PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
12738232-3	2003	In both cells, the rate of uptake of 59Fe from transferrin was insignificant, compared to the rate of uptake from non-transferrin-bound iron (NTBI).	Iron-59	37-41	transferrin	Rattus norvegicus	47-58
12553165-21	2002	Intracerebroventricular injection of [59Fe125I]transferrin led to a higher accumulation of 59Fe than of [125I]transferrin in the brain.	Iron-59	38-42	transferrin	Rattus norvegicus	47-58
12445858-2	2002	Reticulocytes labeled with 59Fe(2)-transferrin in which heme synthesis was inhibited by succinylacetone were used as a model of 59Fe mobilization.	Iron-59	27-31	transferrin	Homo sapiens	35-46
12553165-10	2002	Intravenous injection of [59Fe-125]transferrin led to an almost two-fold higher accumulation of 59Fe than of [125I]transferrin in the brain.	Iron-59	26-30	transferrin	Rattus norvegicus	35-46
12553165-10	2002	Intravenous injection of [59Fe-125]transferrin led to an almost two-fold higher accumulation of 59Fe than of [125I]transferrin in the brain.	Iron-59	26-30	transferrin	Rattus norvegicus	115-126
12553165-21	2002	Intracerebroventricular injection of [59Fe125I]transferrin led to a higher accumulation of 59Fe than of [125I]transferrin in the brain.	Iron-59	38-42	transferrin	Rattus norvegicus	110-121
9578471-11	1998	Incubations carried out using 55Fe-labelled citrate in the presence of 59Fe-labelled diferric transferrin indicated that citrate-mediated iron binding by the cells decreased with increasing diferric transferrin concentrations but the citrate iron was not replaced by iron from transferrin during the 15-min incubation period.	Iron-59	71-75	transferrin	Rattus norvegicus	94-105
11683638-10	2001	Surprisingly, apo-hLF (but not apotransferrin) was almost as effective in blocking 59Fe uptake as bismuth-loaded lactoferrin.	Iron-59	83-87	HLF transcription factor, PAR bZIP family member	Homo sapiens	18-21
10560945-7	1999	These ligands were highly effective at both mobilizing 59Fe from cells and preventing 59Fe uptake from 59Fe-transferrin and caused a marked increase in the RNA-binding activity of the iron-regulatory proteins (IRP).	Iron-59	86-90	transferrin	Homo sapiens	108-119
9989766-3	1999	In the present study we have examined the effect of small molecular weight (M(r)) Fe complexes on Fe uptake from iron 59-labeled transferrin (Tf) and 59Fe-labeled citrate by primary cultures of hepatocytes.	Iron-59	113-120	transferrin	Homo sapiens	129-140
12374293-4	2002	Pulse labeling with 59Fe through the root system shows that the irt1 mutation reduces iron accumulation in the shoots.	Iron-59	20-24	iron-regulated transporter 1	Arabidopsis thaliana	64-68
10945243-8	2000	When the RAW264.7 macrophage cell line was activated to produce NO by incubation with lipopolysaccharide or lipopolysaccharide and interferon-gamma, a decrease in 59Fe uptake from 59Fe-labeled Tf was also observed.	Iron-59	163-167	interferon gamma	Mus musculus	131-147
10945243-8	2000	When the RAW264.7 macrophage cell line was activated to produce NO by incubation with lipopolysaccharide or lipopolysaccharide and interferon-gamma, a decrease in 59Fe uptake from 59Fe-labeled Tf was also observed.	Iron-59	180-184	interferon gamma	Mus musculus	131-147
10865941-4	2000	Cells were incubated with 59Fe-125I-Tf; Fe uptake was shown to increase linearly over time for both cell lines, while Tf uptake reached a plateau within 2 h. Both Tf and Fe uptake were saturable.	Iron-59	26-30	transferrin	Mus musculus	36-38
9989766-6	1999	For example, at a physiologically relevant Tf-Fe concentration of 25 micromol/L, there was an 8-fold increase in 59Fe uptake by cells incubated with FAC compared to control cells.	Iron-59	113-117	FA complementation group C	Homo sapiens	149-152
9989766-7	1999	In contrast, at Tf-Fe concentrations of 0.25 to 2.5 micromol/L, 59Fe uptake in FAC-treated cells was only 1-fold to 3-fold greater than that in the corresponding controls.	Iron-59	64-68	FA complementation group C	Homo sapiens	79-82
9578471-11	1998	Incubations carried out using 55Fe-labelled citrate in the presence of 59Fe-labelled diferric transferrin indicated that citrate-mediated iron binding by the cells decreased with increasing diferric transferrin concentrations but the citrate iron was not replaced by iron from transferrin during the 15-min incubation period.	Iron-59	71-75	transferrin	Rattus norvegicus	199-210
9578471-11	1998	Incubations carried out using 55Fe-labelled citrate in the presence of 59Fe-labelled diferric transferrin indicated that citrate-mediated iron binding by the cells decreased with increasing diferric transferrin concentrations but the citrate iron was not replaced by iron from transferrin during the 15-min incubation period.	Iron-59	71-75	transferrin	Rattus norvegicus	199-210
9353884-7	1997	The presence of the anti-transferrin receptor antibody OX-26 significantly reduced uptake of 59Fe by 60% and 64% into cerebral hemisphere and cerebellum, respectively.	Iron-59	93-97	transferrin	Rattus norvegicus	25-36
9514199-5	1998	The absence of Tf in the media resulted in a significant increase in 59iron uptake in both normal and Hp glial but did not affect Mn uptake.	Iron-59	69-75	transferrin	Mus musculus	15-17
9514199-6	1998	Elevated Tf (10X normal) in the media reduced both 59iron and 54Mn uptake.	Iron-59	51-57	transferrin	Mus musculus	9-11
8756083-1	1996	Injection of bacterial endotoxin or granulocyte/macrophage colony-stimulating factor (GM-CSF) into exhypoxic polycythemic mice simultaneously with erythropoietin (EPO) suppressed erythroid cell formation, as monitored by 59Fe incorporation into circulating red blood cells.	Iron-59	221-225	colony stimulating factor 2 (granulocyte-macrophage)	Mus musculus	36-84
9290151-3	1997	Rat transferrin labelled with 59Fe was added for the final 0.1, 0.5, 6, 24 or 48 h of culture.	Iron-59	30-34	transferrin	Rattus norvegicus	4-15
9226184-7	1997	Cells were incubated with 59Fe-labeled human diferric transferrin (Tf), then chased, and intracellular radioiron distribution between Ft and Hb was determined on subsequent days by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and/or Ft immunoprecipitation and heme extraction.	Iron-59	26-30	transferrin	Homo sapiens	54-65
9108424-5	1997	Additional experiments showed that, in contrast to DFO, the 5 analogues were potent at preventing 59Fe uptake from transferrin (Tf) and increasing 59Fe release from cells at concentrations as low as 10 micromol/L.	Iron-59	98-102	transferrin	Homo sapiens	115-126
9108424-5	1997	Additional experiments showed that, in contrast to DFO, the 5 analogues were potent at preventing 59Fe uptake from transferrin (Tf) and increasing 59Fe release from cells at concentrations as low as 10 micromol/L.	Iron-59	98-102	transferrin	Homo sapiens	128-130
9108424-6	1997	Examination of the distribution of 59Fe in neoplastic cells using native polyacrylamide gel electrophoresis (PAGE)/59Fe-autoradiography showed that most of the 59Fe taken up from Tf was incorporated into ferritin, although 3 other previously unrecognized components (bands A, B, and C) were also identified.	Iron-59	35-39	transferrin	Homo sapiens	179-181
8889603-6	1996	The results show that cellular 59Fe release increased linearly as a function of preincubation time with 59Fe-Tf subsequent to mechanical detachment at 4 degrees C using a spatula.	Iron-59	31-35	transferrin	Homo sapiens	109-111
8889603-6	1996	The results show that cellular 59Fe release increased linearly as a function of preincubation time with 59Fe-Tf subsequent to mechanical detachment at 4 degrees C using a spatula.	Iron-59	104-108	transferrin	Homo sapiens	109-111
8889603-9	1996	Examination of the 59Fe released showed that after a 4-h preincubation with 59Fe-Tf, approximately 50% of the 59Fe was present in ferritin.	Iron-59	19-23	transferrin	Homo sapiens	81-83
8756083-1	1996	Injection of bacterial endotoxin or granulocyte/macrophage colony-stimulating factor (GM-CSF) into exhypoxic polycythemic mice simultaneously with erythropoietin (EPO) suppressed erythroid cell formation, as monitored by 59Fe incorporation into circulating red blood cells.	Iron-59	221-225	colony stimulating factor 2 (granulocyte-macrophage)	Mus musculus	86-92
8756083-1	1996	Injection of bacterial endotoxin or granulocyte/macrophage colony-stimulating factor (GM-CSF) into exhypoxic polycythemic mice simultaneously with erythropoietin (EPO) suppressed erythroid cell formation, as monitored by 59Fe incorporation into circulating red blood cells.	Iron-59	221-225	erythropoietin	Mus musculus	163-166
