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10.1016/j.sbi.2014.09.006

http://scihub22266oqcxt.onion/10.1016/j.sbi.2014.09.006
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C4267917!4267917!25460269
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suck abstract from ncbi


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pmid25460269      Curr+Opin+Struct+Biol 2014 ; ä (ä): 58-66
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  • Structure and Mechanism of Lanthipeptide Biosynthetic Enzymes #MMPMID25460269
  • van der Donk WA; Nair SK
  • Curr Opin Struct Biol 2014[Dec]; ä (ä): 58-66 PMID25460269show 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.
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