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10.1038/ncomms8831 http://scihub22266oqcxt.onion/10.1038/ncomms8831 C4525161!4525161 !26215704     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 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\26215704 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Nat+Commun 2015 ; 6 (ä): 7831 Nephropedia Template TP {{tp|p=26215704 |t=2015. Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation |pdf=|usr=}}{{26215704 }} gab.com Text Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26215704 #FOAvip Amyloids are insoluble protein fibrillar aggregates. The importance of characterizing their aggregation has steadily increased because of their link to human diseases and material science applications. In particular, misfolding and aggregation of the Josephin domain of ataxin-3 is implicated in spinocerebellar ataxia-3. Infrared nanospectroscopy, simultaneously exploiting atomic force microscopy and infrared spectroscopy, can characterize at the nanoscale the conformational rearrangements of proteins during their aggregation. Here we demonstrate that we can individually characterize the oligomeric and fibrillar species formed along the amyloid aggregation. We describe their secondary structure, monitoring at the nanoscale an ?-to-? transition, and couple these studies with an independent measurement of the evolution of their intrinsic stiffness. These results suggest that the aggregation of Josephin proceeds from the monomer state to the formation of spheroidal intermediates with a native structure. Only successively, these intermediates evolve into misfolded aggregates and into the final fibrils. Twit Text FOAVip Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26215704 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26215704 #FOAvip English Wikipedia <ref>{{Cite pmid|26215704 }}</ref> Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation #MMPMID26215704 Ruggeri FS ; Longo G ; Faggiano S ; Lipiec E ; Pastore A ; Dietler G Nat Commun 2015[Jul]; 6 (ä): 7831 PMID26215704 show ga Amyloids are insoluble protein fibrillar aggregates. The importance of characterizing their aggregation has steadily increased because of their link to human diseases and material science applications. In particular, misfolding and aggregation of the Josephin domain of ataxin-3 is implicated in spinocerebellar ataxia-3. Infrared nanospectroscopy, simultaneously exploiting atomic force microscopy and infrared spectroscopy, can characterize at the nanoscale the conformational rearrangements of proteins during their aggregation. Here we demonstrate that we can individually characterize the oligomeric and fibrillar species formed along the amyloid aggregation. We describe their secondary structure, monitoring at the nanoscale an ?-to-? transition, and couple these studies with an independent measurement of the evolution of their intrinsic stiffness. These results suggest that the aggregation of Josephin proceeds from the monomer state to the formation of spheroidal intermediates with a native structure. Only successively, these intermediates evolve into misfolded aggregates and into the final fibrils. |*Protein Aggregates [MESH] |Amyloid/chemistry/*metabolism/ultrastructure [MESH] |Ataxin-3/chemistry/*metabolism/ultrastructure [MESH] |Elastic Modulus [MESH] |Humans [MESH] |Microscopy, Atomic Force [MESH] |Nanotechnology [MESH] |Protein Structure, Secondary [MESH] |Protein Structure, Tertiary [MESH] |Repressor Proteins/chemistry/*metabolism/ultrastructure [MESH]Infrared nanospectroscopy characterization of oligomeric and fibrillar(epmc).pdf DeepDyve Pubget Overpricing