8641663-1	1996	The 59Fe uptake into bone marrow and spleen was measured as a function of time after a single dose of T-2 toxin in mice (2.0 mg/kg, sc).	Iron-59	4-8	brachyury 2	Mus musculus	102-105
8605367-2	1996	When reticulocytes are incubated with 59Fe-transferrin (59Fe-Tf) in the presence of SA, there is an accumulation of 59Fe in the mitochondrion and in a cytosolic non-heme intermediate that has been described as a putative Fe transporter (Adams et al, Biochim Biophys Acta 1012:243, 1989).	Iron-59	38-42	serotransferrin	Oryctolagus cuniculus	43-54
7541668-5	1995	Addition of SCF to the ECFC in serum-free liquid culture, together with erythropoietin (EP) and insulin-like growth factor 1 (IGF-1), resulted in a marked increase in DNA synthesis, associated with a delayed peak in cellular benzidine positivity and a delayed incorporation of 59Fe into hemoglobin compared with cultures without SCF.	Iron-59	277-281	KIT ligand	Homo sapiens	12-15
8558296-4	1996	Full recovery (89-109%) from anemia and increased tissue iron occurred after 28 d of treatment with any of the iron sources, which contrasts to past bioavailability studies using 59Fe-labeled ferritin and generally shorter periods of observation.	Iron-59	179-183	ferritin-1, chloroplastic	Glycine max	192-200
7492790-9	1995	Most of the PIH analogues were considerably more effective than DFO at both preventing 59Fe uptake from 59Fe-transferrin and in mobilizing 59Fe from prelabeled NB cells.	Iron-59	87-91	transferrin	Homo sapiens	109-120
7488642-1	1995	Recent studies have demonstrated that preincubation of SK-Mel-28 melanoma cells with ferric ammonium citrate (FAC) resulted in marked stimulation of 59Fe uptake from 59Fe-125I-transferrin (Tf), but only at Tf concentrations above that required for saturation of the Tf receptor (Richardson and Baker (1992) J. Biol.	Iron-59	149-153	transferrin	Homo sapiens	176-187
7488642-10	1995	However, the addition of free radical scavengers to FAC such as catalase, superoxide dismutase, ceruloplasmin, Hepes, mannitol and high concentrations of BSA or ascorbate, markedly depressed FAC-activated 59Fe uptake from 59Fe-125I-Tf and 59Fe-citrate.	Iron-59	205-209	ceruloplasmin	Homo sapiens	96-109
7488642-10	1995	However, the addition of free radical scavengers to FAC such as catalase, superoxide dismutase, ceruloplasmin, Hepes, mannitol and high concentrations of BSA or ascorbate, markedly depressed FAC-activated 59Fe uptake from 59Fe-125I-Tf and 59Fe-citrate.	Iron-59	222-226	ceruloplasmin	Homo sapiens	96-109
8647512-10	1995	injection of the hormone and sampling by cardiac puncture every hour for 6 h. RESULTS: Administration of rhEPO to mice increased splenic 59Fe uptake significantly without affecting the hematocrit, the plasma EPO level or the plasma disappearance of radiolabeled EPO.	Iron-59	137-141	erythropoietin	Mus musculus	107-110
7556141-7	1995	By comparison, the uptake of 59Fe from the N-fragment was inhibited 70% by excess nonradioactive diferric transferrin.	Iron-59	29-33	transferrin	Rattus norvegicus	106-117
7751970-2	1994	Two 59Fe peaks (peaks 1 and 2) were separated on Sepharose 6B gel filtration from detergent solubilized 20,000 x g precipitate of upper intestinal mucosal homogenate after administration of 59Fe-labelled ferrous materials.	Iron-59	4-8	pseudopodium-enriched atypical kinase 1	Rattus norvegicus	16-29
7814363-13	1995	Similarly, a gain-of-function mutation, MAC1up1, which causes elevated and unregulated transcription from FRE1 and elevated Fe(III) reduction and 59Fe uptake exhibits a similar phenotype with respect to Cu(II) reduction and 64Cu uptake.	Iron-59	146-150	Mac1p	Saccharomyces cerevisiae S288C	40-47
7751970-5	1994	The treatment of mucosal homogenate with 5 mM ethylenediaminetetraacetic acid released 59Fe binding from peak 1.	Iron-59	87-91	pseudopodium-enriched atypical kinase 1	Rattus norvegicus	105-111
7964124-12	1994	Moreover, when pyridoxal isonicotinoyl hydrazone (0.2 mmol/L) was added together with labeled transferrin over a 2-hour incubation, 59Fe uptake from transferrin decreased to 18% of the control value, whereas deferoxamine (0.2 mmol/L) had no appreciable effect.	Iron-59	132-136	transferrin	Homo sapiens	94-105
7964124-12	1994	Moreover, when pyridoxal isonicotinoyl hydrazone (0.2 mmol/L) was added together with labeled transferrin over a 2-hour incubation, 59Fe uptake from transferrin decreased to 18% of the control value, whereas deferoxamine (0.2 mmol/L) had no appreciable effect.	Iron-59	132-136	transferrin	Homo sapiens	149-160
12232304-4	1994	Uptake experiments with 59Fe-labeled DMA, purified from root exudates of either Fe-deficient Alice or ys1 plants, showed up to 20 times lower uptake and translocation of 59Fe in ys1 than in Alice or WF9 plants.	Iron-59	24-28	iron-phytosiderophore transporter yellow stripe 1	Zea mays	102-105
12232304-4	1994	Uptake experiments with 59Fe-labeled DMA, purified from root exudates of either Fe-deficient Alice or ys1 plants, showed up to 20 times lower uptake and translocation of 59Fe in ys1 than in Alice or WF9 plants.	Iron-59	24-28	iron-phytosiderophore transporter yellow stripe 1	Zea mays	178-181
8408013-8	1993	The cells rapidly acquired iron from transferrin, but uptake from lactoferrin was 10-fold slower and probably resulted from transfer of 59Fe from lactoferrin to unlabeled transferrin during culture.	Iron-59	136-140	transferrin	Homo sapiens	171-182
8204100-0	1994	Effects of acute ethanol administration on the uptake of 59Fe-labeled transferrin by rat liver and cerebellum.	Iron-59	57-61	transferrin	Rattus norvegicus	70-81
8147916-6	1994	Inhibitions due to the antibody were less complete in liver and renal cortex, and there was evidence of some non-transferrin-mediated transport during infusion of 59Fe/ascorbate.	Iron-59	163-167	transferrin	Mus musculus	113-124
8196264-9	1994	Subcellular fractionation following the uptake of 59Fe, 125I-Tf in Al-loaded FEC showed increased uptake of 59Fe in the nuclear and mitochondrial compartments with no increase in the cytosol.	Iron-59	50-54	transferrin	Homo sapiens	61-63
8196264-9	1994	Subcellular fractionation following the uptake of 59Fe, 125I-Tf in Al-loaded FEC showed increased uptake of 59Fe in the nuclear and mitochondrial compartments with no increase in the cytosol.	Iron-59	108-112	transferrin	Homo sapiens	61-63
8401252-2	1993	The response to recombinant human EPO was measured in post-hypoxic polycythemic mice by determination of 59Fe uptake into red cells, spleen and femur and/or erythroid colony forming units (CFU-E) and erythroid precursor cell concentrations in femoral marrow.	Iron-59	105-109	erythropoietin	Homo sapiens	34-37
8358725-6	1993	Further studies that quantitated cellular incorporation of 59Fe from added transferrin-59Fe in the presence of DFO indicated that neuroblastoma cells were more sensitive to inhibition of Fe incorporation by the chelator as compared to the other cell line.	Iron-59	59-63	transferrin	Homo sapiens	75-86
8417135-1	1993	Uptake of 59Fe from blood into brains of anaesthetized rats and mice has been studied by intravenous infusion of [59Fe]ferrous ascorbate or of 59Fe-transferrin, the results not being significantly different.	Iron-59	10-14	transferrin	Mus musculus	148-159
1568461-0	1992	Non-transferrin dependent 59Fe uptake in phytohemagglutinin-stimulated human peripheral lymphocytes.	Iron-59	26-30	transferrin	Homo sapiens	4-15
1472048-7	1992	Accumulation of [59Fe]hemin could be blocked by a 100-fold excess of diferric transferrin but not by apotransferrin.	Iron-59	17-22	transferrin	Mus musculus	78-89
1462353-1	1992	Previous studies revealed that a single dose of T-2 toxin produces a strong inhibition of the 59Fe incorporation into circulating erythrocytes in mice.	Iron-59	94-98	brachyury 2	Mus musculus	48-51
1419828-5	1992	Taking into account the specific activity of 59Fe-3H labelled transferrin, we found that 95% of the transferrin uptake was degraded.	Iron-59	45-49	transferrin	Rattus norvegicus	62-73
1419828-5	1992	Taking into account the specific activity of 59Fe-3H labelled transferrin, we found that 95% of the transferrin uptake was degraded.	Iron-59	45-49	transferrin	Rattus norvegicus	100-111
