PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
16129039-3	2005	The results showed at follows: (1) the level of IRP(2) mRNA remained constant in all cells, whether or not treated with DFO or FeCl(3).	Deferoxamine	120-123	iron responsive element binding protein 2	Homo sapiens	48-54
16129039-14	2005	It is concluded that (1) IRP(2) may regulate the iron metabolism in HL-60 cells by altering amounts of the IRP(2) 3.7- or 6.4-kb mRNA at the transcriptional level, or by IRP(2) degradation at the post transcriptional level.	Iron	49-53	iron responsive element binding protein 2	Homo sapiens	25-30
16511074-4	2005	Whereas IRP2 is known to be involved in Fe homeostasis, the role of IRP1 is less clear; it may provide a link between citrate and iron metabolisms and be involved in oxidative stress response.	Iron	40-42	iron responsive element binding protein 2	Homo sapiens	8-12
16039587-0	2005	Involvement of heme regulatory motif in heme-mediated ubiquitination and degradation of IRP2.	Heme	15-19	iron responsive element binding protein 2	Homo sapiens	88-92
16039587-0	2005	Involvement of heme regulatory motif in heme-mediated ubiquitination and degradation of IRP2.	Heme	40-44	iron responsive element binding protein 2	Homo sapiens	88-92
16039587-1	2005	Iron regulatory protein 2 (IRP2), a regulator of iron metabolism, is modulated by ubiquitination and degradation.	Iron	49-53	iron responsive element binding protein 2	Homo sapiens	0-25
16039587-1	2005	Iron regulatory protein 2 (IRP2), a regulator of iron metabolism, is modulated by ubiquitination and degradation.	Iron	49-53	iron responsive element binding protein 2	Homo sapiens	27-31
16039587-2	2005	We have shown that IRP2 degradation is triggered by heme-mediated oxidation.	Heme	52-56	iron responsive element binding protein 2	Homo sapiens	19-23
16039587-3	2005	We report here that not only Cys201, an invariant residue in the heme regulatory motif (HRM), but also His204 is critical for IRP2 degradation.	Heme	65-69	iron responsive element binding protein 2	Homo sapiens	126-130
16039587-6	2005	Although HRMs are known to sense heme concentration by simply binding to heme, the HRM in IRP2 specifically contributes to its oxidative modification, its recognition by the ligase, and its sensing of iron concentration after iron is integrated into heme.	Heme	33-37	iron responsive element binding protein 2	Homo sapiens	90-94
16039587-6	2005	Although HRMs are known to sense heme concentration by simply binding to heme, the HRM in IRP2 specifically contributes to its oxidative modification, its recognition by the ligase, and its sensing of iron concentration after iron is integrated into heme.	Heme	73-77	iron responsive element binding protein 2	Homo sapiens	90-94
16039587-6	2005	Although HRMs are known to sense heme concentration by simply binding to heme, the HRM in IRP2 specifically contributes to its oxidative modification, its recognition by the ligase, and its sensing of iron concentration after iron is integrated into heme.	Iron	201-205	iron responsive element binding protein 2	Homo sapiens	90-94
16039587-6	2005	Although HRMs are known to sense heme concentration by simply binding to heme, the HRM in IRP2 specifically contributes to its oxidative modification, its recognition by the ligase, and its sensing of iron concentration after iron is integrated into heme.	Iron	226-230	iron responsive element binding protein 2	Homo sapiens	90-94
16039587-6	2005	Although HRMs are known to sense heme concentration by simply binding to heme, the HRM in IRP2 specifically contributes to its oxidative modification, its recognition by the ligase, and its sensing of iron concentration after iron is integrated into heme.	Heme	73-77	iron responsive element binding protein 2	Homo sapiens	90-94
15893546-6	2005	A gel shift assay demonstrated that manganese exposure increased the binding of IRP1 and IRP2 to the stem loop-containing mRNAs.	Manganese	36-45	iron responsive element binding protein 2	Homo sapiens	89-93
15684386-0	2005	Nitric oxide inhibits the degradation of IRP2.	Nitric Oxide	0-12	iron responsive element binding protein 2	Homo sapiens	41-45
15777842-1	2005	Iron regulatory protein 2 (IRP2), a posttranscriptional regulator of iron metabolism, is subjected to iron-dependent degradation by the proteasome.	Iron	69-73	iron responsive element binding protein 2	Homo sapiens	0-25
15777842-1	2005	Iron regulatory protein 2 (IRP2), a posttranscriptional regulator of iron metabolism, is subjected to iron-dependent degradation by the proteasome.	Iron	69-73	iron responsive element binding protein 2	Homo sapiens	27-31
15777842-1	2005	Iron regulatory protein 2 (IRP2), a posttranscriptional regulator of iron metabolism, is subjected to iron-dependent degradation by the proteasome.	Iron	102-106	iron responsive element binding protein 2	Homo sapiens	0-25
15777842-1	2005	Iron regulatory protein 2 (IRP2), a posttranscriptional regulator of iron metabolism, is subjected to iron-dependent degradation by the proteasome.	Iron	102-106	iron responsive element binding protein 2	Homo sapiens	27-31
15777842-7	2005	However, the iron-dependent degradation of endogenous IRP2 is not impaired in VHL-deficient cell lines, suggesting that pVHL is not a necessary component of this pathway.	Iron	13-17	iron responsive element binding protein 2	Homo sapiens	54-58
15684386-4	2005	We show here that a treatment of mouse B6 fibroblasts or human H1299 lung cancer cells with the NO-releasing drug S-nitroso-N-acetyl-penicillamine (SNAP) activates IRP2 expression.	S-Nitroso-N-Acetylpenicillamine	114-146	iron responsive element binding protein 2	Homo sapiens	164-168
15684386-4	2005	We show here that a treatment of mouse B6 fibroblasts or human H1299 lung cancer cells with the NO-releasing drug S-nitroso-N-acetyl-penicillamine (SNAP) activates IRP2 expression.	S-Nitroso-N-Acetylpenicillamine	148-152	iron responsive element binding protein 2	Homo sapiens	164-168
15684386-1	2005	Iron-regulatory protein 2 (IRP2), a posttranscriptional regulator of iron metabolism, undergoes proteasomal degradation in iron-replete cells, while it is stabilized in iron deficiency or hypoxia.	Iron	69-73	iron responsive element binding protein 2	Homo sapiens	0-25
15684386-1	2005	Iron-regulatory protein 2 (IRP2), a posttranscriptional regulator of iron metabolism, undergoes proteasomal degradation in iron-replete cells, while it is stabilized in iron deficiency or hypoxia.	Iron	69-73	iron responsive element binding protein 2	Homo sapiens	27-31
15684386-6	2005	Similar results were obtained with IRP2(Delta)(73), a mutant lacking a conserved, IRP2-specific proline- and cysteine-rich domain.	Proline	96-103	iron responsive element binding protein 2	Homo sapiens	35-39
15684386-1	2005	Iron-regulatory protein 2 (IRP2), a posttranscriptional regulator of iron metabolism, undergoes proteasomal degradation in iron-replete cells, while it is stabilized in iron deficiency or hypoxia.	Iron	123-127	iron responsive element binding protein 2	Homo sapiens	0-25
15684386-6	2005	Similar results were obtained with IRP2(Delta)(73), a mutant lacking a conserved, IRP2-specific proline- and cysteine-rich domain.	Proline	96-103	iron responsive element binding protein 2	Homo sapiens	82-86
15684386-1	2005	Iron-regulatory protein 2 (IRP2), a posttranscriptional regulator of iron metabolism, undergoes proteasomal degradation in iron-replete cells, while it is stabilized in iron deficiency or hypoxia.	Iron	123-127	iron responsive element binding protein 2	Homo sapiens	27-31
15684386-2	2005	IRP2 also responds to nitric oxide (NO), as shown in various cell types exposed to pharmacological NO donors and in gamma interferon/lipopolysaccharide-stimulated macrophages.	Nitric Oxide	22-34	iron responsive element binding protein 2	Homo sapiens	0-4
12888568-0	2003	Oxygen and iron regulation of iron regulatory protein 2.	Iron	11-15	iron responsive element binding protein 2	Homo sapiens	30-55
15684386-6	2005	Similar results were obtained with IRP2(Delta)(73), a mutant lacking a conserved, IRP2-specific proline- and cysteine-rich domain.	Cysteine	109-117	iron responsive element binding protein 2	Homo sapiens	35-39
15105251-5	2004	The activities of IRP1 and IRP2 are regulated by distinct posttranslational mechanisms in response to cellular iron levels.	Iron	111-115	iron responsive element binding protein 2	Homo sapiens	27-31
15105251-6	2004	Thus, in iron-replete cells, IRP1 assembles a cubane iron-sulfur cluster, which prevents IRE binding, while IRP2 undergoes proteasomal degradation.	Iron	9-13	iron responsive element binding protein 2	Homo sapiens	108-112
15105251-7	2004	IRP1 and IRP2 also respond, albeit differentially, to iron-independent signals, such as hydrogen peroxide, hypoxia, or nitric oxide.	Iron	54-58	iron responsive element binding protein 2	Homo sapiens	9-13
15105251-7	2004	IRP1 and IRP2 also respond, albeit differentially, to iron-independent signals, such as hydrogen peroxide, hypoxia, or nitric oxide.	Hydrogen Peroxide	88-105	iron responsive element binding protein 2	Homo sapiens	9-13
15105251-7	2004	IRP1 and IRP2 also respond, albeit differentially, to iron-independent signals, such as hydrogen peroxide, hypoxia, or nitric oxide.	Nitric Oxide	119-131	iron responsive element binding protein 2	Homo sapiens	9-13
14729944-0	2004	Iron-mediated degradation of IRP2, an unexpected pathway involving a 2-oxoglutarate-dependent oxygenase activity.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	29-33
14729944-1	2004	Iron regulatory protein 2 (IRP2), a central posttranscriptional regulator of cellular and systemic iron metabolism, undergoes proteasomal degradation in iron-replete cells.	Iron	99-103	iron responsive element binding protein 2	Homo sapiens	0-25
14729944-1	2004	Iron regulatory protein 2 (IRP2), a central posttranscriptional regulator of cellular and systemic iron metabolism, undergoes proteasomal degradation in iron-replete cells.	Iron	99-103	iron responsive element binding protein 2	Homo sapiens	27-31
14729944-1	2004	Iron regulatory protein 2 (IRP2), a central posttranscriptional regulator of cellular and systemic iron metabolism, undergoes proteasomal degradation in iron-replete cells.	Iron	153-157	iron responsive element binding protein 2	Homo sapiens	0-25
14729944-1	2004	Iron regulatory protein 2 (IRP2), a central posttranscriptional regulator of cellular and systemic iron metabolism, undergoes proteasomal degradation in iron-replete cells.	Iron	153-157	iron responsive element binding protein 2	Homo sapiens	27-31
14729944-3	2004	By expressing wild-type and mutated versions of IRP2 in H1299 cells, we find that a C168S C174S C178S triple mutant, or a deletion mutant lacking the entire "73-aa domain," is sensitive to iron-mediated degradation, like wild-type IRP2.	Iron	189-193	iron responsive element binding protein 2	Homo sapiens	48-52
14729944-4	2004	The antioxidants N-acetylcysteine, ascorbate, and alpha-tocopherol not only fail to stabilize IRP2 but, furthermore, promote its proteasomal degradation.	Ascorbic Acid	35-44	iron responsive element binding protein 2	Homo sapiens	94-98
14729944-4	2004	The antioxidants N-acetylcysteine, ascorbate, and alpha-tocopherol not only fail to stabilize IRP2 but, furthermore, promote its proteasomal degradation.	alpha-Tocopherol	50-66	iron responsive element binding protein 2	Homo sapiens	94-98
14729944-5	2004	The pathway for IRP2 degradation is saturable, which may explain earlier data supporting the "cysteine oxidation model," and shows remarkable similarities with the degradation of the hypoxia-inducible factor 1 alpha (HIF-1 alpha): dimethyl-oxalylglycine, a specific inhibitor of 2-oxoglutarate-dependent oxygenases, stabilizes IRP2 following the administration of iron to iron-deficient cells.	Cysteine	94-102	iron responsive element binding protein 2	Homo sapiens	16-20
14729944-5	2004	The pathway for IRP2 degradation is saturable, which may explain earlier data supporting the "cysteine oxidation model," and shows remarkable similarities with the degradation of the hypoxia-inducible factor 1 alpha (HIF-1 alpha): dimethyl-oxalylglycine, a specific inhibitor of 2-oxoglutarate-dependent oxygenases, stabilizes IRP2 following the administration of iron to iron-deficient cells.	oxalylglycine	231-253	iron responsive element binding protein 2	Homo sapiens	16-20
14729944-5	2004	The pathway for IRP2 degradation is saturable, which may explain earlier data supporting the "cysteine oxidation model," and shows remarkable similarities with the degradation of the hypoxia-inducible factor 1 alpha (HIF-1 alpha): dimethyl-oxalylglycine, a specific inhibitor of 2-oxoglutarate-dependent oxygenases, stabilizes IRP2 following the administration of iron to iron-deficient cells.	oxalylglycine	231-253	iron responsive element binding protein 2	Homo sapiens	327-331
14729944-5	2004	The pathway for IRP2 degradation is saturable, which may explain earlier data supporting the "cysteine oxidation model," and shows remarkable similarities with the degradation of the hypoxia-inducible factor 1 alpha (HIF-1 alpha): dimethyl-oxalylglycine, a specific inhibitor of 2-oxoglutarate-dependent oxygenases, stabilizes IRP2 following the administration of iron to iron-deficient cells.	Iron	364-368	iron responsive element binding protein 2	Homo sapiens	16-20
