Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Marie R.B. Binet"'
Autor:
Pascaline Herbelin, Celine Bouteleux, Mathieu Dupuy, Marie R.B. Binet, Sylvie Soreau, Yann Héchard
Publikováno v:
FEMS Microbiology Letters
FEMS Microbiology Letters, Wiley-Blackwell, 2016, 363 (5), pp.fnw022. ⟨10.1093/femsle/fnw022⟩
FEMS Microbiology Letters, Wiley-Blackwell, 2016, 363 (5), pp.fnw022. ⟨10.1093/femsle/fnw022⟩
International audience; Legionella pneumophila is a pathogenic bacterium commonly found in water and responsible for severe pneumonia. Free-living amoebae are protozoa also found in water, which feed on bacteria by phagocytosis. Under favorable condi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fdf432341e6fb7dcbae37e719a6a5d0f
https://hal.archives-ouvertes.fr/hal-01427789
https://hal.archives-ouvertes.fr/hal-01427789
Autor:
Robert K. Poole, Marie R.B. Binet
Publikováno v:
FEBS Letters. 473:67-70
ZntA is a cation-translocating ATPase which exports from Escherichia coli Cd(II) and Pb(II), as well as Zn(II). The metal-dependent ATP hydrolysis activity of purified ZntA was recently characterised and showed a specificity for Cd(II), Pb(II) and Zn
Autor:
Robert K. Poole, Rohani Hashim, Guanghui Wu, Steven J. Beard, Marie R.B. Binet, Martin N. Hughes
Publikováno v:
FEMS Microbiology Letters. 184:231-235
A locus involved in zinc(II) uptake in Escherichia coli K-12 was identified through the generation of a zinc(II)-resistant mutant by transposon (Tn10dCam) mutagenesis. The mutation was located within the pitA gene, which encodes the low-affinity inor
Autor:
Lucy J. Lee, Robert K. Poole, Rachel J. Jackson, Cameron W. McLeod, Marie R.B. Binet, Renli Ma, Alison I. Graham
Publikováno v:
FEMS microbiology letters. 289(2)
Escherichia coli possesses two major systems for inorganic phosphate (P(i)) uptake. The Pst system (pstSCAB) is inducible by low phosphate concentrations whereas the low-affinity transporter (pitA) has been described as constitutively expressed. PitA
Publikováno v:
Analytical biochemistry. 318(1)
Metals bound to proteins play key roles in structure stabilization, catalysis, and metal transport in cells, but metals may also be toxic. As a consequence, cells have developed mechanisms to control metal concentrations through binding to proteins.
Autor:
Arthur J. G. Moir, Marc S. Pittman, Hazel Corker, Guanghui Wu, Robert K. Poole, Marie R.B. Binet
Publikováno v:
The Journal of biological chemistry. 277(51)
Assembly of Escherichia coli cytochrome bd and periplasmic cytochromes requires the ATP-binding cassette transporter CydDC, whose substrate is unknown. Two-dimensional SDS-PAGE comparison of periplasm from wild-type and cydD mutant strains revealed t
Publikováno v:
FEMS microbiology letters. 213(1)
Nitric oxide (NO) has a broad spectrum of signalling and regulatory functions and multiple molecular targets. Recently, the intrabacterial toxicity of NO and mechanisms for NO resistance have been intensively investigated. Here we report for the firs