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10.1038/srep23116 http://scihub22266oqcxt.onion/10.1038/srep23116 C4794800!4794800 !26984067     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 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\26984067 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Sci+Rep 2016 ; 6 (ä): 23116 Nephropedia Template TP {{tp|p=26984067 |t=2016. Functionally different ?-synuclein inclusions yield insight into Parkinson s disease pathology |pdf=|usr=}}{{26984067 }} gab.com Text Functionally different -synuclein inclusions yield insight into Parkinson s disease pathology JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26984067 #FOAvip The formation of ?-synuclein (?-S) amyloid aggregates, called Lewy bodies (LBs), is a hallmark of Parkinson's disease (PD). The function of LBs in the disease process is however still unclear; they have been associated with both neuroprotection and toxicity. To obtain insight into this contradiction, we induced the formation of ?-S inclusions, using three different induction methods in SH-SY5Y cells and rat-derived primary neuronal cells. Using confocal and STED microscopy we observed induction-dependent differences in ?-S inclusion morphology, location and function. The aggregation of ?-S in functionally different compartments correlates with the toxicity of the induction method measured in viability assays. The most cytotoxic treatment largely correlates with the formation of proteasome-associated, juxta-nuclear inclusions. With less toxic methods cytosolic deposits that are not associated with the proteasome are more prevalent. The distribution of ?-S over at least two different types of inclusions is not limited to cell models, but is also observed in primary neuronal cells and in human mesencephalon. The existence of functionally different LBs, in vivo and in vitro, gives important insights in the impact of Lewy Body formation on neuronal functioning and may thereby provide a platform for discovering therapeutics. Twit Text FOAVip Functionally different -synuclein inclusions yield insight into Parkinson s disease pathology ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26984067 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26984067 #FOAvip English Wikipedia <ref>{{Cite pmid|26984067 }}</ref> Functionally different ?-synuclein inclusions yield insight into Parkinson s disease pathology #MMPMID26984067 Raiss CC ; Braun TS ; Konings IB ; Grabmayr H ; Hassink GC ; Sidhu A ; le Feber J ; Bausch AR ; Jansen C ; Subramaniam V ; Claessens MM Sci Rep 2016[Mar]; 6 (ä): 23116 PMID26984067 show ga The formation of ?-synuclein (?-S) amyloid aggregates, called Lewy bodies (LBs), is a hallmark of Parkinson's disease (PD). The function of LBs in the disease process is however still unclear; they have been associated with both neuroprotection and toxicity. To obtain insight into this contradiction, we induced the formation of ?-S inclusions, using three different induction methods in SH-SY5Y cells and rat-derived primary neuronal cells. Using confocal and STED microscopy we observed induction-dependent differences in ?-S inclusion morphology, location and function. The aggregation of ?-S in functionally different compartments correlates with the toxicity of the induction method measured in viability assays. The most cytotoxic treatment largely correlates with the formation of proteasome-associated, juxta-nuclear inclusions. With less toxic methods cytosolic deposits that are not associated with the proteasome are more prevalent. The distribution of ?-S over at least two different types of inclusions is not limited to cell models, but is also observed in primary neuronal cells and in human mesencephalon. The existence of functionally different LBs, in vivo and in vitro, gives important insights in the impact of Lewy Body formation on neuronal functioning and may thereby provide a platform for discovering therapeutics. |Amyloid/metabolism [MESH] |Animals [MESH] |Cells, Cultured [MESH] |Green Fluorescent Proteins/genetics/metabolism [MESH] |Humans [MESH] |Lewy Bodies/*metabolism [MESH] |Mesencephalon/cytology/metabolism [MESH] |Microscopy, Atomic Force [MESH] |Microscopy, Confocal [MESH] |Neurons/cytology/metabolism [MESH] |Parkinson Disease/metabolism/*pathology [MESH] |Proteasome Endopeptidase Complex/metabolism [MESH] |Protein Aggregates [MESH] |Rats [MESH] |Rats, Wistar [MESH] |Recombinant Fusion Proteins/biosynthesis/genetics [MESH] |Transfection [MESH]Functionally different ?-synuclein inclusions yield insight into Parki(epmc).pdf DeepDyve Pubget Overpricing