14729944-5	2004	The pathway for IRP2 degradation is saturable, which may explain earlier data supporting the "cysteine oxidation model," and shows remarkable similarities with the degradation of the hypoxia-inducible factor 1 alpha (HIF-1 alpha): dimethyl-oxalylglycine, a specific inhibitor of 2-oxoglutarate-dependent oxygenases, stabilizes IRP2 following the administration of iron to iron-deficient cells.	Iron	372-376	iron responsive element binding protein 2	Homo sapiens	16-20
16275334-3	2005	Through studies analyzing iron-mediated degradation of iron regulatory protein 2 (IRP2), a central regulator of iron metabolism in mammalian cells, we have identified a RING finger protein, HOIL-1, as an ubiquitin ligase recognizing IRP2 through a signal created by heme-mediated oxidative modification of the protein.	Iron	26-30	iron responsive element binding protein 2	Homo sapiens	55-80
16275334-3	2005	Through studies analyzing iron-mediated degradation of iron regulatory protein 2 (IRP2), a central regulator of iron metabolism in mammalian cells, we have identified a RING finger protein, HOIL-1, as an ubiquitin ligase recognizing IRP2 through a signal created by heme-mediated oxidative modification of the protein.	Iron	26-30	iron responsive element binding protein 2	Homo sapiens	82-86
16275334-3	2005	Through studies analyzing iron-mediated degradation of iron regulatory protein 2 (IRP2), a central regulator of iron metabolism in mammalian cells, we have identified a RING finger protein, HOIL-1, as an ubiquitin ligase recognizing IRP2 through a signal created by heme-mediated oxidative modification of the protein.	Iron	26-30	iron responsive element binding protein 2	Homo sapiens	233-237
16275334-3	2005	Through studies analyzing iron-mediated degradation of iron regulatory protein 2 (IRP2), a central regulator of iron metabolism in mammalian cells, we have identified a RING finger protein, HOIL-1, as an ubiquitin ligase recognizing IRP2 through a signal created by heme-mediated oxidative modification of the protein.	Iron	55-59	iron responsive element binding protein 2	Homo sapiens	82-86
16275334-3	2005	Through studies analyzing iron-mediated degradation of iron regulatory protein 2 (IRP2), a central regulator of iron metabolism in mammalian cells, we have identified a RING finger protein, HOIL-1, as an ubiquitin ligase recognizing IRP2 through a signal created by heme-mediated oxidative modification of the protein.	Iron	55-59	iron responsive element binding protein 2	Homo sapiens	233-237
16275334-3	2005	Through studies analyzing iron-mediated degradation of iron regulatory protein 2 (IRP2), a central regulator of iron metabolism in mammalian cells, we have identified a RING finger protein, HOIL-1, as an ubiquitin ligase recognizing IRP2 through a signal created by heme-mediated oxidative modification of the protein.	Heme	266-270	iron responsive element binding protein 2	Homo sapiens	55-80
16275334-3	2005	Through studies analyzing iron-mediated degradation of iron regulatory protein 2 (IRP2), a central regulator of iron metabolism in mammalian cells, we have identified a RING finger protein, HOIL-1, as an ubiquitin ligase recognizing IRP2 through a signal created by heme-mediated oxidative modification of the protein.	Heme	266-270	iron responsive element binding protein 2	Homo sapiens	82-86
16275334-3	2005	Through studies analyzing iron-mediated degradation of iron regulatory protein 2 (IRP2), a central regulator of iron metabolism in mammalian cells, we have identified a RING finger protein, HOIL-1, as an ubiquitin ligase recognizing IRP2 through a signal created by heme-mediated oxidative modification of the protein.	Heme	266-270	iron responsive element binding protein 2	Homo sapiens	233-237
15604406-3	2004	We found that IRP2-/- cells misregulated iron metabolism when cultured in 3 to 6% oxygen, which is comparable to physiological tissue concentrations, but not in 21% oxygen, a concentration that activated IRP1 and allowed it to substitute for IRP2.	Iron	41-45	iron responsive element binding protein 2	Homo sapiens	14-18
15604406-3	2004	We found that IRP2-/- cells misregulated iron metabolism when cultured in 3 to 6% oxygen, which is comparable to physiological tissue concentrations, but not in 21% oxygen, a concentration that activated IRP1 and allowed it to substitute for IRP2.	Oxygen	82-88	iron responsive element binding protein 2	Homo sapiens	14-18
15604406-4	2004	Thus, IRP2 dominates regulation of mammalian iron homeostasis because it alone registers iron concentrations and modulates its RNA-binding activity at physiological oxygen tensions.	Iron	45-49	iron responsive element binding protein 2	Homo sapiens	6-10
15604406-4	2004	Thus, IRP2 dominates regulation of mammalian iron homeostasis because it alone registers iron concentrations and modulates its RNA-binding activity at physiological oxygen tensions.	Iron	89-93	iron responsive element binding protein 2	Homo sapiens	6-10
15604406-4	2004	Thus, IRP2 dominates regulation of mammalian iron homeostasis because it alone registers iron concentrations and modulates its RNA-binding activity at physiological oxygen tensions.	Oxygen	165-171	iron responsive element binding protein 2	Homo sapiens	6-10
15316013-1	2004	Iron regulatory protein 2 coordinates the cellular regulation of iron metabolism by binding to iron-responsive elements in mRNA.	Iron	65-69	iron responsive element binding protein 2	Homo sapiens	0-25
15316013-1	2004	Iron regulatory protein 2 coordinates the cellular regulation of iron metabolism by binding to iron-responsive elements in mRNA.	Iron	95-99	iron responsive element binding protein 2	Homo sapiens	0-25
15316013-4	2004	Iron regulatory protein 2 contains a domain not present in the closely related iron regulatory protein 1, and we found that this domain binds heme with high affinity.	Heme	142-146	iron responsive element binding protein 2	Homo sapiens	0-25
15316013-7	2004	This covalent modification may thus mark the protein molecule for degradation by the proteasome system, providing another mechanism by which heme can regulate the level of iron regulatory protein 2.	Heme	141-145	iron responsive element binding protein 2	Homo sapiens	172-197
15178542-8	2004	Fetal iron status, as indexed by cord serum ferritin concentration, was inversely related to placental IRP-1 (r = -0.66, P < 0.001) and IRP-2 (r = -0.42, P = 0.05) activities.	Iron	6-10	iron responsive element binding protein 2	Homo sapiens	139-144
15057521-1	2004	IRP2 plays an important role in brain iron metabolism.	Iron	38-42	iron responsive element binding protein 2	Homo sapiens	0-4
12855587-1	2003	Iron regulatory proteins (IRP1 and IRP2) are RNA-binding proteins that affect the translation and stabilization of specific mRNAs by binding to stem-loop structures known as iron responsive elements (IREs).	Iron	174-178	iron responsive element binding protein 2	Homo sapiens	35-39
12855587-4	2003	Here we describe the consequences of IRP regulation and show that iron homeostasis is regulated in 2 phases during hypoxia: an early phase where IRP1 RNA-binding activity decreases and iron uptake and Ft synthesis increase, and a late phase where IRP2 RNA-binding activity increases and iron uptake and Ft synthesis decrease.	Iron	66-70	iron responsive element binding protein 2	Homo sapiens	247-251
12888568-1	2003	Iron regulatory protein 2 (IRP2) is a central regulator of cellular iron homeostasis due to its regulation of specific mRNAs encoding proteins of iron uptake and storage.	Iron	68-72	iron responsive element binding protein 2	Homo sapiens	0-25
12888568-1	2003	Iron regulatory protein 2 (IRP2) is a central regulator of cellular iron homeostasis due to its regulation of specific mRNAs encoding proteins of iron uptake and storage.	Iron	68-72	iron responsive element binding protein 2	Homo sapiens	27-31
12888568-1	2003	Iron regulatory protein 2 (IRP2) is a central regulator of cellular iron homeostasis due to its regulation of specific mRNAs encoding proteins of iron uptake and storage.	Iron	146-150	iron responsive element binding protein 2	Homo sapiens	0-25
12888568-1	2003	Iron regulatory protein 2 (IRP2) is a central regulator of cellular iron homeostasis due to its regulation of specific mRNAs encoding proteins of iron uptake and storage.	Iron	146-150	iron responsive element binding protein 2	Homo sapiens	27-31
12888568-2	2003	Iron regulates IRP2 by mediating its rapid proteasomal degradation, where hypoxia and the hypoxia mimetics CoCl2 and desferrioxamine (DFO) stabilize it.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	15-19
12888568-2	2003	Iron regulates IRP2 by mediating its rapid proteasomal degradation, where hypoxia and the hypoxia mimetics CoCl2 and desferrioxamine (DFO) stabilize it.	cobaltous chloride	107-112	iron responsive element binding protein 2	Homo sapiens	15-19
12888568-2	2003	Iron regulates IRP2 by mediating its rapid proteasomal degradation, where hypoxia and the hypoxia mimetics CoCl2 and desferrioxamine (DFO) stabilize it.	Deferoxamine	117-132	iron responsive element binding protein 2	Homo sapiens	15-19
12888568-2	2003	Iron regulates IRP2 by mediating its rapid proteasomal degradation, where hypoxia and the hypoxia mimetics CoCl2 and desferrioxamine (DFO) stabilize it.	Deferoxamine	134-137	iron responsive element binding protein 2	Homo sapiens	15-19
12888568-3	2003	Previous studies showed that iron-mediated degradation of IRP2 requires the presence of critical cysteines that reside within a 73-amino acid unique region.	Iron	29-33	iron responsive element binding protein 2	Homo sapiens	58-62
12888568-3	2003	Previous studies showed that iron-mediated degradation of IRP2 requires the presence of critical cysteines that reside within a 73-amino acid unique region.	Cysteine	97-106	iron responsive element binding protein 2	Homo sapiens	58-62
12888568-5	2003	In addition, DFO and hypoxia blocked the degradation of both the wild-type and mutant IRP2 proteins.	Deferoxamine	13-16	iron responsive element binding protein 2	Homo sapiens	86-90
12888568-7	2003	Since 2-OG-dependent dioxygenases require iron and oxygen, in addition to 2-OG, for substrate hydroxylation, we hypothesized that this activity may be involved in the regulation of IRP2 stability.	Iron	42-46	iron responsive element binding protein 2	Homo sapiens	181-185
12888568-7	2003	Since 2-OG-dependent dioxygenases require iron and oxygen, in addition to 2-OG, for substrate hydroxylation, we hypothesized that this activity may be involved in the regulation of IRP2 stability.	Oxygen	23-29	iron responsive element binding protein 2	Homo sapiens	181-185
12888568-7	2003	Since 2-OG-dependent dioxygenases require iron and oxygen, in addition to 2-OG, for substrate hydroxylation, we hypothesized that this activity may be involved in the regulation of IRP2 stability.	Ketoglutaric Acids	6-10	iron responsive element binding protein 2	Homo sapiens	181-185
12888568-8	2003	To test this we used the 2-OG-dependent dioxygenase inhibitor dimethyloxalylglycine (DMOG) and showed that it blocked iron-mediated IRP2 degradation.	oxalylglycine	62-83	iron responsive element binding protein 2	Homo sapiens	132-136
12888568-8	2003	To test this we used the 2-OG-dependent dioxygenase inhibitor dimethyloxalylglycine (DMOG) and showed that it blocked iron-mediated IRP2 degradation.	oxalylglycine	85-89	iron responsive element binding protein 2	Homo sapiens	132-136
12888568-8	2003	To test this we used the 2-OG-dependent dioxygenase inhibitor dimethyloxalylglycine (DMOG) and showed that it blocked iron-mediated IRP2 degradation.	Iron	118-122	iron responsive element binding protein 2	Homo sapiens	132-136
12888568-9	2003	In addition, hypoxia, DFO and DMOG blocked IRP2 ubiquitination.	Deferoxamine	22-25	iron responsive element binding protein 2	Homo sapiens	43-47
12888568-9	2003	In addition, hypoxia, DFO and DMOG blocked IRP2 ubiquitination.	oxalylglycine	30-34	iron responsive element binding protein 2	Homo sapiens	43-47
12888568-10	2003	These data indicate that the region of IRP2 that is involved in IRP2 iron-mediated degradation lies outside of the 73-amino acid unique region and suggest a model whereby 2-OG-dependent dioxygenase activity may be involved in the oxygen and iron regulation of IRP2 protein stability.	Iron	69-73	iron responsive element binding protein 2	Homo sapiens	39-43
12888568-10	2003	These data indicate that the region of IRP2 that is involved in IRP2 iron-mediated degradation lies outside of the 73-amino acid unique region and suggest a model whereby 2-OG-dependent dioxygenase activity may be involved in the oxygen and iron regulation of IRP2 protein stability.	Iron	69-73	iron responsive element binding protein 2	Homo sapiens	64-68
12888568-10	2003	These data indicate that the region of IRP2 that is involved in IRP2 iron-mediated degradation lies outside of the 73-amino acid unique region and suggest a model whereby 2-OG-dependent dioxygenase activity may be involved in the oxygen and iron regulation of IRP2 protein stability.	Iron	69-73	iron responsive element binding protein 2	Homo sapiens	64-68
12888568-10	2003	These data indicate that the region of IRP2 that is involved in IRP2 iron-mediated degradation lies outside of the 73-amino acid unique region and suggest a model whereby 2-OG-dependent dioxygenase activity may be involved in the oxygen and iron regulation of IRP2 protein stability.	Oxygen	188-194	iron responsive element binding protein 2	Homo sapiens	39-43
