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10.1016/j.tips.2015.08.003 http://scihub22266oqcxt.onion/10.1016/j.tips.2015.08.003 C4640985!4640985!26538314     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Trends+Pharmacol+Sci 2015 ; 36 (11): 724-36 Nephropedia Template TP {{tp|p=26538314|t=2015. Lessons from hot spot analysis for fragment-based drug discovery |pdf=|usr=}}{{26538314}} gab.com Text Lessons from hot spot analysis for fragment-based drug discovery JO: Trends Pharmacol Sci http://www.kidney.de/pget.php?&tw=1&pmid=26538314 #FOAvip Analysis of binding energy hot spots at protein surfaces can provide crucial insights into the prospects for successful application of fragment-based drug discovery (FBDD), and whether a fragment hit can be advanced into a high affinity, druglike ligand. The key factor is the strength of the top ranking hot spot, and how well a given fragment complements it. We show that published data are sufficient to provide a sophisticated and quantitative understanding of how hot spots derive from protein three-dimensional structure, and how their strength, number and spatial arrangement govern the potential for a surface site to bind to fragment-sized and larger ligands. This improved understanding provides important guidance for the effective application of FBDD in drug discovery. Twit Text FOAVip Lessons from hot spot analysis for fragment-based drug discovery ????Trends Pharmacol Sci http://www.kidney.de/pget.php?&tw=1&pmid=26538314 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26538314 #FOAvip English Wikipedia <ref>{{Cite pmid|26538314}}</ref> Lessons from hot spot analysis for fragment-based drug discovery #MMPMID26538314 Hall DR; Kozakov D; Whitty A; Vajda S Trends Pharmacol Sci 2015[Nov]; 36 (11): 724-36 PMID26538314show ga Analysis of binding energy hot spots at protein surfaces can provide crucial insights into the prospects for successful application of fragment-based drug discovery (FBDD), and whether a fragment hit can be advanced into a high affinity, druglike ligand. The key factor is the strength of the top ranking hot spot, and how well a given fragment complements it. We show that published data are sufficient to provide a sophisticated and quantitative understanding of how hot spots derive from protein three-dimensional structure, and how their strength, number and spatial arrangement govern the potential for a surface site to bind to fragment-sized and larger ligands. This improved understanding provides important guidance for the effective application of FBDD in drug discovery. äLessons from hot spot analysis for fragment-based drug discovery (epmc).pdf DeepDyve Pubget Overpricing