Polypeptide的問題，透過圖書和論文來找解法和答案更準確安心。 我們找到下列問答集和資訊懶人包

Hsf1 and Molecular Chaperones in Biology and Disease

為了解決Polypeptide的問題，作者 這樣論述：

Protein homeostasis, or "Proteostasis", lies at the heart of human health and disease. From the folding of single polypeptide chains into functional proteins, to the regulation of intracellular signaling pathways, to the secreted signals that coordinate cells in tissues and throughout the body, the

proteostasis network operates to support cell health and physiological fitness. However, cancer cells also hijack the proteostasis network and many of these same processes to sustain the growth and spread of tumors.The chapters in this book are written by world experts in the many facets of the prot

eostasis network. They describe cutting-edge insights into the structure and function of the major chaperone and degradation systems in healthy cells and how these systems are co-opted in cancer cells and the cells of the tumor microenvironment. The chapters also cover therapeutic interventions such

as the FDA-approved proteasome inhibitors Velcade and Krypolis as well as other therapies currently under clinical investigation to disarm the ability of the proteostasis network to support malignancy. This compendium is the first of its kind and aims to serve as a reference manual for active inves

tigators and a primer for newcomers to the field.This book is dedicated to the memory of Susan Lindquist, a pioneer of the proteostasis field and a champion of the power of basic scientific inquiry to unlock the mechanisms of human disease. Dr. Ruth Scherz-Shouval is the daughter of Prof. Avigdor

Scherz, a pioneer in the field of photo-dynamic therapy in the Department of Plant and Environmental Sciences at the Weizmann Institute. She earned a BSc in the life sciences with honors at the Hebrew University of Jerusalem in 2002 and a PhD in biological chemistry at the Weizmann Institute of Scie

nce in 2008 (with Prof. Zvulun Elazar). She conducted postdoctoral research in Prof. Moshe Oren’s laboratory at the Weizmann Institute and at the Whitehead Institute for Biomedical Research at the Massachusetts Institute of Technology (MIT), and will join the Weizmann Institute’s Department of Biolo

gical Chemistry in October 2015.Dr. Marc Mendillo is an Assistant Professor of Biochemistry and Molecular Genetics at the Northwestern University. His PhD was obtained from the University Of California-San Diego in Biomedical Sciences followed by a Postdoctoral Fellowship at the Ludwig Institute for

Cancer Research in San Diego and another at the Whitehead Institute. Currently, he runs a lab in the Department of Biochemistry and Molecular Genetics and the Robert H. Lurie Comprehensive Cancer Center.Dr. David Pincus is a fellow at the Whitehead Institute where he tries to reveal the underlying

mechanisms cells employ to maintain homeostasis in inherently fluctuating environments.

Polypeptide進入發燒排行的影片

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Polypeptide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。

Prion Diseases

為了解決Polypeptide的問題，作者Prusiner, Stanley B. (EDT) 這樣論述：

Diseases such as Creutzfeldt-Jakob disease and kuru develop when PrP proteins form prions by misfolding, clumping together, and spreading from cell to cell. Over the past decade, a number of proteins have been reported to possess the characteristics of PrP prions. A growing collection of disorders h

as been found to be caused by prions; some of these prion diseases include such devastating illnesses as Alzheimer's and Parkinson's and possibly type 2 diabetes. Written and edited by experts in the field, this collection from Cold Spring Harbor Perspectives in Medicine covers the progress that has

recently been made in our understanding of the pathophysiology of prion diseases, as well as ongoing efforts to develop effective therapeutics. The contributors discuss how proteins such as tau, islet amyloid polypeptide, and alpha-synuclein adopt alternative shapes that lead them to aggregate, res

ulting in cellular degeneration. Therapies for human and animal diseases caused by prions are also covered. This volume is therefore useful for all biomedical scientists and physicians wishing to understand and treat this expanding group of devastating disorders.

Nucleus Near-Infrared (nNIR) Irradiation of Single A549 Cells Induces DNA Damage and Activates EGFR Leading to Mitochondrial Fission

為了解決Polypeptide的問題，作者MOMOH GBETUWA 這樣論述：

Abstract Background: There has been great interest in identifying the biological substrate for light-cell interaction and their relations to cancer treatment. In our study, a single cell nuclear NIR (nNIR) and cytosol exposed NIR has been used to determine for the first-time mitochondria fragmentat

ion count (MFC) to compare NIR effect on subcellular cells. Near infra-red (NIR) possesses less light scattering and absorption in biological tissues it has a biological window that bears a very small photodamage and thus possesses a deep tissue penetration depth. Aim: To evaluate near-infrared (NIR

) laser focused into the nucleus (nNIR) or cytoplasm (cNIR) of a single living cell by a high numerical aperture condenser to dissect the novel role of cell nucleus in mediating NIR effects on mitochondrial dynamics of A549 non-small cell lung cancer cells.Materials and Methods: Cultured 150 single

cell of A549 nucleus and cytosol were incubated with 0.3 μM mitotracker green for 30 min washed with PBS, imaged control cell then treated with 224.02 J/cm2 NIR for 10 s and cells imaged at different time points of 1, 5, 10, 15 and 20 min. A549 cells were treated with conjugated 100 nM FND-EGF and i

ncubated with PD153035, caffeine and cetuximab for 1 h, and imaged cells. Results: Our analysis showed nNIR, but not cNIR, triggered mitochondrial fission in 10 minutes. On the contrast, the fission/fusion balance of mitochondria directly exposed to cNIR does not change. While the same phenomenon is

also triggered by single molecular interactions between epidermal growth factor (EGF) and its receptor EGFR, pharmacological studies with cetuximab, PD153035 and caffeine suggest EGF signaling crosstalk to DNA damaging response to mediate rapid mitochondrial fission as a result of nNIR irradiation.

These results suggest that nuclear DNA integrity is a novel biological target for cellular response to NIR. Conclusions: These results suggest that nuclear DNA integrity is a novel biological target for cellular response to NIR. Keywords: Keywords: near infrared (NIR), epidermal growth factor recep

tor (EGFR), mitochondrial fragmentation count (MFC), mitochondrial dynamic, cetuximab, caffeine.