Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1016/j.semcdb.2015.03.003 http://scihub22266oqcxt.onion/10.1016/j.semcdb.2015.03.003 C4471145!4471145!25770416     free     free     free       Semin+Cell+Dev+Biol 2015 ; 40 (ä): 142-52 Nephropedia Template TP {{tp|p=25770416|t=2015. Molecular chaperones and neuronal proteostasis |pdf=|usr=}}{{25770416}} gab.com Text Molecular chaperones and neuronal proteostasis JO: Semin Cell Dev Biol http://www.kidney.de/pget.php?&tw=1&pmid=25770416 #FOAvip Protein homeostasis (proteostasis) is essential for maintaining the functionality of the proteome. The disruption of proteostasis, due to genetic mutations or an age-related decline, leads to aberrantly folded proteins that typically lose their function. The accumulation of misfolded and aggregated protein is also cytotoxic and has been implicated in the pathogenesis of neurodegenerative diseases. Neurons have developed an intrinsic protein quality control network, of which molecular chaperones are an essential component. Molecular chaperones function to promote efficient folding and target misfolded proteins for refolding or degradation. Increasing molecular chaperone expression can suppress protein aggregation and toxicity in numerous models of neurodegenerative disease; therefore, molecular chaperones are considered exciting therapeutic targets. Furthermore, mutations in several chaperones cause inherited neurodegenerative diseases. In this review, we focus on the importance of molecular chaperones in neurodegenerative diseases, and discuss the advances in understanding their protective mechanisms. Twit Text FOAVip Molecular chaperones and neuronal proteostasis ????Semin Cell Dev Biol http://www.kidney.de/pget.php?&tw=1&pmid=25770416 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25770416 #FOAvip English Wikipedia <ref>{{Cite pmid|25770416}}</ref> Molecular chaperones and neuronal proteostasis #MMPMID25770416 Smith HL; Li W; Cheetham ME Semin Cell Dev Biol 2015[Apr]; 40 (ä): 142-52 PMID25770416show ga Protein homeostasis (proteostasis) is essential for maintaining the functionality of the proteome. The disruption of proteostasis, due to genetic mutations or an age-related decline, leads to aberrantly folded proteins that typically lose their function. The accumulation of misfolded and aggregated protein is also cytotoxic and has been implicated in the pathogenesis of neurodegenerative diseases. Neurons have developed an intrinsic protein quality control network, of which molecular chaperones are an essential component. Molecular chaperones function to promote efficient folding and target misfolded proteins for refolding or degradation. Increasing molecular chaperone expression can suppress protein aggregation and toxicity in numerous models of neurodegenerative disease; therefore, molecular chaperones are considered exciting therapeutic targets. Furthermore, mutations in several chaperones cause inherited neurodegenerative diseases. In this review, we focus on the importance of molecular chaperones in neurodegenerative diseases, and discuss the advances in understanding their protective mechanisms. äMolecular chaperones and neuronal proteostasis (epmc).pdf DeepDyve Pubget Overpricing