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10.1016/j.celrep.2014.08.009 http://scihub22266oqcxt.onion/10.1016/j.celrep.2014.08.009 C4177365!4177365!25199834     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Rep 2014 ; 8 (6): 1808-18 Nephropedia Template TP {{tp|p=25199834|t=2014. Basal activity of a PARP1-NuA4 complex varies dramatically across cancer cell lines |pdf=|usr=}}{{25199834}} gab.com Text Basal activity of a PARP1-NuA4 complex varies dramatically across cancer cell lines JO: Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=25199834 #FOAvip Poly(ADP-ribose) polymerases (PARPs) catalyze poly(ADP-ribose) addition onto proteins, an important post-translational modification involved in transcription, DNA damage repair, and stem cell identity. Previous studies established the activation of PARP1 in response to DNA damage, but little is known about PARP1 regulation outside of DNA repair. We developed a new assay for measuring PARP activity in cell lysates, and found that the basal activity of PARP1 was highly variable across breast cancer cell lines, independent of DNA damage. Sucrose gradient fractionation demonstrated that PARP1 existed in at least three biochemically distinct states in both high and low activity lines. A newly discovered complex containing the NuA4 chromatin remodeling complex and PARP1 was responsible for high basal PARP1 activity, and NuA4 subunits were required for this activity. These findings present a new pathway for PARP1 activation and a direct link between PARP1 and chromatin remodeling outside of the DNA damage response. Twit Text FOAVip Basal activity of a PARP1-NuA4 complex varies dramatically across cancer cell lines ????Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=25199834 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25199834 #FOAvip English Wikipedia <ref>{{Cite pmid|25199834}}</ref> Basal activity of a PARP1-NuA4 complex varies dramatically across cancer cell lines #MMPMID25199834 Krukenberg KA; Jiang R; Steen JA; Mitchison TJ Cell Rep 2014[Sep]; 8 (6): 1808-18 PMID25199834show ga Poly(ADP-ribose) polymerases (PARPs) catalyze poly(ADP-ribose) addition onto proteins, an important post-translational modification involved in transcription, DNA damage repair, and stem cell identity. Previous studies established the activation of PARP1 in response to DNA damage, but little is known about PARP1 regulation outside of DNA repair. We developed a new assay for measuring PARP activity in cell lysates, and found that the basal activity of PARP1 was highly variable across breast cancer cell lines, independent of DNA damage. Sucrose gradient fractionation demonstrated that PARP1 existed in at least three biochemically distinct states in both high and low activity lines. A newly discovered complex containing the NuA4 chromatin remodeling complex and PARP1 was responsible for high basal PARP1 activity, and NuA4 subunits were required for this activity. These findings present a new pathway for PARP1 activation and a direct link between PARP1 and chromatin remodeling outside of the DNA damage response. äBasal activity of a PARP1-NuA4 complex varies dramatically across canc(epmc).pdf DeepDyve Pubget Overpricing