確認哪些序列更易於形成澱粉樣蛋白，因此對Musashi-1的C-末端進行了序列連續刪除來取得不同長度的片段。我們的研究結果表明Musashi-1 C-末端面對不同pH值和鹽濃度會影響液-液相分離狀態，包含改變蛋白質相分離的出現時間、形狀和大小，隨著時間的推移，Musashi-1 C-末端也可以形成澱粉樣蛋白原纖維。而當在氧化壓力下，它會在細胞內誘導組裝應激顆粒與不可逆的聚集體的形成

，另一方面，當細胞同時表達Musashi-1 C-末端和內源性TDP-43，Musashi-1 C-末端誘導TDP-43從細胞核錯誤定位到細胞質。此外，Musashi-1 C-末端促進磷酸化和泛素化TDP-43。總結來說，我們提出了關於Musashi-1與神經退行性疾病相關蛋白相互作用導致異常聚集的新見解，這些發現有助於提供解決退行性疾病的新思路。