Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1073/pnas.1419425111 http://scihub22266oqcxt.onion/10.1073/pnas.1419425111 C4273350!4273350!25453101     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2014 ; 111 (50): 17833-8 Nephropedia Template TP {{tp|p=25453101|t=2014. Stoichiometry and assembly of mTOR complexes revealed by single-molecule pulldown |pdf=|usr=}}{{25453101}} gab.com Text Stoichiometry and assembly of mTOR complexes revealed by single-molecule pulldown JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25453101 #FOAvip The mammalian target of rapamycin (mTOR) kinase is a central regulator of cell growth, differentiation, and metabolism. mTOR is assembled into two distinct complexes, mTORC1 and mTORC2. Using single-molecule pulldown (SiMPull), we have determined the stoichiometric composition of mTORCs under growth and stress conditions. We find that both mTORC1 and mTORC2 form obligate dimers, in which major components exist in two copies per complex. Importantly, SiMPull allowed us to distinguish complex disassembly from stoichiometry changes, providing insights into the effects of physiological conditions and the drug rapamycin on mTOR complexes. Twit Text FOAVip Stoichiometry and assembly of mTOR complexes revealed by single-molecule pulldown ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25453101 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25453101 #FOAvip English Wikipedia <ref>{{Cite pmid|25453101}}</ref> Stoichiometry and assembly of mTOR complexes revealed by single-molecule pulldown #MMPMID25453101 Jain A; Arauz E; Aggarwal V; Ikon N; Chen J; Ha T Proc Natl Acad Sci U S A 2014[Dec]; 111 (50): 17833-8 PMID25453101show ga The mammalian target of rapamycin (mTOR) kinase is a central regulator of cell growth, differentiation, and metabolism. mTOR is assembled into two distinct complexes, mTORC1 and mTORC2. Using single-molecule pulldown (SiMPull), we have determined the stoichiometric composition of mTORCs under growth and stress conditions. We find that both mTORC1 and mTORC2 form obligate dimers, in which major components exist in two copies per complex. Importantly, SiMPull allowed us to distinguish complex disassembly from stoichiometry changes, providing insights into the effects of physiological conditions and the drug rapamycin on mTOR complexes. äStoichiometry and assembly of mTOR complexes revealed by single-molecu(epmc).pdf DeepDyve Pubget Overpricing