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10.1016/j.sbi.2013.11.006 http://scihub22266oqcxt.onion/10.1016/j.sbi.2013.11.006 C4040187!4040187!24878340     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       Curr+Opin+Struct+Biol 2014 ; ä (ä): 16-24 Nephropedia Template TP {{tp|p=24878340|t=2014. Loading strategies of ring-shaped nucleic acid translocases and helicases |pdf=|usr=}}{{24878340}} gab.com Text Loading strategies of ring-shaped nucleic acid translocases and helicases JO: Curr Opin Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=24878340 #FOAvip Ring-shaped nucleic acid translocases and helicases catalyze the directed and processive movement of nucleic acid strands to support essential transactions such as replication, transcription, and chromosome partitioning. Assembled typically as hexamers, ring helicase/translocase systems use coordinated cycles of nucleoside triphosphate (NTP) hydrolysis to translocate extended DNA or RNA substrates through a central pore. Ring formation presents a topological challenge to the engagement of substrate oligonucleotides, and is frequently overcome by distinct loading strategies for shepherding specific motors onto their respective substrates. Recent structural studies that capture different loading intermediates have begun to reveal how different helicase/translocase rings either assemble around substrates or crack open to allow DNA or RNA strand entry, and how dedicated chaperones facilitate these events in some instances. Both prevailing mechanistic models and remaining knowledge gaps are discussed. Twit Text FOAVip Loading strategies of ring-shaped nucleic acid translocases and helicases ????Curr Opin Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=24878340 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24878340 #FOAvip English Wikipedia <ref>{{Cite pmid|24878340}}</ref> Loading strategies of ring-shaped nucleic acid translocases and helicases #MMPMID24878340 O?Shea VL; Berger JM Curr Opin Struct Biol 2014[Apr]; ä (ä): 16-24 PMID24878340show ga Ring-shaped nucleic acid translocases and helicases catalyze the directed and processive movement of nucleic acid strands to support essential transactions such as replication, transcription, and chromosome partitioning. Assembled typically as hexamers, ring helicase/translocase systems use coordinated cycles of nucleoside triphosphate (NTP) hydrolysis to translocate extended DNA or RNA substrates through a central pore. Ring formation presents a topological challenge to the engagement of substrate oligonucleotides, and is frequently overcome by distinct loading strategies for shepherding specific motors onto their respective substrates. Recent structural studies that capture different loading intermediates have begun to reveal how different helicase/translocase rings either assemble around substrates or crack open to allow DNA or RNA strand entry, and how dedicated chaperones facilitate these events in some instances. Both prevailing mechanistic models and remaining knowledge gaps are discussed. äLoading strategies of ring-shaped nucleic acid translocases and helica(epmc).pdf DeepDyve Pubget Overpricing