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10.1073/pnas.1600749113 http://scihub22266oqcxt.onion/10.1073/pnas.1600749113 C5003276!5003276!27469165     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2016 ; 113 (34): E4976-84 Nephropedia Template TP {{tp|p=27469165|t=2016. Atomic-resolution structure of a disease-relevant A?(1?42) amyloid fibril |pdf=|usr=}}{{27469165}} gab.com Text Atomic-resolution structure of a disease-relevant A (1 42) amyloid fibril JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=27469165 #FOAvip Alzheimer?s disease is the most prevalent neurodegenerative disease still with no known cure. The disease is characterized by the development of extracellular plaques and intracellular neurofibrillary tangles. The senile plaques consist mainly of the peptide amyloid-? (A?) in aggregated form, called amyloid fibrils. It is believed that the A? amyloid fibrils play an important role in disease progression and cell-to-cell transmissibility, and small A? oligomers are often assumed to be the most neurotoxic species. Here, we determined the 3D structure of a disease-relevant A?(1?42) fibril polymorph combining data from solid-state NMR spectroscopy and mass-per-length measurements from EM. The 3D structure is composed of two molecules per fibril layer, forming a double-horseshoe?like cross??-sheet entity with maximally buried hydrophobic side chains. Twit Text FOAVip Atomic-resolution structure of a disease-relevant A (1 42) amyloid fibril ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=27469165 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27469165 #FOAvip English Wikipedia <ref>{{Cite pmid|27469165}}</ref> Atomic-resolution structure of a disease-relevant A?(1?42) amyloid fibril #MMPMID27469165 Wälti MA; Ravotti F; Arai H; Glabe CG; Wall JS; Böckmann A; Güntert P; Meier BH; Riek R Proc Natl Acad Sci U S A 2016[Aug]; 113 (34): E4976-84 PMID27469165show ga Alzheimer?s disease is the most prevalent neurodegenerative disease still with no known cure. The disease is characterized by the development of extracellular plaques and intracellular neurofibrillary tangles. The senile plaques consist mainly of the peptide amyloid-? (A?) in aggregated form, called amyloid fibrils. It is believed that the A? amyloid fibrils play an important role in disease progression and cell-to-cell transmissibility, and small A? oligomers are often assumed to be the most neurotoxic species. Here, we determined the 3D structure of a disease-relevant A?(1?42) fibril polymorph combining data from solid-state NMR spectroscopy and mass-per-length measurements from EM. The 3D structure is composed of two molecules per fibril layer, forming a double-horseshoe?like cross??-sheet entity with maximally buried hydrophobic side chains. äAtomic-resolution structure of a disease-relevant A?(1?42) amyloid fib(epmc).pdf DeepDyve Pubget Overpricing