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1 he interior of the active site, and the heme iron binding.
2 family of proteins and is likely involved in iron binding.
3 oxyornithine residues, which are involved in iron binding.
4 r understand the role of the third C site in iron binding.
5 ed conformation of Fe-Af that is enforced by iron binding.
6 ow for distinguishing between two models for iron binding.
7 tential modes of protein-protein and protein-iron binding.
8 ssential for function and may be involved in iron binding.
9 5 and His280, but not His297, as involved in iron binding.
10 that this function of FHC was independent of iron binding.
11 N(5)-hydroxylated l-ornithines essential for iron binding.
13 ct of AA and EDTA on the catechol or galloyl iron binding ability of pure phenolics, coffee and tea.
14 is reversible but in combination with their iron binding ability to disrupt the active site competit
15 odel of AILI, which was not dependent on its iron-binding ability, inhibition of acetaminophen (APAP)
16 cherichia coli, IscA has a unique and strong iron binding activity and can provide iron for iron-sulp
18 s of iron-sulfur clusters, we reevaluate the iron binding activity of IscA under physiologically rele
20 peroxide, however, IscA completely loses its iron binding activity, whereas CyaY becomes a competent
21 rminal domains of CaM and about the relative iron binding affinities of the N- and C-terminal domains
23 bpA(Y196I), resulted in a greatly diminished iron binding affinity Kd=5.2 x 10(-4) M(-1), approximate
26 magnetic resonance spectroscopy and chemical iron-binding analyses to demonstrate that catecholamine
29 s, revealing dynamic structural changes upon iron binding and core formation, as reflected by a quick
32 the iron primary coordination sphere through iron binding and redox potential modulation may have in
36 nters in iron-dependent enzymes as transient iron binding and shuttling sites to ensure full metal lo
38 o deprotonate the amide moiety of Cys20 upon iron binding and transfer the resulting proton away, thu
39 2.1- to 6-fold while that of genes used for iron binding and transport increased 2.1- to 7.7-fold in
43 ate the role of the synergistic anion in the iron-binding and iron-donating properties of human trans
44 toferrin variants exhibited nearly identical iron-binding and iron-releasing activities and equivalen
45 contrast agents or (phosphorus) metabolites, iron-binding and iron-storage proteins to accumulate iro
46 Human serum transferrin (hTF) is a bilobal iron-binding and transport protein that carries iron in
48 relates with monomeric configuration, labile iron binding, and dynamic contacts with components of th
50 ant correlation between disease severity and iron-binding antioxidant protection (R =.48; p =.00067)
51 on saturation of transferrin) with decreased iron-binding antioxidant protection and elevated plasma
54 and total protein, total antioxidant status, iron-binding antioxidant protection, iron-oxidizing anti
55 n addition to playing a facilitative role in iron binding, appears to have a "gatekeeper" role, there
60 at the E185 residue not only plays a role in iron binding, but also provides the dominant ET pathway
61 and its loss weakens carbonate and therefore iron binding, but maintains the ability of nitrilotriace
63 tructure by circular dichroism spectroscopy, iron-binding by atomic absorption spectrophotometry, oli
66 itin, transferrin saturation (SAT) and total iron binding capacity (TIBC) in 2347 AAs participating i
67 -wide association study of serum iron, total iron binding capacity (TIBC), transferrin saturation, an
70 in secondary structure, DNA binding ability, iron binding capacity, and the ability to form higher-or
72 g, serum ferritin level >15 ng/mL, and total iron-binding capacity <425 mug/dL at the 12-week visit),
73 nsferrin level (1.77 +/- 0.08 g/L) and total iron-binding capacity (46.2 +/- 2.0 microM) were signifi
74 arameters (serum iron, serum ferritin, total iron-binding capacity and transferrin saturation), serum
76 pendent transport system, which exploits the iron-binding capacity of citrate and its natural abundan
77 ence time did not affect the carbon specific iron-binding capacity of the humic substances which was
80 hand, hydrogen peroxide has no effect on the iron binding carboxyl groups in CyaY, allowing the prote
81 wed that the inter-planar angles between the iron-binding catecholamide units in the 5-, 6- and 8-LIC
82 ich the length of the linker between the two iron-binding catecholamide units was increased from four
83 re, we are able to characterize two distinct iron binding channels that facilitate iron ion transport
84 ticle aims to establish the judicious use of iron-binding chemistry of microbial chelators in order t
86 tic iron chelators (e.g., EDTA), and natural iron binding compounds (e.g., desferrioxamine B, ferrich
87 ministration of CO, biliverdin, bilirubin or iron-binding compounds is protective in rodent disease m
90 for membranes and the changes observed upon iron binding could provide unique biological advantages
94 tect them from degeneration, suggesting that iron-binding drugs may one day prove useful in reducing
95 required for completely overcoming negative iron binding effects of polyphenols and similar samples.
