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1 which leads to the induction of ferritin, an iron-binding protein).
2 he levels of frataxin (FXN), a mitochondrial iron binding protein.
3 ity receptors for iron acquisition from host iron-binding proteins.
4 imiting conditions, presumably for essential iron-binding proteins.
5 sparing resulting from reduced synthesis of iron-binding proteins.
6 r findings have for the role of frataxins as iron-binding proteins.
7 a means to remove the hemin from these host iron-binding proteins.
8 rin is a member of the transferrin family of iron-binding proteins.
11 ike proteins are oxygen-carrying non-heme di-iron binding proteins and their functions have effect on
12 ut the dual effects of NGAL as a siderophore:iron-binding protein and as a growth factor and examines
13 g activity, whereas CyaY becomes a competent iron-binding protein and attenuates the iron-mediated pr
14 have the capacity to scavenge iron from host iron-binding proteins and deliver it to the mycobacteria
15 erculosis by removing this element from host iron-binding proteins and transferring it to desferri-my
16 , exomycobactins, compete for iron with host iron-binding proteins and, together with the iron-regula
19 were found, as well as other mRNAs encoding iron-binding proteins, bringing the total number of regu
20 stasis is typically regulated by cytoplasmic iron binding proteins, but here we describe a signal tra
21 this recessive disorder, is a mitochondrial iron-binding protein, but how its deficiency leads to ne
23 iron transporter gene (CBU1766), a putative iron binding protein-encoding gene (CBU0970), and a cati
24 r region of the Neisseria gonorrhoeae ferric iron binding protein-encoding gene fbpA, determined the
25 tion via either transgenic expression of the iron binding protein ferritin or oral administration of
27 f frataxins, a family of small mitochondrial iron-binding proteins found in organisms ranging from ba
28 Aconitase was found to associate with the iron binding protein frataxin exclusively during reperfu
31 our known cDNAs included ferritin, the major iron-binding protein in cells; HSGSA2R, a full-length cl
36 y to utilize the iron bound by high-affinity iron-binding proteins in the vertebrate host is an impor
37 tic transferrins comprise a class of bilobal iron-binding proteins in which each lobe carries a singl
39 p. are capable of iron utilization from host iron-binding proteins including transferrin and lactofer
40 cquire iron by direct interaction with human iron-binding proteins, including the serum glycoprotein,
41 wn siderophores but can employ host-derived, iron-binding proteins, including transferrin and lactofe
42 ding, the first description of a T. pallidum iron-binding protein, indicates that the syphilis spiroc
44 boratory cultures that ferritin and the main iron-binding proteins involved in photosynthesis and nit
46 ke other members of the transferrin class of iron-binding proteins, is a bilobal structure, the produ
47 ), IgG-binding protein A (Spa), and the heme-iron-binding protein (IsdA) were most abundant in the ag
48 ted rat hepatocytes bind and internalize the iron-binding protein lactoferrin (Lf) by a set of high-a
54 solved in complex with human transferrin, an iron binding protein normally responsible for delivering
57 by reduced activity of frataxin, a conserved iron-binding protein of the mitochondrial matrix, though
59 Lactoferrin (LF), traditionally known as an iron-binding protein present in high concentrations in m
60 at the syphilis spirochete lacks most of the iron-binding proteins present in many other bacterial pa
61 xpression of frataxin (FXN), a mitochondrial iron-binding protein required for Fe-S cluster assembly.
63 iron load is, perhaps, by the expression of iron-binding proteins, specifically the iron storage pro
65 f satisfying its iron requirement with human iron-binding proteins such as transferrin and lactoferri
66 sion of receptors that are specific for host iron-binding proteins, such as transferrin and lactoferr
67 hosts, because it is largely sequestered by iron-binding proteins, such as transferrin or lactoferri
68 ria gonorrhoeae is capable of utilizing host iron-binding proteins, such as transferrin, lactoferrin,
69 r, recent evidence indicated that IscA is an iron-binding protein that can provide iron for the iron-
70 er, recent studies indicated that IscA is an iron-binding protein that can provide iron for the iron-
72 ning of the human homologs to IscU and NifU, iron-binding proteins that play a critical role in Fe-S
75 reover, increased apical release of the host iron-binding protein transferrin during RSV infection pr
80 olamines binding to the high-affinity ferric-iron-binding proteins transferrin (Tf) and lactoferrin,
81 l gelatinase-associated lipocalin (NGAL), an iron-binding protein up-regulated in response to kidney
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