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10.1038/srep43577 http://scihub22266oqcxt.onion/10.1038/srep43577 C5327471!5327471 !28240273     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28240273 &cmd=llinks): Failed to open stream: HTTP request failed! 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Amyloid plaque structure and cell surface interactions of ?-amyloid fibrils revealed by electron tomography |pdf=|usr=}}{{28240273 }} gab.com Text Amyloid plaque structure and cell surface interactions of -amyloid fibrils revealed by electron tomography JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28240273 #FOAvip The deposition of amyloid fibrils as plaques is a key feature of several neurodegenerative diseases including in particular Alzheimer's. This disease is characterized, if not provoked, by amyloid aggregates formed from A? peptide that deposit inside the brain or are toxic to neuronal cells. We here used scanning transmission electron microscopy (STEM) to determine the fibril network structure and interactions of A? fibrils within a cell culture model of Alzheimer's disease. STEM images taken from the formed A? amyloid deposits revealed three main types of fibril network structures, termed amorphous meshwork, fibril bundle and amyloid star. All three were infiltrated by different types of lipid inclusions from small-sized exosome-like structures (50-100?nm diameter) to large-sized extracellular vesicles (up to 300?nm). The fibrils also presented strong interactions with the surrounding cells such that fibril bundles extended into tubular invaginations of the plasma membrane. Amyloid formation in the cell model was previously found to have an intracellular origin and we show here that it functionally destroys the integrity of the intracellular membranes as it leads to lysosomal leakage. These data provide a mechanistic link to explain why intracellular fibril formation is toxic to the cell. Twit Text FOAVip Amyloid plaque structure and cell surface interactions of -amyloid fibrils revealed by electron tomography ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28240273 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28240273 #FOAvip English Wikipedia <ref>{{Cite pmid|28240273 }}</ref> Amyloid plaque structure and cell surface interactions of ?-amyloid fibrils revealed by electron tomography #MMPMID28240273 Han S ; Kollmer M ; Markx D ; Claus S ; Walther P ; Fändrich M Sci Rep 2017[Feb]; 7 (ä): 43577 PMID28240273 show ga The deposition of amyloid fibrils as plaques is a key feature of several neurodegenerative diseases including in particular Alzheimer's. This disease is characterized, if not provoked, by amyloid aggregates formed from A? peptide that deposit inside the brain or are toxic to neuronal cells. We here used scanning transmission electron microscopy (STEM) to determine the fibril network structure and interactions of A? fibrils within a cell culture model of Alzheimer's disease. STEM images taken from the formed A? amyloid deposits revealed three main types of fibril network structures, termed amorphous meshwork, fibril bundle and amyloid star. All three were infiltrated by different types of lipid inclusions from small-sized exosome-like structures (50-100?nm diameter) to large-sized extracellular vesicles (up to 300?nm). The fibrils also presented strong interactions with the surrounding cells such that fibril bundles extended into tubular invaginations of the plasma membrane. Amyloid formation in the cell model was previously found to have an intracellular origin and we show here that it functionally destroys the integrity of the intracellular membranes as it leads to lysosomal leakage. These data provide a mechanistic link to explain why intracellular fibril formation is toxic to the cell. |Alzheimer Disease/metabolism [MESH] |Amyloid beta-Peptides/metabolism [MESH] |Amyloid/*metabolism/*ultrastructure [MESH] |Cell Membrane/*metabolism/ultrastructure [MESH] |Cell Survival [MESH] |Cells, Cultured [MESH] |Electron Microscope Tomography [MESH] |Humans [MESH] |Lipids [MESH] |Plaque, Amyloid/*metabolism/pathology/*ultrastructure [MESH] |Protein Aggregates [MESH]Amyloid plaque structure and cell surface interactions of ?-amyloid fi(epmc).pdf DeepDyve Pubget Overpricing