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10.1016/j.sbi.2014.09.006 http://scihub22266oqcxt.onion/10.1016/j.sbi.2014.09.006 C4267917!4267917 !25460269     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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25460269 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Curr+Opin+Struct+Biol 2014 ; 29 (ä): 58-66 Nephropedia Template TP {{tp|p=25460269 |t=2014. Structure and mechanism of lanthipeptide biosynthetic enzymes |pdf=|usr=}}{{25460269 }} gab.com Text Structure and mechanism of lanthipeptide biosynthetic enzymes JO: Curr Opin Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=25460269 #FOAvip Lanthipeptides are members of the ribosomally synthesized and post-translationally modified peptide (RiPP) natural products. They contain thioether crosslinks generated by dehydration of Ser and Thr residues followed by the addition of the thiol of Cys residues to the dehydroamino acids. Recent studies have revealed unexpected mechanisms of the post-translational modifications, and structural studies have started to provide insights into recognition of the peptide substrates by the modification enzymes. Twit Text FOAVip Structure and mechanism of lanthipeptide biosynthetic enzymes ????Curr Opin Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=25460269 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25460269 #FOAvip English Wikipedia <ref>{{Cite pmid|25460269 }}</ref> Structure and mechanism of lanthipeptide biosynthetic enzymes #MMPMID25460269 van der Donk WA ; Nair SK Curr Opin Struct Biol 2014[Dec]; 29 (ä): 58-66 PMID25460269 show ga Lanthipeptides are members of the ribosomally synthesized and post-translationally modified peptide (RiPP) natural products. They contain thioether crosslinks generated by dehydration of Ser and Thr residues followed by the addition of the thiol of Cys residues to the dehydroamino acids. Recent studies have revealed unexpected mechanisms of the post-translational modifications, and structural studies have started to provide insights into recognition of the peptide substrates by the modification enzymes. |*Protein Processing, Post-Translational [MESH] |Anti-Bacterial Agents/biosynthesis/chemistry [MESH] |Bacteria/metabolism [MESH] |Bacteriocins/*biosynthesis/*chemistry [MESH] |Hydro-Lyases/chemistry [MESH] |Oxidoreductases/chemistry [MESH] |Peptide Hydrolases/*chemistry [MESH] |Peptides/*chemistry [MESH] |Protein Conformation [MESH]Structure and mechanism of lanthipeptide biosynthetic enzymes (epmc).pdf DeepDyve Pubget Overpricing