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10.1016/j.cell.2015.03.052 http://scihub22266oqcxt.onion/10.1016/j.cell.2015.03.052 C4432480!4432480!25957688     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell 2015 ; 161 (4): 845-57 Nephropedia Template TP {{tp|p=25957688|t=2015. Structural snapshots of actively translating human ribosomes |pdf=|usr=}}{{25957688}} gab.com Text Structural snapshots of actively translating human ribosomes JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=25957688 #FOAvip Macromolecular machines, such as the ribosome, undergo large-scale conformational changes during their functional cycles. While their mode of action is often compared to that of mechanical machines, a crucial difference is that at the molecular dimension, thermodynamic effects dominate functional cycles, with proteins fluctuating stochastically between functional states defined by energetic minima on an energy landscape. Here, we have used cryo-electron microscopy to image ex vivo-derived human polysomes as a source of actively translating ribosomes. Multiparticle refinement and three-dimensional variability analysis allowed us to visualize a variety of native translation intermediates. Significantly populated states include not only elongation cycle intermediates in pre- and post-translocational states, but also eEF1A-containing decoding and termination/recycling complexes. Focusing on the post-translocational state, we extended this assessment to the single-residue level, uncovering striking details of ribosome-ligand interactions and identifying both static and functionally important dynamic elements. Twit Text FOAVip Structural snapshots of actively translating human ribosomes ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=25957688 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25957688 #FOAvip English Wikipedia <ref>{{Cite pmid|25957688}}</ref> Structural snapshots of actively translating human ribosomes #MMPMID25957688 Behrmann E; Loerke J; Budkevich TV; Yamamoto K; Schmidt A; Penczek PA; Vos MR; Bürger J; Mielke T; Scheerer P; Spahn CM Cell 2015[May]; 161 (4): 845-57 PMID25957688show ga Macromolecular machines, such as the ribosome, undergo large-scale conformational changes during their functional cycles. While their mode of action is often compared to that of mechanical machines, a crucial difference is that at the molecular dimension, thermodynamic effects dominate functional cycles, with proteins fluctuating stochastically between functional states defined by energetic minima on an energy landscape. Here, we have used cryo-electron microscopy to image ex vivo-derived human polysomes as a source of actively translating ribosomes. Multiparticle refinement and three-dimensional variability analysis allowed us to visualize a variety of native translation intermediates. Significantly populated states include not only elongation cycle intermediates in pre- and post-translocational states, but also eEF1A-containing decoding and termination/recycling complexes. Focusing on the post-translocational state, we extended this assessment to the single-residue level, uncovering striking details of ribosome-ligand interactions and identifying both static and functionally important dynamic elements. äStructural snapshots of actively translating human ribosomes (epmc).pdf DeepDyve Pubget Overpricing