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10.1105/tpc.114.131623 http://scihub22266oqcxt.onion/10.1105/tpc.114.131623 C4311201!4311201 !25480369     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25480369 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Plant+Cell 2014 ; 26 (12 ): 4568-83 Nephropedia Template TP {{tp|p=25480369 |t=2014. Phytochromes: an atomic perspective on photoactivation and signaling |pdf=|usr=}}{{25480369 }} gab.com Text Phytochromes: an atomic perspective on photoactivation and signaling JO: Plant Cell http://www.kidney.de/pget.php?&tw=1&pmid=25480369 #FOAvip The superfamily of phytochrome (Phy) photoreceptors regulates a wide array of light responses in plants and microorganisms through their unique ability to reversibly switch between stable dark-adapted and photoactivated end states. Whereas the downstream signaling cascades and biological consequences have been described, the initial events that underpin photochemistry of the coupled bilin chromophore and the ensuing conformational changes needed to propagate the light signal are only now being understood. Especially informative has been the rapidly expanding collection of 3D models developed by x-ray crystallographic, NMR, and single-particle electron microscopic methods from a remarkably diverse array of bacterial Phys. These structures have revealed how the modular architecture of these dimeric photoreceptors engages the buried chromophore through distinctive knot, hairpin, and helical spine features. When collectively viewed, these 3D structures reveal complex structural alterations whereby photoisomerization of the bilin drives nanometer-scale movements within the Phy dimer through bilin sliding, hairpin reconfiguration, and spine deformation that ultimately impinge upon the paired signal output domains. When integrated with the recently described structure of the photosensory module from Arabidopsis thaliana PhyB, new opportunities emerge for the rational redesign of plant Phys with novel photochemistries and signaling properties potentially beneficial to agriculture and their exploitation as optogenetic reagents. Twit Text FOAVip Phytochromes: an atomic perspective on photoactivation and signaling ????Plant Cell http://www.kidney.de/pget.php?&tw=1&pmid=25480369 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25480369 #FOAvip English Wikipedia <ref>{{Cite pmid|25480369 }}</ref> Phytochromes: an atomic perspective on photoactivation and signaling #MMPMID25480369 Burgie ES ; Vierstra RD Plant Cell 2014[Dec]; 26 (12 ): 4568-83 PMID25480369 show ga The superfamily of phytochrome (Phy) photoreceptors regulates a wide array of light responses in plants and microorganisms through their unique ability to reversibly switch between stable dark-adapted and photoactivated end states. Whereas the downstream signaling cascades and biological consequences have been described, the initial events that underpin photochemistry of the coupled bilin chromophore and the ensuing conformational changes needed to propagate the light signal are only now being understood. Especially informative has been the rapidly expanding collection of 3D models developed by x-ray crystallographic, NMR, and single-particle electron microscopic methods from a remarkably diverse array of bacterial Phys. These structures have revealed how the modular architecture of these dimeric photoreceptors engages the buried chromophore through distinctive knot, hairpin, and helical spine features. When collectively viewed, these 3D structures reveal complex structural alterations whereby photoisomerization of the bilin drives nanometer-scale movements within the Phy dimer through bilin sliding, hairpin reconfiguration, and spine deformation that ultimately impinge upon the paired signal output domains. When integrated with the recently described structure of the photosensory module from Arabidopsis thaliana PhyB, new opportunities emerge for the rational redesign of plant Phys with novel photochemistries and signaling properties potentially beneficial to agriculture and their exploitation as optogenetic reagents. |Bacteria/metabolism [MESH] |Cyanobacteria/metabolism [MESH] |Models, Molecular [MESH] |Nuclear Magnetic Resonance, Biomolecular [MESH] |Phytochrome/chemistry/metabolism/*physiology [MESH] |Plants/metabolism [MESH] |Protein Structure, Tertiary [MESH]Phytochromes: an atomic perspective on photoactivation and signaling (epmc).pdf DeepDyve Pubget Overpricing