1419828-7	1992	3H-labelled apotransferrin appears in the supernatant of the cell culture at the same rate as 59Fe-3H labelled diferric transferrin, showing an identical uptake for the two types of transferrin.	Iron-59	94-98	transferrin	Rattus norvegicus	120-131
1568461-7	1992	In contrast, the uptake of 59Fe from non-transferrin 59Fe donors in cells stimulated with 5-20 micrograms/ml PHA was greater than that in cells grown with 1 or 2 micrograms/ml PHA.	Iron-59	27-31	transferrin	Homo sapiens	41-52
1302169-2	1992	Diferric bovine transferrin labeled with 59Fe was used as an iron donor.	Iron-59	41-45	serotransferrin	Bos taurus	16-27
1734036-6	1992	In short-term (1-2 hours) incubation, SA inhibited 59Fe incorporation from transferrin into heme, whereas total cellular 59Fe uptake was increased.	Iron-59	51-55	transferrin	Mus musculus	75-86
1919575-8	1991	125I-Tf uptake by the brains of the iron-deficient rats increased very rapidly after injection of the labelled proteins, within 15 min reaching a plateau level which was maintained for at least 6 h. The uptake of 59Fe, however, increased rapidly for 1 h and then more slowly, and in terms of percentage of injected dose reached much higher values than did 125I-Tf uptake.	Iron-59	213-217	transferrin	Rattus norvegicus	5-7
1793828-3	1991	Activin alone had no effect in polycythemic BDF1 mice, but synergised with epo to significantly enhance 59Fe-incorporation into erythrocytes.	Iron-59	104-108	inhibin subunit beta E	Homo sapiens	0-7
1793828-3	1991	Activin alone had no effect in polycythemic BDF1 mice, but synergised with epo to significantly enhance 59Fe-incorporation into erythrocytes.	Iron-59	104-108	erythropoietin	Mus musculus	75-78
2369744-3	1990	In s.c. RIF-1 tumors (C3H/HeJ mice) ketoconazole potentiated IL-1 alpha induced hemorrhagic necrosis (59Fe labeled RBC uptake) and prolonged intervals of low tumor perfusion (86Rb+ uptake) and attendant depletion of tumor high energy phosphate reserves as determined by in vivo 31P nuclear magnetic resonance spectroscopy.	Iron-59	102-106	interleukin 1 alpha	Mus musculus	61-71
2398066-8	1990	Consistent with these observations, it was found that cells expressing palmitoylation-defective transferrin receptors exhibited an increased rate of accumulation of [59Fe]diferric transferrin.	Iron-59	166-170	transferrin	Homo sapiens	96-107
2398066-8	1990	Consistent with these observations, it was found that cells expressing palmitoylation-defective transferrin receptors exhibited an increased rate of accumulation of [59Fe]diferric transferrin.	Iron-59	166-170	transferrin	Homo sapiens	180-191
1831796-6	1991	When the cells were incubated in the presence of 59Fe-labelled transferrin and 55Fe-labelled ferritin, no difference in relative availability of iron to E. coli was observed, suggesting that differences in the ability of aerobactin and enterochelin to remove iron from intracellular ferritin were not responsible for this preference.	Iron-59	49-53	transferrin	Homo sapiens	63-74
1931436-3	1991	Cell association of rat 125I-Tf was measured at Tf concentrations approaching physiological, where 59Fe uptake obeyed first-order kinetics.	Iron-59	99-103	transferrin	Rattus norvegicus	29-31
1675959-2	1991	The role of specific interaction between transferrin and its receptors in iron uptake by the liver in vivo was investigated using 59Fe-125I-labelled transferrins from several animal species, and adult and 15-day rats.	Iron-59	130-134	transferrin	Rattus norvegicus	41-52
1675959-3	1991	Transferrin-free hepatic uptake of 59Fe was measured 2 or 0.5 hr after intravenous injection of the transferrins.	Iron-59	35-39	transferrin	Rattus norvegicus	0-11
2046086-4	1991	Subsequent to Fe2(III)-transferrin internalization the flux of 59Fe was followed through three compartments: internalized transferrin, membrane, and cytosol.	Iron-59	63-67	serotransferrin	Oryctolagus cuniculus	23-34
2046086-4	1991	Subsequent to Fe2(III)-transferrin internalization the flux of 59Fe was followed through three compartments: internalized transferrin, membrane, and cytosol.	Iron-59	63-67	serotransferrin	Oryctolagus cuniculus	122-133
1763410-1	1991	The 24-h and 72-h incorporation of 59Fe into circulating erythrocytes in mice were strongly inhibited by a single subcutaneous dose of T-2 toxin given 1 h before the radioisotope.	Iron-59	35-39	brachyury 2	Mus musculus	135-152
2250602-3	1990	The plasma space in skin samples taken at the end of the experiment was estimated by a 3-min accumulation of 59Fe-labeled bovine transferrin.	Iron-59	109-113	serotransferrin	Bos taurus	129-140
2140960-4	1990	The particulate 59Fe was localized to the basolateral membranes using the marker enzyme Na+, K+ activated, Mg2+ dependent, ATPase and by washing intact enterocytes with the selective plasma membrane perturbant digitonin.	Iron-59	16-20	dynein, axonemal, heavy chain 8	Mus musculus	123-129
2327400-2	1990	The 1,2-dimethyl (L1) and 1-ethyl-2-methyl (L1NEt) derivatives of 3-hydroxypyrid-4-one markedly enhanced iron mobilisation from macrophages pulsed with 59Fe-transferrin-antitransferrin immune complexes and were more effective than desferrioxamine, maltol, or mimosine.	Iron-59	152-156	transferrin	Mus musculus	157-168
2333967-1	1990	Interaction of 59Fe-labeled rat transferrin, human lactoferrin, and bovine lactoferrin with rat small intestinal brush-border membrane vesicles was investigated with the use of a rapid filtration technique.	Iron-59	15-19	transferrin	Rattus norvegicus	32-43
2333967-2	1990	Specific binding of 59Fe-labeled rat transferrin and bovine lactoferrin to brush-border membrane vesicles from suckling and adult rats was identified.	Iron-59	20-24	transferrin	Rattus norvegicus	37-48
2613917-2	1989	The clearance of 59Fe-labelled transferrin from the plasma was analysed to quantify total, effective, and ineffective erythropoiesis, denoted by the terms marrow iron turnover (MIT), red cell iron turnover (RCIT), and per cent ineffective iron turnover (IIT%), respectively, in 12 cases of this disease.	Iron-59	17-21	transferrin	Homo sapiens	31-42
2386533-1	1990	Hemin inhibited 59Fe uptake from transferrin (Tf) by mouse erythro-leukemia cells (MELC) induced for differentiation by hexamethylene bisacetamide (HMBA), but the rate and the extent of 125I-Tf endocytosis was unaffected.	Iron-59	16-20	transferrin	Mus musculus	33-44
2386533-1	1990	Hemin inhibited 59Fe uptake from transferrin (Tf) by mouse erythro-leukemia cells (MELC) induced for differentiation by hexamethylene bisacetamide (HMBA), but the rate and the extent of 125I-Tf endocytosis was unaffected.	Iron-59	16-20	transferrin	Mus musculus	46-48
2386533-2	1990	Hemin inhibited 59Fe incorporation into heme by a greater proportion than the overall uptake of 59Fe from Tf.	Iron-59	96-100	transferrin	Mus musculus	106-108
2328142-1	1990	The binding of the 59Fe and 239Pu complexes of transferrin and 125I labelled transferrin [Tf (125I)] to isolated cell membranes of rat liver has been studied.	Iron-59	19-23	transferrin	Rattus norvegicus	47-58
2328142-1	1990	The binding of the 59Fe and 239Pu complexes of transferrin and 125I labelled transferrin [Tf (125I)] to isolated cell membranes of rat liver has been studied.	Iron-59	19-23	transferrin	Rattus norvegicus	77-88
2326236-3	1990	Both 125I-labelled and 59Fe-labelled transferrin were internalized by receptor-mediated endocytosis with similar rates.	Iron-59	23-27	transferrin	Homo sapiens	37-48
2128422-4	1990	Kinetic studies using 125I, 59Fe-labeled transferrin indicated that the step of ferrotransferrin internalization was selectively inhibited by the toxin while the surface receptor-binding capacity, the externalization of previously internalized transferrin, and the cellular ATP levels were not affected.	Iron-59	28-32	serotransferrin	Oryctolagus cuniculus	41-52
2128422-4	1990	Kinetic studies using 125I, 59Fe-labeled transferrin indicated that the step of ferrotransferrin internalization was selectively inhibited by the toxin while the surface receptor-binding capacity, the externalization of previously internalized transferrin, and the cellular ATP levels were not affected.	Iron-59	28-32	serotransferrin	Oryctolagus cuniculus	85-96
2732309-5	1989	The participation of transferrin in iron absorption was investigated by the absorption through the intestinal segment of rats, into which 59Fe labeled diferric transferrin was injected.	Iron-59	138-142	transferrin	Rattus norvegicus	160-171
