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10.15252/embj.201592462 http://scihub22266oqcxt.onion/10.15252/embj.201592462 C4818763!4818763!26717941     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       EMBO+J 2016 ; 35 (7): 743-58 Nephropedia Template TP {{tp|p=26717941|t=2016. ATP?dependent DNA binding, unwinding, and resection by the Mre11/Rad50 complex |pdf=|usr=}}{{26717941}} gab.com Text ATP dependent DNA binding, unwinding, and resection by the Mre11/Rad50 complex JO: EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=26717941 #FOAvip ATP?dependent DNA end recognition and nucleolytic processing are central functions of the Mre11/Rad50 (MR) complex in DNA double?strand break repair. However, it is still unclear how ATP binding and hydrolysis primes the MR function and regulates repair pathway choice in cells. Here, Methanococcus jannaschii MR?ATP?S?DNA structure reveals that the partly deformed DNA runs symmetrically across central groove between two ATP?S?bound Rad50 nucleotide?binding domains. Duplex DNA cannot access the Mre11 active site in the ATP?free full?length MR complex. ATP hydrolysis drives rotation of the nucleotide?binding domain and induces the DNA melting so that the substrate DNA can access Mre11. Our findings suggest that the ATP hydrolysis?driven conformational changes in both DNA and the MR complex coordinate the melting and endonuclease activity. Twit Text FOAVip ATP dependent DNA binding, unwinding, and resection by the Mre11/Rad50 complex ????EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=26717941 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26717941 #FOAvip English Wikipedia <ref>{{Cite pmid|26717941}}</ref> ATP?dependent DNA binding, unwinding, and resection by the Mre11/Rad50 complex #MMPMID26717941 Liu Y; Sung S; Kim Y; Li F; Gwon G; Jo A; Kim A; Kim T; Song O; Lee SE; Cho Y EMBO J 2016[Apr]; 35 (7): 743-58 PMID26717941show ga ATP?dependent DNA end recognition and nucleolytic processing are central functions of the Mre11/Rad50 (MR) complex in DNA double?strand break repair. However, it is still unclear how ATP binding and hydrolysis primes the MR function and regulates repair pathway choice in cells. Here, Methanococcus jannaschii MR?ATP?S?DNA structure reveals that the partly deformed DNA runs symmetrically across central groove between two ATP?S?bound Rad50 nucleotide?binding domains. Duplex DNA cannot access the Mre11 active site in the ATP?free full?length MR complex. ATP hydrolysis drives rotation of the nucleotide?binding domain and induces the DNA melting so that the substrate DNA can access Mre11. Our findings suggest that the ATP hydrolysis?driven conformational changes in both DNA and the MR complex coordinate the melting and endonuclease activity. äATP?dependent DNA binding, unwinding, and resection by the Mre11/Rad50(epmc).pdf DeepDyve Pubget Overpricing