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10.1101/cshperspect.a024083 http://scihub22266oqcxt.onion/10.1101/cshperspect.a024083 C4968170!4968170!27481836     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cold+Spring+Harb+Perspect+Med 2016 ; 6 (8): ä Nephropedia Template TP {{tp|p=27481836|t=2016. Molecular Structure of Aggregated Amyloid-?: Insights from Solid-State Nuclear Magnetic Resonance |pdf=|usr=}}{{27481836}} gab.com Text Molecular Structure of Aggregated Amyloid- : Insights from Solid-State Nuclear Magnetic Resonance JO: Cold Spring Harb Perspect Med http://www.kidney.de/pget.php?&tw=1&pmid=27481836 #FOAvip Amyloid-? (A?) peptides aggregate to form polymorphic amyloid fibrils and a variety of intermediate assemblies, including oligomers and protofibrils, both in vitro and in human brain tissue. Since the beginning of the 21st century, considerable progress has been made to characterize the molecular structures of A? aggregates. Full molecular structural models based primarily on data from measurements using solid-state nuclear magnetic resonance (ssNMR) have been developed for several in vitro A? fibrils and one metastable protofibril. Partial structural characterization of other aggregation intermediates has been achieved. One full structural model for fibrils derived from brain tissue has also been reported. Future work is likely to focus on additional structures from brain tissue and on further clarification of nonfibrillar A? aggregates. Twit Text FOAVip Molecular Structure of Aggregated Amyloid- : Insights from Solid-State Nuclear Magnetic Resonance ????Cold Spring Harb Perspect Med http://www.kidney.de/pget.php?&tw=1&pmid=27481836 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27481836 #FOAvip English Wikipedia <ref>{{Cite pmid|27481836}}</ref> Molecular Structure of Aggregated Amyloid-?: Insights from Solid-State Nuclear Magnetic Resonance #MMPMID27481836 Tycko R Cold Spring Harb Perspect Med 2016[Aug]; 6 (8): ä PMID27481836show ga Amyloid-? (A?) peptides aggregate to form polymorphic amyloid fibrils and a variety of intermediate assemblies, including oligomers and protofibrils, both in vitro and in human brain tissue. Since the beginning of the 21st century, considerable progress has been made to characterize the molecular structures of A? aggregates. Full molecular structural models based primarily on data from measurements using solid-state nuclear magnetic resonance (ssNMR) have been developed for several in vitro A? fibrils and one metastable protofibril. Partial structural characterization of other aggregation intermediates has been achieved. One full structural model for fibrils derived from brain tissue has also been reported. Future work is likely to focus on additional structures from brain tissue and on further clarification of nonfibrillar A? aggregates. äMolecular Structure of Aggregated Amyloid-?: Insights from Solid-State(epmc).pdf DeepDyve Pubget Overpricing