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1 NRAMP homologues are also present in bacteria.
2 NRAMPs (natural resistance-associated macrophage protein
3 resistance-associated macrophage protein-1 (NRAMP-1), transferrin, lactoferrin, and heme-binding pro
5 increased fitness when exposed to RNS in an NRAMP(R), C3H/HeN murine model of acute oral infection.
7 r protein architecture compared to classical NRAMPs, with a restructured ion binding site whose incre
8 s immune system responses, pathogen-defense (NRAMP, Mx, CXC), general stress (HSP70), metal-binding (
9 ssion of two importers: the proton-dependent NRAMP family transporter MntH and the ABC transporter Mn
10 typhimurium, and the cloning of two distinct NRAMP genes from Pseudomonas aeruginosa and an internal
11 ignated mntH because the two enterobacterial NRAMPs encode H+-stimulated, highly selective manganese(
13 fty protein interactors of a Brassica juncea NRAMP protein was identified by a Split-Ubiquitin Yeast-
15 l resistance-associated macrophage proteins (NRAMP), and Zn-regulated transporter Fe-regulated transp
16 l resistance associated macrophage proteins (NRAMPs) are evolutionarily conserved metal transporters
17 e cloning and characterization of the single NRAMP genes in Escherichia coli and Salmonella enterica
19 ransition metal ions by members of the SLC11/NRAMP family constitutes a ubiquitous mechanism for the
21 tified an Arabidopsis thaliana member of the NRAMP family of divalent metal transporters, NRAMP2, whi