2605128-3	1989	Haemin inhibited 59Fe incorporation into haem by a greater proportion than the overall uptake of 59Fe from Tf.	Iron-59	97-101	transferrin	Mus musculus	107-109
2605128-4	1989	The reduction of total cellular 59Fe uptake was more pronounced at 59Fe-Tf concentrations closer to saturation.	Iron-59	32-36	transferrin	Mus musculus	72-74
2511038-1	1989	As part of a continuing study of the low MW iron pool, guinea pig reticulocytes were incubated with 59Fe-labeled transferrin, and the reticulocyte hemolysate was chromatographed on Sephadex G-25.	Iron-59	100-104	inhibitor of carbonic anhydrase	Cavia porcellus	113-124
2730581-8	1989	However, under these conditions, the uptake of 59Fe was dramatically inhibited as a result of prolongation of the transferrin-transferrin-receptor complex recycling time.	Iron-59	47-51	transferrin	Homo sapiens	114-125
2730581-8	1989	However, under these conditions, the uptake of 59Fe was dramatically inhibited as a result of prolongation of the transferrin-transferrin-receptor complex recycling time.	Iron-59	47-51	transferrin	Homo sapiens	126-137
2463988-7	1989	The incorporation of 59Fe into protein demonstrated a linear dose response (from 0.002 to 1.5 units of epo/ml) beginning 60 h after addition of the hormone to the cultures, and there was a dose-dependent increase (from 0.1 to 1.0 unit of epo/ml) in the formation of hemoglobin-containing colonies.	Iron-59	21-25	erythropoietin	Homo sapiens	103-106
2751879-1	1989	It is known that a medium conditioned by erythrocytes (ECM) reduces 59Fe uptake into haem in hemopoietic cell cultures.	Iron-59	68-72	multimerin 1	Homo sapiens	55-58
2463988-7	1989	The incorporation of 59Fe into protein demonstrated a linear dose response (from 0.002 to 1.5 units of epo/ml) beginning 60 h after addition of the hormone to the cultures, and there was a dose-dependent increase (from 0.1 to 1.0 unit of epo/ml) in the formation of hemoglobin-containing colonies.	Iron-59	21-25	erythropoietin	Homo sapiens	238-241
3240225-2	1988	Both EPO preparations have been characterized biologically: The proliferation of murine spleen cells in vitro after pretreatment with phenylhydrazine and the 59Fe incorporation into the heme of polycythemic mice have been determined.	Iron-59	158-162	erythropoietin	Mus musculus	5-8
3398696-5	1988	Albuterol, a beta 2-adrenergic agonist, enhanced % 59Fe incorporation in polycythemic mice and low doses of CHA (50 and 100 nmol/kg/day), which were not effective alone on % 59Fe incorporation in polycythemic mice exposed to hypoxia, inhibited the enhancement in radioiron induced by albuterol (25 and 100 micrograms/kg/day, i.p.)	Iron-59	51-55	histocompatibility 2, O region beta locus	Mus musculus	11-19
2784116-8	1989	Although cachectin/TNF-IL 1-, or endotoxin treatment resulted in similar hypoferremia and shortened plasma iron half-life, endotoxin or cachectin/TNF treatment (but not IL 1) significantly reduced the incorporation of plasma 59Fe into newly synthesized RBCs.	Iron-59	225-229	tumor necrosis factor	Homo sapiens	9-18
2784116-8	1989	Although cachectin/TNF-IL 1-, or endotoxin treatment resulted in similar hypoferremia and shortened plasma iron half-life, endotoxin or cachectin/TNF treatment (but not IL 1) significantly reduced the incorporation of plasma 59Fe into newly synthesized RBCs.	Iron-59	225-229	tumor necrosis factor	Homo sapiens	136-145
2784116-8	1989	Although cachectin/TNF-IL 1-, or endotoxin treatment resulted in similar hypoferremia and shortened plasma iron half-life, endotoxin or cachectin/TNF treatment (but not IL 1) significantly reduced the incorporation of plasma 59Fe into newly synthesized RBCs.	Iron-59	225-229	tumor necrosis factor	Homo sapiens	146-149
3402348-4	1988	Iron [59Fe] incorporation was enhanced in the spleens, livers, bone marrow, and blood of the GAA-treated rats, and increased as the time post-[59Fe] injection increased.	Iron-59	6-10	alpha glucosidase	Rattus norvegicus	93-96
3429053-2	1987	This was assessed by measuring the uptake of Fe from 59Fe-125I-labelled rat Tf by Sertoli cells and round spermatids in vitro.	Iron-59	53-57	transferrin	Rattus norvegicus	76-78
3478338-2	1987	The maximal rate of iron uptake from 59Fe-labeled transferrin, 1.5 X 10(6) atoms of Fe/cell per 30 min in uninduced cells, increased to 3 X 10(6) atoms/cell after 5 days of induction.	Iron-59	37-41	transferrin	Homo sapiens	50-61
3689862-6	1987	Furthermore, after a single intratesticular injection of 59Fe-labeled human transferrin, radiolabeled rat transferrin was immunoprecipitated from homogenates of isolated tubules with a specific antibody and appeared as a single radioactive band on fluorographs of urea/polyacrylamide gels.	Iron-59	57-61	transferrin	Homo sapiens	76-87
3689862-6	1987	Furthermore, after a single intratesticular injection of 59Fe-labeled human transferrin, radiolabeled rat transferrin was immunoprecipitated from homogenates of isolated tubules with a specific antibody and appeared as a single radioactive band on fluorographs of urea/polyacrylamide gels.	Iron-59	57-61	transferrin	Rattus norvegicus	106-117
3689862-7	1987	Similarly, 59Fe-labeled rat transferrin but not 125I-transferrin was immunoprecipitated from rete testis fluids of testes infused with either 59Fe- or 125I-labeled human transferrin.	Iron-59	11-15	transferrin	Rattus norvegicus	28-39
3689862-7	1987	Similarly, 59Fe-labeled rat transferrin but not 125I-transferrin was immunoprecipitated from rete testis fluids of testes infused with either 59Fe- or 125I-labeled human transferrin.	Iron-59	142-146	transferrin	Rattus norvegicus	28-39
3478338-6	1987	On the other hand, transferrin release by uninduced cells was significantly slower and a substantial part of internalized 59Fe was released.	Iron-59	122-126	transferrin	Homo sapiens	19-30
3498714-10	1987	This prediction is confirmed by direct measurement of the accumulation of 59Fe-labeled diferric transferrin by A431 cells.	Iron-59	74-78	transferrin	Homo sapiens	96-107
3978231-3	1985	We found that hemin added to reticulocytes in vitro inhibits not only the total cell incorporation of 59Fe from transferrin but also the incorporation of [2-14C]-glycine and transferrin-bound 59Fe into heme.	Iron-59	102-106	transferrin	Homo sapiens	112-123
3472216-11	1987	In transferrin iron-saturated animals, injected 59Fe was removed with a half-time of less than 30 s. Analysis of the distribution of 59Fe in serum samples by polyacrylamide gel electrophoresis demonstrated the presence of 59Fe not bound to transferrin.	Iron-59	48-52	transferrin	Mus musculus	3-14
3465751-6	1986	Although shunting of transferrin-gallium to another cellular compartment has not been ruled out, other studies suggest that transferrin-gallium impairs intracellular release of 59Fe from transferrin by interfering with processes responsible for intracellular acidification.	Iron-59	177-181	transferrin	Homo sapiens	124-135
3465751-6	1986	Although shunting of transferrin-gallium to another cellular compartment has not been ruled out, other studies suggest that transferrin-gallium impairs intracellular release of 59Fe from transferrin by interfering with processes responsible for intracellular acidification.	Iron-59	177-181	transferrin	Homo sapiens	124-135
3730295-2	1986	The applicability of these findings to human subjects was tested by administering diferric transferrin labelled with 3 mg 59Fe to seven patients with pernicious anaemia.	Iron-59	122-126	transferrin	Homo sapiens	91-102
3800875-0	1986	Uptake and subcellular processing of 59Fe-125I-labelled transferrin by rat liver.	Iron-59	37-41	transferrin	Rattus norvegicus	56-67
3790074-4	1986	After 96 h cells, cultured with 20 and 50 microM-desferrioxamine accumulated 59Fe from bovine transferrin at over twice the rate found with control cells, reflecting the increase in transferrin receptors.	Iron-59	77-81	serotransferrin	Bos taurus	94-105
3738431-2	1986	Erythropoietin, indirectly determined by measuring 59Fe incorporation in polycythemic mouse bioassay, was not detected in serum and urine, but was found in cerebrospinal fluid.	Iron-59	51-55	erythropoietin	Mus musculus	0-14
3457008-1	1986	Following a pulse with 59Fe-transferrin, K562 erythroleukemia cells incorporate a significant amount of 59Fe into ferritin.	Iron-59	23-27	transferrin	Homo sapiens	28-39
3947682-9	1986	Incubation at 37 degrees C with 59Fe-labeled transferrin indicated that all iron uptake occurs through high-affinity binding.	Iron-59	32-36	transferrin	Homo sapiens	45-56
