@phdthesis{Picchi2013,
  author    = {Picchi, Douglas Gatte},
  title     = {On the characterisation of biosynthetic pathways and functional metagenomic approaches of cyanobacterial peptides},
  address   = {Potsdam},
  pages     = {146 S},
  year      = {2013},
  language  = {en}
}
@misc{KehrPicchiDittmannThuenemann2011,
  author    = {Kehr, Jan-Christoph and Picchi, Douglas Gatte and Dittmann-Th{\"u}nemann, Elke},
  title     = {Natural product biosyntheses in cyanobacteria a treasure trove of unique enzymes},
  series = {Beilstein journal of organic chemistry},
  volume    = {7},
  journal   = {Beilstein journal of organic chemistry},
  number    = {2},
  publisher = {Beilstein-Institut zur F{\"o}rderung der Chemischen Wissenschaften},
  address   = {Frankfurt, Main},
  issn      = {1860-5397},
  doi       = {10.3762/bjoc.7.191},
  pages     = {1622 -- 1635},
  year      = {2011},
  abstract  = {Cyanobacteria are prolific producers of natural products. Investigations into the biochemistry responsible for the formation of these compounds have revealed fascinating mechanisms that are not, or only rarely, found in other microorganisms. In this article, we survey the biosynthetic pathways of cyanobacteria isolated from freshwater, marine and terrestrial habitats. We especially emphasize modular nonribosomal peptide synthetase (NRPS) and polyketide synthase (PKS) pathways and highlight the unique enzyme mechanisms that were elucidated or can be anticipated for the individual products. We further include ribosomal natural products and UV-absorbing pigments from cyanobacteria. Mechanistic insights obtained from the biochemical studies of cyanobacterial pathways can inspire the development of concepts for the design of bioactive compounds by synthetic-biology approaches in the future.},
  language  = {en}
}
@article{GattePicchiWeizIshidaetal.2014,
  author    = {Gatte-Picchi, Douglas and Weiz, Annika and Ishida, Keishi and Hertweck, Christian and Dittmann-Th{\"u}nemann, Elke},
  title     = {Functional analysis of environmental DNA-derived microviridins provides new insights into the diversity of the tricyclic peptide family},
  series = {Applied and environmental microbiology},
  volume    = {80},
  journal   = {Applied and environmental microbiology},
  number    = {4},
  publisher = {American Society for Microbiology},
  address   = {Washington},
  issn      = {0099-2240},
  doi       = {10.1128/AEM.03502-13},
  pages     = {1380 -- 1387},
  year      = {2014},
  abstract  = {Microviridins represent a unique family of ribosomally synthesized cage-like depsipeptides from cyanobacteria with potent protease-inhibitory activities. The natural diversity of these peptides is largely unexplored. Here, we describe two methodologies that were developed to functionally characterize cryptic microviridin gene clusters from metagenomic DNA. Environmental samples were collected and enriched from cyanobacterial freshwater blooms of different geographical origins containing predominantly Microcystis sp. Microviridins were produced either directly from fosmid clones or after insertion of environmental DNA-derived gene cassettes into a minimal expression platform in Escherichia coli. Three novel microviridin variants were isolated and tested against different serine-type proteases. The comparison of the bioactivity profiles of the new congeners allows deduction of further structure-function relationships for microviridins. Moreover, this study provides new insights into microviridin processing and gene cluster organization.},
  language  = {en}
}