Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1016/j.neuron.2015.03.017 http://scihub22266oqcxt.onion/10.1016/j.neuron.2015.03.017 C4425266!4425266!25950632     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       Neuron 2015 ; 86 (3): 632-45 Nephropedia Template TP {{tp|p=25950632|t=2015. Amyloid Polymorphism: Structural Basis and Neurobiological Relevance |pdf=|usr=}}{{25950632}} gab.com Text Amyloid Polymorphism: Structural Basis and Neurobiological Relevance JO: Neuron http://www.kidney.de/pget.php?&tw=1&pmid=25950632 #FOAvip Our understanding of the molecular structures of amyloid fibrils that are associated with neurodegenerative diseases, of mechanisms by which disease-associated peptides and proteins aggregate into fibrils, and of structural properties of aggregation intermediates has advanced considerably in recent years. Detailed molecular structural models for certain fibrils and aggregation intermediates are now available. It is now well established that amyloid fibrils are generally polymorphic at the molecular level, with a given peptide or protein being capable of forming a variety of distinct, self-propagating fibril structures. Recent results from structural studies and from studies involving cell cultures, transgenic animals, and human tissue provide initial evidence that molecular structural variations in amyloid fibrils and related aggregates may correlate with or even produce variations in disease development. This article reviews our current knowledge of the structural and mechanistic aspects of amyloid formation, as well as current evidence for the biological relevance of structural variations. Twit Text FOAVip Amyloid Polymorphism: Structural Basis and Neurobiological Relevance ????Neuron http://www.kidney.de/pget.php?&tw=1&pmid=25950632 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25950632 #FOAvip English Wikipedia <ref>{{Cite pmid|25950632}}</ref> Amyloid Polymorphism: Structural Basis and Neurobiological Relevance #MMPMID25950632 Tycko R Neuron 2015[May]; 86 (3): 632-45 PMID25950632show ga Our understanding of the molecular structures of amyloid fibrils that are associated with neurodegenerative diseases, of mechanisms by which disease-associated peptides and proteins aggregate into fibrils, and of structural properties of aggregation intermediates has advanced considerably in recent years. Detailed molecular structural models for certain fibrils and aggregation intermediates are now available. It is now well established that amyloid fibrils are generally polymorphic at the molecular level, with a given peptide or protein being capable of forming a variety of distinct, self-propagating fibril structures. Recent results from structural studies and from studies involving cell cultures, transgenic animals, and human tissue provide initial evidence that molecular structural variations in amyloid fibrils and related aggregates may correlate with or even produce variations in disease development. This article reviews our current knowledge of the structural and mechanistic aspects of amyloid formation, as well as current evidence for the biological relevance of structural variations. äAmyloid Polymorphism: Structural Basis and Neurobiological Relevance (epmc).pdf DeepDyve Pubget Overpricing