3948880-2	1986	The subcellular localization of 3H-labelled 59Fe-loaded transferrin accumulated by the liver has been studied by means of cell fractionation techniques.	Iron-59	44-48	transferrin	Rattus norvegicus	56-67
3948880-3	1986	More than 96% of the 59Fe present in the liver of rats perfused with 59Fe-labelled transferrin is recovered in the parenchymal cells.	Iron-59	21-25	transferrin	Rattus norvegicus	83-94
3948880-4	1986	Rat livers were perfused with 10 micrograms/ml 3H-labelled 59Fe-saturated transferrin, homogenized separated in nuclear (N), mitochondrial (M), light mitochondrial (L), microsomal (P) and supernatant (S) fractions; M, L and P fractions were further analysed by isopycnic centrifugation in sucrose gradients.	Iron-59	59-63	transferrin	Rattus norvegicus	74-85
2990576-5	1985	Incubation of these fractions with 125I- or 59Fe-labeled transferrin led to exclusive binding to endothelial cells but not hepatocytes nor Kupffer cells.	Iron-59	44-48	transferrin	Homo sapiens	57-68
3990509-1	1985	Amines, diamines and polyamines inhibit the erythropoietin-stimulated incorporation of 59Fe into newly-synthesized heme by fetal mouse liver cells in short-term culture.	Iron-59	87-91	erythropoietin	Mus musculus	44-58
3435663-5	1987	The dynamics of 59Fe uptake by the lymphoma cells from 50% saturated ferritransferrin were followed and saturation of iron uptake was found to occur at 150 nM iron and transferrin, far below physiological levels.	Iron-59	16-20	transferrin	Mus musculus	74-85
3793616-0	1986	Transferrin-mediated transcellular transport of 59Fe across confluent epithelial sheets of Sertoli cells grown in bicameral cell culture chambers.	Iron-59	48-52	transferrin	Rattus norvegicus	0-11
3793616-12	1986	Serum transferrin delivers the 59Fe to the basal cytoplasm of the Sertoli cells.	Iron-59	31-35	transferrin	Rattus norvegicus	6-17
3978231-3	1985	We found that hemin added to reticulocytes in vitro inhibits not only the total cell incorporation of 59Fe from transferrin but also the incorporation of [2-14C]-glycine and transferrin-bound 59Fe into heme.	Iron-59	192-196	transferrin	Homo sapiens	174-185
3966565-6	1985	Apotransferrin and desferrioxamine released a maximum of about 20% iron-59 with little effect on transferrin binding.	Iron-59	67-74	transferrin	Rattus norvegicus	3-14
6720680-2	1984	Monocytes from nine control subjects and 17 patients with hemochromatosis were cultured in the presence of 59Fe-labelled human transferrin.	Iron-59	107-111	transferrin	Homo sapiens	127-138
6092356-11	1984	The new receptors were functionally active and produced an increase in 59Fe uptake from 59Fe-transferrin.	Iron-59	71-75	transferrin	Homo sapiens	93-104
6377946-1	1984	The hepatic uptake of 59Fe from diferric rat and rabbit asialotransferrins and from human transferrin lacking two sialyl residues was investigated in rats in experiments lasting for 1 hr.	Iron-59	22-26	transferrin	Homo sapiens	62-73
6241781-5	1984	Administration of ASA prior to administration of erythropoietin (Epo) into post-hypoxic polycythemic mice depresses the incorporation of 59Fe into erythrocytes.	Iron-59	137-141	erythropoietin	Mus musculus	49-63
6328486-5	1984	Moreover, despite the decrease in surface receptors, uptake of 59Fe from transferrin proceeded at a rate comparable to that seen in untreated cells.	Iron-59	63-67	transferrin	Homo sapiens	73-84
6241781-5	1984	Administration of ASA prior to administration of erythropoietin (Epo) into post-hypoxic polycythemic mice depresses the incorporation of 59Fe into erythrocytes.	Iron-59	137-141	erythropoietin	Mus musculus	65-68
7126464-5	1982	Transferrin 59Fe was distinguished by a greater reflux to the erythron in iron deficient rats, and by excretion of a larger proportion of 59Fe chelated by DF in the urine.	Iron-59	12-16	transferrin	Rattus norvegicus	0-11
6651865-3	1983	In the presence of apotransferrin, most of the 59Fe released from the cells distributes as transferrin whereas with desferrioxamine B, almost all the 59Fe is extracted by benzyl alcohol indicating its chelation by the drug.	Iron-59	47-51	transferrin	Rattus norvegicus	22-33
6641829-4	1983	When hypertransfused mice were exposed to hypoxia before transfusions, a linear increase in 59Fe uptake values in response to hypoxia was observed with exposures between 6 and 30 h. No further increase was observed for exposures of 46 to 216 h. These results suggest a sensitization of the erythropoietin-producing organ(s) by hypoxia.	Iron-59	92-96	erythropoietin	Mus musculus	290-304
6575810-2	1983	After incubation of the cells with 59Fe-labelled transferrin, 59Fe was incorporated into haemoglobin, various ferritin fractions, and into the pellet obtained by centrifugation.	Iron-59	35-39	transferrin	Mus musculus	49-60
6575810-2	1983	After incubation of the cells with 59Fe-labelled transferrin, 59Fe was incorporated into haemoglobin, various ferritin fractions, and into the pellet obtained by centrifugation.	Iron-59	62-66	transferrin	Mus musculus	49-60
6887639-0	1983	[Ferrokinetics--pretreatment for intravenous injection of 59-Fe in cases with low unsaturated iron binding capacity (UIBC)--a method for removal of iron from the plasma and complete binding of 59-Fe to autogenous transferrin].	Iron-59	58-63	transferrin	Homo sapiens	213-224
6296362-8	1983	The combined administration of DFO and PYP contributed more than DFO or PYP separately, to the increase of urinary excretion of 59Fe and to the significant decrease of the radioiron concentration in liver (.01 less than P less than .05).	Iron-59	128-132	pyrophosphatase (inorganic) 1	Mus musculus	39-42
6296362-8	1983	The combined administration of DFO and PYP contributed more than DFO or PYP separately, to the increase of urinary excretion of 59Fe and to the significant decrease of the radioiron concentration in liver (.01 less than P less than .05).	Iron-59	128-132	pyrophosphatase (inorganic) 1	Mus musculus	72-75
7160481-1	1982	The binding and uptake of 59Fe-loaded 3H-labelled rat transferrin by cultured rat hepatocytes was investigated.	Iron-59	26-30	transferrin	Rattus norvegicus	54-65
7138909-2	1982	Transferrin-depleted reticulocytes showed a time-, temperature- and concentration-dependent incorporation of 59Fe when incubated with 20-200 microM 59Fe-PIH.	Iron-59	109-113	transferrin	Homo sapiens	0-11
6310669-2	1983	The animals were injected intravenously with a mixture of 59Fe-125I-labelled rabbit diferric transferrin and 131I-labelled rabbit albumin.	Iron-59	58-62	serotransferrin	Oryctolagus cuniculus	93-104
7075741-3	1982	It was found that in the 12--24-h period following administration of PLE or purified sphingomyelin a significant increase in 59Fe uptake by circulating RBC an by their hemic fraction takes place.	Iron-59	125-129	perinatal lethality	Mus musculus	69-72
7137164-3	1982	The rate of subsequent release of 59Fe to the extracellular transferrin pool was two- to fourfold greater for macrophages as compared to the other two cell types.	Iron-59	34-38	transferrin	Homo sapiens	60-71
7059619-8	1982	Reincubation of washed succinylacetone- and 59Fe-transferrin-pretreated reticulocytes results in the transfer of 59Fe from the particulate fraction (plasma membrane plus mitochondria) into hemoglobin and this process is considerably stimulated by added protoporphyrin.	Iron-59	44-48	serotransferrin	Oryctolagus cuniculus	49-60
7061895-3	1982	We studied ferrokinetics with 59Fe specific binding transferrin by 59Fe-NTAmethod.	Iron-59	30-34	transferrin	Rattus norvegicus	52-63
7061895-3	1982	We studied ferrokinetics with 59Fe specific binding transferrin by 59Fe-NTAmethod.	Iron-59	67-71	transferrin	Rattus norvegicus	52-63
7296013-2	1981	In intestinal mucosal tissue a transferrin-like immunoreactivity (TLIR) was determined after loading with 59Fe-(FeCl3) in vivo.	Iron-59	106-111	transferrin	Rattus norvegicus	31-42
7437473-2	1980	Addition of apotransferrin during reincubation of 59Fe-labelled reticulocytes was accompanied by the transfer of 59Fe from low-molecular-weight pool to transferrin, which was found in the reticulocyte cytosol both free and bound to a carrier.	Iron-59	50-54	transferrin	Homo sapiens	15-26
6285071-3	1981	In all cases with MTX concentrations greater than or equal to 5 x 10(-8) M the 59Fe-utilization as the measure of effective erythropoiesis was reduced pathologically below normal range.	Iron-59	79-83	metaxin 1	Homo sapiens	18-21
