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10.1371/journal.ppat.1005835 http://scihub22266oqcxt.onion/10.1371/journal.ppat.1005835 C5015997!5015997!27606840     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27606840&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       PLoS+Pathog 2016 ; 12 (9): ä Nephropedia Template TP {{tp|p=27606840|t=2016. The Structural Architecture of an Infectious Mammalian Prion Using Electron Cryomicroscopy |pdf=|usr=}}{{27606840}} gab.com Text The Structural Architecture of an Infectious Mammalian Prion Using Electron Cryomicroscopy JO: PLoS Pathog http://www.kidney.de/pget.php?&tw=1&pmid=27606840 #FOAvip The structure of the infectious prion protein (PrPSc), which is responsible for Creutzfeldt-Jakob disease in humans and bovine spongiform encephalopathy, has escaped all attempts at elucidation due to its insolubility and propensity to aggregate. PrPSc replicates by converting the non-infectious, cellular prion protein (PrPC) into the misfolded, infectious conformer through an unknown mechanism. PrPSc and its N-terminally truncated variant, PrP 27?30, aggregate into amorphous aggregates, 2D crystals, and amyloid fibrils. The structure of these infectious conformers is essential to understanding prion replication and the development of structure-based therapeutic interventions. Here we used the repetitive organization inherent to GPI-anchorless PrP 27?30 amyloid fibrils to analyze their structure via electron cryomicroscopy. Fourier-transform analyses of averaged fibril segments indicate a repeating unit of 19.1 Ĺ. 3D reconstructions of these fibrils revealed two distinct protofilaments, and, together with a molecular volume of 18,990 Ĺ3, predicted the height of each PrP 27?30 molecule as ~17.7 Ĺ. Together, the data indicate a four-rung ?-solenoid structure as a key feature for the architecture of infectious mammalian prions. Furthermore, they allow to formulate a molecular mechanism for the replication of prions. Knowledge of the prion structure will provide important insights into the self-propagation mechanisms of protein misfolding. Twit Text FOAVip The Structural Architecture of an Infectious Mammalian Prion Using Electron Cryomicroscopy ????PLoS Pathog http://www.kidney.de/pget.php?&tw=1&pmid=27606840 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27606840 #FOAvip English Wikipedia <ref>{{Cite pmid|27606840}}</ref> The Structural Architecture of an Infectious Mammalian Prion Using Electron Cryomicroscopy #MMPMID27606840 Vázquez-Fernández E; Vos MR; Afanasyev P; Cebey L; Sevillano AM; Vidal E; Rosa I; Renault L; Ramos A; Peters PJ; Fernández JJ; van Heel M; Young HS; Requena JR; Wille H PLoS Pathog 2016[Sep]; 12 (9): ä PMID27606840show ga The structure of the infectious prion protein (PrPSc), which is responsible for Creutzfeldt-Jakob disease in humans and bovine spongiform encephalopathy, has escaped all attempts at elucidation due to its insolubility and propensity to aggregate. PrPSc replicates by converting the non-infectious, cellular prion protein (PrPC) into the misfolded, infectious conformer through an unknown mechanism. PrPSc and its N-terminally truncated variant, PrP 27?30, aggregate into amorphous aggregates, 2D crystals, and amyloid fibrils. The structure of these infectious conformers is essential to understanding prion replication and the development of structure-based therapeutic interventions. Here we used the repetitive organization inherent to GPI-anchorless PrP 27?30 amyloid fibrils to analyze their structure via electron cryomicroscopy. Fourier-transform analyses of averaged fibril segments indicate a repeating unit of 19.1 Ĺ. 3D reconstructions of these fibrils revealed two distinct protofilaments, and, together with a molecular volume of 18,990 Ĺ3, predicted the height of each PrP 27?30 molecule as ~17.7 Ĺ. Together, the data indicate a four-rung ?-solenoid structure as a key feature for the architecture of infectious mammalian prions. Furthermore, they allow to formulate a molecular mechanism for the replication of prions. Knowledge of the prion structure will provide important insights into the self-propagation mechanisms of protein misfolding. äThe Structural Architecture of an Infectious Mammalian Prion Using Ele(epmc).pdf DeepDyve Pubget Overpricing