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10.3390/biom4010101 http://scihub22266oqcxt.onion/10.3390/biom4010101 C4030978!4030978!24970207     free     free     free Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biomolecules 2014 ; 4 (1): 101-16 Nephropedia Template TP {{tp|p=24970207|t=2014. Effect of Metals on Kinetic Pathways of Amyloid-? Aggregation |pdf=|usr=}}{{24970207}} gab.com Text Effect of Metals on Kinetic Pathways of Amyloid- Aggregation JO: Biomolecules http://www.kidney.de/pget.php?&tw=1&pmid=24970207 #FOAvip Metal ions, including copper and zinc, have been implicated in the pathogenesis of Alzheimer?s disease through a variety of mechanisms including increased amyloid-? affinity and redox effects. Recent reports have demonstrated that the amyloid-? monomer does not necessarily travel through a definitive intermediary en-route to a stable amyloid fibril structure. Rather, amyloid-? misfolding may follow a variety of pathways resulting in a fibrillar end-product or a variety of oligomeric end-products with a diversity of structures and sizes. The presence of metal ions has been demonstrated to alter the kinetic pathway of the amyloid-? peptide which may lead to more toxic oligomeric end-products. In this work, we review the contemporary literature supporting the hypothesis that metal ions alter the reaction pathway of amyloid-? misfolding leading to more neurotoxic species. Twit Text FOAVip Effect of Metals on Kinetic Pathways of Amyloid- Aggregation ????Biomolecules http://www.kidney.de/pget.php?&tw=1&pmid=24970207 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24970207 #FOAvip English Wikipedia <ref>{{Cite pmid|24970207}}</ref> Effect of Metals on Kinetic Pathways of Amyloid-? Aggregation #MMPMID24970207 Hane F; Leonenko Z Biomolecules 2014[Mar]; 4 (1): 101-16 PMID24970207show ga Metal ions, including copper and zinc, have been implicated in the pathogenesis of Alzheimer?s disease through a variety of mechanisms including increased amyloid-? affinity and redox effects. Recent reports have demonstrated that the amyloid-? monomer does not necessarily travel through a definitive intermediary en-route to a stable amyloid fibril structure. Rather, amyloid-? misfolding may follow a variety of pathways resulting in a fibrillar end-product or a variety of oligomeric end-products with a diversity of structures and sizes. The presence of metal ions has been demonstrated to alter the kinetic pathway of the amyloid-? peptide which may lead to more toxic oligomeric end-products. In this work, we review the contemporary literature supporting the hypothesis that metal ions alter the reaction pathway of amyloid-? misfolding leading to more neurotoxic species. äEffect of Metals on Kinetic Pathways of Amyloid-? Aggregation (epmc).pdf DeepDyve Pubget Overpricing