標(biāo)題: Titlebook: HSF1 and Molecular Chaperones in Biology and Cancer; Marc Laurence Mendillo,David Pincus,Ruth Scherz-Sh Book 2020 Springer Nature Switzerl [打印本頁] 作者: 縮寫 時(shí)間: 2025-3-21 17:59
書目名稱HSF1 and Molecular Chaperones in Biology and Cancer影響因子(影響力)
書目名稱HSF1 and Molecular Chaperones in Biology and Cancer影響因子(影響力)學(xué)科排名
書目名稱HSF1 and Molecular Chaperones in Biology and Cancer網(wǎng)絡(luò)公開度
書目名稱HSF1 and Molecular Chaperones in Biology and Cancer網(wǎng)絡(luò)公開度學(xué)科排名
書目名稱HSF1 and Molecular Chaperones in Biology and Cancer被引頻次
書目名稱HSF1 and Molecular Chaperones in Biology and Cancer被引頻次學(xué)科排名
書目名稱HSF1 and Molecular Chaperones in Biology and Cancer年度引用
書目名稱HSF1 and Molecular Chaperones in Biology and Cancer年度引用學(xué)科排名
書目名稱HSF1 and Molecular Chaperones in Biology and Cancer讀者反饋
書目名稱HSF1 and Molecular Chaperones in Biology and Cancer讀者反饋學(xué)科排名
作者: 細(xì)胞學(xué) 時(shí)間: 2025-3-21 21:09 作者: ASSAY 時(shí)間: 2025-3-22 02:31 作者: garrulous 時(shí)間: 2025-3-22 07:34
Book 2020proteins, 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 o作者: 改進(jìn) 時(shí)間: 2025-3-22 12:02
https://doi.org/10.1007/978-1-349-13445-8the various members of this network. In this chapter we describe the emerging working principles of the Hsp70 machine and its co-chaperones, and highlight how mechanistic aspects of this network are tied to distinct protein folding functions.作者: lambaste 時(shí)間: 2025-3-22 15:09
https://doi.org/10.1007/978-3-031-05017-6 from Hsf1, releasing Hsf1 to induce the full arsenal of cellular chaperones to restore protein homeostasis. In metazoans, this cell-autonomous feedback loop is modulated by the microenvironment and neuronal cues to enable tissue-level and organism-wide coordination.作者: 名字 時(shí)間: 2025-3-22 21:01
https://doi.org/10.1057/9780230273979ancer-cell-autonomous activity of chaperones in human patients and mouse models of cancer, discuss the mechanisms by which this non-cell-autonomous activity is mediated and provide an evolutionary perspective on the basis of this phenomenon.作者: eulogize 時(shí)間: 2025-3-22 21:23 作者: 正式通知 時(shí)間: 2025-3-23 03:35 作者: 無底 時(shí)間: 2025-3-23 06:24 作者: STEER 時(shí)間: 2025-3-23 12:15 作者: 走路左晃右晃 時(shí)間: 2025-3-23 16:38 作者: 小卒 時(shí)間: 2025-3-23 18:15
The Industrial Revolution: A Compendiumequatorial domain, which contains all the inter-ring contacts, most of the intra-ring contacts and the ATP binding site, whose binding and hydrolysis triggers the conformational changes that take place during the functional cycle. All chaperonins display an open substrate-receptive conformation, whe作者: DEMN 時(shí)間: 2025-3-23 23:47 作者: 約會(huì) 時(shí)間: 2025-3-24 04:44 作者: 傳授知識 時(shí)間: 2025-3-24 09:30 作者: BACLE 時(shí)間: 2025-3-24 14:28 作者: 內(nèi)閣 時(shí)間: 2025-3-24 15:38 作者: 高原 時(shí)間: 2025-3-24 19:39 作者: 一小塊 時(shí)間: 2025-3-25 00:23
Challenging Proteostasis: Role of the Chaperone Network to Control Aggregation-Prone Proteins in Humas the undesirable effect of promoting cellular survival and tumor growth by stabilizing mutant oncoproteins. In both situations, physiological levels of molecular chaperones eventually become functionally compromised by the persistence of misfolded substrates, leading to a decline in global protein作者: pacific 時(shí)間: 2025-3-25 05:33
Chaperome Networks?– Redundancy and Implications for Cancer Treatmente where no redundant pathways can be deployed, and is a state of vulnerability, amenable for chaperome therapy. We conclude by proposing a change in how we discover and implement chaperome inhibitor strategies, and suggest an approach to chaperome therapy where the properties of chaperome networks, 作者: 使成核 時(shí)間: 2025-3-25 11:29 作者: 慢跑鞋 時(shí)間: 2025-3-25 14:47
Lessons Learned from Proteasome Inhibitors, the Paradigm for Targeting Protein Homeostasis in Cancersurprisingly?complex. Here, we attempt to draw lessons from experience with proteasome inhibitors that may be relevant for other compounds targeting proteostasis in cancer, as well as extending the reach of proteasome inhibitors beyond blood cancers.作者: Vulvodynia 時(shí)間: 2025-3-25 15:54 作者: Glucose 時(shí)間: 2025-3-25 20:41 作者: Inflamed 時(shí)間: 2025-3-26 03:47
Correction to: Reflections and Outlook on Targeting HSP90, HSP70 and HSF1 in Cancer: A Personal Per作者: upstart 時(shí)間: 2025-3-26 05:35 作者: 脫離 時(shí)間: 2025-3-26 11:56
0065-2598 es 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 inv978-3-030-40206-8978-3-030-40204-4Series ISSN 0065-2598 Series E-ISSN 2214-8019 作者: defibrillator 時(shí)間: 2025-3-26 12:48 作者: Cardiac 時(shí)間: 2025-3-26 17:59
