Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Franziska Zähringer"'
Autor:
Felix Kuhne, Katrin Heinrich, Martin Winter, Jürgen Fichtl, Gabriel Hoffmann, Franziska Zähringer, Katharina Spitzauer, Monika Meier, Tarik A. Khan, Lea Bonnington, Katharina Wagner, Jan Olaf Stracke, Dietmar Reusch, Harald Wegele, Michael Mormann, Patrick Bulau
Publikováno v:
Analytical Chemistry. 95:2203-2212
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::331b03c39357f6720c2a66af938caf48
https://doi.org/10.1021/acs.analchem.2c03099
https://doi.org/10.1021/acs.analchem.2c03099
Publikováno v:
Nature. 531:533-537
Polyketide synthases (PKSs) are biosynthetic factories that produce natural products with important biological and pharmacological activities1, 2, 3. Their exceptional product diversity is encoded in a modular architecture. Modular PKSs (modPKSs) cat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a043c69185206d1707343ca7099c8d0f
https://doi.org/10.1038/nature16993
https://doi.org/10.1038/nature16993
Publikováno v:
Applied Biochemistry and Biotechnology. 163:71-79
Cyclic di-GMP (c-di-GMP) is an almost universal bacterial second messenger involved in the regulation of cell surface-associated traits and the persistence of infections. GGDEF and EAL domain-containing proteins catalyse c-di-GMP synthesis and degrad
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61150897f6ed227a863faf45674c7e75
https://doi.org/10.1007/s12010-010-9017-x
https://doi.org/10.1007/s12010-010-9017-x
Autor:
Fabian Gruss, Björn M. Burmann, Timm Maier, Franziska Zähringer, Sebastian Hiller, Roman P. Jakob
Publikováno v:
Nature Structural & Molecular Biology
Nat. Struct. Mol. Biol.
Nat. Struct. Mol. Biol.
TamA is an Escherichia coli Omp85 protein involved in autotransporter biogenesis. It comprises a 16-stranded transmembrane β-barrel and three POTRA domains. The 2.3-Å crystal structure reveals that the TamA barrel is closed at the extracellular fac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69753d18abe7196835804a18de8c5eb5
https://doi.org/10.1038/nsmb.2689
https://doi.org/10.1038/nsmb.2689
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 72:s29-s29
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e2bc433b006c9c4f9ad7a77534ac8739
https://doi.org/10.1107/s2053273316099538
https://doi.org/10.1107/s2053273316099538
Publikováno v:
Nature. 536:360-360
Nature 531, 533–537 (2016); doi:10.1038/nature16993 In this Letter, we studied the three-dimensional structure of a protein from Mycobacterium smegmatis assigned as mycocerosic acid synthase (MAS) in sequence databases as A0R1E8 in Uniprot (http://
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0e6504441df8009ec5902a53fbd217e3
https://doi.org/10.1038/nature18281
https://doi.org/10.1038/nature18281
Publikováno v:
Structure
Structure (London England : 1993)
Structure (London England : 1993)
SummaryDiguanylate cyclases synthesize the second messenger c-di-GMP, which in turn governs a plethora of physiological processes in bacteria. Although most diguanylate cyclases harbor sensory domains, their input signals are largely unknown. Here, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::908691f97aa3898c9b099b2126d33fac