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10.1038/ncomms12419 http://scihub22266oqcxt.onion/10.1038/ncomms12419 C4996947!4996947 !27546208     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27546208 &cmd=llinks): Failed to open stream: HTTP request failed! 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Rapid ?-oligomer formation mediated by the A? C terminus initiates an amyloid assembly pathway |pdf=|usr=}}{{27546208 }} gab.com Text Rapid -oligomer formation mediated by the A C terminus initiates an amyloid assembly pathway JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=27546208 #FOAvip Since early oligomeric intermediates in amyloid assembly are often transient and difficult to distinguish, characterize and quantify, the mechanistic basis of the initiation of spontaneous amyloid growth is often opaque. We describe here an approach to the analysis of the A? aggregation mechanism that uses A?-polyglutamine hybrid peptides designed to retard amyloid maturation and an adjusted thioflavin intensity scale that reveals structural features of aggregation intermediates. The results support an aggregation initiation mechanism for A?-polyQ hybrids, and by extension for full-length A? peptides, in which a modular A? C-terminal segment mediates rapid, non-nucleated formation of ?-helical oligomers. The resulting high local concentration of tethered amyloidogenic segments within these ?-oligomers facilitates transition to a ?-oligomer population that, via further remodelling and/or elongation steps, ultimately generates mature amyloid. Consistent with this mechanism, an engineered A? C-terminal fragment delays aggregation onset by A?-polyglutamine peptides and redirects assembly of A?42 fibrils. Twit Text FOAVip Rapid -oligomer formation mediated by the A C terminus initiates an amyloid assembly pathway ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=27546208 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27546208 #FOAvip English Wikipedia <ref>{{Cite pmid|27546208 }}</ref> Rapid ?-oligomer formation mediated by the A? C terminus initiates an amyloid assembly pathway #MMPMID27546208 Misra P ; Kodali R ; Chemuru S ; Kar K ; Wetzel R Nat Commun 2016[Aug]; 7 (ä): 12419 PMID27546208 show ga Since early oligomeric intermediates in amyloid assembly are often transient and difficult to distinguish, characterize and quantify, the mechanistic basis of the initiation of spontaneous amyloid growth is often opaque. We describe here an approach to the analysis of the A? aggregation mechanism that uses A?-polyglutamine hybrid peptides designed to retard amyloid maturation and an adjusted thioflavin intensity scale that reveals structural features of aggregation intermediates. The results support an aggregation initiation mechanism for A?-polyQ hybrids, and by extension for full-length A? peptides, in which a modular A? C-terminal segment mediates rapid, non-nucleated formation of ?-helical oligomers. The resulting high local concentration of tethered amyloidogenic segments within these ?-oligomers facilitates transition to a ?-oligomer population that, via further remodelling and/or elongation steps, ultimately generates mature amyloid. Consistent with this mechanism, an engineered A? C-terminal fragment delays aggregation onset by A?-polyglutamine peptides and redirects assembly of A?42 fibrils. |*Protein Multimerization [MESH] |Alzheimer Disease/*pathology [MESH] |Amyloid beta-Peptides/chemistry/genetics/*metabolism [MESH] |Benzothiazoles [MESH] |Circular Dichroism [MESH] |Fluorescent Dyes/chemistry [MESH] |Humans [MESH] |Peptide Fragments/chemistry/genetics/*metabolism [MESH] |Peptides/chemistry/genetics/*metabolism [MESH] |Protein Aggregation, Pathological/*pathology [MESH] |Protein Engineering [MESH] |Protein Structure, Secondary [MESH] |Spectrum Analysis/methods [MESH] |Thiazoles/chemistry [MESH]Rapid ?-oligomer formation mediated by the A? C terminus initiates an (epmc).pdf DeepDyve Pubget Overpricing