12888568-10	2003	These data indicate that the region of IRP2 that is involved in IRP2 iron-mediated degradation lies outside of the 73-amino acid unique region and suggest a model whereby 2-OG-dependent dioxygenase activity may be involved in the oxygen and iron regulation of IRP2 protein stability.	Oxygen	188-194	iron responsive element binding protein 2	Homo sapiens	64-68
12888568-10	2003	These data indicate that the region of IRP2 that is involved in IRP2 iron-mediated degradation lies outside of the 73-amino acid unique region and suggest a model whereby 2-OG-dependent dioxygenase activity may be involved in the oxygen and iron regulation of IRP2 protein stability.	Oxygen	188-194	iron responsive element binding protein 2	Homo sapiens	64-68
12888568-10	2003	These data indicate that the region of IRP2 that is involved in IRP2 iron-mediated degradation lies outside of the 73-amino acid unique region and suggest a model whereby 2-OG-dependent dioxygenase activity may be involved in the oxygen and iron regulation of IRP2 protein stability.	Iron	241-245	iron responsive element binding protein 2	Homo sapiens	39-43
12888568-10	2003	These data indicate that the region of IRP2 that is involved in IRP2 iron-mediated degradation lies outside of the 73-amino acid unique region and suggest a model whereby 2-OG-dependent dioxygenase activity may be involved in the oxygen and iron regulation of IRP2 protein stability.	Iron	241-245	iron responsive element binding protein 2	Homo sapiens	64-68
12888568-10	2003	These data indicate that the region of IRP2 that is involved in IRP2 iron-mediated degradation lies outside of the 73-amino acid unique region and suggest a model whereby 2-OG-dependent dioxygenase activity may be involved in the oxygen and iron regulation of IRP2 protein stability.	Iron	241-245	iron responsive element binding protein 2	Homo sapiens	64-68
12629548-5	2003	Iron regulatory protein 2 (IRP2), a modulator of iron metabolism, is regulated by iron-induced ubiquitination and degradation.	Iron	49-53	iron responsive element binding protein 2	Homo sapiens	0-25
12972033-0	2003	The role of endogenous heme synthesis and degradation domain cysteines in cellular iron-dependent degradation of IRP2.	Heme	23-27	iron responsive element binding protein 2	Homo sapiens	113-117
12972033-0	2003	The role of endogenous heme synthesis and degradation domain cysteines in cellular iron-dependent degradation of IRP2.	Cysteine	61-70	iron responsive element binding protein 2	Homo sapiens	113-117
12972033-0	2003	The role of endogenous heme synthesis and degradation domain cysteines in cellular iron-dependent degradation of IRP2.	Iron	83-87	iron responsive element binding protein 2	Homo sapiens	113-117
12972033-1	2003	Iron regulatory protein 2 (IRP2) is a mammalian cytosolic iron-sensing protein that regulates expression of iron metabolism proteins, including ferritin and transferrin receptor 1.	Iron	58-62	iron responsive element binding protein 2	Homo sapiens	0-25
12972033-1	2003	Iron regulatory protein 2 (IRP2) is a mammalian cytosolic iron-sensing protein that regulates expression of iron metabolism proteins, including ferritin and transferrin receptor 1.	Iron	58-62	iron responsive element binding protein 2	Homo sapiens	27-31
12972033-1	2003	Iron regulatory protein 2 (IRP2) is a mammalian cytosolic iron-sensing protein that regulates expression of iron metabolism proteins, including ferritin and transferrin receptor 1.	Iron	108-112	iron responsive element binding protein 2	Homo sapiens	0-25
12972033-1	2003	Iron regulatory protein 2 (IRP2) is a mammalian cytosolic iron-sensing protein that regulates expression of iron metabolism proteins, including ferritin and transferrin receptor 1.	Iron	108-112	iron responsive element binding protein 2	Homo sapiens	27-31
12972033-2	2003	IRP2 is ubiquitinated and degraded by the proteasome in iron-replete cells but is relatively stable in iron-depleted cells.	Iron	56-60	iron responsive element binding protein 2	Homo sapiens	0-4
12972033-2	2003	IRP2 is ubiquitinated and degraded by the proteasome in iron-replete cells but is relatively stable in iron-depleted cells.	Iron	103-107	iron responsive element binding protein 2	Homo sapiens	0-4
12972033-3	2003	Recent work has shown that IRP2 contains a unique 73-amino-acid domain that binds iron in vitro and undergoes iron-dependent oxidation and cleavage (J. Biol.	Iron	82-86	iron responsive element binding protein 2	Homo sapiens	27-31
12972033-3	2003	Recent work has shown that IRP2 contains a unique 73-amino-acid domain that binds iron in vitro and undergoes iron-dependent oxidation and cleavage (J. Biol.	Iron	110-114	iron responsive element binding protein 2	Homo sapiens	27-31
12972033-7	2003	To assess the role of these cysteines in cellular iron- dependent degradation of IRP2, we mutagenized these cysteines in various combinations in the context of full-length protein and generated cell lines in which recombinant IRP2 expression was inducible.	Iron	50-54	iron responsive element binding protein 2	Homo sapiens	81-85
12972033-8	2003	Iron-dependent degradation of IRP2 mutagenized at any or all of the cysteines of the putative degradation domain in cells was comparable to wild-type (WT).	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	30-34
12972033-8	2003	Iron-dependent degradation of IRP2 mutagenized at any or all of the cysteines of the putative degradation domain in cells was comparable to wild-type (WT).	Cysteine	68-77	iron responsive element binding protein 2	Homo sapiens	30-34
12972033-10	2003	Treatment with sodium nitroprusside (SNP), an NO+ donor, caused a decrease in cellular IRP2 concentrations, but the SNP effect was abrogated by simultaneous addition of the iron chelator desferal and was not affected by cysteine mutations.	Nitroprusside	15-35	iron responsive element binding protein 2	Homo sapiens	87-91
12972033-11	2003	Inhibition of endogenous heme synthesis with succinylacetone significantly inhibited iron- dependent degradation of IRP2.	succinylacetone	45-60	iron responsive element binding protein 2	Homo sapiens	116-120
12972033-11	2003	Inhibition of endogenous heme synthesis with succinylacetone significantly inhibited iron- dependent degradation of IRP2.	Iron	85-89	iron responsive element binding protein 2	Homo sapiens	116-120
12972033-12	2003	Addition of cobalt chloride inhibited degradation of both WT and mutagenized IRP2.	cobaltous chloride	12-27	iron responsive element binding protein 2	Homo sapiens	77-81
12972033-14	2003	The early molecular events in iron-dependent degradation of IRP2 remain to be elucidated.	Iron	30-34	iron responsive element binding protein 2	Homo sapiens	60-64
12591920-0	2003	Iron regulatory protein 2 as iron sensor.	Iron	29-33	iron responsive element binding protein 2	Homo sapiens	0-25
12591920-2	2003	Iron regulatory protein 2 coordinates cellular regulation of iron metabolism by binding to iron responsive elements in mRNA.	Iron	61-65	iron responsive element binding protein 2	Homo sapiens	0-25
12591920-2	2003	Iron regulatory protein 2 coordinates cellular regulation of iron metabolism by binding to iron responsive elements in mRNA.	Iron	91-95	iron responsive element binding protein 2	Homo sapiens	0-25
12629548-5	2003	Iron regulatory protein 2 (IRP2), a modulator of iron metabolism, is regulated by iron-induced ubiquitination and degradation.	Iron	49-53	iron responsive element binding protein 2	Homo sapiens	27-31
12629548-5	2003	Iron regulatory protein 2 (IRP2), a modulator of iron metabolism, is regulated by iron-induced ubiquitination and degradation.	Iron	82-86	iron responsive element binding protein 2	Homo sapiens	0-25
12629548-5	2003	Iron regulatory protein 2 (IRP2), a modulator of iron metabolism, is regulated by iron-induced ubiquitination and degradation.	Iron	82-86	iron responsive element binding protein 2	Homo sapiens	27-31
12629548-7	2003	The oxidation of IRP2 is generated by haem, which binds to IRP2 in iron-rich cells, and by oxygen, indicating that the iron sensing of IRP2 depends on the synthesis and availability of haem.	Iron	67-71	iron responsive element binding protein 2	Homo sapiens	17-21
12629548-7	2003	The oxidation of IRP2 is generated by haem, which binds to IRP2 in iron-rich cells, and by oxygen, indicating that the iron sensing of IRP2 depends on the synthesis and availability of haem.	Iron	67-71	iron responsive element binding protein 2	Homo sapiens	59-63
12629548-7	2003	The oxidation of IRP2 is generated by haem, which binds to IRP2 in iron-rich cells, and by oxygen, indicating that the iron sensing of IRP2 depends on the synthesis and availability of haem.	Iron	67-71	iron responsive element binding protein 2	Homo sapiens	59-63
12629548-7	2003	The oxidation of IRP2 is generated by haem, which binds to IRP2 in iron-rich cells, and by oxygen, indicating that the iron sensing of IRP2 depends on the synthesis and availability of haem.	Oxygen	91-97	iron responsive element binding protein 2	Homo sapiens	17-21
12629548-7	2003	The oxidation of IRP2 is generated by haem, which binds to IRP2 in iron-rich cells, and by oxygen, indicating that the iron sensing of IRP2 depends on the synthesis and availability of haem.	Iron	119-123	iron responsive element binding protein 2	Homo sapiens	17-21
12629548-7	2003	The oxidation of IRP2 is generated by haem, which binds to IRP2 in iron-rich cells, and by oxygen, indicating that the iron sensing of IRP2 depends on the synthesis and availability of haem.	Iron	119-123	iron responsive element binding protein 2	Homo sapiens	59-63
12629548-7	2003	The oxidation of IRP2 is generated by haem, which binds to IRP2 in iron-rich cells, and by oxygen, indicating that the iron sensing of IRP2 depends on the synthesis and availability of haem.	Iron	119-123	iron responsive element binding protein 2	Homo sapiens	59-63
12592010-1	2003	Regulated expression of proteins involved in mammalian iron metabolism is achieved in part through the interaction of the iron regulatory proteins IRP1 and IRP2 with highly conserved RNA stem-loop structures, known as iron-responsive elements (IREs), that are located within the 5" or 3" untranslated regions of regulated transcripts.	Iron	55-59	iron responsive element binding protein 2	Homo sapiens	156-160
12572667-5	2003	When cells were incubated with up to 20 microM of iron, a typical decrease in IRP1 and IRP2 activity was observed.	Iron	50-54	iron responsive element binding protein 2	Homo sapiens	87-91
12592010-1	2003	Regulated expression of proteins involved in mammalian iron metabolism is achieved in part through the interaction of the iron regulatory proteins IRP1 and IRP2 with highly conserved RNA stem-loop structures, known as iron-responsive elements (IREs), that are located within the 5" or 3" untranslated regions of regulated transcripts.	Iron	122-126	iron responsive element binding protein 2	Homo sapiens	156-160
12592010-1	2003	Regulated expression of proteins involved in mammalian iron metabolism is achieved in part through the interaction of the iron regulatory proteins IRP1 and IRP2 with highly conserved RNA stem-loop structures, known as iron-responsive elements (IREs), that are located within the 5" or 3" untranslated regions of regulated transcripts.	Iron	122-126	iron responsive element binding protein 2	Homo sapiens	156-160
12237336-11	2002	Interestingly, the effect of DOX on primary cultures of cardiomyocytes was similar to that observed using neoplastic cells, and particularly notable was the decrease in IRP2-RNA-binding activity.	Doxorubicin	29-32	iron responsive element binding protein 2	Homo sapiens	169-173
12200453-0	2002	Multiple, conserved iron-responsive elements in the 3"-untranslated region of transferrin receptor mRNA enhance binding of iron regulatory protein 2.	Iron	20-24	iron responsive element binding protein 2	Homo sapiens	123-148
12200453-1	2002	Synthesis of proteins for iron homeostasis is regulated by specific, combinatorial mRNA/protein interactions between RNA stem-loop structures (iron-responsive elements, IREs) and iron-regulatory proteins (IRP1 and IRP2), controlling either mRNA translation or stability.	Iron	26-30	iron responsive element binding protein 2	Homo sapiens	214-218
12465072-1	2002	Mice with targeted disruptions in the iron-responsive binding protein 2 (IRP2) gene accumulate iron in distinct regions of the brain and develop neurodegenerative characteristics resembling Parkinson"s disease after 6 months of age.	Iron	38-42	iron responsive element binding protein 2	Homo sapiens	73-77
12057761-3	2002	A major mechanism for the regulation of iron homeostasis relies on the post-transcriptional control of ferritin and transferrin receptor mRNAs, which are recognized by two cytoplasmic iron regulatory proteins (IRP-1 and IRP-2) that modulate their translation and stability, respectively.	Iron	40-44	iron responsive element binding protein 2	Homo sapiens	220-225
12416730-4	2002	When cellular iron is abundant, IRPs become inactivated (IRP-1) or degraded (IRP-2).	Iron	14-18	iron responsive element binding protein 2	Homo sapiens	77-82
12139757-6	2002	Thereby, EPO weakened the binding affinity of IRP-2 to the iron responsive element (IRE) within e-ALAS mRNA which resulted in the increased expression of e-ALAS IRE-controlled reporter gene constructs, following EPO stimulation.	Iron	59-63	iron responsive element binding protein 2	Homo sapiens	46-51
12192037-0	2002	Novel translational control through an iron-responsive element by interaction of multifunctional protein YB-1 and IRP2.	Iron	39-43	iron responsive element binding protein 2	Homo sapiens	114-118
