Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Veronika M. Meier"'
Publikováno v:
Journal of Bacteriology. 200
The chemosensory system in Sinorhizobium meliloti has several important deviations from the widely studied enterobacterial paradigm. To better understand the differences between the two systems and how they are optimally tuned, we determined the cell
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12fb0ec9b3931c5faca052b5020e4593
https://doi.org/10.1128/jb.00614-17
https://doi.org/10.1128/jb.00614-17
Autor:
Cristina Pop, Gheorghe-Doru Roiban, Ioana Dumitru, Niculina D. Hădade, Guy S. Salvesen, Veronika M. Meier, Domenico Fasci, Mihaela Matache, Cristian Dobrota, Daniel P. Funeriu
Publikováno v:
ChemBioChem. 13:80-84
We report here the synthesis and biochemical properties of a new peptidyl activity-based probe 1 for SUMO proteases, SENPs. The activity-based probe has at its C terminus a glycine-derived fluoromethylketone moiety as a reactive group designed to tar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25993eefe4a08da0c2c0d853cf8c6551
https://doi.org/10.1002/cbic.201100645
https://doi.org/10.1002/cbic.201100645
Autor:
Veronika M. Meier, Birgit E. Scharf
Publikováno v:
Journal of Bacteriology. 191:5724-5733
Bacterial chemoreceptors primarily locate in clusters at the cell pole, where they form large sensory complexes which recruit cytoplasmic components of the signaling pathway. The genome of the soil bacterium Sinorhizobium meliloti encodes seven trans
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca90d1561e2db91f77fb9e7f08afc73e
https://doi.org/10.1128/jb.01286-08
https://doi.org/10.1128/jb.01286-08
Publikováno v:
Journal of Bacteriology. 189:1816-1826
The genome of the symbiotic soil bacterium Sinorhizobium meliloti contains eight genes coding for methyl-accepting chemotaxis proteins (MCPs) McpS to McpZ and one gene coding for a transducer-like protein, IcpA. Seven of the MCPs are localized in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f91a5c7879cad4048366af4e6b8325a
https://doi.org/10.1128/jb.00883-06
https://doi.org/10.1128/jb.00883-06
Autor:
Gheorghe-Doru Roiban, Veronika M. Meier, Daniel P. Funeriu, Mihaela Matache, Cristian Dobrota, Niculina D. Bogdan
Publikováno v:
Biomacromolecules. 12(10)
Self-assembled inorganic-protein arrays with well-defined and controllable size and structure were obtained through the Fe(II) complexation of protein-conjugated terpyridine units (ligand). The atom-level control of the ligand is obtained through res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73488ba44bad8eec6437d9b19aac3868
https://pubmed.ncbi.nlm.nih.gov/21875057
https://pubmed.ncbi.nlm.nih.gov/21875057
Autor:
Ioana Dumitru, Mihaela Matache, Daniel P. Funeriu, Veronika M. Meier, Cristian Dobrota, Niculina D. Bogdan, Gheorghe D. Roiban
Publikováno v:
Chemistry (Weinheim an der Bergstrasse, Germany). 16(7)
Herein we describe the design and synthesis of the first series of di-functional ligands for the directed construction of inorganic-protein frameworks. The synthesized ligands are composed of a metal-ion binding moiety (terpyridine-based) conjugated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e76f854a9423189bea562b4b5eafe5ea
https://pubmed.ncbi.nlm.nih.gov/20063328
https://pubmed.ncbi.nlm.nih.gov/20063328
Autor:
Veronika M. Meier, Martin Haslbeck, Birgit E. Scharf, Till Maurer, Hubert Riepl, Rüdiger Schmitt, Hans Robert Kalbitzer
Publikováno v:
Molecular microbiology. 69(6)
An unusual regulatory mechanism involving two response regulators, CheY1 and CheY2, but no CheZ phosphatase, operates in the chemotactic signalling chain of Sinorhizobium meliloti. Active CheY2-P, phosphorylated by the cognate histidine kinase, CheA,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f19bac7ffaaedb9b328d4239c148610
https://pubmed.ncbi.nlm.nih.gov/18573176
https://pubmed.ncbi.nlm.nih.gov/18573176