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10.1242/jcs.194241 http://scihub22266oqcxt.onion/10.1242/jcs.194241 C5278670!5278670!28049716     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 269.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Cell+Sci 2017 ; 130 (2): 325-31 Nephropedia Template TP {{tp|p=28049716|t=2017. Sideroflexin 3 is an ?-synuclein-dependent mitochondrial protein that regulates synaptic morphology |pdf=|usr=}}{{28049716}} gab.com Text Sideroflexin 3 is an -synuclein-dependent mitochondrial protein that regulates synaptic morphology JO: J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=28049716 #FOAvip ?-Synuclein plays a central role in Parkinson's disease, where it contributes to the vulnerability of synapses to degeneration. However, the downstream mechanisms through which ?-synuclein controls synaptic stability and degeneration are not fully understood. Here, comparative proteomics on synapses isolated from ?-synuclein?/? mouse brain identified mitochondrial proteins as primary targets of ?-synuclein, revealing 37 mitochondrial proteins not previously linked to ?-synuclein or neurodegeneration pathways. Of these, sideroflexin 3 (SFXN3) was found to be a mitochondrial protein localized to the inner mitochondrial membrane. Loss of SFXN3 did not disturb mitochondrial electron transport chain function in mouse synapses, suggesting that its function in mitochondria is likely to be independent of canonical bioenergetic pathways. In contrast, experimental manipulation of SFXN3 levels disrupted synaptic morphology at the Drosophila neuromuscular junction. These results provide novel insights into ?-synuclein-dependent pathways, highlighting an important influence on mitochondrial proteins at the synapse, including SFXN3. We also identify SFXN3 as a new mitochondrial protein capable of regulating synaptic morphology in vivo. Twit Text FOAVip Sideroflexin 3 is an -synuclein-dependent mitochondrial protein that regulates synaptic morphology ????J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=28049716 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28049716 #FOAvip English Wikipedia <ref>{{Cite pmid|28049716}}</ref> Sideroflexin 3 is an ?-synuclein-dependent mitochondrial protein that regulates synaptic morphology #MMPMID28049716 Amorim IS; Graham LC; Carter RN; Morton NM; Hammachi F; Kunath T; Pennetta G; Carpanini SM; Manson JC; Lamont DJ; Wishart TM; Gillingwater TH J Cell Sci 2017[Jan]; 130 (2): 325-31 PMID28049716show ga ?-Synuclein plays a central role in Parkinson's disease, where it contributes to the vulnerability of synapses to degeneration. However, the downstream mechanisms through which ?-synuclein controls synaptic stability and degeneration are not fully understood. Here, comparative proteomics on synapses isolated from ?-synuclein?/? mouse brain identified mitochondrial proteins as primary targets of ?-synuclein, revealing 37 mitochondrial proteins not previously linked to ?-synuclein or neurodegeneration pathways. Of these, sideroflexin 3 (SFXN3) was found to be a mitochondrial protein localized to the inner mitochondrial membrane. Loss of SFXN3 did not disturb mitochondrial electron transport chain function in mouse synapses, suggesting that its function in mitochondria is likely to be independent of canonical bioenergetic pathways. In contrast, experimental manipulation of SFXN3 levels disrupted synaptic morphology at the Drosophila neuromuscular junction. These results provide novel insights into ?-synuclein-dependent pathways, highlighting an important influence on mitochondrial proteins at the synapse, including SFXN3. We also identify SFXN3 as a new mitochondrial protein capable of regulating synaptic morphology in vivo. äSideroflexin 3 is an ?-synuclein-dependent mitochondrial protein that (epmc).pdf DeepDyve Pubget Overpricing