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10.1021/jacs.6b05129 http://scihub22266oqcxt.onion/10.1021/jacs.6b05129 C5389415!5389415!27355699     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27355699&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 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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27355699.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Am+Chem+Soc 2016 ; 138 (30): 9663-74 Nephropedia Template TP {{tp|p=27355699|t=2016. Atomic Resolution Structure of Monomorphic A?42 Amyloid Fibrils |pdf=|usr=}}{{27355699}} gab.com Text Atomic Resolution Structure of Monomorphic A 42 Amyloid Fibrils JO: J Am Chem Soc http://www.kidney.de/pget.php?&tw=1&pmid=27355699 #FOAvip Amyloid-? (A?) is a 39?42 residue protein produced by the cleavage of the amyloid precursor protein (APP), which subsequently aggregates to form cross-? amyloid fibrils that are a hallmark of Alzheimer?s disease (AD). The most prominent forms of A? are A?1?40 and A?1?42, which differ by two amino acids (I and A) at the C-terminus. However, A?42 is more neurotoxic and essential to the etiology of AD. Here, we present an atomic resolution structure of a monomorphic form of A?M01?42 amyloid fibrils derived from over 500 13C?13C, 13C?15N distance and backbone angle structural constraints obtained from high field magic angle spinning NMR spectra. The structure (PDB ID: 5KK3) shows that the fibril core consists of a dimer of A?42 molecules, each containing four ?-strands in a S-shaped amyloid fold, and arranged in a manner that generates two hydrophobic cores that are capped at the end of the chain by a salt bridge. The outer surface of the monomers presents hydrophilic side chains to the solvent. The interface between the monomers of the dimer shows clear contacts between M35 of one molecule and L17 and Q15 of the second. Intermolecular 13C?15N constraints demonstrate that the amyloid fibrils are parallel in register. The RMSD of the backbone structure (Q15?A42) is 0.71 ± 0.12 Å and of all heavy atoms is 1.07 ± 0.08 Å. The structure provides a point of departure for the design of drugs that bind to the fibril surface and therefore interfere with secondary nucleation and for other therapeutic approaches to mitigate A?42 aggregation. Twit Text FOAVip Atomic Resolution Structure of Monomorphic A 42 Amyloid Fibrils ????J Am Chem Soc http://www.kidney.de/pget.php?&tw=1&pmid=27355699 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27355699 #FOAvip English Wikipedia <ref>{{Cite pmid|27355699}}</ref> Atomic Resolution Structure of Monomorphic A?42 Amyloid Fibrils #MMPMID27355699 Colvin MT; Silvers R; Ni QZ; Can TV; Sergeyev I; Rosay M; Donovan KJ; Michael B; Wall J; Linse S; Griffin RG J Am Chem Soc 2016[Aug]; 138 (30): 9663-74 PMID27355699show ga Amyloid-? (A?) is a 39?42 residue protein produced by the cleavage of the amyloid precursor protein (APP), which subsequently aggregates to form cross-? amyloid fibrils that are a hallmark of Alzheimer?s disease (AD). The most prominent forms of A? are A?1?40 and A?1?42, which differ by two amino acids (I and A) at the C-terminus. However, A?42 is more neurotoxic and essential to the etiology of AD. Here, we present an atomic resolution structure of a monomorphic form of A?M01?42 amyloid fibrils derived from over 500 13C?13C, 13C?15N distance and backbone angle structural constraints obtained from high field magic angle spinning NMR spectra. The structure (PDB ID: 5KK3) shows that the fibril core consists of a dimer of A?42 molecules, each containing four ?-strands in a S-shaped amyloid fold, and arranged in a manner that generates two hydrophobic cores that are capped at the end of the chain by a salt bridge. The outer surface of the monomers presents hydrophilic side chains to the solvent. The interface between the monomers of the dimer shows clear contacts between M35 of one molecule and L17 and Q15 of the second. Intermolecular 13C?15N constraints demonstrate that the amyloid fibrils are parallel in register. The RMSD of the backbone structure (Q15?A42) is 0.71 ± 0.12 Å and of all heavy atoms is 1.07 ± 0.08 Å. The structure provides a point of departure for the design of drugs that bind to the fibril surface and therefore interfere with secondary nucleation and for other therapeutic approaches to mitigate A?42 aggregation. äAtomic Resolution Structure of Monomorphic A?42 Amyloid Fibrils (epmc).pdf DeepDyve Pubget Overpricing