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10.1038/srep44064 http://scihub22266oqcxt.onion/10.1038/srep44064 C5341037!5341037!28272432     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       Sci+Rep 2017 ; 7 (ä): ä Nephropedia Template TP {{tp|p=28272432|t=2017. Melanosomal formation of PMEL core amyloid is driven by aromatic residues |pdf=|usr=}}{{28272432}} gab.com Text Melanosomal formation of PMEL core amyloid is driven by aromatic residues JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28272432 #FOAvip PMEL is a pigment cell protein that forms physiological amyloid in melanosomes. Many amyloids and/or their oligomeric precursors are toxic, causing or contributing to severe, incurable diseases including Alzheimer?s and prion diseases. Striking similarities in intracellular formation pathways between PMEL and various pathological amyloids including A? and PrPSc suggest PMEL is an excellent model system to study endocytic amyloid. Learning how PMEL fibrils assemble without apparent toxicity may help developing novel therapies for amyloid diseases. Here we identify the critical PMEL domain that forms the melanosomal amyloid core (CAF). An unbiased alanine-scanning screen covering the entire region combined with quantitative electron microscopy analysis of the full set of mutants uncovers numerous essential residues. Many of these rely on aromaticity for function suggesting a role for ?-stacking in melanosomal amyloid assembly. Various mutants are defective in amyloid nucleation. This extensive data set informs the first structural model of the CAF and provides insights into how the melanosomal amyloid core forms. Twit Text FOAVip Melanosomal formation of PMEL core amyloid is driven by aromatic residues ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28272432 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28272432 #FOAvip English Wikipedia <ref>{{Cite pmid|28272432}}</ref> Melanosomal formation of PMEL core amyloid is driven by aromatic residues #MMPMID28272432 Hee JS; Mitchell SM; Liu X; Leonhardt RM Sci Rep 2017[]; 7 (ä): ä PMID28272432show ga PMEL is a pigment cell protein that forms physiological amyloid in melanosomes. Many amyloids and/or their oligomeric precursors are toxic, causing or contributing to severe, incurable diseases including Alzheimer?s and prion diseases. Striking similarities in intracellular formation pathways between PMEL and various pathological amyloids including A? and PrPSc suggest PMEL is an excellent model system to study endocytic amyloid. Learning how PMEL fibrils assemble without apparent toxicity may help developing novel therapies for amyloid diseases. Here we identify the critical PMEL domain that forms the melanosomal amyloid core (CAF). An unbiased alanine-scanning screen covering the entire region combined with quantitative electron microscopy analysis of the full set of mutants uncovers numerous essential residues. Many of these rely on aromaticity for function suggesting a role for ?-stacking in melanosomal amyloid assembly. Various mutants are defective in amyloid nucleation. This extensive data set informs the first structural model of the CAF and provides insights into how the melanosomal amyloid core forms. äMelanosomal formation of PMEL core amyloid is driven by aromatic resid(epmc).pdf DeepDyve Pubget Overpricing