Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Achim, Heck"'
Publikováno v:
BIOspektrum. 29:88-90
Terpenoids offer various properties relevant for biotech and pharma industries. Production in microbes is a sustainable way to provide these compounds for industrial use. The phototrophic bacterium Rhodobacter capsulatus has some unique characteristi
Autor:
Fabienne Hilgers, Samer S. Habash, Anita Loeschcke, Yannic Sebastian Ackermann, Stefan Neumann, Achim Heck, Oliver Klaus, Jennifer Hage-Hülsmann, Florian M. W. Grundler, Karl-Erich Jaeger, A. Sylvia S. Schleker, Thomas Drepper
Publikováno v:
Microorganisms, Vol 9, Iss 1, p 168 (2021)
Terpenoids constitute one of the largest and most diverse groups within the class of secondary metabolites, comprising over 80,000 compounds. They not only exhibit important functions in plant physiology but also have commercial potential in the biot
Externí odkaz:
https://doaj.org/article/65fe34620c504550a86ddbe7eb91bc78
Autor:
Thomas Drepper, Achim Heck
Publikováno v:
Modern Topics in the Phototrophic Prokaryotes ISBN: 9783319462592
Phototrophic non-sulfur purple α-proteobacteria are able to harvest sunlight and to fix atmospheric carbon dioxide and dinitrogen. Consequently, these microbes are used as model organisms for the investigation of regulation and activity of the photo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::05d8cce7eaf3e3bfe2e3d1546496b609
https://doi.org/10.1007/978-3-319-46261-5_12
https://doi.org/10.1007/978-3-319-46261-5_12
Autor:
Achim Heck, Franco Circolone, Vera Svensson, Rene Bergmann, Nadine Katzke, Annette Markert, Thomas Drepper, Karl-Erich Jaeger, Solmaz Arvani
Publikováno v:
Protein Expression and Purification. 69:137-146
The functional expression of heterologous genes using standard bacterial expression hosts such as Escherichia coli is often limited, e.g. by incorrect folding, assembly or targeting of recombinant proteins. Consequently, alternative bacterial express
Autor:
Wolfgang Wiechert, Achim Heck, Thomas Drepper, Denis Tielker, Joachim F. Ernst, Jörg Pietruszka, Frank Rosenau, Roland Freudl, Michael Bott, Karl-Erich Jaeger, Marco Oldiges, Susanne Wilhelm
Publikováno v:
BIOspektrum. 18:449-451
The genome era lead to the identification of a tremendous number of genes encoding potentially scientific and biotechnological relevant proteins. Moreover, the number of these proteins is still exponentially growing. Nevertheless, the corresponding g
Autor:
Marco, Kaschner, Anita, Loeschcke, Judith, Krause, Bui Quang, Minh, Achim, Heck, Stephan, Endres, Vera, Svensson, Astrid, Wirtz, Arndt, von Haeseler, Karl-Erich, Jaeger, Thomas, Drepper, Ulrich, Krauss
Publikováno v:
Molecular microbiology. 93(5)
In all photosynthetic organisms, chlorophylls function as light-absorbing photopigments allowing the efficient harvesting of light energy. Chlorophyll biosynthesis recurs in similar ways in anoxygenic phototrophic proteobacteria as well as oxygenic p
Publikováno v:
Journal of Biotechnology. 191:1-2
Autor:
Achim Heck, Jochen Büchs, Franco Circolone, Robert Huber, Anne-Kathrin Hillmer, Karl-Erich Jaeger, Thomas Drepper
Fluorescent proteins of the green fluorescent protein (GFP) family are commonly used as reporter proteins for quantitative analysis of complex biological processes in living microorganisms. Here we demonstrate that the fluorescence signal intensity o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5288941c234dcd32237d79a2985d7cd
https://europepmc.org/articles/PMC2935039/
https://europepmc.org/articles/PMC2935039/
Autor:
Franco Circolone, Marion Wendorff, Ulrich Krauss, Thorsten Eggert, Thomas Drepper, Achim Heck, Wolfgang Gärtner, Jan-Karl Guterl, Karl-Erich Jaeger, Aba Losi
Publikováno v:
Nature biotechnology. 25(4)
Fluorescent reporter proteins such as green fluorescent protein are valuable noninvasive molecular tools for in vivo real-time imaging of living specimens. However, their use is generally restricted to aerobic systems, as the formation of their chrom
Publikováno v:
Biochemistry. 43(30)
Human mitochondrial methionyl-tRNA synthetase (human mtMetRS) has been identified from the human EST database. The cDNA encodes a 593 amino acid protein with an 18 amino acid mitochondrial import signal sequence. Sequence analysis indicates that this