6267048-7	1981	With unlabeled horse apoprotein and [59Fe]hemin, the yield of a [59Fe-labeled horse cytochrome c-like species was up to 7% with respect to the apoprotein incubated.	Iron-59	37-41	cytochrome c, somatic	Equus caballus	84-96
6267048-7	1981	With unlabeled horse apoprotein and [59Fe]hemin, the yield of a [59Fe-labeled horse cytochrome c-like species was up to 7% with respect to the apoprotein incubated.	Iron-59	65-69	cytochrome c, somatic	Equus caballus	84-96
6267048-10	1981	The formation of both 125I- and 59Fe-labeled cytochrome c-like species was sensitive to heat.	Iron-59	32-36	LOC102147344	Equus caballus	45-62
7227479-3	1981	59Fe labeled young RBC were found at a density of p 1.09.	Iron-59	0-4	zinc finger protein 185	Mus musculus	50-53
7437473-2	1980	Addition of apotransferrin during reincubation of 59Fe-labelled reticulocytes was accompanied by the transfer of 59Fe from low-molecular-weight pool to transferrin, which was found in the reticulocyte cytosol both free and bound to a carrier.	Iron-59	113-117	transferrin	Homo sapiens	15-26
7437475-1	1980	Mechanism of transferrin iron uptake by rat reticulocytes was studied using 59Fe- and 125I-labelled rat transferrin.	Iron-59	76-80	transferrin	Rattus norvegicus	13-24
7371472-2	1980	Between 2 and 4% of a tracer dose of 59Fe added to normal serum was retained by DEAE Sephadex and has been designated non-transferrin-bound.	Iron-59	37-41	transferrin	Homo sapiens	122-133
7378578-5	1980	When the reticulocytes were incubated with unlabeled plasma after pulse-labeling with 59Fe-labeled plasma, 59Fe radioactivity in these cytosol components decreased; after 15 min of chase, the 59Fe in ferritin, transferrin, and IBP-I fell to 64.6%, 26.5%, and 65.8% of the initial values, respectively.	Iron-59	86-90	serotransferrin	Oryctolagus cuniculus	210-221
6246947-8	1980	The 59Fe/125I ratio in the transferrin complex purified from Peak I was the same as in the original transferrin and thus contained membrane-bound transferrin to which the 59Fe was still attached.	Iron-59	4-8	serotransferrin	Oryctolagus cuniculus	27-38
429862-1	1979	Three aspects of iron metabolism were studies in reticulocytes from iron-deficient, phlebotomized, and phenylhydrazine-treated rats: (1) the number of transferrin binding sites; (2) the uptake of 59Fe-transferrin; and (3) the ability of cytosol to mobilize 59Fe from 59Fe-labeled reticulocyte plasma membrane.	Iron-59	196-200	transferrin	Rattus norvegicus	201-212
7356552-2	1980	59Fe is used to quantify ferrochelatase activity in rat liver.	Iron-59	0-4	ferrochelatase	Rattus norvegicus	25-39
7055537-2	1982	When 59Fe-labelled diferric transferrin is injected into normal, anaemic or hypertransfused, polycythaemic rabbits, iron is removed from diferric transferrin in essentially pairwise fashion.	Iron-59	5-9	serotransferrin	Oryctolagus cuniculus	28-39
7055537-2	1982	When 59Fe-labelled diferric transferrin is injected into normal, anaemic or hypertransfused, polycythaemic rabbits, iron is removed from diferric transferrin in essentially pairwise fashion.	Iron-59	5-9	serotransferrin	Oryctolagus cuniculus	146-157
105542-0	1979	The preparation of 59Fe-labelled transferrin of high radioactivity for ferrokinetic studies on small laboratory animals.	Iron-59	19-23	transferrin	Homo sapiens	33-44
19087-2	1977	Rabbit transferrin labelled with 59Fe was incubated with human apotransferrin in the presence of the metabolites.	Iron-59	33-37	serotransferrin	Oryctolagus cuniculus	7-18
34369-1	1978	Terbutaline sulfate, a new synthetic beta2-adrenoceptor agonist, was found to produce a dose-related increase in 59Fe-incorporation into newly formed red blood cells of exhypoxic polycythemic mice.	Iron-59	113-117	adrenergic receptor, beta 2	Mus musculus	37-55
684293-9	1978	In anemia due to protein deficiency the typical increase of 59Fe incorporation into the fraction of mucosal transferrin--usually occuring in iron deficiency--could not be observed.	Iron-59	60-64	transferrin	Rattus norvegicus	108-119
647005-3	1978	Plasma membranes prepared by pre-incumbation of mouse reticulocytes with 125I, 59Fe-labeled murine transferrin were able to release 59Fe in preference to 125I when incubated in the presence of murine reticulocyte cytosol, demonstrating that the latter mobilized iron which had been dissociated from transferrin.	Iron-59	79-83	transferrin	Mus musculus	99-110
647005-3	1978	Plasma membranes prepared by pre-incumbation of mouse reticulocytes with 125I, 59Fe-labeled murine transferrin were able to release 59Fe in preference to 125I when incubated in the presence of murine reticulocyte cytosol, demonstrating that the latter mobilized iron which had been dissociated from transferrin.	Iron-59	79-83	transferrin	Mus musculus	299-310
647005-3	1978	Plasma membranes prepared by pre-incumbation of mouse reticulocytes with 125I, 59Fe-labeled murine transferrin were able to release 59Fe in preference to 125I when incubated in the presence of murine reticulocyte cytosol, demonstrating that the latter mobilized iron which had been dissociated from transferrin.	Iron-59	132-136	transferrin	Mus musculus	99-110
732308-4	1978	The ability of bone marrow cells in culture to respond to the hormone erythropoietin, as measured by the incorporation of 59Fe into cyclohexanone-extractable heme, was also not affected by neuraminidase, making a cytotoxic effect of the VCN preparation unlikely.	Iron-59	122-126	erythropoietin	Homo sapiens	70-84
594498-4	1977	Under these conditions the 59Fe uptake into transferrin and ferritin of the mucosal "cytosol" and SDS treated "membrane" fraction has been measured together with the 59Fe amount transferred into the body.	Iron-59	27-31	transferrin	Homo sapiens	44-55
594498-6	1977	The increase of the intestinal 59Fe absorption due to a progressive iron deficiency is associated with an increase of the 59Fe uptake into the mucosal transferrin of the "cytosol" and the "membrane" fraction; the reverse is observed with regard to mucosal ferritin.	Iron-59	31-35	transferrin	Homo sapiens	151-162
594498-6	1977	The increase of the intestinal 59Fe absorption due to a progressive iron deficiency is associated with an increase of the 59Fe uptake into the mucosal transferrin of the "cytosol" and the "membrane" fraction; the reverse is observed with regard to mucosal ferritin.	Iron-59	122-126	transferrin	Homo sapiens	151-162
594498-11	1977	The 59Fe content in the ferritin fraction increased simultaneously, whereas the 59Fe content in the transferrin fraction remained the same.	Iron-59	80-84	transferrin	Homo sapiens	100-111
594503-2	1977	Increased amount of erythropoietin resulted in a higher incorporation of 59Fe+++ -ions in this fraction.	Iron-59	73-80	erythropoietin	Homo sapiens	20-34
561654-5	1977	Pretreatment of human transferrin with saturating amounts of nonradioactive Fe3+ canceled its ability to promote 59Fe uptake, but it had little effect on its promotion of 67Ga uptake.	Iron-59	113-117	transferrin	Homo sapiens	22-33
889717-4	1977	Iron transport, determined by measurement of the rate of 59Fe uptake from 59Fe-labelled transferrin, was proportional to the number of receptors at all stages of differentiation.	Iron-59	57-61	transferrin	Mus musculus	88-99
948032-2	1976	Perfusion and PO2 were measured polarographically and small vessel blood content was measured with 59Fe-siderophilin-labeled blood.	Iron-59	99-103	transferrin	Rattus norvegicus	104-116
13868-1	1977	Human transferrin was labeled with 59Fe at one of its two metal-binding sites (designated A) at pH 6.0.	Iron-59	35-39	transferrin	Homo sapiens	6-17
189804-4	1977	Transferrin was labeled at site A with 59Fe at pH 6.0 and at site B with 55Fe at pH 7.5.	Iron-59	39-43	transferrin	Homo sapiens	0-11
272031-1	1977	The transfer of iron from the iron carbohydrate complexes, Ferastral, Imferon, and Jectofer, and from ferric chloride has been studied by the effect of such transfer in reducing reticulocyte uptake of 59Fe from labelled transferrin.	Iron-59	201-205	transferrin	Homo sapiens	220-231
932199-3	1976	The biosynthesis of this glycosylated hemoglobin was studied in vitro by incubating suspensions of reticulocytes and bone marrow cells with [3H]leucine or 59Fe-bound transferrin.	Iron-59	155-159	transferrin	Homo sapiens	166-177
932199-5	1976	The formation of Hb A1c in vivo was determined in two individuals who were given an infusion of 59Fe-labeled transferrin.	Iron-59	96-100	transferrin	Homo sapiens	109-120