12192037-4	2002	Both in vitro binding and coimmunoprecipitation assays showed the direct interaction of YB-1 and IRP2 in the presence of a high concentration of iron.	Iron	145-149	iron responsive element binding protein 2	Homo sapiens	97-101
12192037-5	2002	RNA gel shift assays showed that YB-1 reduced the formation of the IRP2-mRNA complex when the iron-responsive element of the ferritin mRNA 5" untranslated region (UTR) was used as a probe.	Iron	94-98	iron responsive element binding protein 2	Homo sapiens	67-71
12192037-8	2002	An In vivo coimmunoprecipitation assay showed that IRP2 bound to YB-1 in the presence of iron and a proteasome inhibitor.	Iron	89-93	iron responsive element binding protein 2	Homo sapiens	51-55
12192037-9	2002	The direct interaction of YB-1 and IRP2 provides the first evidence of the involvement of YB-1 in the translational regulation of an iron-related protein.	Iron	133-137	iron responsive element binding protein 2	Homo sapiens	35-39
12121757-3	2002	Current views on cellular iron homeostasis involving the iron regulatory proteins IRP1 and IRP2 and their interactions with the iron regulatory elements, affecting either mRNA translation (ferritin and erythroid cell delta-aminolaevulinate synthase) or mRNA stability (transferrin receptor) are discussed.	Iron	26-30	iron responsive element binding protein 2	Homo sapiens	91-95
12121757-10	2002	With the latter compound, iron also increases, which may reflect an effect of aluminium on the IRP2 protein.	Iron	26-30	iron responsive element binding protein 2	Homo sapiens	95-99
12121757-10	2002	With the latter compound, iron also increases, which may reflect an effect of aluminium on the IRP2 protein.	Aluminum	78-87	iron responsive element binding protein 2	Homo sapiens	95-99
11807826-0	2002	Increased IRP1 and IRP2 RNA binding activity accompanies a reduction of the labile iron pool in HFE-expressing cells.	Iron	83-87	iron responsive element binding protein 2	Homo sapiens	19-23
11991850-4	2002	This article outlines the current state of knowledge on cellular iron homeostasis, with particular reference to the iron regulatory proteins (IRP1, IRP2 and HFE) and the iron membrane transport proteins, two of which have been shown to be members of the natural resistance- associated macrophage protein family (Nramp1 and 2).	Iron	65-69	iron responsive element binding protein 2	Homo sapiens	148-152
12401949-2	2002	Previous studies of regulation of the cytosolic iron sensor, iron-regulatory protein 2 (IRP2), indicate that iron-dependent oxidation triggers ubiquitination and proteasomal degradation of IRP2.	Iron	48-52	iron responsive element binding protein 2	Homo sapiens	61-86
12401949-2	2002	Previous studies of regulation of the cytosolic iron sensor, iron-regulatory protein 2 (IRP2), indicate that iron-dependent oxidation triggers ubiquitination and proteasomal degradation of IRP2.	Iron	48-52	iron responsive element binding protein 2	Homo sapiens	88-92
12401949-2	2002	Previous studies of regulation of the cytosolic iron sensor, iron-regulatory protein 2 (IRP2), indicate that iron-dependent oxidation triggers ubiquitination and proteasomal degradation of IRP2.	Iron	48-52	iron responsive element binding protein 2	Homo sapiens	189-193
12401949-2	2002	Previous studies of regulation of the cytosolic iron sensor, iron-regulatory protein 2 (IRP2), indicate that iron-dependent oxidation triggers ubiquitination and proteasomal degradation of IRP2.	Iron	61-65	iron responsive element binding protein 2	Homo sapiens	88-92
12401949-2	2002	Previous studies of regulation of the cytosolic iron sensor, iron-regulatory protein 2 (IRP2), indicate that iron-dependent oxidation triggers ubiquitination and proteasomal degradation of IRP2.	Iron	61-65	iron responsive element binding protein 2	Homo sapiens	189-193
11326747-6	2001	Our results suggest distinct roles for IRP1 and IRP2 in the regulation of iron homeostasis in the mammalian nervous system where IRP1 may provide a maintenance function in contrast to IRP2 that could participate in modulating proper CAN functions, including cardiopulmonary, gustatory as well as fine motor control.	Iron	74-78	iron responsive element binding protein 2	Homo sapiens	48-52
11981450-1	2002	Iron regulatory proteins, IRP1 and IRP2, are cytoplasmic proteins of the iron-sulfur cluster isomerase family and serve as major post-transcriptional regulators of cellular iron metabolism.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	35-39
11981450-1	2002	Iron regulatory proteins, IRP1 and IRP2, are cytoplasmic proteins of the iron-sulfur cluster isomerase family and serve as major post-transcriptional regulators of cellular iron metabolism.	Iron	73-77	iron responsive element binding protein 2	Homo sapiens	35-39
11981450-1	2002	Iron regulatory proteins, IRP1 and IRP2, are cytoplasmic proteins of the iron-sulfur cluster isomerase family and serve as major post-transcriptional regulators of cellular iron metabolism.	Iron	173-177	iron responsive element binding protein 2	Homo sapiens	35-39
11981450-3	2002	IRP1 and IRP2 respond to alterations in intracellular iron levels, but also to other signals such as nitric oxide (NO) and reactive oxygen species (ROS).	Iron	54-58	iron responsive element binding protein 2	Homo sapiens	9-13
11981450-3	2002	IRP1 and IRP2 respond to alterations in intracellular iron levels, but also to other signals such as nitric oxide (NO) and reactive oxygen species (ROS).	Nitric Oxide	101-113	iron responsive element binding protein 2	Homo sapiens	9-13
11981450-3	2002	IRP1 and IRP2 respond to alterations in intracellular iron levels, but also to other signals such as nitric oxide (NO) and reactive oxygen species (ROS).	Reactive Oxygen Species	123-146	iron responsive element binding protein 2	Homo sapiens	9-13
11981450-3	2002	IRP1 and IRP2 respond to alterations in intracellular iron levels, but also to other signals such as nitric oxide (NO) and reactive oxygen species (ROS).	Reactive Oxygen Species	148-151	iron responsive element binding protein 2	Homo sapiens	9-13
11981450-4	2002	The redox regulation of IRP1 and IRP2 provides direct links between the control of iron homeostasis and oxidative stress.	Iron	83-87	iron responsive element binding protein 2	Homo sapiens	33-37
11313346-2	2001	The translation of many iron proteins is controlled by the binding of two cytoplasmic proteins, iron regulatory protein 1 and 2 (IRP1 and IRP2) to stem loop structures, known as iron-responsive elements (IREs), found in the untranslated regions of their mRNAs.	Iron	24-28	iron responsive element binding protein 2	Homo sapiens	138-142
11313346-2	2001	The translation of many iron proteins is controlled by the binding of two cytoplasmic proteins, iron regulatory protein 1 and 2 (IRP1 and IRP2) to stem loop structures, known as iron-responsive elements (IREs), found in the untranslated regions of their mRNAs.	Iron	96-100	iron responsive element binding protein 2	Homo sapiens	138-142
11313346-3	2001	In short, when iron is depleted, IRP1 or IRP2 bind IREs; this decreases the synthesis of proteins involved in iron storage and mitochondrial metabolism (e.g. ferritin and mitochondrial aconitase) and increases the synthesis of those involved in iron uptake (e.g. transferrin receptor).	Iron	15-19	iron responsive element binding protein 2	Homo sapiens	41-45
11313346-3	2001	In short, when iron is depleted, IRP1 or IRP2 bind IREs; this decreases the synthesis of proteins involved in iron storage and mitochondrial metabolism (e.g. ferritin and mitochondrial aconitase) and increases the synthesis of those involved in iron uptake (e.g. transferrin receptor).	Iron	110-114	iron responsive element binding protein 2	Homo sapiens	41-45
11313346-3	2001	In short, when iron is depleted, IRP1 or IRP2 bind IREs; this decreases the synthesis of proteins involved in iron storage and mitochondrial metabolism (e.g. ferritin and mitochondrial aconitase) and increases the synthesis of those involved in iron uptake (e.g. transferrin receptor).	Iron	110-114	iron responsive element binding protein 2	Homo sapiens	41-45
11085915-3	2000	Iron homoeostasis is controlled through several genes, an increasing number of which have been found to contain non-coding sequences [i.e. the iron-responsive elements (IREs)] which are recognized at the mRNA level by two cytoplasmic iron-regulatory proteins (IRP-1 and IRP-2).	Iron	143-147	iron responsive element binding protein 2	Homo sapiens	270-275
11085915-3	2000	Iron homoeostasis is controlled through several genes, an increasing number of which have been found to contain non-coding sequences [i.e. the iron-responsive elements (IREs)] which are recognized at the mRNA level by two cytoplasmic iron-regulatory proteins (IRP-1 and IRP-2).	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	270-275
11175792-2	2001	Two distinct but highly homologous proteins, IRP1 and IRP2, bind IREs with high affinity when cells are depleted of iron, inhibiting translation of some transcripts, such as ferritin, or turnover of others, such as the transferrin receptor (TFRC).	Iron	116-120	iron responsive element binding protein 2	Homo sapiens	54-58
9868172-7	1998	Multiple factors modulate the RNA binding activity of IRP1 and/or IRP2 including iron, nitric oxide, phosphorylation by protein kinase C, oxidative stress and hypoxia/reoxygenation.	Iron	81-85	iron responsive element binding protein 2	Homo sapiens	66-70
10580122-0	1999	Stabilization of iron regulatory protein 2, IRP2, by aluminum.	Aluminum	53-61	iron responsive element binding protein 2	Homo sapiens	17-42
10580122-0	1999	Stabilization of iron regulatory protein 2, IRP2, by aluminum.	Aluminum	53-61	iron responsive element binding protein 2	Homo sapiens	44-48
10580122-1	1999	Iron regulatory protein 2 (IRP2) is one of the central regulators of iron homeostasis.	Iron	69-73	iron responsive element binding protein 2	Homo sapiens	0-25
10580122-1	1999	Iron regulatory protein 2 (IRP2) is one of the central regulators of iron homeostasis.	Iron	69-73	iron responsive element binding protein 2	Homo sapiens	27-31
10580122-2	1999	IRP2 regulates expression of molecules involved in iron metabolism by binding to iron responsive elements (IREs) in the transcripts of those molecules in iron depletion.	Iron	51-55	iron responsive element binding protein 2	Homo sapiens	0-4
10580122-2	1999	IRP2 regulates expression of molecules involved in iron metabolism by binding to iron responsive elements (IREs) in the transcripts of those molecules in iron depletion.	Iron	81-85	iron responsive element binding protein 2	Homo sapiens	0-4
10580122-2	1999	IRP2 regulates expression of molecules involved in iron metabolism by binding to iron responsive elements (IREs) in the transcripts of those molecules in iron depletion.	Iron	81-85	iron responsive element binding protein 2	Homo sapiens	0-4
10580122-3	1999	IRP2 is regulated by the accelerated degradation initiated by the iron-catalyzed oxidation.	Iron	66-70	iron responsive element binding protein 2	Homo sapiens	0-4
10580122-4	1999	Here we report that aluminum antagonizes the iron-induced decrease in IRE binding activity of IRP2.	Aluminum	20-28	iron responsive element binding protein 2	Homo sapiens	94-98
10580122-4	1999	Here we report that aluminum antagonizes the iron-induced decrease in IRE binding activity of IRP2.	Iron	45-49	iron responsive element binding protein 2	Homo sapiens	94-98
10580122-5	1999	Aluminum also inhibits iron-induced oxidation of IRP2 in vitro.	Aluminum	0-8	iron responsive element binding protein 2	Homo sapiens	49-53
10580122-5	1999	Aluminum also inhibits iron-induced oxidation of IRP2 in vitro.	Iron	23-27	iron responsive element binding protein 2	Homo sapiens	49-53
10580122-6	1999	These results suggest that aluminum stabilizes IRP2 by interfering with the iron-catalyzed oxidation, which results in perturbation of iron metabolism.	Aluminum	27-35	iron responsive element binding protein 2	Homo sapiens	47-51
10580122-6	1999	These results suggest that aluminum stabilizes IRP2 by interfering with the iron-catalyzed oxidation, which results in perturbation of iron metabolism.	Iron	76-80	iron responsive element binding protein 2	Homo sapiens	47-51
10580122-6	1999	These results suggest that aluminum stabilizes IRP2 by interfering with the iron-catalyzed oxidation, which results in perturbation of iron metabolism.	Iron	135-139	iron responsive element binding protein 2	Homo sapiens	47-51
10522551-2	1999	The uptake of iron by mammalian cells is post-transcriptionally regulated by the interaction of iron-response proteins (IRP1 and IRP2) with iron-response elements (IREs) found in the mRNAs of genes of iron metabolism, such as ferritin, the transferrin receptor, erythroid aminolevulinic acid synthase, and mitochondrial aconitase.	Iron	14-18	iron responsive element binding protein 2	Homo sapiens	129-133
10522551-2	1999	The uptake of iron by mammalian cells is post-transcriptionally regulated by the interaction of iron-response proteins (IRP1 and IRP2) with iron-response elements (IREs) found in the mRNAs of genes of iron metabolism, such as ferritin, the transferrin receptor, erythroid aminolevulinic acid synthase, and mitochondrial aconitase.	Iron	96-100	iron responsive element binding protein 2	Homo sapiens	129-133
10522551-2	1999	The uptake of iron by mammalian cells is post-transcriptionally regulated by the interaction of iron-response proteins (IRP1 and IRP2) with iron-response elements (IREs) found in the mRNAs of genes of iron metabolism, such as ferritin, the transferrin receptor, erythroid aminolevulinic acid synthase, and mitochondrial aconitase.	Iron	96-100	iron responsive element binding protein 2	Homo sapiens	129-133
