Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Siderophores/chemistry"'
Publikováno v:
Biometals, vol. 24, no. 3, pp. 513-522
The bacterial siderophore pyochelin is composed of salicylate and two cysteine-derived heterocycles, the second of which is modified by reduction and N-methylation during biosynthesis. In Pseudomonas aeruginosa, the first cysteine residue is converte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______1900::843acbdb3db7e095e51ed884cadc11e3
https://serval.unil.ch/notice/serval:BIB_EA42BFAB130C
https://serval.unil.ch/notice/serval:BIB_EA42BFAB130C
Publikováno v:
Biometals, Vol. 22, No 4 (2009) pp. 615-24
The outer membrane permeability barrier is an important resistance factor of bacterial pathogens. In combination with drug inactivating enzymes, target alteration and efflux, it can increase resistance dramatically. A strategy to overcome this membra
Autor:
Tseng, C. F., Burger, A., Mislin, G. L., Schalk, I. J., Yu, S. S., Chan, S. I., Abdallah, M. A.
Publikováno v:
Journal of Biological Inorganic Chemistry
Journal of Biological Inorganic Chemistry, Springer Verlag, 2006, 11, pp.419-32
Journal of Biological Inorganic Chemistry, Springer Verlag, 2006, 11, pp.419-32
0949-8257 (Print) Journal Article; Pyochelin, its analog 3''-nor-NH-pyochelin, and the related methyl hydroxamate, 2-(2'-hydroxyphenyl)-4,5-dihydrothiazol-4-carboxylic acid methoxymethyl amide, have been prepared together with their Fe(III) complexes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::bf52574bc3baf166af05f357e4040cc3
https://hal.archives-ouvertes.fr/hal-00129998
https://hal.archives-ouvertes.fr/hal-00129998
Autor:
Bruno Kieffer, L. Rochet, Gaëtan L.A. Mislin, V. Schons, R. A. Atkinson, Isabelle J. Schalk, Christophe Hennard, R. Graff, Mohamed A. Abdallah, C. Dugave
Publikováno v:
Biochemistry
Biochemistry, American Chemical Society, 2005, 44 (43), pp.14069-79. ⟨10.1021/bi051155s⟩
Biochemistry, American Chemical Society, 2005, 44, pp.14069-79
Biochemistry, 2005, 44 (43), pp.14069-79. ⟨10.1021/bi051155s⟩
Biochemistry, American Chemical Society, 2005, 44 (43), pp.14069-79. ⟨10.1021/bi051155s⟩
Biochemistry, American Chemical Society, 2005, 44, pp.14069-79
Biochemistry, 2005, 44 (43), pp.14069-79. ⟨10.1021/bi051155s⟩
0006-2960 (Print) Journal Article; Under iron limitation, Pseudomonas aeruginosa ATCC 15692 secretes a major siderophore, pyoverdine I (PvdI). This molecule chelates iron in the extracellular medium and shuttles it into the cells via a specific outer
Autor:
Isabelle J. Schalk, Nicolas Folschweiller, Franc Pattus, David Cobessi, Mohamed A. Abdallah, Hervé Celia
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2005, 347, pp.121-34
Journal of Molecular Biology, Elsevier, 2005, 347 (1), pp.121-34. ⟨10.1016/j.jmb.2005.01.021⟩
Journal of Molecular Biology, Elsevier, 2005, 347, pp.121-34
Journal of Molecular Biology, Elsevier, 2005, 347 (1), pp.121-34. ⟨10.1016/j.jmb.2005.01.021⟩
0022-2836 (Print) Journal Article; The pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa translocates ferric-pyoverdine across the outer membrane via an energy consuming mechanism that involves the inner membrane energy transducing
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27d0ac17e05d6a9be9d0786f430ab584
https://hal.archives-ouvertes.fr/hal-00129835
https://hal.archives-ouvertes.fr/hal-00129835