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.

10.1074/jbc.M116.730218 http://scihub22266oqcxt.onion/10.1074/jbc.M116.730218 C5076525!5076525!27528606     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 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       J+Biol+Chem 2016 ; 291 (40): 21171-83 Nephropedia Template TP {{tp|p=27528606|t=2016. Recognition Elements in the Histone H3 and H4 Tails for Seven Different Importins* |pdf=|usr=}}{{27528606}} gab.com Text Recognition Elements in the Histone H3 and H4 Tails for Seven Different Importins* JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=27528606 #FOAvip N-terminal tails of histones H3 and H4 are known to bind several different Importins to import the histones into the cell nucleus. However, it is not known what binding elements in the histone tails are recognized by the individual Importins. Biochemical studies of H3 and H4 tails binding to seven Importins, Imp?, Kap?2, Imp4, Imp5, Imp7, Imp9, and Imp?, show the H3 tail binding more tightly than the H4 tail. The H3 tail binds Kap?2 and Imp5 with KD values of 77 and 57 nm, respectively, and binds the other five Importins more weakly. Mutagenic analysis shows H3 tail residues 11?27 to be the sole binding segment for Imp?, Kap?2, and Imp4. However, Imp5, Imp7, Imp9, and Imp? bind two separate elements in the H3 tail: the segment at residues 11?27 and an isoleucine-lysine nuclear localization signal (IK-NLS) motif at residues 35?40. The H4 tail also uses either one or two basic segments to bind the same set of Importins with a similar trend of relative affinities as the H3 tail, albeit at least 10-fold weaker. Of the many lysine residues in the H3 and H4 tails, only acetylation of the H3 Lys14 substantially decreased binding to several Importins. Lastly, we show that, in addition to the N-terminal tails, the histone fold domains of H3 and H4 and/or the histone chaperone Asf1b are important for Importin-histone recognition. Twit Text FOAVip Recognition Elements in the Histone H3 and H4 Tails for Seven Different Importins* ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=27528606 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27528606 #FOAvip English Wikipedia <ref>{{Cite pmid|27528606}}</ref> Recognition Elements in the Histone H3 and H4 Tails for Seven Different Importins* #MMPMID27528606 Soniat M; Ca?atay T; Chook YM J Biol Chem 2016[Sep]; 291 (40): 21171-83 PMID27528606show ga N-terminal tails of histones H3 and H4 are known to bind several different Importins to import the histones into the cell nucleus. However, it is not known what binding elements in the histone tails are recognized by the individual Importins. Biochemical studies of H3 and H4 tails binding to seven Importins, Imp?, Kap?2, Imp4, Imp5, Imp7, Imp9, and Imp?, show the H3 tail binding more tightly than the H4 tail. The H3 tail binds Kap?2 and Imp5 with KD values of 77 and 57 nm, respectively, and binds the other five Importins more weakly. Mutagenic analysis shows H3 tail residues 11?27 to be the sole binding segment for Imp?, Kap?2, and Imp4. However, Imp5, Imp7, Imp9, and Imp? bind two separate elements in the H3 tail: the segment at residues 11?27 and an isoleucine-lysine nuclear localization signal (IK-NLS) motif at residues 35?40. The H4 tail also uses either one or two basic segments to bind the same set of Importins with a similar trend of relative affinities as the H3 tail, albeit at least 10-fold weaker. Of the many lysine residues in the H3 and H4 tails, only acetylation of the H3 Lys14 substantially decreased binding to several Importins. Lastly, we show that, in addition to the N-terminal tails, the histone fold domains of H3 and H4 and/or the histone chaperone Asf1b are important for Importin-histone recognition. äRecognition Elements in the Histone H3 and H4 Tails for Seven Differen(epmc).pdf DeepDyve Pubget Overpricing