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10.1111/febs.14576 http://scihub22266oqcxt.onion/10.1111/febs.14576 29890022!7164077!29890022     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       FEBS+J 2018 ; 285 (18): 3353-3361 Nephropedia Template TP {{tp|p=29890022|t=2018. Molecular chaperones: from proteostasis to pathogenesis |pdf=|usr=}}{{29890022}} gab.com Text Molecular chaperones: from proteostasis to pathogenesis JO: FEBS J http://www.kidney.de/pget.php?&tw=1&pmid=29890022 #FOAvip Maintaining protein homeostasis (proteostasis) is essential for a functional proteome. A wide range of extrinsic and intrinsic factors perturb proteostasis, causing protein misfolding, misassembly, and aggregation. This compromises cellular integrity and leads to aging and disease, including neurodegeneration and cancer. At the cellular level, protein aggregation is counteracted by powerful mechanisms comprising of a cascade of enzymes and chaperones that operate in a coordinated multistep manner to sense, prevent, and/or dispose of aberrant proteins. Although these processes are well understood for soluble proteins, there is a major gap in our understanding of how cells handle misfolded or aggregated membrane proteins. This article provides an overview of cellular proteostasis with emphasis on membrane protein substrates and suggests host-virus interaction as a tool to clarify outstanding questions in proteostasis. Twit Text FOAVip Molecular chaperones: from proteostasis to pathogenesis ????FEBS J http://www.kidney.de/pget.php?&tw=1&pmid=29890022 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29890022 #FOAvip English Wikipedia <ref>{{Cite pmid|29890022}}</ref> Molecular chaperones: from proteostasis to pathogenesis #MMPMID29890022 Ravindran MS FEBS J 2018[Sep]; 285 (18): 3353-3361 PMID29890022show ga Maintaining protein homeostasis (proteostasis) is essential for a functional proteome. A wide range of extrinsic and intrinsic factors perturb proteostasis, causing protein misfolding, misassembly, and aggregation. This compromises cellular integrity and leads to aging and disease, including neurodegeneration and cancer. At the cellular level, protein aggregation is counteracted by powerful mechanisms comprising of a cascade of enzymes and chaperones that operate in a coordinated multistep manner to sense, prevent, and/or dispose of aberrant proteins. Although these processes are well understood for soluble proteins, there is a major gap in our understanding of how cells handle misfolded or aggregated membrane proteins. This article provides an overview of cellular proteostasis with emphasis on membrane protein substrates and suggests host-virus interaction as a tool to clarify outstanding questions in proteostasis. |*Host-Pathogen Interactions[MESH] |*Molecular Chaperones[MESH] |*Protein Aggregation, Pathological[MESH] |*Proteostasis[MESH] |Animals[MESH] |Humans[MESH] |Proteome/*metabolism[MESH]Molecular chaperones: from proteostasis to pathogenesis (epmc).pdf DeepDyve Pubget Overpricing