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10.3390/pathogens7020050 http://scihub22266oqcxt.onion/10.3390/pathogens7020050 C6027354!6027354!29734684     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Pathogens 2018 ; 7 (2): ä Nephropedia Template TP {{tp|p=29734684|t=2018. Comparing the Folds of Prions and Other Pathogenic Amyloids |pdf=|usr=}}{{29734684}} gab.com Text Comparing the Folds of Prions and Other Pathogenic Amyloids JO: Pathogens http://www.kidney.de/pget.php?&tw=1&pmid=29734684 #FOAvip Pathogenic amyloids are the main feature of several neurodegenerative disorders, such as Creutzfeldt?Jakob disease, Alzheimer?s disease, and Parkinson?s disease. High resolution structures of tau paired helical filaments (PHFs), amyloid-?(1-42) (A?(1-42)) fibrils, and ?-synuclein fibrils were recently reported using cryo-electron microscopy. A high-resolution structure for the infectious prion protein, PrPSc, is not yet available due to its insolubility and its propensity to aggregate, but cryo-electron microscopy, X-ray fiber diffraction, and other approaches have defined the overall architecture of PrPSc as a 4-rung ?-solenoid. Thus, the structure of PrPSc must have a high similarity to that of the fungal prion HET-s, which is part of the fungal heterokaryon incompatibility system and contains a 2-rung ?-solenoid. This review compares the structures of tau PHFs, A?(1-42), and ?-synuclein fibrils, where the ?-strands of each molecule stack on top of each other in a parallel in-register arrangement, with the ?-solenoid folds of HET-s and PrPSc. Twit Text FOAVip Comparing the Folds of Prions and Other Pathogenic Amyloids ????Pathogens http://www.kidney.de/pget.php?&tw=1&pmid=29734684 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29734684 #FOAvip English Wikipedia <ref>{{Cite pmid|29734684}}</ref> Comparing the Folds of Prions and Other Pathogenic Amyloids #MMPMID29734684 Flores-Fernández JM; Rathod V; Wille H Pathogens 2018[Jun]; 7 (2): ä PMID29734684show ga Pathogenic amyloids are the main feature of several neurodegenerative disorders, such as Creutzfeldt?Jakob disease, Alzheimer?s disease, and Parkinson?s disease. High resolution structures of tau paired helical filaments (PHFs), amyloid-?(1-42) (A?(1-42)) fibrils, and ?-synuclein fibrils were recently reported using cryo-electron microscopy. A high-resolution structure for the infectious prion protein, PrPSc, is not yet available due to its insolubility and its propensity to aggregate, but cryo-electron microscopy, X-ray fiber diffraction, and other approaches have defined the overall architecture of PrPSc as a 4-rung ?-solenoid. Thus, the structure of PrPSc must have a high similarity to that of the fungal prion HET-s, which is part of the fungal heterokaryon incompatibility system and contains a 2-rung ?-solenoid. This review compares the structures of tau PHFs, A?(1-42), and ?-synuclein fibrils, where the ?-strands of each molecule stack on top of each other in a parallel in-register arrangement, with the ?-solenoid folds of HET-s and PrPSc. äComparing the Folds of Prions and Other Pathogenic Amyloids (epmc).pdf DeepDyve Pubget Overpricing