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10.1021/cb500791f http://scihub22266oqcxt.onion/10.1021/cb500791f C4301080!4301080!25402849     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       ACS+Chem+Biol 2015 ; 10 (1): 51-62 Nephropedia Template TP {{tp|p=25402849|t=2015. Protein Prenylation: Enzymes, Therapeutics, and Biotechnology Applications |pdf=|usr=}}{{25402849}} gab.com Text Protein Prenylation: Enzymes, Therapeutics, and Biotechnology Applications JO: ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=25402849 #FOAvip Protein prenylation is a ubiquitous covalent post-translational modification found in all eukaryotic cells, comprising attachment of either a farnesyl or a geranylgeranyl isoprenoid. It is essential for the proper cellular activity of numerous proteins, including Ras family GTPases and heterotrimeric G-proteins. Inhibition of prenylation has been extensively investigated to suppress the activity of oncogenic Ras proteins to achieve antitumor activity. Here, we review the biochemistry of the prenyltransferase enzymes and numerous isoprenoid analogs synthesized to investigate various aspects of prenylation and prenyltransferases. We also give an account of the current status of prenyltransferase inhibitors as potential therapeutics against several diseases including cancers, progeria, aging, parasitic diseases, and bacterial and viral infections. Finally, we discuss recent progress in utilizing protein prenylation for site-specific protein labeling for various biotechnology applications. Twit Text FOAVip Protein Prenylation: Enzymes, Therapeutics, and Biotechnology Applications ????ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=25402849 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25402849 #FOAvip English Wikipedia <ref>{{Cite pmid|25402849}}</ref> Protein Prenylation: Enzymes, Therapeutics, and Biotechnology Applications #MMPMID25402849 Palsuledesai CC; Distefano MD ACS Chem Biol 2015[Jan]; 10 (1): 51-62 PMID25402849show ga Protein prenylation is a ubiquitous covalent post-translational modification found in all eukaryotic cells, comprising attachment of either a farnesyl or a geranylgeranyl isoprenoid. It is essential for the proper cellular activity of numerous proteins, including Ras family GTPases and heterotrimeric G-proteins. Inhibition of prenylation has been extensively investigated to suppress the activity of oncogenic Ras proteins to achieve antitumor activity. Here, we review the biochemistry of the prenyltransferase enzymes and numerous isoprenoid analogs synthesized to investigate various aspects of prenylation and prenyltransferases. We also give an account of the current status of prenyltransferase inhibitors as potential therapeutics against several diseases including cancers, progeria, aging, parasitic diseases, and bacterial and viral infections. Finally, we discuss recent progress in utilizing protein prenylation for site-specific protein labeling for various biotechnology applications. äProtein Prenylation: Enzymes, Therapeutics, and Biotechnology Applicat(epmc).pdf DeepDyve Pubget Overpricing