10522551-2	1999	The uptake of iron by mammalian cells is post-transcriptionally regulated by the interaction of iron-response proteins (IRP1 and IRP2) with iron-response elements (IREs) found in the mRNAs of genes of iron metabolism, such as ferritin, the transferrin receptor, erythroid aminolevulinic acid synthase, and mitochondrial aconitase.	Iron	96-100	iron responsive element binding protein 2	Homo sapiens	129-133
10484662-2	1999	Iron regulatory proteins (IRP1 and IRP2), two post-transcriptional regulators of gene expression, are particularly sensitive to NO synthesis and to oxidative stress.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	35-39
10484662-4	1999	IRP2 has no Fe-S cluster but exhibits several redox-sensitive cysteine residues.	Cysteine	62-70	iron responsive element binding protein 2	Homo sapiens	0-4
10084280-5	1999	Cellular iron storage and uptake are coordinately regulated post-transcriptionally by cytoplasmic factors, iron-regulatory proteins 1 and 2 (IRP-1 and IRP-2).	Iron	9-13	iron responsive element binding protein 2	Homo sapiens	151-156
9867873-2	1999	Iron regulatory proteins (IRP1 and IRP2) are redox-sensitive RNA-binding proteins that modulate the expression of several genes encoding key proteins of iron metabolism.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	35-39
9867873-2	1999	Iron regulatory proteins (IRP1 and IRP2) are redox-sensitive RNA-binding proteins that modulate the expression of several genes encoding key proteins of iron metabolism.	Iron	153-157	iron responsive element binding protein 2	Homo sapiens	35-39
10551872-5	1999	In this study, we showed that a short exposure of RAW 264.7 cells (a murine macrophage cell line) to the NO(+) donor, sodium nitroprusside (SNP), caused a significant decrease in IRP-2 binding to the IREs followed by IRP-2 degradation and that these changes occurred without affecting IRP-1 binding.	Nitroprusside	118-138	iron responsive element binding protein 2	Homo sapiens	179-184
10551872-5	1999	In this study, we showed that a short exposure of RAW 264.7 cells (a murine macrophage cell line) to the NO(+) donor, sodium nitroprusside (SNP), caused a significant decrease in IRP-2 binding to the IREs followed by IRP-2 degradation and that these changes occurred without affecting IRP-1 binding.	Nitroprusside	118-138	iron responsive element binding protein 2	Homo sapiens	217-222
9924025-0	1999	Coordinated regulation of iron-controlling genes, H-ferritin and IRP2, by c-MYC.	Iron	26-30	iron responsive element binding protein 2	Homo sapiens	65-69
9924025-2	1999	Here, c-MYC is shown to repress the expression of the heavy subunit of the protein ferritin (H-ferritin), which sequesters intracellular iron, and to stimulate the expression of the iron regulatory protein-2 (IRP2), which increases the intracellular iron pool.	Iron	182-186	iron responsive element binding protein 2	Homo sapiens	209-213
10440237-1	1999	Iron regulatory proteins 1 and 2 (IRP1 and IRP2) are RNA binding proteins that posttranscriptionally regulate the expression of mRNAs coding for proteins involved in the maintenance of iron and energy homeostasis.	Iron	185-189	iron responsive element binding protein 2	Homo sapiens	43-47
10440237-7	1999	The recent observations that changes in oxygen tension regulate both IRP1 and IRP2 RNA binding activities will be addressed in light of ROS regulation of the IRPs.	Oxygen	40-46	iron responsive element binding protein 2	Homo sapiens	78-82
9868172-7	1998	Multiple factors modulate the RNA binding activity of IRP1 and/or IRP2 including iron, nitric oxide, phosphorylation by protein kinase C, oxidative stress and hypoxia/reoxygenation.	Nitric Oxide	87-99	iron responsive element binding protein 2	Homo sapiens	66-70
9560204-0	1998	Iron-dependent oxidation, ubiquitination, and degradation of iron regulatory protein 2: implications for degradation of oxidized proteins.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	61-86
9726965-9	1998	Variations in IRE structure and cellular IRP1/IRP2 ratios can provide a range of finely tuned, mRNA-specific responses to the same (iron) signal.	Iron	132-136	iron responsive element binding protein 2	Homo sapiens	46-50
9560204-2	1998	Iron uptake and distribution is regulated tightly in mammalian cells, in part by iron regulatory protein 2 (IRP2), a protein that is degraded efficiently by the proteasome in iron-replete cells.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	81-106
9560204-2	1998	Iron uptake and distribution is regulated tightly in mammalian cells, in part by iron regulatory protein 2 (IRP2), a protein that is degraded efficiently by the proteasome in iron-replete cells.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	108-112
9560204-2	1998	Iron uptake and distribution is regulated tightly in mammalian cells, in part by iron regulatory protein 2 (IRP2), a protein that is degraded efficiently by the proteasome in iron-replete cells.	Iron	81-85	iron responsive element binding protein 2	Homo sapiens	108-112
9560204-4	1998	Moreover, iron-dependent oxidation converts IRP2 into a substrate for ubiquitination in vitro.	Iron	10-14	iron responsive element binding protein 2	Homo sapiens	44-48
9560204-5	1998	A regulatory pathway is described in which excess iron is sensed by its ability to catalyze site-specific oxidations in IRP2, oxidized IRP2 is ubiquitinated, and ubiquitinated IRP2 subsequently is degraded by the proteasome.	Iron	50-54	iron responsive element binding protein 2	Homo sapiens	120-124
9560204-5	1998	A regulatory pathway is described in which excess iron is sensed by its ability to catalyze site-specific oxidations in IRP2, oxidized IRP2 is ubiquitinated, and ubiquitinated IRP2 subsequently is degraded by the proteasome.	Iron	50-54	iron responsive element binding protein 2	Homo sapiens	135-139
9560204-5	1998	A regulatory pathway is described in which excess iron is sensed by its ability to catalyze site-specific oxidations in IRP2, oxidized IRP2 is ubiquitinated, and ubiquitinated IRP2 subsequently is degraded by the proteasome.	Iron	50-54	iron responsive element binding protein 2	Homo sapiens	135-139
9242665-1	1997	Expression of several proteins of higher eukaryotes is post-transcriptionally regulated by interaction of iron-responsive elements (IREs) on their mRNAs and iron regulatory proteins (IRP1 and IRP2).	Iron	106-110	iron responsive element binding protein 2	Homo sapiens	192-196
9545264-1	1998	Iron regulatory proteins (IRP1 and IRP2) are two cytoplasmic RNA-binding proteins that control iron metabolism in mammalian cells.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	35-39
9545264-1	1998	Iron regulatory proteins (IRP1 and IRP2) are two cytoplasmic RNA-binding proteins that control iron metabolism in mammalian cells.	Iron	95-99	iron responsive element binding protein 2	Homo sapiens	35-39
9555030-2	1998	We hypothesized that the abnormal distribution of iron in Alzheimer brain might result from alterations in iron regulatory proteins (IRP) such as IRP-1 and IRP-2, the main control elements of cellular iron homeostasis.	Iron	50-54	iron responsive element binding protein 2	Homo sapiens	156-161
9555030-2	1998	We hypothesized that the abnormal distribution of iron in Alzheimer brain might result from alterations in iron regulatory proteins (IRP) such as IRP-1 and IRP-2, the main control elements of cellular iron homeostasis.	Iron	107-111	iron responsive element binding protein 2	Homo sapiens	156-161
9555030-2	1998	We hypothesized that the abnormal distribution of iron in Alzheimer brain might result from alterations in iron regulatory proteins (IRP) such as IRP-1 and IRP-2, the main control elements of cellular iron homeostasis.	Iron	107-111	iron responsive element binding protein 2	Homo sapiens	156-161
9555030-4	1998	Since IRP-2 colocalizes with redox-active iron, our results suggest that alterations in IRP-2 might be directly linked to impaired iron homeostasis in Alzheimer"s disease.	Iron	42-46	iron responsive element binding protein 2	Homo sapiens	88-93
9482759-1	1998	Iron regulatory protein 1 (IRP1) and IRP2 are cytoplasmic RNA binding proteins that are central regulators of mammalian iron homeostasis.	Iron	120-124	iron responsive element binding protein 2	Homo sapiens	37-41
9430733-1	1998	Iron regulatory proteins 1 and 2 (IRP-1, IRP-2) interact with iron-responsive elements (IREs) present in the 5"- or 3"-untranslated regions (UTR) of several mRNAs coding for proteins in iron metabolism.	Iron	62-66	iron responsive element binding protein 2	Homo sapiens	41-46
9430733-1	1998	Iron regulatory proteins 1 and 2 (IRP-1, IRP-2) interact with iron-responsive elements (IREs) present in the 5"- or 3"-untranslated regions (UTR) of several mRNAs coding for proteins in iron metabolism.	Iron	186-190	iron responsive element binding protein 2	Homo sapiens	41-46
9242665-4	1997	IRP2 is also regulated by intracellular iron level, but it is assumed that regulation is achieved by accelerated turn-over.	Iron	40-44	iron responsive element binding protein 2	Homo sapiens	0-4
9242665-5	1997	In this report, the effect of peroxynitrite, a strong oxidant produced when nitric oxide and O-2 are biosynthesized simultaneously, on the RNA binding activity of IRP1 and IRP2 was investigated in vitro.	Peroxynitrous Acid	30-43	iron responsive element binding protein 2	Homo sapiens	172-176
9242665-5	1997	In this report, the effect of peroxynitrite, a strong oxidant produced when nitric oxide and O-2 are biosynthesized simultaneously, on the RNA binding activity of IRP1 and IRP2 was investigated in vitro.	Nitric Oxide	76-88	iron responsive element binding protein 2	Homo sapiens	172-176
9242665-5	1997	In this report, the effect of peroxynitrite, a strong oxidant produced when nitric oxide and O-2 are biosynthesized simultaneously, on the RNA binding activity of IRP1 and IRP2 was investigated in vitro.	Oosponol	93-96	iron responsive element binding protein 2	Homo sapiens	172-176
9242665-13	1997	When exposed to peroxynitrite, IRP2 lost its spontaneous IRE binding activity, which was restored by further exposure to 2-mercaptoethanol, thus showing that peroxynitrite can also regulate IRP2 by a post-translational event.	Peroxynitrous Acid	16-29	iron responsive element binding protein 2	Homo sapiens	31-35
9242665-13	1997	When exposed to peroxynitrite, IRP2 lost its spontaneous IRE binding activity, which was restored by further exposure to 2-mercaptoethanol, thus showing that peroxynitrite can also regulate IRP2 by a post-translational event.	Peroxynitrous Acid	16-29	iron responsive element binding protein 2	Homo sapiens	190-194
9242665-13	1997	When exposed to peroxynitrite, IRP2 lost its spontaneous IRE binding activity, which was restored by further exposure to 2-mercaptoethanol, thus showing that peroxynitrite can also regulate IRP2 by a post-translational event.	Mercaptoethanol	121-138	iron responsive element binding protein 2	Homo sapiens	31-35
9242665-13	1997	When exposed to peroxynitrite, IRP2 lost its spontaneous IRE binding activity, which was restored by further exposure to 2-mercaptoethanol, thus showing that peroxynitrite can also regulate IRP2 by a post-translational event.	Mercaptoethanol	121-138	iron responsive element binding protein 2	Homo sapiens	190-194
9242665-13	1997	When exposed to peroxynitrite, IRP2 lost its spontaneous IRE binding activity, which was restored by further exposure to 2-mercaptoethanol, thus showing that peroxynitrite can also regulate IRP2 by a post-translational event.	Peroxynitrous Acid	158-171	iron responsive element binding protein 2	Homo sapiens	31-35
9242665-13	1997	When exposed to peroxynitrite, IRP2 lost its spontaneous IRE binding activity, which was restored by further exposure to 2-mercaptoethanol, thus showing that peroxynitrite can also regulate IRP2 by a post-translational event.	Peroxynitrous Acid	158-171	iron responsive element binding protein 2	Homo sapiens	190-194
9192174-5	1997	Iron regulatory proteins are regulated either by assembly or by disassembly of an iron-sulfur cluster (IRP1) or by rapid degradation in the presence of iron (IRP2).	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	158-162
9325434-11	1997	Cellular Fe uptake and storage are coordinately regulated through a feedback control mechanism mediated at the post-transcriptional level by cytoplasmic factors known as IRP1 and IRP2.	Iron	9-11	iron responsive element binding protein 2	Homo sapiens	179-183
9192174-5	1997	Iron regulatory proteins are regulated either by assembly or by disassembly of an iron-sulfur cluster (IRP1) or by rapid degradation in the presence of iron (IRP2).	Sulfur	87-93	iron responsive element binding protein 2	Homo sapiens	158-162
9192174-5	1997	Iron regulatory proteins are regulated either by assembly or by disassembly of an iron-sulfur cluster (IRP1) or by rapid degradation in the presence of iron (IRP2).	Iron	152-156	iron responsive element binding protein 2	Homo sapiens	158-162
8831290-1	1996	Iron uptake and storage in mammalian cells is at least partly regulated at a post-transcriptional level by the iron regulatory proteins (IRP-1 and IRP-2).	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	147-152
8994263-3	1997	IRP-1 and IRP-2 are trans-acting regulators of mRNAs involved in iron uptake, storage and utilisation.	Iron	65-69	iron responsive element binding protein 2	Homo sapiens	10-15