The TRiC/CCT Chaperonin and Its Role in Uncontrolled Proliferationerted manner to regulate and transfer the genetic material to daughter cells. CCT (chaperonin containing TCP-1, also known as TRiC) is a molecular machine that forms a high molecular weight complex (1000?KDa). CCT is emerging as a key molecule during mitosis due to its essential role in the folding 作者: 親屬 時(shí)間: 2025-3-26 22:15 作者: Intuitive 時(shí)間: 2025-3-27 03:19
Challenging Proteostasis: Role of the Chaperone Network to Control Aggregation-Prone Proteins in Hume Proteostasis Network (PN) are molecular chaperones that serve widely in protein biogenesis under physiological conditions, and prevent protein misfolding and aggregation enhanced by conditions of cellular stress. For Alzheimer’s, Parkinson’s, Huntington’s diseases and ALS, multiple classes of mole作者: 不要嚴(yán)酷 時(shí)間: 2025-3-27 09:16 作者: 確認(rèn) 時(shí)間: 2025-3-27 10:26
Chaperome Networks?– Redundancy and Implications for Cancer Treatment organisms have paved the road to how we currently understand the complex organization of this large family into protein networks. The goal of this chapter is to provide an overview of chaperome networks in cancer cells, with a focus on two cellular states defined by chaperome network organization. 作者: Armada 時(shí)間: 2025-3-27 13:56 作者: Obstreperous 時(shí)間: 2025-3-27 19:41
The Impact of the ER Unfolded Protein Response on Cancer Initiation and Progression: Therapeutic Imphe unfolded protein response (UPR). This adaptive response is mediated by the transmembrane signal transducers IRE1, PERK, and ATF6 to decide cell fate of recovery or death. In malignant cells, UPR signalling may be required to maintain ER homeostasis and survival in the tumor microenvironment chara作者: BAIT 時(shí)間: 2025-3-28 01:27
The Right Tool for the Job: An Overview of Hsp90 Inhibitorsns as well as the refolding of denatured proteins. While there are several classes of molecular chaperones in the cell, this chapter will focus solely on the small molecule modulation of Hsp90, the 90?kDa heat shock protein. Hsp90 is not only responsible for folding nascent proteins, but it also reg作者: MENT 時(shí)間: 2025-3-28 03:15
Lessons Learned from Proteasome Inhibitors, the Paradigm for Targeting Protein Homeostasis in Cancericult to bring to clinical practice, with one major exception: proteasome inhibition. These small molecules have dramatically transformed outcomes for patients with the blood cancer multiple myeloma. However, these agents have failed to make an impact in more common solid tumors. Major questions rem作者: Mast-Cell 時(shí)間: 2025-3-28 10:02 作者: 四溢 時(shí)間: 2025-3-28 11:42 作者: 神秘 時(shí)間: 2025-3-28 14:45 作者: larder 時(shí)間: 2025-3-28 19:25 作者: CRASS 時(shí)間: 2025-3-29 01:11
https://doi.org/10.1007/978-1-349-04524-2e Proteostasis Network (PN) are molecular chaperones that serve widely in protein biogenesis under physiological conditions, and prevent protein misfolding and aggregation enhanced by conditions of cellular stress. For Alzheimer’s, Parkinson’s, Huntington’s diseases and ALS, multiple classes of mole作者: landmark 時(shí)間: 2025-3-29 07:06 作者: FER 時(shí)間: 2025-3-29 11:18
https://doi.org/10.1007/978-1-349-14942-1 organisms have paved the road to how we currently understand the complex organization of this large family into protein networks. The goal of this chapter is to provide an overview of chaperome networks in cancer cells, with a focus on two cellular states defined by chaperome network organization. 作者: 感情脆弱 時(shí)間: 2025-3-29 14:25
https://doi.org/10.1057/9780230273979 and barriers imposed by a hostile microenvironment. To achieve this, cancer cells recruit and rewire cells in their microenvironment to become pro-tumorigenic. We propose that chaperones are vital players in this process, and that activation of stress responses helps tumors adapt and evolve into ag作者: 放逐某人 時(shí)間: 2025-3-29 16:17
https://doi.org/10.1057/978-1-137-36238-4he unfolded protein response (UPR). This adaptive response is mediated by the transmembrane signal transducers IRE1, PERK, and ATF6 to decide cell fate of recovery or death. In malignant cells, UPR signalling may be required to maintain ER homeostasis and survival in the tumor microenvironment chara作者: circuit 時(shí)間: 2025-3-29 20:45 作者: Vasoconstrictor 時(shí)間: 2025-3-30 01:25
The Inexorable Evolution of Financialisationicult to bring to clinical practice, with one major exception: proteasome inhibition. These small molecules have dramatically transformed outcomes for patients with the blood cancer multiple myeloma. However, these agents have failed to make an impact in more common solid tumors. Major questions rem作者: 悄悄移動(dòng) 時(shí)間: 2025-3-30 07:55