810795-4	1975	These flagellates, in the presence of protoporphyrin IX, incorporated 59Fe into heme, indicating that they possess ferrochelatase (EC 4.99.1.1), the terminal enzyme in the heme biosynthetic pathway, which catalyzes the insertion of iron into protoporphyrin IX.	Iron-59	70-74	ferrochelatase	Homo sapiens	115-129
6057-1	1976	Human diferric transferrin was partially labeled with 59Fe at low or neutral pH (chemically labeled) and by replacement of diferric iron previously donated to rabbit reticulocytes (biologically labeled).	Iron-59	54-58	serotransferrin	Oryctolagus cuniculus	15-26
1125327-1	1975	This paper describes a study of the incorporation of 59-Fe from 59-Fe-labelled rat transferrin into rat bone marrow cells in culture.	Iron-59	53-58	transferrin	Rattus norvegicus	83-94
1125327-1	1975	This paper describes a study of the incorporation of 59-Fe from 59-Fe-labelled rat transferrin into rat bone marrow cells in culture.	Iron-59	64-69	transferrin	Rattus norvegicus	83-94
1125327-5	1975	A proportion of the 59-Fe incorporated into the stroma and low molecular weight iron fractions during a 1 h incubation with 59-Fe-labelled transferrin was mobilised into ferritin and haemoglobin during a subsequent 4-h "cold-chase".	Iron-59	20-25	transferrin	Rattus norvegicus	139-150
1125327-5	1975	A proportion of the 59-Fe incorporated into the stroma and low molecular weight iron fractions during a 1 h incubation with 59-Fe-labelled transferrin was mobilised into ferritin and haemoglobin during a subsequent 4-h "cold-chase".	Iron-59	124-129	transferrin	Rattus norvegicus	139-150
1125327-7	1975	The erythropoietin stimulation of 59-Fe incorporation into ferritin, one of the earliest erythropoietin effects to be recorded, was therefore considered to be due to an increase of 59-Fe uptake by the hormone-responsive cells rather than a direct effect on ferritin synthesis.	Iron-59	34-39	erythropoietin	Rattus norvegicus	4-18
1125327-7	1975	The erythropoietin stimulation of 59-Fe incorporation into ferritin, one of the earliest erythropoietin effects to be recorded, was therefore considered to be due to an increase of 59-Fe uptake by the hormone-responsive cells rather than a direct effect on ferritin synthesis.	Iron-59	34-39	erythropoietin	Rattus norvegicus	89-103
1125327-7	1975	The erythropoietin stimulation of 59-Fe incorporation into ferritin, one of the earliest erythropoietin effects to be recorded, was therefore considered to be due to an increase of 59-Fe uptake by the hormone-responsive cells rather than a direct effect on ferritin synthesis.	Iron-59	181-186	erythropoietin	Rattus norvegicus	4-18
1125327-7	1975	The erythropoietin stimulation of 59-Fe incorporation into ferritin, one of the earliest erythropoietin effects to be recorded, was therefore considered to be due to an increase of 59-Fe uptake by the hormone-responsive cells rather than a direct effect on ferritin synthesis.	Iron-59	181-186	erythropoietin	Rattus norvegicus	89-103
1125327-8	1975	20-h cultures containing erythropoietin when incubated with 59-Fe-labelled transferrin for 4 h, showed dose-related erythropoietin stimulation of 59-Fe incorporation into haemoglobin only.	Iron-59	60-65	erythropoietin	Rattus norvegicus	25-39
1125327-8	1975	20-h cultures containing erythropoietin when incubated with 59-Fe-labelled transferrin for 4 h, showed dose-related erythropoietin stimulation of 59-Fe incorporation into haemoglobin only.	Iron-59	60-65	transferrin	Rattus norvegicus	75-86
1125327-8	1975	20-h cultures containing erythropoietin when incubated with 59-Fe-labelled transferrin for 4 h, showed dose-related erythropoietin stimulation of 59-Fe incorporation into haemoglobin only.	Iron-59	60-65	erythropoietin	Rattus norvegicus	116-130
1125327-8	1975	20-h cultures containing erythropoietin when incubated with 59-Fe-labelled transferrin for 4 h, showed dose-related erythropoietin stimulation of 59-Fe incorporation into haemoglobin only.	Iron-59	146-151	erythropoietin	Rattus norvegicus	25-39
1125327-8	1975	20-h cultures containing erythropoietin when incubated with 59-Fe-labelled transferrin for 4 h, showed dose-related erythropoietin stimulation of 59-Fe incorporation into haemoglobin only.	Iron-59	146-151	transferrin	Rattus norvegicus	75-86
1125327-8	1975	20-h cultures containing erythropoietin when incubated with 59-Fe-labelled transferrin for 4 h, showed dose-related erythropoietin stimulation of 59-Fe incorporation into haemoglobin only.	Iron-59	146-151	erythropoietin	Rattus norvegicus	116-130
1129279-4	1975	Sera from nephrectomized rabbits significantly (p smaller than 0.05) inhibited 59-Fe incorporation into heme in normal rabbit bone marrow cultures incubated with erythropoietin (ESF) when compared with the response in control culutres with normal serum and ESF.	Iron-59	79-84	erythropoietin	Oryctolagus cuniculus	162-176
1123558-4	1975	Serum transferrin was selectively double-labeled by adding 59Fe to 90 per cent saturation of iron binding capacity, incubation with rat reticulocytes to reduce the saturation to 50 per cent or less, and then adding back 55Fe.	Iron-59	59-63	transferrin	Rattus norvegicus	6-17
1123559-4	1975	Rat serum transferrin was selectively double-labeled with 55Fe bound to the A-site and 59Fe bound to the B-site and injected intravenously into pregnant rats at 11 to 20 days gestation.	Iron-59	87-91	transferrin	Rattus norvegicus	10-21
4475966-0	1974	[Rate of transferrin-bound 59Fe uptake by peripheral reticulocytes].	Iron-59	27-31	transferrin	Homo sapiens	9-20
4821403-0	1974	A comparison of the behavior of 111In and 59Fe-labeled transferrin on incubation with human and rat reticulocytes.	Iron-59	42-46	transferrin	Homo sapiens	55-66
5838669-0	1964	Studies on the intracellular localization and incorporation of 59Fe into catalase in rat liver.	Iron-59	63-67	catalase	Rattus norvegicus	73-81
14494235-0	1962	Erythropoietin assays using iron59 incorporation into blood and spleen of the polycythemic mouse.	Iron-59	28-34	erythropoietin	Mus musculus	0-14
911316-1	1977	59Fe uptake by rabbit reticulocytes from human transferrin-bound iron was studied by using transferrin solutions (35, 50, 65, 80 and 100% saturated with iron) whose only common characteristic was their content of diferric transferrin.	Iron-59	0-4	transferrin	Homo sapiens	47-58
911316-1	1977	59Fe uptake by rabbit reticulocytes from human transferrin-bound iron was studied by using transferrin solutions (35, 50, 65, 80 and 100% saturated with iron) whose only common characteristic was their content of diferric transferrin.	Iron-59	0-4	transferrin	Homo sapiens	91-102
911316-1	1977	59Fe uptake by rabbit reticulocytes from human transferrin-bound iron was studied by using transferrin solutions (35, 50, 65, 80 and 100% saturated with iron) whose only common characteristic was their content of diferric transferrin.	Iron-59	0-4	transferrin	Homo sapiens	91-102
30538134-10	2019	We further show that these cells can acquire 59Fe from 59Fe-transferrin, presumably via Tfr2.	Iron-59	45-49	transferrin	Mus musculus	60-71
30538134-10	2019	We further show that these cells can acquire 59Fe from 59Fe-transferrin, presumably via Tfr2.	Iron-59	45-49	transferrin receptor 2	Mus musculus	88-92
27866158-10	2016	This was confirmed by silencing nuclear factor-erythroid 2-related factor 2 (Nrf2), which decreased MRP1 and GSTP1 expression, concomitant with reduced 59Fe release and macrophage survival.	Iron-59	152-156	NFE2 like bZIP transcription factor 2	Homo sapiens	32-75
28193158-8	2017	The supply of 1 muM 59Fe, as soluble (Fe-Citrate and Fe-PS) or sparingly soluble (Ferrihydrite) sources to deficient plants, caused a rapid down-regulation of genes coding for PS and Fe(III)-PS transport, as well as of ZmNRAMP1 and ZmPHT1;7.	Iron-59	20-24	Metal transporter Nramp5	Zea mays	219-227
28193158-8	2017	The supply of 1 muM 59Fe, as soluble (Fe-Citrate and Fe-PS) or sparingly soluble (Ferrihydrite) sources to deficient plants, caused a rapid down-regulation of genes coding for PS and Fe(III)-PS transport, as well as of ZmNRAMP1 and ZmPHT1;7.	Iron-59	20-24	phosphate transporter protein 1	Zea mays	232-240
27866158-10	2016	This was confirmed by silencing nuclear factor-erythroid 2-related factor 2 (Nrf2), which decreased MRP1 and GSTP1 expression, concomitant with reduced 59Fe release and macrophage survival.	Iron-59	152-156	NFE2 like bZIP transcription factor 2	Homo sapiens	77-81