8831290-1	1996	Iron uptake and storage in mammalian cells is at least partly regulated at a post-transcriptional level by the iron regulatory proteins (IRP-1 and IRP-2).	Iron	111-115	iron responsive element binding protein 2	Homo sapiens	147-152
8831290-6	1996	They are coordinately regulated by cellular iron, but whereas IRP-1 is inactivated by high iron levels, IRP-2 is rapidly degraded.	Iron	44-48	iron responsive element binding protein 2	Homo sapiens	104-109
8831290-9	1996	These findings hint that IRP-1 and IRP-2 may bind preferentially to certain mRNAs in vivo, possibly extending their known functions beyond the regulation of intracellular iron homeostasis.	Iron	171-175	iron responsive element binding protein 2	Homo sapiens	35-40
8710843-3	1996	Two cytoplasmic RNA-binding proteins, iron-regulatory protein-1 (IRP-1) and IRP-2, respond to changes in cellular iron availability and coordinate the expression of mRNAs that harbor IRP-binding sites, iron-responsive elements (IREs).	Iron	38-42	iron responsive element binding protein 2	Homo sapiens	76-81
8710843-3	1996	Two cytoplasmic RNA-binding proteins, iron-regulatory protein-1 (IRP-1) and IRP-2, respond to changes in cellular iron availability and coordinate the expression of mRNAs that harbor IRP-binding sites, iron-responsive elements (IREs).	Iron	114-118	iron responsive element binding protein 2	Homo sapiens	76-81
8617762-8	1996	These findings suggest that IRP-1 and IRP-2 may each regulate unique mRNA targets in vivo, possibly extending their function beyond the regulation of intracellular iron homeostasis.	Iron	164-168	iron responsive element binding protein 2	Homo sapiens	38-43
8636154-3	1996	We have investigated changes in activity and expression of both IRP1 and IRP2 during phorbol 12-myristate 13-acetate (PMA)-induced differentiation of HL-60 cells.	Tetradecanoylphorbol Acetate	85-116	iron responsive element binding protein 2	Homo sapiens	73-77
8636154-3	1996	We have investigated changes in activity and expression of both IRP1 and IRP2 during phorbol 12-myristate 13-acetate (PMA)-induced differentiation of HL-60 cells.	Tetradecanoylphorbol Acetate	118-121	iron responsive element binding protein 2	Homo sapiens	73-77
8636154-10	1996	Hemin appeared to reduce the abundance of phosphorylated IRP2.	Hemin	0-5	iron responsive element binding protein 2	Homo sapiens	57-61
8633068-3	1996	Site-directed mutagenesis of IRP1 and IRP2 reveals that, although the binding affinities for consensus IREs are indistinguishable, the contributions of arginine residues in the active-site cleft to the binding affinity are different in the two RNA binding sites.	Arginine	152-160	iron responsive element binding protein 2	Homo sapiens	38-42
7665579-0	1995	Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	48-73
8856975-8	1996	Iron regulatory protein 2 (IRP2) binds similar stem-loop structures, but the mode of regulation of IRP2 is different in that IRP2 is rapidly degraded in iron-replete cells.	Iron	153-157	iron responsive element binding protein 2	Homo sapiens	0-25
8856975-8	1996	Iron regulatory protein 2 (IRP2) binds similar stem-loop structures, but the mode of regulation of IRP2 is different in that IRP2 is rapidly degraded in iron-replete cells.	Iron	153-157	iron responsive element binding protein 2	Homo sapiens	27-31
8856975-8	1996	Iron regulatory protein 2 (IRP2) binds similar stem-loop structures, but the mode of regulation of IRP2 is different in that IRP2 is rapidly degraded in iron-replete cells.	Iron	153-157	iron responsive element binding protein 2	Homo sapiens	99-103
8856975-8	1996	Iron regulatory protein 2 (IRP2) binds similar stem-loop structures, but the mode of regulation of IRP2 is different in that IRP2 is rapidly degraded in iron-replete cells.	Iron	153-157	iron responsive element binding protein 2	Homo sapiens	99-103
7489724-0	1995	Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2.	Iron	17-21	iron responsive element binding protein 2	Homo sapiens	72-97
7489724-4	1995	The binding activity of IRP2 is regulated by the degradation of the protein when cells are iron-replete.	Iron	91-95	iron responsive element binding protein 2	Homo sapiens	24-28
7489724-5	1995	Here, we demonstrate that a 73 amino acid sequence that corresponds to a unique exon in IRP2 contains a sequence required for rapid degradation in iron-replete cells.	Iron	147-151	iron responsive element binding protein 2	Homo sapiens	88-92
7489724-7	1995	Site-directed mutagenesis has demonstrated that specific cysteines within the IRP2 exon are required for iron-dependent degradation.	Cysteine	57-66	iron responsive element binding protein 2	Homo sapiens	78-82
7489724-7	1995	Site-directed mutagenesis has demonstrated that specific cysteines within the IRP2 exon are required for iron-dependent degradation.	Iron	105-109	iron responsive element binding protein 2	Homo sapiens	78-82
7489724-8	1995	The degradation of IRP2 appears to be mediated by the proteasome in iron-replete cells.	Iron	68-72	iron responsive element binding protein 2	Homo sapiens	19-23
7665579-2	1995	IRP1 and IRP2 RNA binding activities are regulated by iron; IRP1 and IRP2 bind IREs with high affinity in iron-depleted cells and with low affinity in iron-repleted cells.	Iron	54-58	iron responsive element binding protein 2	Homo sapiens	9-13
7665579-2	1995	IRP1 and IRP2 RNA binding activities are regulated by iron; IRP1 and IRP2 bind IREs with high affinity in iron-depleted cells and with low affinity in iron-repleted cells.	Iron	106-110	iron responsive element binding protein 2	Homo sapiens	9-13
7665579-2	1995	IRP1 and IRP2 RNA binding activities are regulated by iron; IRP1 and IRP2 bind IREs with high affinity in iron-depleted cells and with low affinity in iron-repleted cells.	Iron	106-110	iron responsive element binding protein 2	Homo sapiens	69-73
7665579-2	1995	IRP1 and IRP2 RNA binding activities are regulated by iron; IRP1 and IRP2 bind IREs with high affinity in iron-depleted cells and with low affinity in iron-repleted cells.	Iron	106-110	iron responsive element binding protein 2	Homo sapiens	9-13
7665579-2	1995	IRP1 and IRP2 RNA binding activities are regulated by iron; IRP1 and IRP2 bind IREs with high affinity in iron-depleted cells and with low affinity in iron-repleted cells.	Iron	106-110	iron responsive element binding protein 2	Homo sapiens	69-73
7665579-5	1995	The iron-dependent decrease in IRP2 levels was not due to a decrease in the amount of IRP2 mRNA or to a decrease in the rate of IRP2 synthesis.	Iron	4-8	iron responsive element binding protein 2	Homo sapiens	31-35
7665579-6	1995	Pulse-chase experiments demonstrated that iron resulted in a 3-fold increase in the degradation rate of IRP2.	Iron	42-46	iron responsive element binding protein 2	Homo sapiens	104-108
7665579-9	1995	These data suggest the involvement of the proteasome in iron-mediated IRP2 proteolysis.	Iron	56-60	iron responsive element binding protein 2	Homo sapiens	70-74
26319559-2	2016	In response to hypoxia, in the PWM, there was increased expression of proteins involved in iron acquisition, such as iron regulatory proteins (IRP1, IRP2) and transferrin receptor in oligodendrocytes.	Iron	91-95	iron responsive element binding protein 2	Homo sapiens	149-153
8407882-7	1993	The oxygen consumption activity of cytochrome aco3 was measured using several kinds of cytochromes c as the electron mediators.	Oxygen	4-10	iron responsive element binding protein 2	Homo sapiens	46-50
8407882-8	1993	The reaction between cytochrome aco3 and eucaryotic cytochromes c was completely inhibited by poly-L-lysine.	Lysine	94-107	iron responsive element binding protein 2	Homo sapiens	32-36
7544791-0	1995	Differential modulation of the RNA-binding proteins IRP-1 and IRP-2 in response to iron.	Iron	83-87	iron responsive element binding protein 2	Homo sapiens	62-67
7544791-5	1995	The in vivo iron regulation of IRP-1 and IRP-2 appeared to involve different pathways.	Iron	12-16	iron responsive element binding protein 2	Homo sapiens	41-46
7544791-7	1995	This induction, however, was distinguishable by the addition of translation inhibitors, which temporarily delayed activation of IRP-1 by up to 8 h, but fully blocked IRP-2 induction for up to 20 h. The activation of IRP-2 was also prevented by transcription inhibition with actinomycin D.	Dactinomycin	274-287	iron responsive element binding protein 2	Homo sapiens	216-221
7544791-11	1995	IRP-2 inactivation/degradation occurred upon readdition of iron, but it required translation of another protein.	Iron	59-63	iron responsive element binding protein 2	Homo sapiens	0-5
7890603-0	1995	Translational repressor activity is equivalent and is quantitatively predicted by in vitro RNA binding for two iron-responsive element-binding proteins, IRP1 and IRP2.	Iron	111-115	iron responsive element binding protein 2	Homo sapiens	162-166
7890603-14	1995	In contrast to IRP1, IRP2 is not inactivated for RNA binding by alkylation with N-ethylmaleimide or phenylmaleimide, and as we would therefore predict, IRP2 treated with N-ethylmaleimide remains an effective repressor of ferritin translation.	Ethylmaleimide	170-186	iron responsive element binding protein 2	Homo sapiens	152-156
7983023-0	1994	Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2.	Iron	39-43	iron responsive element binding protein 2	Homo sapiens	80-105
7983023-9	1994	In most cell lines tested, levels of IRP2 are inversely regulated by iron levels due to iron-dependent regulation of the half-life of the protein.	Iron	69-73	iron responsive element binding protein 2	Homo sapiens	37-41
7983023-9	1994	In most cell lines tested, levels of IRP2 are inversely regulated by iron levels due to iron-dependent regulation of the half-life of the protein.	Iron	88-92	iron responsive element binding protein 2	Homo sapiens	37-41
8518212-1	1993	Treatment of 19-[oxygenated]-androst-4-ene-3,17-dione with Mn(AcO)3 and ClCH2COOH in benzene gave epimeric mixtures of the corresponding 2 zeta-chloroacetates and 2 zeta-acetates.	Androstenedione	27-53	iron responsive element binding protein 2	Homo sapiens	62-67
8518212-1	1993	Treatment of 19-[oxygenated]-androst-4-ene-3,17-dione with Mn(AcO)3 and ClCH2COOH in benzene gave epimeric mixtures of the corresponding 2 zeta-chloroacetates and 2 zeta-acetates.	Benzene	85-92	iron responsive element binding protein 2	Homo sapiens	62-67
8518212-1	1993	Treatment of 19-[oxygenated]-androst-4-ene-3,17-dione with Mn(AcO)3 and ClCH2COOH in benzene gave epimeric mixtures of the corresponding 2 zeta-chloroacetates and 2 zeta-acetates.	zeta-chloroacetates	139-158	iron responsive element binding protein 2	Homo sapiens	62-67
8518212-1	1993	Treatment of 19-[oxygenated]-androst-4-ene-3,17-dione with Mn(AcO)3 and ClCH2COOH in benzene gave epimeric mixtures of the corresponding 2 zeta-chloroacetates and 2 zeta-acetates.	Acetates	169-178	iron responsive element binding protein 2	Homo sapiens	62-67
26319559-2	2016	In response to hypoxia, in the PWM, there was increased expression of proteins involved in iron acquisition, such as iron regulatory proteins (IRP1, IRP2) and transferrin receptor in oligodendrocytes.	Iron	117-121	iron responsive element binding protein 2	Homo sapiens	149-153
34747587-0	2021	Robust Visible-Blind Wearable Infrared Sensor Based on IrP2 Nanoparticle-Embedded Few-Layer Graphene and the Effect of Photogating.	Graphite	92-100	iron responsive element binding protein 2	Homo sapiens	55-59
34747587-2	2021	Here, we report the synthesis of IrP2 nanoparticle-embedded few-layer graphene by one-step solid-state pyrolysis and its application in visible-blind infrared sensing.	Graphite	70-78	iron responsive element binding protein 2	Homo sapiens	33-37
34747587-3	2021	A linear photodetector device was fabricated by drop casting IrP2 nanoparticle-embedded few-layer graphene onto a flexible PET substrate with two gold electrodes separated by ~16 mum.	Graphite	98-106	iron responsive element binding protein 2	Homo sapiens	61-65
34573347-1	2021	Iron responsive elements (IREs) are mRNA stem-loop targets for translational control by the two iron regulatory proteins IRP1 and IRP2.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	130-134
34675764-2	2021	Our previous in vitro data have demonstrated that Irp2 depletion upregulates hypoxia-inducible factor subunits Hif1alpha and Hif2alpha expression; inhibition of Hif2alpha rescues Irp2 ablation-induced mitochondrial dysfunction; and inhibition of Hif1alpha suppresses the overdose production of lactic acid derived from actively aerobic glycolysis.	Lactic Acid	294-305	iron responsive element binding protein 2	Homo sapiens	50-54
34573347-1	2021	Iron responsive elements (IREs) are mRNA stem-loop targets for translational control by the two iron regulatory proteins IRP1 and IRP2.	Iron	96-100	iron responsive element binding protein 2	Homo sapiens	130-134
34389108-4	2021	At the cellular level, iron regulatory proteins 1 and 2 (IRP1 and IRP2) register cytosolic iron concentrations and post-transcriptionally regulate the expression of iron metabolism genes to optimize iron availability for essential cellular processes, including heme biosynthesis and iron-sulfur cluster biogenesis.	Iron	91-95	iron responsive element binding protein 2	Homo sapiens	66-70
34462321-5	2021	We also uncovered a paralogous synthetic lethal mechanism behind a genetic interaction between STAG2 and the iron regulatory gene IREB2 Finally, investigation of an unusually strong context-dependent genetic interaction in HAP1 cells revealed factors that could be important for alleviating cohesin loading stress.	Iron	109-113	iron responsive element binding protein 2	Homo sapiens	130-135
