@misc{ArnisonBibbBierbaumetal.2013,
  author    = {Arnison, Paul G. and Bibb, Mervyn J. and Bierbaum, Gabriele and Bowers, Albert A. and Bugni, Tim S. and Bulaj, Grzegorz and Camarero, Julio A. and Campopiano, Dominic J. and Challis, Gregory L. and Clardy, Jon and Cotter, Paul D. and Craik, David J. and Dawson, Michael and Dittmann-Th{\"u}nemann, Elke and Donadio, Stefano and Dorrestein, Pieter C. and Entian, Karl-Dieter and Fischbach, Michael A. and Garavelli, John S. and Goeransson, Ulf and Gruber, Christian W. and Haft, Daniel H. and Hemscheidt, Thomas K. and Hertweck, Christian and Hill, Colin and Horswill, Alexander R. and Jaspars, Marcel and Kelly, Wendy L. and Klinman, Judith P. and Kuipers, Oscar P. and Link, A. James and Liu, Wen and Marahiel, Mohamed A. and Mitchell, Douglas A. and Moll, Gert N. and Moore, Bradley S. and Mueller, Rolf and Nair, Satish K. and Nes, Ingolf F. and Norris, Gillian E. and Olivera, Baldomero M. and Onaka, Hiroyasu and Patchett, Mark L. and Piel, J{\"o}rn and Reaney, Martin J. T. and Rebuffat, Sylvie and Ross, R. Paul and Sahl, Hans-Georg and Schmidt, Eric W. and Selsted, Michael E. and Severinov, Konstantin and Shen, Ben and Sivonen, Kaarina and Smith, Leif and Stein, Torsten and Suessmuth, Roderich D. and Tagg, John R. and Tang, Gong-Li and Truman, Andrew W. and Vederas, John C. and Walsh, Christopher T. and Walton, Jonathan D. and Wenzel, Silke C. and Willey, Joanne M. and van der Donk, Wilfred A.},
  title     = {Ribosomally synthesized and post-translationally modified peptide natural products overview and recommendations for a universal nomenclature},
  series = {Natural product reports : a journal of current developments in bio-organic chemistry},
  volume    = {30},
  journal   = {Natural product reports : a journal of current developments in bio-organic chemistry},
  number    = {1},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {0265-0568},
  doi       = {10.1039/c2np20085f},
  pages     = {108 -- 160},
  year      = {2013},
  abstract  = {This review presents recommended nomenclature for the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs), a rapidly growing class of natural products. The current knowledge regarding the biosynthesis of the >20 distinct compound classes is also reviewed, and commonalities are discussed.},
  language  = {en}
}
@article{AhmedReynaGonzalezSchmidetal.2017,
  author    = {Ahmed, Muhammad N. and Reyna-Gonzalez, Emmanuel and Schmid, Bianca and Wiebach, Vincent and Suessmuth, Roderich D. and Dittmann, Elke and Fewer, David P.},
  title     = {Phylogenomic Analysis of the Microviridin Biosynthetic Pathway Coupled with Targeted Chemo-Enzymatic Synthesis Yields Potent Protease Inhibitors},
  series = {ACS chemical biology},
  volume    = {12},
  journal   = {ACS chemical biology},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {1554-8929},
  doi       = {10.1021/acschembio.7b00124},
  pages     = {1538 -- 1546},
  year      = {2017},
  abstract  = {Natural products and their semisynthetic derivatives are an important source of drugs for the pharmaceutical industry. Bacteria are prolific producers of natural products and encode a vast diversity of natural product biosynthetic gene clusters. However, much of this diversity is inaccessible to natural product discovery. Here, we use a combination of phylogenomic analysis of the microviridin biosynthetic pathway and chemo-enzymatic synthesis of bioinformatically predicted microviridins to yield new protease inhibitors. Phylogenomic analysis demonstrated that microviridin biosynthetic gene clusters occur across the bacterial domain and encode three distinct subtypes of precursor peptides. Our analysis shed light on the evolution of microviridin biosynthesis and enabled prioritization of their chemo-enzymatic production. Targeted one-pot synthesis of four microviridins encoded by the cyanobacterium Cyanothece sp. PCC 7822 identified a set of novel and potent serine protease inhibitors, the most active of which had an IC50 value of 21.5 nM. This study advances the genome mining techniques available for natural product discovery and obviates the need to culture bacteria.},
  language  = {en}
}