Zobrazeno 1 - 5
of 5
pro vyhledávání: '"MESH: Proteus mirabilis"'
Autor:
Philippe Glaser, Thierry Naas, Rémy A. Bonnin, Daniel T. Huang, Pierre Bogaerts, Laurent Dortet, Morgane De Laveleye, Delphine Girlich, Youri Glupczynski
Publikováno v:
Antimicrobial Agents and Chemotherapy
Antimicrobial Agents and Chemotherapy, American Society for Microbiology, 2017, 61 (2), pp.e01697-16. ⟨10.1128/AAC.01697-16⟩
Antimicrobial Agents and Chemotherapy, 2017, 61 (2), pp.e01697-16. ⟨10.1128/AAC.01697-16⟩
Antimicrobial Agents and Chemotherapy, American Society for Microbiology, 2017, 61 (2), pp.e01697-16. ⟨10.1128/AAC.01697-16⟩
Antimicrobial Agents and Chemotherapy, 2017, 61 (2), pp.e01697-16. ⟨10.1128/AAC.01697-16⟩
Horizontal gene transfer may occur between distantly related bacteria, thus leading to genetic plasticity and in some cases to acquisition of novel resistance traits . Proteus mirabilis is an enterobacterial species responsible for human infections t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c82b1ee243e92161c8f29bb391f041ce
https://hal-pasteur.archives-ouvertes.fr/pasteur-03107700
https://hal-pasteur.archives-ouvertes.fr/pasteur-03107700
Publikováno v:
Microbes and Infection
Microbes and Infection, Elsevier, 2013, 15 (8-9), pp.535-539. ⟨10.1016/j.micinf.2013.06.005⟩
Microbes and Infection, Elsevier, 2013, 15 (8-9), pp.535-539. ⟨10.1016/j.micinf.2013.06.005⟩
International audience
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::856276d2a4ac81edb264abf4b323f2ed
https://doi.org/10.1016/j.micinf.2013.06.005
https://doi.org/10.1016/j.micinf.2013.06.005
Publikováno v:
Biomolecular NMR Assignments
Biomolecular NMR Assignments, 2015, 9 (2), pp.397-401. ⟨10.1007/s12104-015-9617-z⟩
Biomolecular NMR Assignments, Springer, 2015, 9 (2), pp.397-401. ⟨10.1007/s12104-015-9617-z⟩
Biomolecular NMR Assignments, 2015, 9 (2), pp.397-401. ⟨10.1007/s12104-015-9617-z⟩
Biomolecular NMR Assignments, Springer, 2015, 9 (2), pp.397-401. ⟨10.1007/s12104-015-9617-z⟩
The general stress response in Enterobacteria, like Escherichia coli or Salmonella, is controlled by the transcription factor σS, encoded by the rpoS gene, which accumulates during stationary phase growth and associates with the core RNA polymerase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::898ac162edfdaa003afee48bbdbe959a
https://hal-pasteur.archives-ouvertes.fr/pasteur-01413051/document
https://hal-pasteur.archives-ouvertes.fr/pasteur-01413051/document
Autor:
Claudine Mayer, Frederick Saul, Ahmed Haouz, Patrick Weber, Véronique Monteil, Bertrand Raynal, Françoise Norel, Patrick England, Fabienne Levi-Acobas, Paola Cavaliere, Jacques Bellalou
Publikováno v:
Biochemical Journal
Biochemical Journal, Portland Press, 2014, 463 (2), pp.215-24. ⟨10.1042/BJ20140578⟩
Biochemical Journal, 2014, 463 (2), pp.215-24. ⟨10.1042/BJ20140578⟩
Biochemical Journal, Portland Press, 2014, 463 (2), pp.215-24. ⟨10.1042/BJ20140578⟩
Biochemical Journal, 2014, 463 (2), pp.215-24. ⟨10.1042/BJ20140578⟩
International audience; In many γ-proteobacteria, the RpoS/σS sigma factor associates with the core RNAP (RNA polymerase) to modify global gene transcription in stationary phase and under stress conditions. The small regulatory protein Crl stimulat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2973ef8438055a248372c56cf77a38b7
https://hal-pasteur.archives-ouvertes.fr/pasteur-01120659
https://hal-pasteur.archives-ouvertes.fr/pasteur-01120659
Publikováno v:
Proteins-Structure, Function and Bioinformatics
Proteins-Structure, Function and Bioinformatics, Wiley, 2003, 50 (2), pp.261-71. ⟨10.1002/prot.10283⟩
Proteins-Structure, Function and Bioinformatics, 2003, 50 (2), pp.261-71. ⟨10.1002/prot.10283⟩
Proteins-Structure, Function and Bioinformatics, Wiley, 2003, 50 (2), pp.261-71. ⟨10.1002/prot.10283⟩
Proteins-Structure, Function and Bioinformatics, 2003, 50 (2), pp.261-71. ⟨10.1002/prot.10283⟩
Heme catalases are homotetrameric enzymes with a highly conserved complex quaternary structure, and their functional role is still not well understood. Proteus mirabilis catalase (PMC), a heme enzyme belonging to the family of NADPH-binding catalases
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b60851ca3a8e31e3be81587cc64470c
https://hal.archives-ouvertes.fr/hal-00173312
https://hal.archives-ouvertes.fr/hal-00173312