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10.4161/nucl.29404 http://scihub22266oqcxt.onion/10.4161/nucl.29404 C4152345!4152345!25482120     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 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nucleus 2014 ; 5 (4): 311-7 Nephropedia Template TP {{tp|p=25482120|t=2014. Pathology and function of nuclear amyloid: Protein homeostasis matters |pdf=|usr=}}{{25482120}} gab.com Text Pathology and function of nuclear amyloid: Protein homeostasis matters JO: Nucleus http://www.kidney.de/pget.php?&tw=1&pmid=25482120 #FOAvip In aging societies increasing cases of neurodegenerative protein deposit diseases urge for the identification of the underlying mechanisms. Expectations are that in 2050 the percentage of population over age 60 is 42% in Japan, 34% in China, and 27% in the US. The cell nucleus is a major target of amyloid-like protein fibrillation in a variety of disorders that are characterized by widespread aggregation of proteins with instable homopolymeric amino acid repeats, ubiquitin, and other proteinaceous components. Additionally, accumulation of insoluble, SDS-resistant proteins has been identified as an intrinsic property of organismal aging. This review collects current knowledge about the composition and function of insoluble, nuclear protein inclusions from the protein homeostasis perspective. It discusses the occurrence and role of nuclear amyloid in the diseased as well as the healthy cell. Features of nuclear inclusions such as protein composition and locally active protein degradation may predict neural fitness and survival in a variety of health or disease settings. Twit Text FOAVip Pathology and function of nuclear amyloid: Protein homeostasis matters ????Nucleus http://www.kidney.de/pget.php?&tw=1&pmid=25482120 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25482120 #FOAvip English Wikipedia <ref>{{Cite pmid|25482120}}</ref> Pathology and function of nuclear amyloid: Protein homeostasis matters #MMPMID25482120 von Mikecz A Nucleus 2014[Jul]; 5 (4): 311-7 PMID25482120show ga In aging societies increasing cases of neurodegenerative protein deposit diseases urge for the identification of the underlying mechanisms. Expectations are that in 2050 the percentage of population over age 60 is 42% in Japan, 34% in China, and 27% in the US. The cell nucleus is a major target of amyloid-like protein fibrillation in a variety of disorders that are characterized by widespread aggregation of proteins with instable homopolymeric amino acid repeats, ubiquitin, and other proteinaceous components. Additionally, accumulation of insoluble, SDS-resistant proteins has been identified as an intrinsic property of organismal aging. This review collects current knowledge about the composition and function of insoluble, nuclear protein inclusions from the protein homeostasis perspective. It discusses the occurrence and role of nuclear amyloid in the diseased as well as the healthy cell. Features of nuclear inclusions such as protein composition and locally active protein degradation may predict neural fitness and survival in a variety of health or disease settings. äPathology and function of nuclear amyloid: Protein homeostasis matters(epmc).pdf DeepDyve Pubget Overpricing