PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8561510-9 1996 Transferrin receptor mRNA expression in liver was induced as soon as iron levels decreased early in scurvy, which is similar to results reported for iron-depleted cultured cells. Iron 69-73 inhibitor of carbonic anhydrase Cavia porcellus 0-11 17942369-4 2008 Accumulation of iron within primary lesions was preceded by an increase in expression of heavy chain (H) ferritin, lactoferrin and receptors for transferrin, primarily by macrophages and granulocytes. Iron 16-20 inhibitor of carbonic anhydrase Cavia porcellus 145-156 8561510-9 1996 Transferrin receptor mRNA expression in liver was induced as soon as iron levels decreased early in scurvy, which is similar to results reported for iron-depleted cultured cells. Iron 149-153 inhibitor of carbonic anhydrase Cavia porcellus 0-11 2092051-8 1990 Since it is known that N-ethylmaleimide inhibits the endosomal proton pump, our results strongly suggest that the endocytotic pathway is a necessary route in transferrin mediated transplacental iron transfer. Iron 194-198 inhibitor of carbonic anhydrase Cavia porcellus 158-169 8083500-1 1993 Transferrin receptors (TfR"s) on the syncytiotrophoblast mediate transferrin (Tf) dependent Fe uptake and transfer to the fetus. Iron 92-94 inhibitor of carbonic anhydrase Cavia porcellus 0-11 8083500-1 1993 Transferrin receptors (TfR"s) on the syncytiotrophoblast mediate transferrin (Tf) dependent Fe uptake and transfer to the fetus. Iron 92-94 inhibitor of carbonic anhydrase Cavia porcellus 65-76 8083500-1 1993 Transferrin receptors (TfR"s) on the syncytiotrophoblast mediate transferrin (Tf) dependent Fe uptake and transfer to the fetus. Iron 92-94 inhibitor of carbonic anhydrase Cavia porcellus 23-25 2736234-9 1989 Presaturation of endogenous transferrin with oral carbonyl iron prevented iron release from the feto-placental unit back into the maternal circulation. Iron 59-63 inhibitor of carbonic anhydrase Cavia porcellus 28-39 2379560-1 1990 We have demonstrated that the intracellular processing of transferrin to effect iron removal involves two pathways, one sensitive to rotenone and the other not. Iron 80-84 inhibitor of carbonic anhydrase Cavia porcellus 58-69 2379560-2 1990 We have also found that the effect of the rotenone is dependent on the transferrin concentration: iron uptake was suppressed with concentrations of transferrin in the micromolar range, and was not suppressed at physiologic concentrations of transferrin. Iron 98-102 inhibitor of carbonic anhydrase Cavia porcellus 71-82 2379560-2 1990 We have also found that the effect of the rotenone is dependent on the transferrin concentration: iron uptake was suppressed with concentrations of transferrin in the micromolar range, and was not suppressed at physiologic concentrations of transferrin. Iron 98-102 inhibitor of carbonic anhydrase Cavia porcellus 148-159 2379560-2 1990 We have also found that the effect of the rotenone is dependent on the transferrin concentration: iron uptake was suppressed with concentrations of transferrin in the micromolar range, and was not suppressed at physiologic concentrations of transferrin. Iron 98-102 inhibitor of carbonic anhydrase Cavia porcellus 148-159 2379560-7 1990 The second pathway begins with an intracellular site which has a high capacity (but low affinity) for either iron or transferrin and is utilized when transferrin is in physiologic concentration (and the low-capacity, high-affinity site is saturated); the pathway it initiates is dominant when transferrin is abundant. Iron 109-113 inhibitor of carbonic anhydrase Cavia porcellus 150-161 2379560-7 1990 The second pathway begins with an intracellular site which has a high capacity (but low affinity) for either iron or transferrin and is utilized when transferrin is in physiologic concentration (and the low-capacity, high-affinity site is saturated); the pathway it initiates is dominant when transferrin is abundant. Iron 109-113 inhibitor of carbonic anhydrase Cavia porcellus 150-161 2803243-4 1989 AMP-bound Fe was a minor component of the cytosol following rapid (NH1)2SO4 precipitation, and the major component when iron was released from transferrin by haemolysates. Iron 10-12 inhibitor of carbonic anhydrase Cavia porcellus 143-154 2803243-4 1989 AMP-bound Fe was a minor component of the cytosol following rapid (NH1)2SO4 precipitation, and the major component when iron was released from transferrin by haemolysates. Iron 120-124 inhibitor of carbonic anhydrase Cavia porcellus 143-154 2736234-9 1989 Presaturation of endogenous transferrin with oral carbonyl iron prevented iron release from the feto-placental unit back into the maternal circulation. Iron 74-78 inhibitor of carbonic anhydrase Cavia porcellus 28-39 2444393-4 1987 In this report the presence of lactoferrin and transferrin in guinea pig tears was investigated using an iron-binding assay, Ouchterlony immunodiffusion, ELISA and immunoblotting techniques. Iron 105-109 inhibitor of carbonic anhydrase Cavia porcellus 47-58 3036246-5 1987 Iron accumulation from transferrin was inhibited by ferritin to a greater extent than could be accounted for by the decreased rate of endocytosis. Iron 0-4 inhibitor of carbonic anhydrase Cavia porcellus 23-34 6527986-6 1984 The results of the present study indicate that after the ferric iron is liberated from maternal haemoglobin its ionic state, subcellular distribution and, probably, its route of transport seem to be similar to that in the guinea-pig placenta which is characterized by the uptake of iron from maternal transferrin. Iron 64-68 inhibitor of carbonic anhydrase Cavia porcellus 301-312 7225422-3 1981 Transferrin, the III-X component and the low molecular weight fraction are the first to accumulate radioactive iron during the reticulocyte incubation. Iron 111-115 inhibitor of carbonic anhydrase Cavia porcellus 0-11 6882688-3 1983 Up to 70% of the iron taken up by the cells was utilized in haem synthesis and competed directly with iron derived from transferrin. Iron 17-21 inhibitor of carbonic anhydrase Cavia porcellus 120-131 6882688-3 1983 Up to 70% of the iron taken up by the cells was utilized in haem synthesis and competed directly with iron derived from transferrin. Iron 102-106 inhibitor of carbonic anhydrase Cavia porcellus 120-131 6882688-8 1983 The endocytotic vesicle fuses with a lysosome, iron is removed from the protein and enters a cytosolic pool in which it competes directly with transferrin-derived iron to provide iron for mitochondrial haem synthesis. Iron 163-167 inhibitor of carbonic anhydrase Cavia porcellus 143-154 6882688-8 1983 The endocytotic vesicle fuses with a lysosome, iron is removed from the protein and enters a cytosolic pool in which it competes directly with transferrin-derived iron to provide iron for mitochondrial haem synthesis. Iron 163-167 inhibitor of carbonic anhydrase Cavia porcellus 143-154 4899010-4 1969 The amount of available iron in serum is determined by the ratio between iron-saturated and iron-free transferrin; a low value for the ratio is associated with tuberculostasis (e.g., human serum, 0.4), whereas a high value is associated with the growth-supporting quality (e.g., guinea pig serum, 5.6). Iron 24-28 inhibitor of carbonic anhydrase Cavia porcellus 102-113 28469086-1 2017 Non-transferrin-bound iron (NTBI) and free hemoglobin (Hb) accumulate in circulation following stored RBC transfusions. Iron 22-26 inhibitor of carbonic anhydrase Cavia porcellus 4-15