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10.1016/j.cell.2015.03.032 http://scihub22266oqcxt.onion/10.1016/j.cell.2015.03.032 C4643853!4643853!25957690     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell 2015 ; 161 (4): 919-32 Nephropedia Template TP {{tp|p=25957690|t=2015. Proteome Imbalance is Linked With Proteostasis Decline and Aggregation in Aging C elegans |pdf=|usr=}}{{25957690}} gab.com Text Proteome Imbalance is Linked With Proteostasis Decline and Aggregation in Aging C elegans JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=25957690 #FOAvip Aging has been associated with a progressive decline of proteostasis, but how this process manifests itself at the level of proteome composition remains largely unexplored. Here we profiled more than 5,000 proteins along the lifespan of the nematode C. elegans. We find that one third of proteins change in abundance at least 2-fold during aging, resulting in a severe proteome imbalance. These changes are reduced in the long-lived daf-2 mutant, but enhanced in the short-lived daf-16 mutant. While ribosomal proteins decline and lose normal stoichiometry, proteasome complexes increase. Proteome imbalance is accompanied by widespread protein aggregation, with abundant proteins that exceed solubility contributing most to aggregate load. Notably, the properties by which proteins are selected for aggregation differ in the daf-2 mutant, and an increased formation of aggregates associated with small heat shock proteins is observed. We suggest that sequestering proteins into chaperone-enriched aggregates is a protective strategy to slow proteostasis decline during nematode aging. Twit Text FOAVip Proteome Imbalance is Linked With Proteostasis Decline and Aggregation in Aging C elegans ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=25957690 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25957690 #FOAvip English Wikipedia <ref>{{Cite pmid|25957690}}</ref> Proteome Imbalance is Linked With Proteostasis Decline and Aggregation in Aging C elegans #MMPMID25957690 Walther DM; Kasturi P; Zheng M; Pinkert S; Vecchi G; Ciryam P; Morimoto RI; Dobson CM; Vendruscolo M; Mann M; Hartl FU Cell 2015[May]; 161 (4): 919-32 PMID25957690show ga Aging has been associated with a progressive decline of proteostasis, but how this process manifests itself at the level of proteome composition remains largely unexplored. Here we profiled more than 5,000 proteins along the lifespan of the nematode C. elegans. We find that one third of proteins change in abundance at least 2-fold during aging, resulting in a severe proteome imbalance. These changes are reduced in the long-lived daf-2 mutant, but enhanced in the short-lived daf-16 mutant. While ribosomal proteins decline and lose normal stoichiometry, proteasome complexes increase. Proteome imbalance is accompanied by widespread protein aggregation, with abundant proteins that exceed solubility contributing most to aggregate load. Notably, the properties by which proteins are selected for aggregation differ in the daf-2 mutant, and an increased formation of aggregates associated with small heat shock proteins is observed. We suggest that sequestering proteins into chaperone-enriched aggregates is a protective strategy to slow proteostasis decline during nematode aging. äProteome Imbalance is Linked With Proteostasis Decline and Aggregation(epmc).pdf DeepDyve Pubget Overpricing