Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Sabrina, Burschel"'
Autor:
Bram Van den Bergh, Hannah Schramke, Joran Elie Michiels, Tom E. P. Kimkes, Jakub Leszek Radzikowski, Johannes Schimpf, Silke R. Vedelaar, Sabrina Burschel, Liselot Dewachter, Nikola Lončar, Alexander Schmidt, Tim Meijer, Maarten Fauvart, Thorsten Friedrich, Jan Michiels, Matthias Heinemann
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-18 (2022)
Antibiotic persisters are phenotypic variants within an isogenic bacterial population that are transiently tolerant to antibiotic treatment. Here, the authors provide evidence that cytoplasmic acidification, amplified by a compromised respiratory com
Externí odkaz:
https://doaj.org/article/0e4b4b380cf34e90a750b02dfc2a0648
Autor:
Philipp Skorupa, Ute Lindenstrauß, Sabrina Burschel, Christian Blumenscheit, Thorsten Friedrich, Constanze Pinske
Publikováno v:
FEBS Open Bio, Vol 10, Iss 3, Pp 371-385 (2020)
Formate hydrogenlyase (FHL) is the main hydrogen‐producing enzyme complex in enterobacteria. It converts formate to CO2 and H2 via a formate dehydrogenase and a [NiFe]‐hydrogenase. FHL and complex I are evolutionarily related and share a common c
Externí odkaz:
https://doaj.org/article/f3bd28d365064eb9930b6468bd6b5581
Autor:
Alexander Theßeling, Tim Rasmussen, Sabrina Burschel, Daniel Wohlwend, Jan Kägi, Rolf Müller, Bettina Böttcher, Thorsten Friedrich
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-7 (2019)
Cytochrome bd oxidases couple quinol oxidation and the release of protons to the periplasmic side with proton uptake from the cytoplasmic side to reduce dioxygen to water and they are the terminal reductases in bacterial and archaeal respiratory chai
Externí odkaz:
https://doaj.org/article/380da862893749fc97e0898f2e736f22
Autor:
Marius Schulte, Klaudia Frick, Emmanuel Gnandt, Sascha Jurkovic, Sabrina Burschel, Ramona Labatzke, Karoline Aierstock, Dennis Fiegen, Daniel Wohlwend, Stefan Gerhardt, Oliver Einsle, Thorsten Friedrich
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-9 (2019)
Respiratory complex I plays a central role in cellular energy metabolism coupling NADH oxidation to proton translocation. Here, the authors report the structure of the electron input part of Aquifex aeolicus complex I at up to 1.8 Å resolution with
Externí odkaz:
https://doaj.org/article/cbb18c1443da4b2783df8204ef6ed1bb
Publikováno v:
FEBS Letters. 594:1577-1585
Cytochrome bd-I oxidase is a terminal reductase of bacterial respiratory chains produced under low oxygen concentrations, oxidative stress, and during pathogenicity. While the bulk of the protein forms transmembrane helices, a periplasmic domain, the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7776591358f9574912ead7205f07f6ef
https://doi.org/10.1002/1873-3468.13749
https://doi.org/10.1002/1873-3468.13749
Autor:
Tim Rasmussen, Daniel Wohlwend, Bettina Böttcher, Jan Kägi, Thorsten Friedrich, Rolf Müller, Sabrina Burschel, Alexander Theßeling
Publikováno v:
Nature communications
Nature Communications
Nature Communications, Vol 10, Iss 1, Pp 1-7 (2019)
Nature Communications
Nature Communications, Vol 10, Iss 1, Pp 1-7 (2019)
Cytochrome bd oxidases are terminal reductases of bacterial and archaeal respiratory chains. The enzyme couples the oxidation of ubiquinol or menaquinol with the reduction of dioxygen to water, thus contributing to the generation of the protonmotive
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f518d88f8dcf02661cf39194ad18732
https://hdl.handle.net/10033/622041
https://hdl.handle.net/10033/622041
Autor:
Sabrina, Burschel, Doris, Kreuzer Decovic, Franziska, Nuber, Marie, Stiller, Maud, Hofmann, Arkadiusz, Zupok, Beata, Siemiatkowska, Michal, Gorka, Silke, Leimkühler, Thorsten, Friedrich
Publikováno v:
Molecular microbiology. 111(1)
The NADH:ubiquinone oxidoreductase (respiratory complex I) is the main entry point for electrons into the Escherichia coli aerobic respiratory chain. With its sophisticated setup of 13 different subunits and 10 cofactors, it is anticipated that vario
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5421f21822ea4e88591ba398a44d5a5e
https://pubmed.ncbi.nlm.nih.gov/30251413
https://pubmed.ncbi.nlm.nih.gov/30251413
Autor:
Philippe Bisel, Michael Müller, Iris Peintner, Thomas Paululat, Anja Greule, Christian De Ford, Denise Deubel, Andreas Bechthold, Irmgard Merfort, Claudia Jessen-Trefzer, Marija Marolt, Sabrina Burschel, Songya Zhang, Shu Ming Li, Thorsten Friedrich, Steffen Lüdeke
Publikováno v:
Frontiers in Microbiology. 8
Streptomyces diastatochromogenes Tü6028 is known to produce the polyketide antibiotic polyketomycin. The deletion of the pokOIV oxygenase gene led to a non-polyketomycin-producing mutant. Instead, novel compounds were produced by the mutant, which h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::706a6caa053f05e7fdc5937e66dc4775
Autor:
Anja, Greule, Marija, Marolt, Denise, Deubel, Iris, Peintner, Songya, Zhang, Claudia, Jessen-Trefzer, Christian, De Ford, Sabrina, Burschel, Shu-Ming, Li, Thorsten, Friedrich, Irmgard, Merfort, Steffen, Lüdeke, Philippe, Bisel, Michael, Müller, Thomas, Paululat, Andreas, Bechthold
Publikováno v:
Frontiers in Microbiology
Streptomyces diastatochromogenes Tü6028 is known to produce the polyketide antibiotic polyketomycin. The deletion of the pokOIV oxygenase gene led to a non-polyketomycin-producing mutant. Instead, novel compounds were produced by the mutant, which h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::98fdc7293d87c547115fbe3e34c8ff74
https://pubmed.ncbi.nlm.nih.gov/28270798
https://pubmed.ncbi.nlm.nih.gov/28270798
Autor:
Marie A. Stiller, Thorsten Friedrich, Franziska Nuber, Sabrina Burschel, Doris Kreuzer Decovic
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1859:e42
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ab59a2648c2f4e36dcaab24e8567698d
https://doi.org/10.1016/j.bbabio.2018.09.126
https://doi.org/10.1016/j.bbabio.2018.09.126