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Titlebook: Cell Stress Proteins; Stuart K. Calderwood Book 2007 Springer-Verlag New York 2007 Antigen.Cell Stress.Chaperone.Immunity.Nucleotide.Prote

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發(fā)表于 2025-3-21 20:03:14 | 只看該作者 |倒序瀏覽 |閱讀模式
書目名稱Cell Stress Proteins
編輯Stuart K. Calderwood
視頻videohttp://file.papertrans.cn/223/222878/222878.mp4
概述Provides overview of the diversity and complex evolutionary history of cell stress proteins
叢書名稱Protein Reviews
圖書封面Titlebook: Cell Stress Proteins;  Stuart K. Calderwood Book 2007 Springer-Verlag New York 2007 Antigen.Cell Stress.Chaperone.Immunity.Nucleotide.Prote
描述Stressproteinssuchastheheatshockproteins(Hsp)andglucose-regulatedproteins (Grp) are front-line molecules in responses to cellular insult and play key roles in the viability of single cell organisms exposed to environmental stresses. However, the discovery of the roles of Hsp and Grp as molecular chaperones indicates much wider functions in the physiology of cells and organisms. It is now clear that some stress proteins are expressed constitutively and are key mediators of housekeeping protein folding in the day-to-day existence of the cell. The maturation of enzymes, transcriptionfactors,andcellsurfacereceptorsreliesonthesefunctionsofthestress proteins. In addition, the ability of stress proteins to manipulate the structures of target proteins has lent them cell regulatory properties over and above their role in folding the proteome and they play key roles in controlling signal transduction, cell death pathways and transcription. Recently, novel extracellular roles for the Hsp have also emerged as it has become apparent that the Hsp can escape from the cytoplasm of cells and play a signi?cant extracellular role in signaling to neighbor cells and in immunosurveiIlance. As might be e
出版日期Book 2007
關(guān)鍵詞Antigen; Cell Stress; Chaperone; Immunity; Nucleotide; Proteins; Regulation; biochemistry; cell biology; mole
版次1
doihttps://doi.org/10.1007/978-0-387-39717-7
isbn_softcover978-1-4419-2291-5
isbn_ebook978-0-387-39717-7
copyrightSpringer-Verlag New York 2007
The information of publication is updating

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Biology of the Heat Shock Response and Stress Conditionings (yeast primarily), and cultured animal cells. Often these cultured cells are tumor cell lines, i.e., cells that are functionally eukaryotic microorganisms as a consequence of genetic changes that change their social behavior and proliferative control. These systems have provided useful information
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Unfolded Protein Response: Contributions to Development and Disease in the environment of the endoplasmic reticulum (ER) that adversely affect protein folding and assembly in the secretory pathway. The response is generally thought to protect cells from the transient alterations that can occur in the ER environment and serves to restore homeostatis in this organell
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HSF1 and HSP Gene Regulationck elements (abbreviated HSEs) (.; .). HSEs are arrays of three or more modules of the sequence element NGAAN (or AGAAN) or variations thereof (.; .). Heat shock factors (HSFs) are defined as proteins that are capable of specifically binding HSE sequences. The first attempts at identifying and/or pu
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Regulation of Hsp70 Function: Hsp40 Co-Chaperones and Nucleotide Exchange Factors acid sequence (.). However, Afinsen’s experiments were performed in vitro with dilute solutions of a small globular protein (ribonuclease A), and these conditions are distinct from the highly crowded environment inside a cell where protein conformations vary and protein concentrations may be as hig
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Protein Disassembly by Hsp40-Hsp70sp70 actively unfolds proteins during translocation across membranes (.), whether it fragments aggregates or extracts polypeptides (.), and whether it acts a “holdase” or a “foldase” (.,.). These are related questions because they ask whether Hsp70 exerts a force on its clients during these processe
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