Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Dorothea Dittrich"'
Autor:
Anita Schultz, Ying Lan Guo, Dorothea Dittrich, Hermann A. Mayer, Peter Sander, Waldemar Vollmer, Joachim E. Schultz
Publikováno v:
FEBS Journal. 276:1094-1103
cAMP generation in bacteria is often stimulated by sudden, but lasting, changes in extracellular conditions, whereas intracellular cAMP concentrations quickly settle at new levels. As bacteria lack G-proteins, it is unknown how bacterial adenylate cy
Autor:
Joachim E. Schultz, Anita Schultz, Peter Sander, Jürgen U. Linder, Ying Lan Guo, Stefan Ehlers, Christine Keller, Dorothea Dittrich, Ursula Kurz
Publikováno v:
Molecular Microbiology. 57:667-677
The adenylyl cyclase Rv1625c from Mycobacterium tuberculosis codes for a protein with six transmembrane spans and a catalytic domain, i.e. it corresponds to one half of the pseudoheterodimeric mammalian adenylyl cyclases (ACs). Rv1625c is active as a
Autor:
Ying Lan, Guo, Hermann, Mayer, Waldemar, Vollmer, Dorothea, Dittrich, Peter, Sander, Anita, Schultz, Joachim E, Schultz
Publikováno v:
FEBS JOURNAL
cAMP generation in bacteria is often stimulated by sudden, but lasting, changes in extracellular conditions, whereas intracellular cAMP concentrations quickly settle at new levels. As bacteria lack G-proteins, it is unknown how bacterial adenylate cy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::849bc421112467c0bcad85897cf7fbd3
https://doi.org/10.5167/uzh-12293
https://doi.org/10.5167/uzh-12293
Mycobacterium tuberculosis open reading frame Rv1264 encodes an adenylate cyclase that exhibits its highest enzymatic activity at an acidic pH of 6.0. This is the pH M. tuberculosis encounters in the phagosome. Consequently Rv1264 has been suggested
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc7e11f76e3c3d3afc17a0198ac45c1e
https://www.zora.uzh.ch/id/eprint/3146/
https://www.zora.uzh.ch/id/eprint/3146/
Autor:
Ying Lan, Guo, Ursula, Kurz, Anita, Schultz, Jürgen U, Linder, Dorothea, Dittrich, Christine, Keller, Stefan, Ehlers, Peter, Sander, Joachim E, Schultz
Publikováno v:
Molecular microbiology. 57(3)
The adenylyl cyclase Rv1625c from Mycobacterium tuberculosis codes for a protein with six transmembrane spans and a catalytic domain, i.e. it corresponds to one half of the pseudoheterodimeric mammalian adenylyl cyclases (ACs). Rv1625c is active as a
Publikováno v:
Journal of bacteriology. 184(17)
IS 256 is a highly active insertion sequence (IS) element of multiresistant staphylococci and enterococci. Here we show that, in a Staphylococcus epidermidis clinical isolate, as well as in recombinant Staphylococcus aureus and Escherichia coli carry