34389108-4	2021	At the cellular level, iron regulatory proteins 1 and 2 (IRP1 and IRP2) register cytosolic iron concentrations and post-transcriptionally regulate the expression of iron metabolism genes to optimize iron availability for essential cellular processes, including heme biosynthesis and iron-sulfur cluster biogenesis.	Iron	165-169	iron responsive element binding protein 2	Homo sapiens	66-70
34389108-4	2021	At the cellular level, iron regulatory proteins 1 and 2 (IRP1 and IRP2) register cytosolic iron concentrations and post-transcriptionally regulate the expression of iron metabolism genes to optimize iron availability for essential cellular processes, including heme biosynthesis and iron-sulfur cluster biogenesis.	Iron	199-203	iron responsive element binding protein 2	Homo sapiens	66-70
34389108-4	2021	At the cellular level, iron regulatory proteins 1 and 2 (IRP1 and IRP2) register cytosolic iron concentrations and post-transcriptionally regulate the expression of iron metabolism genes to optimize iron availability for essential cellular processes, including heme biosynthesis and iron-sulfur cluster biogenesis.	Heme	261-265	iron responsive element binding protein 2	Homo sapiens	66-70
34389108-4	2021	At the cellular level, iron regulatory proteins 1 and 2 (IRP1 and IRP2) register cytosolic iron concentrations and post-transcriptionally regulate the expression of iron metabolism genes to optimize iron availability for essential cellular processes, including heme biosynthesis and iron-sulfur cluster biogenesis.	Iron	283-287	iron responsive element binding protein 2	Homo sapiens	66-70
34389108-4	2021	At the cellular level, iron regulatory proteins 1 and 2 (IRP1 and IRP2) register cytosolic iron concentrations and post-transcriptionally regulate the expression of iron metabolism genes to optimize iron availability for essential cellular processes, including heme biosynthesis and iron-sulfur cluster biogenesis.	Sulfur	288-294	iron responsive element binding protein 2	Homo sapiens	66-70
34064225-3	2021	A canonical IRE is a mRNA structure that interacts with the iron regulatory proteins (IRP1 and IRP2) to post-transcriptionally regulate the expression of proteins related to iron metabolism.	Iron	60-64	iron responsive element binding protein 2	Homo sapiens	95-99
34064225-3	2021	A canonical IRE is a mRNA structure that interacts with the iron regulatory proteins (IRP1 and IRP2) to post-transcriptionally regulate the expression of proteins related to iron metabolism.	Iron	174-178	iron responsive element binding protein 2	Homo sapiens	95-99
35602653-0	2022	Disruption of cellular iron homeostasis by IREB2 missense variants causes severe neurodevelopmental delay, dystonia and seizures.	Iron	23-27	iron responsive element binding protein 2	Homo sapiens	43-48
35602653-7	2022	These results, in addition to confirming the essential role of IRP2 in the regulation of iron metabolism in humans, expand the scope of the known IRP2-related neurodegenerative disorders and underscore that IREB2 pathological variants may impact the iron-responsive element-binding activity of IRP2 with varying degrees of severity.	Iron	250-254	iron responsive element binding protein 2	Homo sapiens	207-212
35602653-2	2022	Intracellular iron homeostasis in mammals is maintained by two homologous ubiquitously expressed iron-responsive element-binding proteins (IRP1 and IRP2).	Iron	14-18	iron responsive element binding protein 2	Homo sapiens	148-152
35602653-2	2022	Intracellular iron homeostasis in mammals is maintained by two homologous ubiquitously expressed iron-responsive element-binding proteins (IRP1 and IRP2).	Iron	97-101	iron responsive element binding protein 2	Homo sapiens	148-152
35602653-7	2022	These results, in addition to confirming the essential role of IRP2 in the regulation of iron metabolism in humans, expand the scope of the known IRP2-related neurodegenerative disorders and underscore that IREB2 pathological variants may impact the iron-responsive element-binding activity of IRP2 with varying degrees of severity.	Iron	89-93	iron responsive element binding protein 2	Homo sapiens	63-67
35602653-7	2022	These results, in addition to confirming the essential role of IRP2 in the regulation of iron metabolism in humans, expand the scope of the known IRP2-related neurodegenerative disorders and underscore that IREB2 pathological variants may impact the iron-responsive element-binding activity of IRP2 with varying degrees of severity.	Iron	89-93	iron responsive element binding protein 2	Homo sapiens	207-212
34039609-3	2021	Iron-responsive element-binding proteins IRP1 and IRP2 posttranscriptionally regulate iron homeostasis.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	50-54
34039609-3	2021	Iron-responsive element-binding proteins IRP1 and IRP2 posttranscriptionally regulate iron homeostasis.	Iron	86-90	iron responsive element binding protein 2	Homo sapiens	50-54
34039609-8	2021	Deletion of both IRP1 and IRP2 abolishes the iron-starvation response, preventing its activation by ISC synthesis inhibition.	Iron	45-49	iron responsive element binding protein 2	Homo sapiens	26-30
32564977-5	2020	Cellular iron metabolism is post-transcriptionally controlled by iron regulatory proteins, IRP1 and IRP2, while systemic iron balance is regulated by the iron hormone hepcidin.	Iron	9-13	iron responsive element binding protein 2	Homo sapiens	100-104
33656766-12	2021	Incubation of ferroptosis inhibitors ferrostatin-1 (Fer-1) or knockdown of iron-responsive element-binding protein 2 (IREB2) notably weakened curcumin-induced anti-tumor effect and ferroptosis in A549 and H1299 cells.	Curcumin	142-150	iron responsive element binding protein 2	Homo sapiens	75-116
33656766-12	2021	Incubation of ferroptosis inhibitors ferrostatin-1 (Fer-1) or knockdown of iron-responsive element-binding protein 2 (IREB2) notably weakened curcumin-induced anti-tumor effect and ferroptosis in A549 and H1299 cells.	Curcumin	142-150	iron responsive element binding protein 2	Homo sapiens	118-123
33684901-0	2021	A porous heterostructure catalyst for oxygen evolution: synergy between IrP2nanocrystals and ultrathin P,N-codoped carbon nanosheets.	Oxygen	38-44	iron responsive element binding protein 2	Homo sapiens	72-76
33684901-2	2021	Herein, we developed IrP2 nanocrystals uniformly anchored in P,N-codoped carbon nanosheets (IrP2@PNC-NS) as highly active OER electrocatalysts.	Carbon	73-79	iron responsive element binding protein 2	Homo sapiens	21-25
33684901-2	2021	Herein, we developed IrP2 nanocrystals uniformly anchored in P,N-codoped carbon nanosheets (IrP2@PNC-NS) as highly active OER electrocatalysts.	Carbon	73-79	iron responsive element binding protein 2	Homo sapiens	92-96
33684901-6	2021	DFT calculations reveal that the synergistic effects derived from the IrP2/PNC interface, which can effectively tune the activation barriers towards facilitating the oxygen evolution process.	Oxygen	166-172	iron responsive element binding protein 2	Homo sapiens	70-74
32678895-7	2020	Treatment of UROS-deficient erythroid cell lines and peripheral blood CD34+-derived erythroid cultures from a CEP patient with deferiprone inhibited iron-dependent protein ALAS2 and IRP2 expression and reduced porphyrin production.	Deferiprone	127-138	iron responsive element binding protein 2	Homo sapiens	182-186
33393230-6	2021	Mechanistically, OTUD1 promotes transferrin receptor protein 1 (TFRC)-mediated iron transportation through deubiquitinating and stabilizing IREB2, leading to increased ROS generation and ferroptosis.	Iron	79-83	iron responsive element binding protein 2	Homo sapiens	140-145
33393230-9	2021	Our data demonstrate that OTUD1 plays a stimulatory role in iron transportation and highlight the importance of OTUD1-IREB2-TFRC signaling axis in host antitumor immunity.	Iron	60-64	iron responsive element binding protein 2	Homo sapiens	118-123
32947011-0	2020	Iron Regulatory Protein 2 is required for artemether -mediated anti-hepatic fibrosis through ferroptosis pathway.	Artemether	42-52	iron responsive element binding protein 2	Homo sapiens	0-25
32112499-8	2020	These changes were accompanied by upregulation of iron regulatory protein 2 (IRP-2), which led to an increase in transferrin receptor 1 (TfR-1), thus increasing iron entry into cells and potentially leading to ferroptosis.	Iron	50-54	iron responsive element binding protein 2	Homo sapiens	77-82
32377332-3	2020	In addition, 2-oxoglutarate- (OG-) dependent dioxygenase activity of PHD2 is involved in the oxygen and iron regulation of iron-responsive element binding protein 2 (IRP2) stability.	Ketoglutaric Acids	13-27	iron responsive element binding protein 2	Homo sapiens	123-164
33295723-3	2020	Iron responding protein-2 (IRP2) is the protein product of IREB2 gene, which is a COPD susceptibility gene that regulates cellular iron homeostasis and has a key role in hypoxic conditions.	Iron	131-135	iron responsive element binding protein 2	Homo sapiens	0-25
33295723-3	2020	Iron responding protein-2 (IRP2) is the protein product of IREB2 gene, which is a COPD susceptibility gene that regulates cellular iron homeostasis and has a key role in hypoxic conditions.	Iron	131-135	iron responsive element binding protein 2	Homo sapiens	27-31
33295723-3	2020	Iron responding protein-2 (IRP2) is the protein product of IREB2 gene, which is a COPD susceptibility gene that regulates cellular iron homeostasis and has a key role in hypoxic conditions.	Iron	131-135	iron responsive element binding protein 2	Homo sapiens	59-64
32250954-13	2020	In addition, several stress and iron response genes, HSP70, SOD1, ATM and IRP2 did not change in the cells on ABIKO iron, while these genes were induced with exogenous application of FeSO4.	ferrous sulfate	183-188	iron responsive element binding protein 2	Homo sapiens	74-78
32276991-1	2020	Iron regulatory protein 2 (IRP2) is a key regulator of iron homeostasis and is found to be altered in several types of human cancer.	Iron	55-59	iron responsive element binding protein 2	Homo sapiens	0-25
32276991-1	2020	Iron regulatory protein 2 (IRP2) is a key regulator of iron homeostasis and is found to be altered in several types of human cancer.	Iron	55-59	iron responsive element binding protein 2	Homo sapiens	27-31
32377332-3	2020	In addition, 2-oxoglutarate- (OG-) dependent dioxygenase activity of PHD2 is involved in the oxygen and iron regulation of iron-responsive element binding protein 2 (IRP2) stability.	Ketoglutaric Acids	13-27	iron responsive element binding protein 2	Homo sapiens	166-170
32377332-3	2020	In addition, 2-oxoglutarate- (OG-) dependent dioxygenase activity of PHD2 is involved in the oxygen and iron regulation of iron-responsive element binding protein 2 (IRP2) stability.	Oxygen	47-53	iron responsive element binding protein 2	Homo sapiens	123-164
32377332-3	2020	In addition, 2-oxoglutarate- (OG-) dependent dioxygenase activity of PHD2 is involved in the oxygen and iron regulation of iron-responsive element binding protein 2 (IRP2) stability.	Oxygen	47-53	iron responsive element binding protein 2	Homo sapiens	166-170
32377332-3	2020	In addition, 2-oxoglutarate- (OG-) dependent dioxygenase activity of PHD2 is involved in the oxygen and iron regulation of iron-responsive element binding protein 2 (IRP2) stability.	Iron	104-108	iron responsive element binding protein 2	Homo sapiens	123-164
32377332-3	2020	In addition, 2-oxoglutarate- (OG-) dependent dioxygenase activity of PHD2 is involved in the oxygen and iron regulation of iron-responsive element binding protein 2 (IRP2) stability.	Iron	104-108	iron responsive element binding protein 2	Homo sapiens	166-170
32126207-0	2020	FBXL5 Regulates IRP2 Stability in Iron Homeostasis via an Oxygen-Responsive [2Fe2S] Cluster.	Iron	34-38	iron responsive element binding protein 2	Homo sapiens	16-20
32126207-6	2020	Steric incompatibility also allows FBXL5 to physically dislodge IRP2 from iron-responsive element RNA to facilitate its turnover.	Iron	74-78	iron responsive element binding protein 2	Homo sapiens	64-68
32243827-0	2020	How Oxidation of a Unique Iron-Sulfur Cluster in FBXL5 Regulates IRP2 Levels and Promotes Regulation of Iron Metabolism Proteins.	Iron	26-30	iron responsive element binding protein 2	Homo sapiens	65-69
32243827-0	2020	How Oxidation of a Unique Iron-Sulfur Cluster in FBXL5 Regulates IRP2 Levels and Promotes Regulation of Iron Metabolism Proteins.	Sulfur	31-37	iron responsive element binding protein 2	Homo sapiens	65-69
32126207-0	2020	FBXL5 Regulates IRP2 Stability in Iron Homeostasis via an Oxygen-Responsive [2Fe2S] Cluster.	Oxygen	58-64	iron responsive element binding protein 2	Homo sapiens	16-20
32243827-0	2020	How Oxidation of a Unique Iron-Sulfur Cluster in FBXL5 Regulates IRP2 Levels and Promotes Regulation of Iron Metabolism Proteins.	Iron	104-108	iron responsive element binding protein 2	Homo sapiens	65-69
32126207-7	2020	Taken together, our studies have identified an iron-sulfur cluster within FBXL5, which promotes IRP2 polyubiquitination and degradation in response to both iron and oxygen concentrations.	Iron	47-51	iron responsive element binding protein 2	Homo sapiens	96-100
