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10.1016/j.molcel.2016.07.016 http://scihub22266oqcxt.onion/10.1016/j.molcel.2016.07.016 C5234082!5234082!27570072     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27570072.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Mol+Cell 2016 ; 63 (5): 768-80 Nephropedia Template TP {{tp|p=27570072|t=2016. Polyphosphate: A Conserved Modifier of Amyloidogenic Processes |pdf=|usr=}}{{27570072}} gab.com Text Polyphosphate: A Conserved Modifier of Amyloidogenic Processes JO: Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=27570072 #FOAvip Polyphosphate (polyP), a several billion year old biopolymer, is produced in every cell, tissue, and organism studied. Structurally extremely simple, polyP consists of long chains of covalently linked inorganic phosphate groups. We report here the surprising discovery that polyP shows a remarkable efficacy in accelerating amyloid fibril formation. We found that polyP serves as an effective nucleation source for various different amyloid proteins, ranging from bacterial CsgA to human ?-Synuclein, A?1-40/42 and Tau. PolyP-associated ?-Synuclein fibrils show distinct differences in seeding behavior, morphology and fibril stability compared to fibrils formed in the absence of polyP. In vivo, the amyloid-stimulating and fibril-stabilizing effects of polyP have wide-reaching consequences, increasing the rate of biofilm formation in pathogenic bacteria and mitigating amyloid toxicity in differentiated neuroblastoma cells and C. elegans strains that serve as models for human folding diseases. These results suggest that we have discovered a conserved cytoprotective modifier of amyloidogenic processes. Twit Text FOAVip Polyphosphate: A Conserved Modifier of Amyloidogenic Processes ????Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=27570072 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27570072 #FOAvip English Wikipedia <ref>{{Cite pmid|27570072}}</ref> Polyphosphate: A Conserved Modifier of Amyloidogenic Processes #MMPMID27570072 Cremers CM; Knoefler D; Gates S; Martin N; Dahl JU; Lempart J; Xie L; Chapman MR; Galvan V; Southworth DR; Jakob U Mol Cell 2016[Sep]; 63 (5): 768-80 PMID27570072show ga Polyphosphate (polyP), a several billion year old biopolymer, is produced in every cell, tissue, and organism studied. Structurally extremely simple, polyP consists of long chains of covalently linked inorganic phosphate groups. We report here the surprising discovery that polyP shows a remarkable efficacy in accelerating amyloid fibril formation. We found that polyP serves as an effective nucleation source for various different amyloid proteins, ranging from bacterial CsgA to human ?-Synuclein, A?1-40/42 and Tau. PolyP-associated ?-Synuclein fibrils show distinct differences in seeding behavior, morphology and fibril stability compared to fibrils formed in the absence of polyP. In vivo, the amyloid-stimulating and fibril-stabilizing effects of polyP have wide-reaching consequences, increasing the rate of biofilm formation in pathogenic bacteria and mitigating amyloid toxicity in differentiated neuroblastoma cells and C. elegans strains that serve as models for human folding diseases. These results suggest that we have discovered a conserved cytoprotective modifier of amyloidogenic processes. äPolyphosphate: A Conserved Modifier of Amyloidogenic Processes (epmc).pdf DeepDyve Pubget Overpricing