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10.1371/journal.pgen.1005367 http://scihub22266oqcxt.onion/10.1371/journal.pgen.1005367 C4489885!4489885!26134849     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26134849&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 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       PLoS+Genet 2015 ; 11 (7): ä Nephropedia Template TP {{tp|p=26134849|t=2015. SAMHD1 Inhibits LINE-1 Retrotransposition by Promoting Stress Granule Formation |pdf=|usr=}}{{26134849}} gab.com Text SAMHD1 Inhibits LINE-1 Retrotransposition by Promoting Stress Granule Formation JO: PLoS Genet http://www.kidney.de/pget.php?&tw=1&pmid=26134849 #FOAvip The SAM domain and HD domain containing protein 1 (SAMHD1) inhibits retroviruses, DNA viruses and long interspersed element 1 (LINE-1). Given that in dividing cells, SAMHD1 loses its antiviral function yet still potently restricts LINE-1, we propose that, instead of blocking viral DNA synthesis by virtue of its dNTP triphosphohydrolase activity, SAMHD1 may exploit a different mechanism to control LINE-1. Here, we report a new activity of SAMHD1 in promoting cellular stress granule assembly, which correlates with increased phosphorylation of eIF2? and diminished eIF4A/eIF4G interaction. This function of SAMHD1 enhances sequestration of LINE-1 RNP in stress granules and consequent blockade to LINE-1 retrotransposition. In support of this new mechanism of action, depletion of stress granule marker proteins G3BP1 or TIA1 abrogates stress granule formation and overcomes SAMHD1 inhibition of LINE-1. Together, these data reveal a new mechanism for SAMHD1 to control LINE-1 by activating cellular stress granule pathway. Twit Text FOAVip SAMHD1 Inhibits LINE-1 Retrotransposition by Promoting Stress Granule Formation ????PLoS Genet http://www.kidney.de/pget.php?&tw=1&pmid=26134849 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26134849 #FOAvip English Wikipedia <ref>{{Cite pmid|26134849}}</ref> SAMHD1 Inhibits LINE-1 Retrotransposition by Promoting Stress Granule Formation #MMPMID26134849 Hu S; Li J; Xu F; Mei S; Le Duff Y; Yin L; Pang X; Cen S; Jin Q; Liang C; Guo F PLoS Genet 2015[Jul]; 11 (7): ä PMID26134849show ga The SAM domain and HD domain containing protein 1 (SAMHD1) inhibits retroviruses, DNA viruses and long interspersed element 1 (LINE-1). Given that in dividing cells, SAMHD1 loses its antiviral function yet still potently restricts LINE-1, we propose that, instead of blocking viral DNA synthesis by virtue of its dNTP triphosphohydrolase activity, SAMHD1 may exploit a different mechanism to control LINE-1. Here, we report a new activity of SAMHD1 in promoting cellular stress granule assembly, which correlates with increased phosphorylation of eIF2? and diminished eIF4A/eIF4G interaction. This function of SAMHD1 enhances sequestration of LINE-1 RNP in stress granules and consequent blockade to LINE-1 retrotransposition. In support of this new mechanism of action, depletion of stress granule marker proteins G3BP1 or TIA1 abrogates stress granule formation and overcomes SAMHD1 inhibition of LINE-1. Together, these data reveal a new mechanism for SAMHD1 to control LINE-1 by activating cellular stress granule pathway. äSAMHD1 Inhibits LINE-1 Retrotransposition by Promoting Stress Granule (epmc).pdf DeepDyve Pubget Overpricing