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The Flying Laptop University Satellite Mission: Ground Infrastructure and Operations after one Year in Orbit

Autor: K.-S. Klemich, J. Keim, N. Bucher, J. Burgdorf, M. Böttcher, S. Wenzel, U. Mohr, B. Bätz, S. Gaißer, P. Hagel, S. Klinkner, J. Eickhoff

The small satellite Flying Laptop, launched in July 2017, was developed and built by PhD, graduate and undergraduate students at the Institute of Space Systems (IRS) of the University of Stuttgart with assistance by industry and research institutions

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::17b3b15077dda078ab27882ed8120957

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A locus coding for putative non-ribosomal peptide/polyketide synthase functions is mutated in a swarming-defective Proteus mirabilis strain

Autor: S. Gaisser, Colin Hughes

Publikováno v: Molecular and General Genetics MGG. 253:415-427

We describe a large bacterial locus that, unusually, encodes components typically required for both the non-ribosomal synthesis of peptides and also polyketide/fatty acid synthase function. Two tandem ABC transporter genes in this putative nrp (non-r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74d121ccf5f38ae6ffa0f9297ed93389
https://doi.org/10.1007/s004380050339

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Activity domains of the TonB protein

Autor: Volkmar Braun, I. Traub, S. Gaisser

Publikováno v: Molecular Microbiology. 8:409-423

Summary Escherichia coli and related Gram-negative bacteria contain an energy-coupied transport system through the outer membrane which consists of the proteins TonB, ExbB, ExbD anchored in the cytoplasmic membrane and receptors in the outer membrane

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6eb9bcd48d4644d02c8658044f2e17a8
https://doi.org/10.1111/j.1365-2958.1993.tb01584.x

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The tonB gene of Serratia marcescens: sequence, activity and partial complementation of Escherichia coli tonB mutants

Autor: Volkmar Braun, S. Gaisser

Publikováno v: Molecular Microbiology. 5:2777-2787

Summary The TonB protein plays a key role in the energy-coupled transport of iron siderophores, of vitamin B12, and of colicins of the B-group across the outer membrane of Escherichia coli. In order to obtain more data about which of its particular a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ee497465164520e48c2a0939a734639
https://doi.org/10.1111/j.1365-2958.1991.tb01986.x

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Analysis of a C-methyltransferase gene (aviG1) involved in avilamycin biosynthesis in Streptomyces viridochromogenes Tü57 and complementation of a Saccharopolyspora erythraea eryBIII mutant by aviG1

Autor: G, Weitnauer, S, Gaisser, L, Kellenberger, P F, Leadlay, A, Bechthold

Publikováno v: Microbiology (Reading, England). 148(Pt 2)

Streptomyces viridochromogenes Tü57 is the principal producer of avilamycin A. aviG1, a putative methyltransferase gene, was detected in the avilamycin biosynthetic gene cluster. To determine the function of aviG1, a targeted gene inactivation exper

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::52471bbc63cae184b0850be0a81fcf69
https://pubmed.ncbi.nlm.nih.gov/11832501

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New erythromycin derivatives from Saccharopolyspora erythraea using sugar O-methyltransferases from the spinosyn biosynthetic gene cluster

Autor: S, Gaisser, R, Lill, G, Wirtz, F, Grolle, J, Staunton, P F, Leadlay

Publikováno v: Molecular microbiology. 41(5)

Using a previously developed expression system based on the erythromycin-producing strain of Saccharopolyspora erythraea, O-methyltransferases from the spinosyn biosynthetic gene cluster of Saccharopolyspora spinosa have been shown to modify a rhamno

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c3e76069860c32fe28c7cea27e0c88ad
https://pubmed.ncbi.nlm.nih.gov/11555300

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Akademický článek

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Import and Export of Colicin M

Autor: R. Harkness, C. Glaser, J. Mende, S. Gaisser, Volkmar Braun, T. Ölschäger

Publikováno v: Bacteriocins, Microcins and Lantibiotics ISBN: 9783642769764

Colicin M is unique among the colicins in that it does not belong to the colicins which form pores in the cytoplasmic membrane oftarget cells, or display nuclease activities (Braun et a.., 1974; Harkness & Olschlager, 1991). Rather, colicin M inhibit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7f77d618a02753b49ed8614c6c856376
https://doi.org/10.1007/978-3-642-76974-0_22

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