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10.1371/journal.pone.0140248 http://scihub22266oqcxt.onion/10.1371/journal.pone.0140248 C4596857!4596857!26444430     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26444430&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       PLoS+One 2015 ; 10 (10): ä Nephropedia Template TP {{tp|p=26444430|t=2015. Inflammation Induces TDP-43 Mislocalization and Aggregation |pdf=|usr=}}{{26444430}} gab.com Text Inflammation Induces TDP-43 Mislocalization and Aggregation JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=26444430 #FOAvip TAR DNA-binding protein 43 (TDP-43) is a major component in aggregates of ubiquitinated proteins in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). Here we report that lipopolysaccharide (LPS)-induced inflammation can promote TDP-43 mislocalization and aggregation. In culture, microglia and astrocytes exhibited TDP-43 mislocalization after exposure to LPS. Likewise, treatment of the motoneuron-like NSC-34 cells with TNF-alpha (TNF-?) increased the cytoplasmic levels of TDP-43. In addition, the chronic intraperitoneal injection of LPS at a dose of 1mg/kg in TDP-43A315T transgenic mice exacerbated the pathological TDP-43 accumulation in the cytoplasm of spinal motor neurons and it enhanced the levels of TDP-43 aggregation. These results suggest that inflammation may contribute to development or exacerbation of TDP-43 proteinopathies in neurodegenerative disorders. Twit Text FOAVip Inflammation Induces TDP-43 Mislocalization and Aggregation ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=26444430 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26444430 #FOAvip English Wikipedia <ref>{{Cite pmid|26444430}}</ref> Inflammation Induces TDP-43 Mislocalization and Aggregation #MMPMID26444430 Correia AS; Patel P; Dutta K; Julien JP PLoS One 2015[]; 10 (10): ä PMID26444430show ga TAR DNA-binding protein 43 (TDP-43) is a major component in aggregates of ubiquitinated proteins in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). Here we report that lipopolysaccharide (LPS)-induced inflammation can promote TDP-43 mislocalization and aggregation. In culture, microglia and astrocytes exhibited TDP-43 mislocalization after exposure to LPS. Likewise, treatment of the motoneuron-like NSC-34 cells with TNF-alpha (TNF-?) increased the cytoplasmic levels of TDP-43. In addition, the chronic intraperitoneal injection of LPS at a dose of 1mg/kg in TDP-43A315T transgenic mice exacerbated the pathological TDP-43 accumulation in the cytoplasm of spinal motor neurons and it enhanced the levels of TDP-43 aggregation. These results suggest that inflammation may contribute to development or exacerbation of TDP-43 proteinopathies in neurodegenerative disorders. äInflammation Induces TDP-43 Mislocalization and Aggregation (epmc).pdf DeepDyve Pubget Overpricing