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10.1080/19491034.2015.1017167 http://scihub22266oqcxt.onion/10.1080/19491034.2015.1017167 C4615644!4615644!25793944     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nucleus 2015 ; 6 (3): 166-71 Nephropedia Template TP {{tp|p=25793944|t=2015. Phosphorylation of lamins determine their structural properties and signaling functions |pdf=|usr=}}{{25793944}} gab.com Text Phosphorylation of lamins determine their structural properties and signaling functions JO: Nucleus http://www.kidney.de/pget.php?&tw=1&pmid=25793944 #FOAvip Lamin A/C is part of the nuclear lamina, a meshwork of intermediate filaments underlying the inner nuclear membrane. The lamin network is anchoring a complex set of structural and linker proteins and is either directly or through partner proteins also associated or interacting with a number of signaling protein and transcription factors. During mitosis the nuclear lamina is dissociated by well established phosphorylation- dependent mechanisms. A-type lamins are, however, also phosphorylated during interphase. A recent study identified 20 interphase phosphorylation sites on lamin A/C and explored their functions related to lamin dynamics; movements, localization and solubility. Here we discuss these findings in the light of lamin functions in health and disease. Twit Text FOAVip Phosphorylation of lamins determine their structural properties and signaling functions ????Nucleus http://www.kidney.de/pget.php?&tw=1&pmid=25793944 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25793944 #FOAvip English Wikipedia <ref>{{Cite pmid|25793944}}</ref> Phosphorylation of lamins determine their structural properties and signaling functions #MMPMID25793944 Torvaldson E; Kochin V; Eriksson JE Nucleus 2015[]; 6 (3): 166-71 PMID25793944show ga Lamin A/C is part of the nuclear lamina, a meshwork of intermediate filaments underlying the inner nuclear membrane. The lamin network is anchoring a complex set of structural and linker proteins and is either directly or through partner proteins also associated or interacting with a number of signaling protein and transcription factors. During mitosis the nuclear lamina is dissociated by well established phosphorylation- dependent mechanisms. A-type lamins are, however, also phosphorylated during interphase. A recent study identified 20 interphase phosphorylation sites on lamin A/C and explored their functions related to lamin dynamics; movements, localization and solubility. Here we discuss these findings in the light of lamin functions in health and disease. äPhosphorylation of lamins determine their structural properties and si(epmc).pdf DeepDyve Pubget Overpricing