97 after 24 h of incubation at 110 microm IBE (iron-binding equivalents) in comparison to simple dialky
98 y after 30 min incubation at 110 microM IBE (iron-binding equivalents), as compared with deferiprone
100 tryptophan residue in close proximity to the iron-binding ferroxidase site (W52 in E. coli Dps).
102 acteriostatic activity of transferrin to its iron-binding function: neither iron-saturated transferri
105 ortem human brain tissue have shown that the iron-binding glycoprotein lactoferrin is upregulated in
107 of the lactotransferrin family of non-haem, iron-binding glycoproteins and is found at high concentr
108 rin is a member of the transferrin family of iron-binding glycoproteins present in milk, mucosal secr
109 e nonfluorescent ferribactin, containing two iron binding groups, into a fluorescent pyoverdine, form
110 ments with PSII(-Mn,+Fe) membranes show that iron binding has little effect on the maximum and minimu
113 ygen depletion in a process that required an iron-binding hemerythrin-like domain in its N terminus.
118 cysteine residues that are essential for the iron binding in IscA abolishes the copper binding activi
121 ctase system are essential for mediating the iron binding in IscA, only catalytic amounts of thioredo
123 expression results in increased capacity for iron binding in the chloroplast of iron-limited cells, w
125 histidine and aspartate residues involved in iron-binding in ETHE1, occupy similar positions to those
129 does not affect aggregation, suggesting that iron binding is a non-conserved part of a more complex c
131 Because Gly65 is hydrogen-bonded to the iron-binding ligand Asp63, it comprises part of the seco
132 containing longer tether lengths between the iron binding ligands (C5) were more efficacious and led
133 entrations of redox-active compounds, strong iron binding ligands (i.e., log K(FeL) > 6), and compoun
135 presumed "dissolved" iron (and probably also iron-binding ligands) are present in colloidal size rang
137 glycine spacers, whereas in enterobactin the iron-binding moieties are directly attached to a tri-l-s
138 hore structures have been characterized, the iron-binding moieties often contain catecholate or hydro
144 y to capture and deplete siderophores, small iron-binding molecules that are synthesized by certain b
153 ones and inotropes could directly affect the iron binding of serum-transferrin so that the normally h
154 nism(s) by which the stress hormones perturb iron binding of these key innate immune defense proteins
155 iron to DOHH stoichiometry and dependence of iron binding on each of the four conserved His-Glu motif
156 l transferrins is the absolute dependence of iron binding on the concomitant binding of a synergistic
158 t concentrations of soluble iron and soluble iron-binding organic ligands are much lower than previou
159 strate Hs holofrataxin to be a high affinity iron binding partner for Hs ferrochelatase that is capab
162 bove-mentioned tyrosine at the corresponding iron-binding position, with that of Schizosaccharomyces
163 The use of the synergistic anion and this iron binding process results in an extremely high affini
164 have characterized the overall stability and iron binding properties of the Drosophila frataxin homol
165 f the citric acid stereocenter perturbed the iron-binding properties and siderophore function of SB a
166 tes (one in each lobe), they differ in their iron-binding properties and their responsiveness to comp
167 wed that the ATCC 19606(T) NfuA ortholog has iron-binding properties compatible with the formation of
169 Selective (lobe-specific) modulation of the iron-binding properties of hTF using recombinant forms o
173 ortholog of human Dph4 also shows a similar iron-binding property, indicating the conserved nature o
175 tion via either transgenic expression of the iron binding protein ferritin or oral administration of
176 Aconitase was found to associate with the iron binding protein frataxin exclusively during reperfu
177 solved in complex with human transferrin, an iron binding protein normally responsible for delivering
178 iron transporter gene (CBU1766), a putative iron binding protein-encoding gene (CBU0970), and a cati
180 ), IgG-binding protein A (Spa), and the heme-iron-binding protein (IsdA) were most abundant in the ag
182 ut the dual effects of NGAL as a siderophore:iron-binding protein and as a growth factor and examines
183 g activity, whereas CyaY becomes a competent iron-binding protein and attenuates the iron-mediated pr
189 Finally, LF was identified as the major iron-binding protein in parotid saliva by 59Fe autoradio
195 by reduced activity of frataxin, a conserved iron-binding protein of the mitochondrial matrix, though
197 xpression of frataxin (FXN), a mitochondrial iron-binding protein required for Fe-S cluster assembly.
