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Peter Franke

Researcher at Free University of Berlin

Publications -  54
Citations -  3679

Peter Franke is an academic researcher from Free University of Berlin. The author has contributed to research in topics: Bacillus subtilis & Amino acid. The author has an hindex of 28, co-authored 50 publications receiving 3415 citations. Previous affiliations of Peter Franke include Russian Academy of Sciences & Technical University of Berlin.

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Structural and Functional Characterization of Gene Clusters Directing Nonribosomal Synthesis of Bioactive Cyclic Lipopeptides in Bacillus amyloliquefaciens Strain FZB42

TL;DR: A double mutant lacking both bacillomycin D and fengycin was heavily impaired in its ability to inhibit growth of phytopathogenic fungi, suggesting that both lipopeptides act in a synergistic manner.
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Matrix-assisted laser desorption ionization--time of flight mass spectrometry of lipopeptide biosurfactants in whole cells and culture filtrates of Bacillus subtilis C-1 isolated from petroleum sludge.

TL;DR: An innovative method was developed for rapid sensitive detection and efficient structural characterization of lipopeptide biosurfactants by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry by using whole microbial cells and crude culture filtrates as targets in combination with surface tension measurements.
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Structural and Functional Characterization of Three Polyketide Synthase Gene Clusters in Bacillus amyloliquefaciens FZB 42

TL;DR: Cassette mutagenesis combined with advanced mass spectrometric techniques revealed that the pks1 (bae) and pks3 (dif) gene clusters encode the biosynthesis of the polyene antibiotics bacillaene and difficid in or oxydifficidin, respectively.
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Stabilin-1 and −2 constitute a novel family of fasciclin-like hyaluronan receptor homologues

TL;DR: Stabilin-1 and stabilin-2 define a novel family of fasciclin-like hyaluronan receptor homologues that might play a role in cell—cell and cell—matrix interactions in vascular function and inflammatory processes.
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The Multiple Carrier Model of Nonribosomal Peptide Biosynthesis at Modular Multienzymatic Templates

TL;DR: It was demonstrated that a 4′-phosphopantetheine cofactor is attached to the central serine of the thiolation motif in each amino acid-activating module of the gramicidin S synthetase multienzyme system forming the thioester binding sites for the amino acid substrates and catalyzing the elongation process.