27866158-10	2016	This was confirmed by silencing nuclear factor-erythroid 2-related factor 2 (Nrf2), which decreased MRP1 and GSTP1 expression, concomitant with reduced 59Fe release and macrophage survival.	Iron-59	152-156	glutathione S-transferase pi 1	Homo sapiens	109-114
28573162-3	2016	The measurement of tissue transferrin- and non-transferrin-bound iron (TBI and NTBI, respectively) uptake in vivo can be achieved via intravenous administration of 59Fe-labeled TBI or NTBI followed by gamma counting of various organs.	Iron-59	164-168	transferrin	Mus musculus	26-37
28573162-3	2016	The measurement of tissue transferrin- and non-transferrin-bound iron (TBI and NTBI, respectively) uptake in vivo can be achieved via intravenous administration of 59Fe-labeled TBI or NTBI followed by gamma counting of various organs.	Iron-59	164-168	transferrin	Mus musculus	47-58
26460540-6	2015	The metabolites also lost the ability to: (1) promote the redox cycling of iron; (2) bind and mobilize iron from labile intracellular pools; and (3) prevent 59Fe uptake from 59Fe-labeled transferrin by MCF-7 cells.	Iron-59	157-161	transferrin	Homo sapiens	187-198
27714044-10	2016	Interestingly, 59Fe uptake and efflux were impaired in both cell lines by Atp7a silencing.	Iron-59	15-19	ATPase copper transporting alpha	Homo sapiens	74-79
26460540-6	2015	The metabolites also lost the ability to: (1) promote the redox cycling of iron; (2) bind and mobilize iron from labile intracellular pools; and (3) prevent 59Fe uptake from 59Fe-labeled transferrin by MCF-7 cells.	Iron-59	174-178	transferrin	Homo sapiens	187-198
22084240-11	2012	Cells transfected with GSTP1 (but not GSTA1 or GSTM1) significantly decreased NO-mediated 59Fe release from cells.	Iron-59	90-94	glutathione S-transferase pi 1	Homo sapiens	23-28
24194187-3	2013	In the current study, we examined uptake and intracellular distribution of 59Fe from iron transport protein transferrin or ferric chloride (nontransferrin-bound iron [NTBI]) in cultured canine lens epithelial cells (LECs).	Iron-59	75-79	inhibitor of carbonic anhydrase	Canis lupus familiaris	108-119
22084240-13	2012	Notably, 59Fe accumulated in cells within GST P1-1-containing fractions, indicating an alteration in intracellular 59Fe distribution.	Iron-59	9-13	glutathione S-transferase pi 1	Homo sapiens	42-50
22084240-13	2012	Notably, 59Fe accumulated in cells within GST P1-1-containing fractions, indicating an alteration in intracellular 59Fe distribution.	Iron-59	115-119	glutathione S-transferase pi 1	Homo sapiens	42-50
20805568-8	2010	Iron uptake into cells and incorporation into ferritin was measured by incubating the cells with 59Fe-labeled transferrin.	Iron-59	97-101	inhibitor of carbonic anhydrase	Canis lupus familiaris	110-121
18492824-7	2008	Cells expressing Dcytb exhibited enhanced ferric reductase activity as well as increased 59Fe uptake compared with cells transfected with empty vector as a control.	Iron-59	89-93	cytochrome b reductase 1	Homo sapiens	17-22
16679408-6	2006	Other MRP1 inhibitors, MK571, probenecid, and difloxacin, significantly inhibited NO-mediated 59Fe release.	Iron-59	94-98	ATP binding cassette subfamily C member 1	Homo sapiens	6-10
16968894-4	2007	In one case, the in vivo half-life of 59Fe-labeled transferrin was shown to be prolonged (206 minutes versus 75 minutes for controls).	Iron-59	38-42	transferrin	Homo sapiens	51-62
15331447-5	2005	Importantly, both the myosin light chain kinase inhibitor wortmannin and the calmodulin antagonist, N-(6-aminohexyl)-5-chloro-1-naphthalene-sulfonamide (W-7), caused significant inhibition of 59Fe incorporation from 59Fe-Tf-labeled endosomes into heme, suggesting that myosin is required for Tf-vesicle movement.	Iron-59	192-196	myosin light chain kinase	Homo sapiens	22-47
15665091-7	2005	Subsequent fractionation of the total released 59Fe into heme and nonheme compounds revealed that hepcidin treatment reduced the release of nonheme 59Fe by 50% and 25% from control and FPN1-overexpressing cells, respectively, but did not diminish efflux of 59Fe-heme.	Iron-59	47-51	hepcidin antimicrobial peptide	Mus musculus	98-106
15665091-7	2005	Subsequent fractionation of the total released 59Fe into heme and nonheme compounds revealed that hepcidin treatment reduced the release of nonheme 59Fe by 50% and 25% from control and FPN1-overexpressing cells, respectively, but did not diminish efflux of 59Fe-heme.	Iron-59	148-152	hepcidin antimicrobial peptide	Mus musculus	98-106
15665091-7	2005	Subsequent fractionation of the total released 59Fe into heme and nonheme compounds revealed that hepcidin treatment reduced the release of nonheme 59Fe by 50% and 25% from control and FPN1-overexpressing cells, respectively, but did not diminish efflux of 59Fe-heme.	Iron-59	148-152	solute carrier family 40 (iron-regulated transporter), member 1	Mus musculus	185-189
15665091-7	2005	Subsequent fractionation of the total released 59Fe into heme and nonheme compounds revealed that hepcidin treatment reduced the release of nonheme 59Fe by 50% and 25% from control and FPN1-overexpressing cells, respectively, but did not diminish efflux of 59Fe-heme.	Iron-59	148-152	hepcidin antimicrobial peptide	Mus musculus	98-106
15665091-7	2005	Subsequent fractionation of the total released 59Fe into heme and nonheme compounds revealed that hepcidin treatment reduced the release of nonheme 59Fe by 50% and 25% from control and FPN1-overexpressing cells, respectively, but did not diminish efflux of 59Fe-heme.	Iron-59	148-152	solute carrier family 40 (iron-regulated transporter), member 1	Mus musculus	185-189
15331447-5	2005	Importantly, both the myosin light chain kinase inhibitor wortmannin and the calmodulin antagonist, N-(6-aminohexyl)-5-chloro-1-naphthalene-sulfonamide (W-7), caused significant inhibition of 59Fe incorporation from 59Fe-Tf-labeled endosomes into heme, suggesting that myosin is required for Tf-vesicle movement.	Iron-59	192-196	calmodulin 1	Homo sapiens	77-87
15331447-5	2005	Importantly, both the myosin light chain kinase inhibitor wortmannin and the calmodulin antagonist, N-(6-aminohexyl)-5-chloro-1-naphthalene-sulfonamide (W-7), caused significant inhibition of 59Fe incorporation from 59Fe-Tf-labeled endosomes into heme, suggesting that myosin is required for Tf-vesicle movement.	Iron-59	192-196	myosin heavy chain 14	Homo sapiens	22-28
15331447-5	2005	Importantly, both the myosin light chain kinase inhibitor wortmannin and the calmodulin antagonist, N-(6-aminohexyl)-5-chloro-1-naphthalene-sulfonamide (W-7), caused significant inhibition of 59Fe incorporation from 59Fe-Tf-labeled endosomes into heme, suggesting that myosin is required for Tf-vesicle movement.	Iron-59	216-220	myosin light chain kinase	Homo sapiens	22-47
15331447-5	2005	Importantly, both the myosin light chain kinase inhibitor wortmannin and the calmodulin antagonist, N-(6-aminohexyl)-5-chloro-1-naphthalene-sulfonamide (W-7), caused significant inhibition of 59Fe incorporation from 59Fe-Tf-labeled endosomes into heme, suggesting that myosin is required for Tf-vesicle movement.	Iron-59	216-220	calmodulin 1	Homo sapiens	77-87
15331447-5	2005	Importantly, both the myosin light chain kinase inhibitor wortmannin and the calmodulin antagonist, N-(6-aminohexyl)-5-chloro-1-naphthalene-sulfonamide (W-7), caused significant inhibition of 59Fe incorporation from 59Fe-Tf-labeled endosomes into heme, suggesting that myosin is required for Tf-vesicle movement.	Iron-59	216-220	myosin heavy chain 14	Homo sapiens	22-28
15305020-7	2004	We suspected that the uptake of 59Fe by the liver tissue was the highest because of the high binding affinity of Tf-59Fe to Tf-receptor.	Iron-59	32-36	transferrin	Rattus norvegicus	113-115
15158359-7	2004	Incubation of cells with CO inhibited 59Fe uptake from 59Fe-Tf by cells, and like NO, reduced ATP levels.	Iron-59	38-42	transferrin	Homo sapiens	60-62
15158359-9	2004	These results showing a CO-mediated decrease in 59Fe uptake from 59Fe-Tf using exogenous CO were in agreement with studies implementing cells transfected with HO1.	Iron-59	48-52	transferrin	Homo sapiens	70-72
15158359-9	2004	These results showing a CO-mediated decrease in 59Fe uptake from 59Fe-Tf using exogenous CO were in agreement with studies implementing cells transfected with HO1.	Iron-59	48-52	heme oxygenase 1	Homo sapiens	159-162