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10.1073/pnas.1606721113 http://scihub22266oqcxt.onion/10.1073/pnas.1606721113 C5081608!5081608!27702897     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27702897&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2016 ; 113 (42): 11853-8 Nephropedia Template TP {{tp|p=27702897|t=2016. Real-time analysis of RAG complex activity in V(D)J recombination |pdf=|usr=}}{{27702897}} gab.com Text Real-time analysis of RAG complex activity in V(D)J recombination JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=27702897 #FOAvip Recombination-activating genes 1 and 2 (RAG1/2) and high mobility group box 1 (HMGB1) create dsDNA breaks at recombination signal sequences (RSSs), initiating the variable, diversity, and joining [V(D)J] recombination pathway for antigen?receptor gene assembly. We have discovered that RAG complex binds and bends RSS DNA at the heptamer, with different binding modes for 12RSS and 23RSS substrates. Our experimentally derived binding kinetics have established that binding, bending, and synapsis precede catalysis. We have also directly observed the dynamics of the synaptic complex, revealing that RAG1/2 bending places the nonamers at nearly perpendicular orientations and that the RAG:12RSS:23RSS synaptic complex is very stable. We provide a kinetic model that integrates physical binding, bending, and synapsis steps of the RAG1/2 pathway. Twit Text FOAVip Real-time analysis of RAG complex activity in V(D)J recombination ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=27702897 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27702897 #FOAvip English Wikipedia <ref>{{Cite pmid|27702897}}</ref> Real-time analysis of RAG complex activity in V(D)J recombination #MMPMID27702897 Zagelbaum J; Shimazaki N; Esguerra ZA; Watanabe G; Lieber MR; Rothenberg E Proc Natl Acad Sci U S A 2016[Oct]; 113 (42): 11853-8 PMID27702897show ga Recombination-activating genes 1 and 2 (RAG1/2) and high mobility group box 1 (HMGB1) create dsDNA breaks at recombination signal sequences (RSSs), initiating the variable, diversity, and joining [V(D)J] recombination pathway for antigen?receptor gene assembly. We have discovered that RAG complex binds and bends RSS DNA at the heptamer, with different binding modes for 12RSS and 23RSS substrates. Our experimentally derived binding kinetics have established that binding, bending, and synapsis precede catalysis. We have also directly observed the dynamics of the synaptic complex, revealing that RAG1/2 bending places the nonamers at nearly perpendicular orientations and that the RAG:12RSS:23RSS synaptic complex is very stable. We provide a kinetic model that integrates physical binding, bending, and synapsis steps of the RAG1/2 pathway. äReal-time analysis of RAG complex activity in V(D)J recombination (epmc).pdf DeepDyve Pubget Overpricing