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10.1016/j.neuron.2017.03.023 http://scihub22266oqcxt.onion/10.1016/j.neuron.2017.03.023 C5595097!5595097!28384479     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28384479.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Neuron 2017 ; 94 (1): 93-107.e6 Nephropedia Template TP {{tp|p=28384479|t=2017. Mutant Huntingtin Disrupts the Nuclear Pore Complex |pdf=|usr=}}{{28384479}} gab.com Text Mutant Huntingtin Disrupts the Nuclear Pore Complex JO: Neuron http://www.kidney.de/pget.php?&tw=1&pmid=28384479 #FOAvip Huntington?s disease (HD) is caused by an expanded CAG repeat in the Huntingtin (HTT) gene. The mechanism(s) by which mutant HTT (mHTT) causes disease is unclear. Nucleocytoplasmic transport, the trafficking of macromolecules between the nucleus and cytoplasm is tightly regulated by nuclear pore complexes (NPCs) made up of nucleoporins (NUPs). Previous studies offered clues that mHTT may disrupt nucleocytoplasmic transport and a mutation of a NUP can cause HD-like pathology. Therefore, we evaluated the NPC and nucleocytoplasmic transport in multiple models of HD including mouse and fly models, neurons transfected with mHTT, HD iPSC-derived neurons and human HD brain regions. These studies revealed severe mislocalization and aggregation of NUPs and defective nucleocytoplasmic transport. HD repeat-associated non-ATG (RAN) translation proteins also disrupted nucleocytoplasmic transport. Additionally, overexpression of NUPs and treatment with drugs that prevent aberrant NUP biology also mitigated this transport defect and neurotoxicity, providing future novel therapy targets. Twit Text FOAVip Mutant Huntingtin Disrupts the Nuclear Pore Complex ????Neuron http://www.kidney.de/pget.php?&tw=1&pmid=28384479 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28384479 #FOAvip English Wikipedia <ref>{{Cite pmid|28384479}}</ref> Mutant Huntingtin Disrupts the Nuclear Pore Complex #MMPMID28384479 Grima JC; Daigle JG; Arbez N; Cunningham KC; Zhang K; Ochaba J; Geater C; Morozko E; Stocksdale J; Glatzer JC; Pham JT; Ahmed I; Peng Q; Wadhwa H; Pletnikova O; Troncoso JC; Duan W; Snyder SH; Ranum LP; Thompson LM; Lloyd TE; Ross CA; Rothstein JD Neuron 2017[Apr]; 94 (1): 93-107.e6 PMID28384479show ga Huntington?s disease (HD) is caused by an expanded CAG repeat in the Huntingtin (HTT) gene. The mechanism(s) by which mutant HTT (mHTT) causes disease is unclear. Nucleocytoplasmic transport, the trafficking of macromolecules between the nucleus and cytoplasm is tightly regulated by nuclear pore complexes (NPCs) made up of nucleoporins (NUPs). Previous studies offered clues that mHTT may disrupt nucleocytoplasmic transport and a mutation of a NUP can cause HD-like pathology. Therefore, we evaluated the NPC and nucleocytoplasmic transport in multiple models of HD including mouse and fly models, neurons transfected with mHTT, HD iPSC-derived neurons and human HD brain regions. These studies revealed severe mislocalization and aggregation of NUPs and defective nucleocytoplasmic transport. HD repeat-associated non-ATG (RAN) translation proteins also disrupted nucleocytoplasmic transport. Additionally, overexpression of NUPs and treatment with drugs that prevent aberrant NUP biology also mitigated this transport defect and neurotoxicity, providing future novel therapy targets. äMutant Huntingtin Disrupts the Nuclear Pore Complex (epmc).pdf DeepDyve Pubget Overpricing