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10.1038/nature14471 http://scihub22266oqcxt.onion/10.1038/nature14471 C4608048!4608048!26083744     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       Nature 2015 ; 522 (7557): 450-4 Nephropedia Template TP {{tp|p=26083744|t=2015. Atomic structure of the APC/C and its mechanism of protein ubiquitination |pdf=|usr=}}{{26083744}} gab.com Text Atomic structure of the APC/C and its mechanism of protein ubiquitination JO: Nature http://www.kidney.de/pget.php?&tw=1&pmid=26083744 #FOAvip The anaphase-promoting complex (APC/C) is a multimeric RING E3 ubiquitin ligase that controls chromosome segregation and mitotic exit. Its regulation by coactivator subunits, phosphorylation, the mitotic checkpoint complex, and interphase inhibitor Emi1 ensures the correct order and timing of distinct cell cycle transitions. Here, we used cryo-electron microscopy to determine atomic structures of APC/C-coactivator complexes with either Emi1 or a UbcH10-ubiquitin conjugate. These structures define the architecture of all APC/C subunits, the position of the catalytic module, and explain how Emi1 mediates inhibition of the two E2s UbcH10 and Ube2S. Definition of Cdh1 interactions with the APC/C indicates how they are antagonized by Cdh1 phosphorylation. The structure of the APC/C with UbcH10-ubiquitin reveals insights into the initiating ubiquitination reaction. Our results provide a quantitative framework for the design of experiments to further investigate APC/C functions in vivo. Twit Text FOAVip Atomic structure of the APC/C and its mechanism of protein ubiquitination ????Nature http://www.kidney.de/pget.php?&tw=1&pmid=26083744 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26083744 #FOAvip English Wikipedia <ref>{{Cite pmid|26083744}}</ref> Atomic structure of the APC/C and its mechanism of protein ubiquitination #MMPMID26083744 Chang L; Zhang Z; Yang J; McLaughlin SH; Barford D Nature 2015[Jun]; 522 (7557): 450-4 PMID26083744show ga The anaphase-promoting complex (APC/C) is a multimeric RING E3 ubiquitin ligase that controls chromosome segregation and mitotic exit. Its regulation by coactivator subunits, phosphorylation, the mitotic checkpoint complex, and interphase inhibitor Emi1 ensures the correct order and timing of distinct cell cycle transitions. Here, we used cryo-electron microscopy to determine atomic structures of APC/C-coactivator complexes with either Emi1 or a UbcH10-ubiquitin conjugate. These structures define the architecture of all APC/C subunits, the position of the catalytic module, and explain how Emi1 mediates inhibition of the two E2s UbcH10 and Ube2S. Definition of Cdh1 interactions with the APC/C indicates how they are antagonized by Cdh1 phosphorylation. The structure of the APC/C with UbcH10-ubiquitin reveals insights into the initiating ubiquitination reaction. Our results provide a quantitative framework for the design of experiments to further investigate APC/C functions in vivo. äAtomic structure of the APC/C and its mechanism of protein ubiquitinat(epmc).pdf DeepDyve Pubget Overpricing