198 r, recent evidence indicated that IscA is an iron-binding protein that can provide iron for the iron-
199 er, recent studies indicated that IscA is an iron-binding protein that can provide iron for the iron-
200 reover, increased apical release of the host iron-binding protein transferrin during RSV infection pr
204 l gelatinase-associated lipocalin (NGAL), an iron-binding protein up-regulated in response to kidney
207 this recessive disorder, is a mitochondrial iron-binding protein, but how its deficiency leads to ne
208 ike proteins are oxygen-carrying non-heme di-iron binding proteins and their functions have effect on
211 stasis is typically regulated by cytoplasmic iron binding proteins, but here we describe a signal tra
212 In the present study, we tested whether iron binding proteins; apotransferrin, lactoferrin and o
214 , exomycobactins, compete for iron with host iron-binding proteins and, together with the iron-regula
215 f frataxins, a family of small mitochondrial iron-binding proteins found in organisms ranging from ba
216 tic transferrins comprise a class of bilobal iron-binding proteins in which each lobe carries a singl
218 boratory cultures that ferritin and the main iron-binding proteins involved in photosynthesis and nit
220 at the syphilis spirochete lacks most of the iron-binding proteins present in many other bacterial pa
221 f satisfying its iron requirement with human iron-binding proteins such as transferrin and lactoferri
222 ning of the human homologs to IscU and NifU, iron-binding proteins that play a critical role in Fe-S
224 olamines binding to the high-affinity ferric-iron-binding proteins transferrin (Tf) and lactoferrin,
225 were found, as well as other mRNAs encoding iron-binding proteins, bringing the total number of regu
226 wn siderophores but can employ host-derived, iron-binding proteins, including transferrin and lactofe
227 ke other members of the transferrin class of iron-binding proteins, is a bilobal structure, the produ
228 iron load is, perhaps, by the expression of iron-binding proteins, specifically the iron storage pro
229 sion of receptors that are specific for host iron-binding proteins, such as transferrin and lactoferr
230 ria gonorrhoeae is capable of utilizing host iron-binding proteins, such as transferrin, lactoferrin,
236 cles (OMVs) by directly interacting with the iron-binding Pseudomonas quinolone signal (PQS), a cell-
237 native iron sequestration behavior; however, iron binding rates are altered, enabling assignment of s
238 , whereas mutations of the non-conserved/non-iron binding residues resulted in 20-30% reduction of SH
239 double stranded beta-helix fold and ferrous iron binding residues that are present in 2-oxoglutarate
240 site anion appears to arrange the C-terminal iron-binding residues conducive to complementary binding
245 om other organisms, Y4 lacks three conserved iron-binding residues, and its exact function is unclear
246 e of the beta-sheet, adjacent to the acidic, iron binding ridge, is important for interaction of Yfh1
250 ear whether ferric iron uptake or the ferric iron binding siderophores enterobactin and salmochelin a
252 ear whether frataxin is directly involved in iron binding, since the yeast orthologue, but not the hu
253 that in fact the Zn2 site is the regulatory iron binding site and the Zn1 site plays an auxiliary ro
254 human transferrin, a bilobal protein with an iron binding site in each lobe, we have selectively muta
255 ult of self-assembly of 24 subunits, to a di-iron binding site, the ferroxidase center, buried in the
256 The structures reveal a novel trinuclear iron binding site, which is implicated in catalysis and
259 ins are highly conserved, EcFtnA has a third iron-binding site (C site) in close proximity to the din
260 MJD1A in intact cells, and disruption of the iron-binding site decreases binding of nickel ions to AB
261 ive activation only occurred when a putative iron-binding site in FirS and the key phosphorylation as
265 bal protein, with each lobe bearing a single iron-binding site, functions to transport iron into cell
276 ity and identical ligand structures of their iron-binding sites (one in each lobe), they differ in th
278 N-lobe but leads to the appearance of novel iron-binding sites of varying structure and stability.
282 Because the mutant proteins are impaired in iron binding, these residues are concluded to coordinate
283 Hydrogen peroxide appears to oxidize the iron binding thiol groups in IscA, thus blocking the iro
284 As shown by others, Cp markedly increased iron binding to apotransferrin at acidic pH; however, th
292 tion of the His 249 residue does not abolish iron binding to the transferrin N-lobe but leads to the
294 The major yolk protein of sea urchins is an iron-binding, transferrin-like molecule that is made in
296 r iron revealed an uncommon mode of non-heme iron binding trapped by the non-catalytic Co(2+), which,
298 c binding parameters for protein partner and iron binding were measured for the yeast orthologs using
300 didacidal ability of Hst 5 was observed upon iron binding, with increasing iron concentrations being
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