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10.1016/j.celrep.2018.01.062 http://scihub22266oqcxt.onion/10.1016/j.celrep.2018.01.062 C5851489!5851489!29444440     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       Cell+Rep 2018 ; 22 (7): 1903-12 Nephropedia Template TP {{tp|p=29444440|t=2018. Measuring Integrin Conformational Change on the Cell Surface with Super-Resolution Microscopy |pdf=|usr=}}{{29444440}} gab.com Text Measuring Integrin Conformational Change on the Cell Surface with Super-Resolution Microscopy JO: Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=29444440 #FOAvip We use super-resolution interferometric photoactivation and localization microscopy (iPALM) and a constrained photoactivatable fluorescent protein integrin fusion to measure the displacement of the head of integrin lymphocyte function-associated 1 (LFA-1) resulting from integrin conformational change on the cell surface. We demonstrate that the distance of the LFA-1 head increases substantially between basal and ligand-engaged conformations, which can only be explained at the molecular level by integrin extension. We further demonstrate that one class of integrin antagonist maintains the bent conformation, while another antagonist class induces extension. Our molecular scale measurements on cell-surface LFA-1 are in excellent agreement with distances derived from crystallographic and electron microscopy structures of bent and extended integrins. Our distance measurements are also in excellent agreement with a previous model of LFA-1 bound to ICAM-1 derived from the orientation of LFA-1 on the cell surface measured using fluorescence polarization microscopy. Twit Text FOAVip Measuring Integrin Conformational Change on the Cell Surface with Super-Resolution Microscopy ????Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=29444440 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29444440 #FOAvip English Wikipedia <ref>{{Cite pmid|29444440}}</ref> Measuring Integrin Conformational Change on the Cell Surface with Super-Resolution Microscopy #MMPMID29444440 Moore TI; Aaron J; Chew TL; Springer TA Cell Rep 2018[Feb]; 22 (7): 1903-12 PMID29444440show ga We use super-resolution interferometric photoactivation and localization microscopy (iPALM) and a constrained photoactivatable fluorescent protein integrin fusion to measure the displacement of the head of integrin lymphocyte function-associated 1 (LFA-1) resulting from integrin conformational change on the cell surface. We demonstrate that the distance of the LFA-1 head increases substantially between basal and ligand-engaged conformations, which can only be explained at the molecular level by integrin extension. We further demonstrate that one class of integrin antagonist maintains the bent conformation, while another antagonist class induces extension. Our molecular scale measurements on cell-surface LFA-1 are in excellent agreement with distances derived from crystallographic and electron microscopy structures of bent and extended integrins. Our distance measurements are also in excellent agreement with a previous model of LFA-1 bound to ICAM-1 derived from the orientation of LFA-1 on the cell surface measured using fluorescence polarization microscopy. äMeasuring Integrin Conformational Change on the Cell Surface with Supe(epmc).pdf DeepDyve Pubget Overpricing