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10.1016/j.ccr.2014.07.015 http://scihub22266oqcxt.onion/10.1016/j.ccr.2014.07.015 C4160413!4160413!25175806     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cancer+Cell 2014 ; 26 (3): 414-27 Nephropedia Template TP {{tp|p=25175806|t=2014. Drugging MYCN through an allosteric transition in Aurora Kinase A |pdf=|usr=}}{{25175806}} gab.com Text Drugging MYCN through an allosteric transition in Aurora Kinase A JO: Cancer Cell http://www.kidney.de/pget.php?&tw=1&pmid=25175806 #FOAvip MYC proteins are major drivers of cancer, yet are considered undruggable, as their DNA binding domains are composed of two extended alpha helices with no apparent surfaces for small molecule binding. Proteolytic degradation of MYCN protein is regulated in part by a kinase-independent function of Aurora A. We describe a class of inhibitors that disrupts the native conformation of Aurora A, and drives degradation of MYCN protein across MYCN-driven cancers. Comparison of co-crystal structures with structure-activity relationships across multiple inhibitors and chemotypes, coupled with mechanistic studies and biochemical assays, delineates an Aurora A conformation-specific effect on proteolytic degradation of MYCN, rather than simple nanomolar-level inhibition of Aurora A kinase activity. Twit Text FOAVip Drugging MYCN through an allosteric transition in Aurora Kinase A ????Cancer Cell http://www.kidney.de/pget.php?&tw=1&pmid=25175806 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25175806 #FOAvip English Wikipedia <ref>{{Cite pmid|25175806}}</ref> Drugging MYCN through an allosteric transition in Aurora Kinase A #MMPMID25175806 Gustafson WC; Meyerowitz JG; Nekritz EA; Chen J; Benes C; Charron E; Simonds EF; Seeger R; Matthay K; Hertz NT; Eilers M; Shokat KM; Weiss WA Cancer Cell 2014[Sep]; 26 (3): 414-27 PMID25175806show ga MYC proteins are major drivers of cancer, yet are considered undruggable, as their DNA binding domains are composed of two extended alpha helices with no apparent surfaces for small molecule binding. Proteolytic degradation of MYCN protein is regulated in part by a kinase-independent function of Aurora A. We describe a class of inhibitors that disrupts the native conformation of Aurora A, and drives degradation of MYCN protein across MYCN-driven cancers. Comparison of co-crystal structures with structure-activity relationships across multiple inhibitors and chemotypes, coupled with mechanistic studies and biochemical assays, delineates an Aurora A conformation-specific effect on proteolytic degradation of MYCN, rather than simple nanomolar-level inhibition of Aurora A kinase activity. äDrugging MYCN through an allosteric transition in Aurora Kinase A (epmc).pdf DeepDyve Pubget Overpricing