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.

10.1091/mbc.E14-09-1382 http://scihub22266oqcxt.onion/10.1091/mbc.E14-09-1382 C4325844!4325844!25518939     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Mol+Biol+Cell 2015 ; 26 (4): 751-61 Nephropedia Template TP {{tp|p=25518939|t=2015. PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity |pdf=|usr=}}{{25518939}} gab.com Text PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity JO: Mol Biol Cell http://www.kidney.de/pget.php?&tw=1&pmid=25518939 #FOAvip A PAR complex (PAR3, PAR6, and aPKC) plays a central role in the establishment of cell polarity. Another polarity protein, CLASP2, binds directly with PAR3 and is phosphorylated by aPKC. Through CLASP2 phosphorylation, aPKC and PAR3 regulate the localization of CLASP2 to the trans-Golgi network, thereby controlling the Golgi organization. Twit Text FOAVip PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity ????Mol Biol Cell http://www.kidney.de/pget.php?&tw=1&pmid=25518939 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25518939 #FOAvip English Wikipedia <ref>{{Cite pmid|25518939}}</ref> PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity #MMPMID25518939 Matsui T; Watanabe T; Matsuzawa K; Kakeno M; Okumura N; Sugiyama I; Itoh N; Kaibuchi K Mol Biol Cell 2015[Feb]; 26 (4): 751-61 PMID25518939show ga A PAR complex (PAR3, PAR6, and aPKC) plays a central role in the establishment of cell polarity. Another polarity protein, CLASP2, binds directly with PAR3 and is phosphorylated by aPKC. Through CLASP2 phosphorylation, aPKC and PAR3 regulate the localization of CLASP2 to the trans-Golgi network, thereby controlling the Golgi organization. äPAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylati(epmc).pdf DeepDyve Pubget Overpricing