Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.4161/15384101.2014.947197 http://scihub22266oqcxt.onion/10.4161/15384101.2014.947197 C4614318!4614318!25486481     free     free     free Deprecated: Implicit conversion from float 213.6 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\25486481.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell+Cycle 2014 ; 13 (18): 2944-51 Nephropedia Template TP {{tp|p=25486481|t=2014. Poly(ADP-ribosyl)ation is recognized by ECT2 during mitosis |pdf=|usr=}}{{25486481}} gab.com Text Poly(ADP-ribosyl)ation is recognized by ECT2 during mitosis JO: Cell Cycle http://www.kidney.de/pget.php?&tw=1&pmid=25486481 #FOAvip Poly(ADP-ribosyl)ation is an unique posttranslational modification and required for spindle assembly and function during mitosis. However, the molecular mechanism of poly(ADP-ribose) (PAR) in mitosis remains elusive. Here, we show the evidence that PAR is recognized by ECT2, a key guanine nucleotide exchange factor in mitosis. The BRCT domain of ECT2 directly binds to PAR both in vitro and in vivo. We further found that ?-tubulin is PARylated during mitosis. PARylation of ?-tubulin is recognized by ECT2 and recruits ECT2 to mitotic spindle for completing mitosis. Taken together, our study reveals a novel mechanism by which PAR regulates mitosis. Twit Text FOAVip Poly(ADP-ribosyl)ation is recognized by ECT2 during mitosis ????Cell Cycle http://www.kidney.de/pget.php?&tw=1&pmid=25486481 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25486481 #FOAvip English Wikipedia <ref>{{Cite pmid|25486481}}</ref> Poly(ADP-ribosyl)ation is recognized by ECT2 during mitosis #MMPMID25486481 Li M; Bian C; Yu X Cell Cycle 2014[Sep]; 13 (18): 2944-51 PMID25486481show ga Poly(ADP-ribosyl)ation is an unique posttranslational modification and required for spindle assembly and function during mitosis. However, the molecular mechanism of poly(ADP-ribose) (PAR) in mitosis remains elusive. Here, we show the evidence that PAR is recognized by ECT2, a key guanine nucleotide exchange factor in mitosis. The BRCT domain of ECT2 directly binds to PAR both in vitro and in vivo. We further found that ?-tubulin is PARylated during mitosis. PARylation of ?-tubulin is recognized by ECT2 and recruits ECT2 to mitotic spindle for completing mitosis. Taken together, our study reveals a novel mechanism by which PAR regulates mitosis. äPoly(ADP-ribosyl)ation is recognized by ECT2 during mitosis (epmc).pdf DeepDyve Pubget Overpricing