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.

10.1126/science.aag2516 http://scihub22266oqcxt.onion/10.1126/science.aag2516 C5441561!5441561!28302851     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       Science 2017 ; 355 (6330): 1174-80 Nephropedia Template TP {{tp|p=28302851|t=2017. Structural basis of the day-night transition in a bacterial circadian clock |pdf=|usr=}}{{28302851}} gab.com Text Structural basis of the day-night transition in a bacterial circadian clock JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=28302851 #FOAvip Circadian clocks are ubiquitous timing systems that induce rhythms of biological activities in synchrony with night and day. In cyanobacteria, timing is generated by a posttranslational clock consisting of KaiA, KaiB, and KaiC proteins and a set of output signaling proteins, SasA and CikA, which transduce this rhythm to control gene expression. Here, we describe crystal and nuclear magnetic resonance structures of KaiB-KaiC, KaiA-KaiB-KaiC, and CikA-KaiB complexes. They reveal how the metamorphic properties of KaiB, a protein that adopts two distinct folds, and the post?adenosine triphosphate hydrolysis state of KaiC create a hub around which nighttime signaling events revolve, including inactivation of KaiA and reciprocal regulation of the mutually antagonistic signaling proteins, SasA and CikA. Twit Text FOAVip Structural basis of the day-night transition in a bacterial circadian clock ????Science http://www.kidney.de/pget.php?&tw=1&pmid=28302851 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28302851 #FOAvip English Wikipedia <ref>{{Cite pmid|28302851}}</ref> Structural basis of the day-night transition in a bacterial circadian clock #MMPMID28302851 Tseng R; Goularte NF; Chavan A; Luu J; Cohen SE; Chang YG; Heisler J; Li S; Michael AK; Tripathi S; Golden SS; LiWang A; Partch CL Science 2017[Mar]; 355 (6330): 1174-80 PMID28302851show ga Circadian clocks are ubiquitous timing systems that induce rhythms of biological activities in synchrony with night and day. In cyanobacteria, timing is generated by a posttranslational clock consisting of KaiA, KaiB, and KaiC proteins and a set of output signaling proteins, SasA and CikA, which transduce this rhythm to control gene expression. Here, we describe crystal and nuclear magnetic resonance structures of KaiB-KaiC, KaiA-KaiB-KaiC, and CikA-KaiB complexes. They reveal how the metamorphic properties of KaiB, a protein that adopts two distinct folds, and the post?adenosine triphosphate hydrolysis state of KaiC create a hub around which nighttime signaling events revolve, including inactivation of KaiA and reciprocal regulation of the mutually antagonistic signaling proteins, SasA and CikA. äStructural basis of the day-night transition in a bacterial circadian (epmc).pdf DeepDyve Pubget Overpricing