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10.1016/j.jmb.2015.05.010 http://scihub22266oqcxt.onion/10.1016/j.jmb.2015.05.010 C4569545!4569545!26003923     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Mol+Biol 2015 ; 427 (18): 2931-47 Nephropedia Template TP {{tp|p=26003923|t=2015. The chemical biology of molecular chaperones - Implications for modulation of proteostasis |pdf=|usr=}}{{26003923}} gab.com Text The chemical biology of molecular chaperones - Implications for modulation of proteostasis JO: J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=26003923 #FOAvip Protein homeostasis (proteostasis) is inextricably tied to cellular health and organismal lifespan. Aging, exposure to physiological and environmental stress, and expression of mutant and metastable proteins can cause an imbalance in the protein folding landscape, resulting in the formation of non-native protein aggregates that challenge the capacity of the proteostasis network (PN), increasing the risk for diseases associated with misfolding, aggregation and aberrant regulation of cell stress responses. Molecular chaperones have central roles in each of the arms of the PN (protein synthesis, folding, disaggregation, and degradation), leading to the proposal that modulation of chaperone function could have therapeutic benefits for the large and growing family of diseases of protein conformation including neurodegeneration, metabolic diseases, and cancer. In this review, we will discuss the current strategies used to tune the PN through targeting molecular chaperones and assess the potential of the chemical biology of proteostasis. Twit Text FOAVip The chemical biology of molecular chaperones - Implications for modulation of proteostasis ????J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=26003923 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26003923 #FOAvip English Wikipedia <ref>{{Cite pmid|26003923}}</ref> The chemical biology of molecular chaperones - Implications for modulation of proteostasis #MMPMID26003923 Brandvold KR; Morimoto RI J Mol Biol 2015[Sep]; 427 (18): 2931-47 PMID26003923show ga Protein homeostasis (proteostasis) is inextricably tied to cellular health and organismal lifespan. Aging, exposure to physiological and environmental stress, and expression of mutant and metastable proteins can cause an imbalance in the protein folding landscape, resulting in the formation of non-native protein aggregates that challenge the capacity of the proteostasis network (PN), increasing the risk for diseases associated with misfolding, aggregation and aberrant regulation of cell stress responses. Molecular chaperones have central roles in each of the arms of the PN (protein synthesis, folding, disaggregation, and degradation), leading to the proposal that modulation of chaperone function could have therapeutic benefits for the large and growing family of diseases of protein conformation including neurodegeneration, metabolic diseases, and cancer. In this review, we will discuss the current strategies used to tune the PN through targeting molecular chaperones and assess the potential of the chemical biology of proteostasis. äThe chemical biology of molecular chaperones - Implications for modula(epmc).pdf DeepDyve Pubget Overpricing