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10.1073/pnas.1403383111 http://scihub22266oqcxt.onion/10.1073/pnas.1403383111 C4267366!4267366!25422469     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       Proc+Natl+Acad+Sci+U+S+A 2014 ; 111 (49): E5282-91 Nephropedia Template TP {{tp|p=25422469|t=2014. Disruption of FAT10?MAD2 binding inhibits tumor progression |pdf=|usr=}}{{25422469}} gab.com Text Disruption of FAT10 MAD2 binding inhibits tumor progression JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25422469 #FOAvip FAT10, a ubiquitin-like modifier, is an oncogene that interacts with mitotic arrest-deficient 2 (MAD2) and confers cellular malignancy. Here we identified the MAD2-binding residues of FAT10 and determined the first solution structure, to our knowledge, of the first FAT10 ubiquitin-like domain. Importantly, we demonstrated the proof-of-mechanism for a novel and specific drug-targeting strategy that entails the specific inhibition of the pathological activity of a therapeutic target but not its reported physiological function, thus minimizing undesirable side effects: Abrogation of the FAT10?MAD2 interaction curtailed tumor progression without affecting FAT10?s interaction with its other known physiological binding partners. This study presents a paradigm for drug targeting and paves the way for the development of a novel small-molecule anticancer inhibitor targeting the MAD2-binding interface of FAT10. Twit Text FOAVip Disruption of FAT10 MAD2 binding inhibits tumor progression ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25422469 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25422469 #FOAvip English Wikipedia <ref>{{Cite pmid|25422469}}</ref> Disruption of FAT10?MAD2 binding inhibits tumor progression #MMPMID25422469 Theng SS; Wang W; Mah WC; Chan C; Zhuo J; Gao Y; Qin H; Lim L; Chong SS; Song J; Lee CG Proc Natl Acad Sci U S A 2014[Dec]; 111 (49): E5282-91 PMID25422469show ga FAT10, a ubiquitin-like modifier, is an oncogene that interacts with mitotic arrest-deficient 2 (MAD2) and confers cellular malignancy. Here we identified the MAD2-binding residues of FAT10 and determined the first solution structure, to our knowledge, of the first FAT10 ubiquitin-like domain. Importantly, we demonstrated the proof-of-mechanism for a novel and specific drug-targeting strategy that entails the specific inhibition of the pathological activity of a therapeutic target but not its reported physiological function, thus minimizing undesirable side effects: Abrogation of the FAT10?MAD2 interaction curtailed tumor progression without affecting FAT10?s interaction with its other known physiological binding partners. This study presents a paradigm for drug targeting and paves the way for the development of a novel small-molecule anticancer inhibitor targeting the MAD2-binding interface of FAT10. äDisruption of FAT10?MAD2 binding inhibits tumor progression (epmc).pdf DeepDyve Pubget Overpricing