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10.3390/biom3010001 http://scihub22266oqcxt.onion/10.3390/biom3010001 C4030884!4030884 !24970154     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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\24970154 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biomolecules 2012 ; 3 (1 ): 1-17 Nephropedia Template TP {{tp|p=24970154 |t=2012. Molecular Insights into Poly(ADP-ribose) Recognition and Processing |pdf=|usr=}}{{24970154 }} gab.com Text Molecular Insights into Poly(ADP-ribose) Recognition and Processing JO: Biomolecules http://www.kidney.de/pget.php?&tw=1&pmid=24970154 #FOAvip Poly(ADP-ribosyl)ation is a post-translational protein modification involved in the regulation of important cellular functions including DNA repair, transcription, mitosis and apoptosis. The amount of poly(ADP-ribosyl)ation (PAR) in cells reflects the balance of synthesis, mediated by the PARP protein family, and degradation, which is catalyzed by a glycohydrolase, PARG. Many of the proteins mediating PAR metabolism possess specialised high affinity PAR-binding modules that allow the efficient sensing or processing of the PAR signal. The identification of four such PAR-binding modules and the characterization of a number of proteins utilising these elements during the last decade has provided important insights into how PAR regulates different cellular activities. The macrodomain represents a unique PAR-binding module which is, in some instances, known to possess enzymatic activity on ADP-ribose derivatives (in addition to PAR-binding). The most recently discovered example for this is the PARG protein, and several available PARG structures have provided an understanding into how the PARG macrodomain evolved into a major enzyme that maintains PAR homeostasis in living cells. Twit Text FOAVip Molecular Insights into Poly(ADP-ribose) Recognition and Processing ????Biomolecules http://www.kidney.de/pget.php?&tw=1&pmid=24970154 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24970154 #FOAvip English Wikipedia <ref>{{Cite pmid|24970154 }}</ref> Molecular Insights into Poly(ADP-ribose) Recognition and Processing #MMPMID24970154 Zaja R ; Miko? A ; Barkauskaite E ; Ahel I Biomolecules 2012[Dec]; 3 (1 ): 1-17 PMID24970154 show ga Poly(ADP-ribosyl)ation is a post-translational protein modification involved in the regulation of important cellular functions including DNA repair, transcription, mitosis and apoptosis. The amount of poly(ADP-ribosyl)ation (PAR) in cells reflects the balance of synthesis, mediated by the PARP protein family, and degradation, which is catalyzed by a glycohydrolase, PARG. Many of the proteins mediating PAR metabolism possess specialised high affinity PAR-binding modules that allow the efficient sensing or processing of the PAR signal. The identification of four such PAR-binding modules and the characterization of a number of proteins utilising these elements during the last decade has provided important insights into how PAR regulates different cellular activities. The macrodomain represents a unique PAR-binding module which is, in some instances, known to possess enzymatic activity on ADP-ribose derivatives (in addition to PAR-binding). The most recently discovered example for this is the PARG protein, and several available PARG structures have provided an understanding into how the PARG macrodomain evolved into a major enzyme that maintains PAR homeostasis in living cells. äMolecular Insights into Poly(ADP-ribose) Recognition and Processing (epmc).pdf DeepDyve Pubget Overpricing