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10.1016/j.cell.2015.04.011 http://scihub22266oqcxt.onion/10.1016/j.cell.2015.04.011 C4427029!4427029!25913193     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell 2015 ; 161 (4): 833-44 Nephropedia Template TP {{tp|p=25913193|t=2015. Structure of the Angiotensin Receptor Revealed by Serial Femtosecond Crystallography |pdf=|usr=}}{{25913193}} gab.com Text Structure of the Angiotensin Receptor Revealed by Serial Femtosecond Crystallography JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=25913193 #FOAvip Angiotensin II type 1 receptor (AT1R) is a G protein-coupled receptor that serves as a primary regulator for blood pressure maintenance. Although several anti-hypertensive drugs have been developed as AT1R blockers (ARBs), the structural basis for AT1R ligand-binding and regulation has remained elusive, mostly due to the difficulties of growing high quality crystals for structure determination using synchrotron radiation. By applying the recently developed method of serial femtosecond crystallography at an X-ray free-electron laser, we successfully determined the room-temperature crystal structure of the human AT1R in complex with its selective antagonist ZD7155 at 2.9 Å resolution. The AT1R-ZD7155 complex structure revealed key structural features of AT1R and critical interactions for ZD7155 binding. Docking simulations of the clinically used ARBs into the AT1R structure further elucidated both the common and distinct binding modes for these anti-hypertensive drugs. Our results thereby provide fundamental insights into AT1R structure-function relationship and structure-based drug design. Twit Text FOAVip Structure of the Angiotensin Receptor Revealed by Serial Femtosecond Crystallography ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=25913193 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25913193 #FOAvip English Wikipedia <ref>{{Cite pmid|25913193}}</ref> Structure of the Angiotensin Receptor Revealed by Serial Femtosecond Crystallography #MMPMID25913193 Zhang H; Unal H; Gati C; Han GW; Liu W; Zatsepin NA; James D; Wang D; Nelson G; Weierstall U; Sawaya MR; Xu Q; Messerschmidt M; Williams GJ; Boutet S; Yefanov OM; White TA; Wang C; Ishchenko A; Tirupula KC; Desnoyer R; Coe J; Conrad CE; Fromme P; Stevens RC; Katritch V; Karnik SS; Cherezov V Cell 2015[May]; 161 (4): 833-44 PMID25913193show ga Angiotensin II type 1 receptor (AT1R) is a G protein-coupled receptor that serves as a primary regulator for blood pressure maintenance. Although several anti-hypertensive drugs have been developed as AT1R blockers (ARBs), the structural basis for AT1R ligand-binding and regulation has remained elusive, mostly due to the difficulties of growing high quality crystals for structure determination using synchrotron radiation. By applying the recently developed method of serial femtosecond crystallography at an X-ray free-electron laser, we successfully determined the room-temperature crystal structure of the human AT1R in complex with its selective antagonist ZD7155 at 2.9 Å resolution. The AT1R-ZD7155 complex structure revealed key structural features of AT1R and critical interactions for ZD7155 binding. Docking simulations of the clinically used ARBs into the AT1R structure further elucidated both the common and distinct binding modes for these anti-hypertensive drugs. Our results thereby provide fundamental insights into AT1R structure-function relationship and structure-based drug design. äStructure of the Angiotensin Receptor Revealed by Serial Femtosecond C(epmc).pdf DeepDyve Pubget Overpricing