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10.3389/fnmol.2016.00029 http://scihub22266oqcxt.onion/10.3389/fnmol.2016.00029 C4840800!4840800!27147962     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       Front+Mol+Neurosci 2016 ; 9 (ä): ä Nephropedia Template TP {{tp|p=27147962|t=2016. Key Points Concerning Amyloid Infectivity and Prion-Like Neuronal Invasion |pdf=|usr=}}{{27147962}} gab.com Text Key Points Concerning Amyloid Infectivity and Prion-Like Neuronal Invasion JO: Front Mol Neurosci http://www.kidney.de/pget.php?&tw=1&pmid=27147962 #FOAvip Amyloid aggregation has been related to an increasing number of human illnesses, from Alzheimer?s and Parkinson?s diseases (AD/PD) to Creutzfeldt-Jakob disease. Commonly, only prions have been considered as infectious agents with a high capacity of propagation. However, recent publications have shown that many amyloid proteins, including amyloid ?-peptide, ?-synuclein (?-syn) and tau protein, also propagate in a ?prion-like? manner. Meanwhile, no link between propagation of pathological proteins and neurotoxicity has been demonstrated. The extremely low infectivity under natural conditions of most non-prion amyloids is far below the capacity to spread exhibited by prions. Nonetheless, it is important to elucidate the key factors that cause non-prion amyloids to become infectious agents. In recent years, important advances in our understanding of the amyloid processes of amyloid-like proteins and unrelated prions (i.e., yeast and fungal prions) have yielded essential information that can shed light on the prion phenomenon in mammals and humans. As shown in this review, recent evidence suggests that there are key factors that could dramatically modulate the prion capacity of proteins in the amyloid conformation. The concentration of nuclei, the presence of oligomers, and the toxicity, resistance and localization of these aggregates could all be key factors affecting their spread. In short, those factors that favor the high concentration of extracellular nuclei or oligomers, characterized by small size, with a low toxicity could dramatically increase prion propensity; whereas low concentrations of highly toxic intracellular amyloids, with a large size, would effectively prevent infectivity. Twit Text FOAVip Key Points Concerning Amyloid Infectivity and Prion-Like Neuronal Invasion ????Front Mol Neurosci http://www.kidney.de/pget.php?&tw=1&pmid=27147962 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27147962 #FOAvip English Wikipedia <ref>{{Cite pmid|27147962}}</ref> Key Points Concerning Amyloid Infectivity and Prion-Like Neuronal Invasion #MMPMID27147962 Espargaró A; Busquets MA; Estelrich J; Sabate R Front Mol Neurosci 2016[]; 9 (ä): ä PMID27147962show ga Amyloid aggregation has been related to an increasing number of human illnesses, from Alzheimer?s and Parkinson?s diseases (AD/PD) to Creutzfeldt-Jakob disease. Commonly, only prions have been considered as infectious agents with a high capacity of propagation. However, recent publications have shown that many amyloid proteins, including amyloid ?-peptide, ?-synuclein (?-syn) and tau protein, also propagate in a ?prion-like? manner. Meanwhile, no link between propagation of pathological proteins and neurotoxicity has been demonstrated. The extremely low infectivity under natural conditions of most non-prion amyloids is far below the capacity to spread exhibited by prions. Nonetheless, it is important to elucidate the key factors that cause non-prion amyloids to become infectious agents. In recent years, important advances in our understanding of the amyloid processes of amyloid-like proteins and unrelated prions (i.e., yeast and fungal prions) have yielded essential information that can shed light on the prion phenomenon in mammals and humans. As shown in this review, recent evidence suggests that there are key factors that could dramatically modulate the prion capacity of proteins in the amyloid conformation. The concentration of nuclei, the presence of oligomers, and the toxicity, resistance and localization of these aggregates could all be key factors affecting their spread. In short, those factors that favor the high concentration of extracellular nuclei or oligomers, characterized by small size, with a low toxicity could dramatically increase prion propensity; whereas low concentrations of highly toxic intracellular amyloids, with a large size, would effectively prevent infectivity. äKey Points Concerning Amyloid Infectivity and Prion-Like Neuronal Inva(epmc).pdf DeepDyve Pubget Overpricing