32126207-7	2020	Taken together, our studies have identified an iron-sulfur cluster within FBXL5, which promotes IRP2 polyubiquitination and degradation in response to both iron and oxygen concentrations.	Sulfur	52-58	iron responsive element binding protein 2	Homo sapiens	96-100
32126207-1	2020	Cellular iron homeostasis is dominated by FBXL5-mediated degradation of iron regulatory protein 2 (IRP2), which is dependent on both iron and oxygen.	Iron	9-13	iron responsive element binding protein 2	Homo sapiens	72-97
32126207-7	2020	Taken together, our studies have identified an iron-sulfur cluster within FBXL5, which promotes IRP2 polyubiquitination and degradation in response to both iron and oxygen concentrations.	Iron	156-160	iron responsive element binding protein 2	Homo sapiens	96-100
32126207-7	2020	Taken together, our studies have identified an iron-sulfur cluster within FBXL5, which promotes IRP2 polyubiquitination and degradation in response to both iron and oxygen concentrations.	Oxygen	165-171	iron responsive element binding protein 2	Homo sapiens	96-100
32243827-2	2020	(2020) discover that the C-terminal substrate-binding domain of FBXL5 contains a redox-sensitive [2Fe-2S] cluster that, upon oxidation, promotes FBXL5 binding to IRP2 to effect its oxygen-dependent degradation, unveiling a novel and previously unrecognized mechanism involved in regulation of cellular iron homeostasis.	Oxygen	181-187	iron responsive element binding protein 2	Homo sapiens	162-166
32243827-2	2020	(2020) discover that the C-terminal substrate-binding domain of FBXL5 contains a redox-sensitive [2Fe-2S] cluster that, upon oxidation, promotes FBXL5 binding to IRP2 to effect its oxygen-dependent degradation, unveiling a novel and previously unrecognized mechanism involved in regulation of cellular iron homeostasis.	Iron	302-306	iron responsive element binding protein 2	Homo sapiens	162-166
32126207-1	2020	Cellular iron homeostasis is dominated by FBXL5-mediated degradation of iron regulatory protein 2 (IRP2), which is dependent on both iron and oxygen.	Iron	9-13	iron responsive element binding protein 2	Homo sapiens	99-103
32126207-1	2020	Cellular iron homeostasis is dominated by FBXL5-mediated degradation of iron regulatory protein 2 (IRP2), which is dependent on both iron and oxygen.	Iron	72-76	iron responsive element binding protein 2	Homo sapiens	99-103
32126207-1	2020	Cellular iron homeostasis is dominated by FBXL5-mediated degradation of iron regulatory protein 2 (IRP2), which is dependent on both iron and oxygen.	Oxygen	142-148	iron responsive element binding protein 2	Homo sapiens	72-97
32126207-1	2020	Cellular iron homeostasis is dominated by FBXL5-mediated degradation of iron regulatory protein 2 (IRP2), which is dependent on both iron and oxygen.	Oxygen	142-148	iron responsive element binding protein 2	Homo sapiens	99-103
32126207-5	2020	Interestingly, IRP2 binding to FBXL5 hinges on the oxidized state of the [2Fe2S] cluster maintained by ambient oxygen, which could explain hypoxia-induced IRP2 stabilization.	Oxygen	111-117	iron responsive element binding protein 2	Homo sapiens	15-19
32126207-5	2020	Interestingly, IRP2 binding to FBXL5 hinges on the oxidized state of the [2Fe2S] cluster maintained by ambient oxygen, which could explain hypoxia-induced IRP2 stabilization.	Oxygen	111-117	iron responsive element binding protein 2	Homo sapiens	155-159
31907996-5	2020	We also showed that Iron Regulatory Protein 2 (IRP2) mediated iron-regulated Mdm2 expression.	Iron	62-66	iron responsive element binding protein 2	Homo sapiens	20-45
32057234-5	2020	As an example, the resultant IrP2-rGO displays better HER electrocatalytic performance and longer durability than the benchmark materials of commercial Pt/C under acidic, neutral and basic electrolytes.	Platinum	152-154	iron responsive element binding protein 2	Homo sapiens	29-33
32057234-5	2020	As an example, the resultant IrP2-rGO displays better HER electrocatalytic performance and longer durability than the benchmark materials of commercial Pt/C under acidic, neutral and basic electrolytes.	Carbon	155-156	iron responsive element binding protein 2	Homo sapiens	29-33
32057234-6	2020	To attain a current density of 10 milliamperes per square centimeter (mA cm-2), IrP2-rGO shows overpotentials of 8, 51 and 13 millivolts in 0.5 M dilute sulfuric acid, 1.0 M PBS and 1.0 M potassium hydroxide solutions, respectively.	Sulfuric Acids	153-166	iron responsive element binding protein 2	Homo sapiens	80-84
32057234-6	2020	To attain a current density of 10 milliamperes per square centimeter (mA cm-2), IrP2-rGO shows overpotentials of 8, 51 and 13 millivolts in 0.5 M dilute sulfuric acid, 1.0 M PBS and 1.0 M potassium hydroxide solutions, respectively.	potassium hydroxide	188-207	iron responsive element binding protein 2	Homo sapiens	80-84
32057234-7	2020	Additionally, IrP2-rGO also exhibits exceptional HOR performance in 0.1 M HClO4 medium.	1,2,3,4-tetrahydroisoquinoline	74-79	iron responsive element binding protein 2	Homo sapiens	14-18
31907996-5	2020	We also showed that Iron Regulatory Protein 2 (IRP2) mediated iron-regulated Mdm2 expression.	Iron	62-66	iron responsive element binding protein 2	Homo sapiens	47-51
31941883-0	2020	Irp2 regulates insulin production through iron-mediated Cdkal1-catalyzed tRNA modification.	Iron	42-46	iron responsive element binding protein 2	Homo sapiens	0-4
31941883-3	2020	Irp2 post-transcriptionally regulates the iron-uptake protein transferrin receptor 1 (TfR1) and the iron-storage protein ferritin, and dysregulation of these proteins due to Irp2 loss causes functional iron deficiency in beta cells.	Iron	42-46	iron responsive element binding protein 2	Homo sapiens	0-4
31941883-6	2020	Iron normalizes ms2t6A37 and proinsulin lysine incorporation, restoring insulin content and secretion in Irp2-/- beta cells.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	105-109
31941883-3	2020	Irp2 post-transcriptionally regulates the iron-uptake protein transferrin receptor 1 (TfR1) and the iron-storage protein ferritin, and dysregulation of these proteins due to Irp2 loss causes functional iron deficiency in beta cells.	Iron	100-104	iron responsive element binding protein 2	Homo sapiens	0-4
31076252-6	2019	When iron is limited, iron response element binding protein 2 (IRP2) binds to the IRE of ALAS2 mRNA and suppresses its translation.	Iron	5-9	iron responsive element binding protein 2	Homo sapiens	63-67
31076252-6	2019	When iron is limited, iron response element binding protein 2 (IRP2) binds to the IRE of ALAS2 mRNA and suppresses its translation.	Iron	22-26	iron responsive element binding protein 2	Homo sapiens	63-67
31092704-0	2019	Zinc induces iron uptake and DMT1 expression in Caco-2 cells via a PI3K/IRP2 dependent mechanism.	Iron	13-17	iron responsive element binding protein 2	Homo sapiens	72-76
31220756-2	2019	Heme regulatory motifs (HRMs) are conserved in the two IRP homologues IRP1 and IRP2 that specifically bind to two and three heme equivalents, respectively; however, only the heme binding to the iron-dependent degradation (IDD) domain of IRP2 causes heme-mediated oxidation, which does not occur in IRP1.	Heme	0-4	iron responsive element binding protein 2	Homo sapiens	79-83
31220756-2	2019	Heme regulatory motifs (HRMs) are conserved in the two IRP homologues IRP1 and IRP2 that specifically bind to two and three heme equivalents, respectively; however, only the heme binding to the iron-dependent degradation (IDD) domain of IRP2 causes heme-mediated oxidation, which does not occur in IRP1.	Heme	0-4	iron responsive element binding protein 2	Homo sapiens	237-241
31220756-2	2019	Heme regulatory motifs (HRMs) are conserved in the two IRP homologues IRP1 and IRP2 that specifically bind to two and three heme equivalents, respectively; however, only the heme binding to the iron-dependent degradation (IDD) domain of IRP2 causes heme-mediated oxidation, which does not occur in IRP1.	Heme	124-128	iron responsive element binding protein 2	Homo sapiens	79-83
31220756-2	2019	Heme regulatory motifs (HRMs) are conserved in the two IRP homologues IRP1 and IRP2 that specifically bind to two and three heme equivalents, respectively; however, only the heme binding to the iron-dependent degradation (IDD) domain of IRP2 causes heme-mediated oxidation, which does not occur in IRP1.	Heme	174-178	iron responsive element binding protein 2	Homo sapiens	79-83
31220756-2	2019	Heme regulatory motifs (HRMs) are conserved in the two IRP homologues IRP1 and IRP2 that specifically bind to two and three heme equivalents, respectively; however, only the heme binding to the iron-dependent degradation (IDD) domain of IRP2 causes heme-mediated oxidation, which does not occur in IRP1.	Heme	174-178	iron responsive element binding protein 2	Homo sapiens	237-241
31220756-2	2019	Heme regulatory motifs (HRMs) are conserved in the two IRP homologues IRP1 and IRP2 that specifically bind to two and three heme equivalents, respectively; however, only the heme binding to the iron-dependent degradation (IDD) domain of IRP2 causes heme-mediated oxidation, which does not occur in IRP1.	Iron	194-198	iron responsive element binding protein 2	Homo sapiens	79-83
31220756-2	2019	Heme regulatory motifs (HRMs) are conserved in the two IRP homologues IRP1 and IRP2 that specifically bind to two and three heme equivalents, respectively; however, only the heme binding to the iron-dependent degradation (IDD) domain of IRP2 causes heme-mediated oxidation, which does not occur in IRP1.	Iron	194-198	iron responsive element binding protein 2	Homo sapiens	237-241
31220756-2	2019	Heme regulatory motifs (HRMs) are conserved in the two IRP homologues IRP1 and IRP2 that specifically bind to two and three heme equivalents, respectively; however, only the heme binding to the iron-dependent degradation (IDD) domain of IRP2 causes heme-mediated oxidation, which does not occur in IRP1.	Heme	174-178	iron responsive element binding protein 2	Homo sapiens	79-83
31220756-2	2019	Heme regulatory motifs (HRMs) are conserved in the two IRP homologues IRP1 and IRP2 that specifically bind to two and three heme equivalents, respectively; however, only the heme binding to the iron-dependent degradation (IDD) domain of IRP2 causes heme-mediated oxidation, which does not occur in IRP1.	Heme	174-178	iron responsive element binding protein 2	Homo sapiens	237-241
31092704-8	2019	LY294002, a specific inhibitor of PI3K inhibited zinc-induced Akt phosphorylation, iron uptake, DMT1 and IRP2 expression.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	0-8	iron responsive element binding protein 2	Homo sapiens	105-109
31092704-12	2019	Based on these findings, we conclude that zinc-induced iron absorption involves elevation of DMT1 expression by stabilization of its mRNA, by a PI3K/IRP2-dependent mechanism.	Iron	55-59	iron responsive element binding protein 2	Homo sapiens	149-153
31002222-0	2019	Coupling a Low Loading of IrP2, PtP2, or Pd3P with Heteroatom-Doped Nanocarbon for Overall Water-Splitting Cells and Zinc-Air Batteries.	Water	91-96	iron responsive element binding protein 2	Homo sapiens	26-30
31002222-3	2019	Herein, for the first time, three novel electrocatalysts composed of noble metal phosphide (IrP2, Pd3P, or PtP2) nanoparticles with N,P-codoped nanocarbon were synthesized by the pyrolysis of mixtures of IrCl4, PdCl2, or PtCl4 with phytic acid under an ammonia atmosphere.	metal phosphide	75-90	iron responsive element binding protein 2	Homo sapiens	92-96
31002222-5	2019	Notably, the IrP2/NPC-, Pd3P/NPC-, and PtP2/NPC-based water-splitting cells required only 1.62, 1.65, and 1.68 V, respectively, to deliver the current density of 10 mA cm-2.	Water	54-59	iron responsive element binding protein 2	Homo sapiens	13-17
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Heme	204-208	iron responsive element binding protein 2	Homo sapiens	143-147
30915432-9	2019	These results confirm that IRP2 is essential for regulation of iron metabolism in humans, and reveal a previously unrecognized subclass of neurodegenerative disease.	Iron	63-67	iron responsive element binding protein 2	Homo sapiens	27-31
30218771-2	2019	In mammalian cells, iron regulatory protein 1 and 2 (IRP1 and IRP2) are the central regulators of cellular iron metabolism.	Iron	20-24	iron responsive element binding protein 2	Homo sapiens	62-66
30760976-0	2019	Oxidative Stress Regulated Iron Regulatory Protein IRP2 Through FBXL5-Mediated Ubiquitination-Proteasome Way in SH-SY5Y Cells.	Iron	27-31	iron responsive element binding protein 2	Homo sapiens	51-55
30760976-1	2019	Iron regulatory protein 2 (IRP2) plays a key role in the cellular iron homeostasis and could be regulated by a variety of factors, such as oxidative stress, hypoxia and iron, etc.	Iron	66-70	iron responsive element binding protein 2	Homo sapiens	0-25
30760976-1	2019	Iron regulatory protein 2 (IRP2) plays a key role in the cellular iron homeostasis and could be regulated by a variety of factors, such as oxidative stress, hypoxia and iron, etc.	Iron	66-70	iron responsive element binding protein 2	Homo sapiens	27-31
30760976-1	2019	Iron regulatory protein 2 (IRP2) plays a key role in the cellular iron homeostasis and could be regulated by a variety of factors, such as oxidative stress, hypoxia and iron, etc.	Iron	169-173	iron responsive element binding protein 2	Homo sapiens	0-25
30760976-1	2019	Iron regulatory protein 2 (IRP2) plays a key role in the cellular iron homeostasis and could be regulated by a variety of factors, such as oxidative stress, hypoxia and iron, etc.	Iron	169-173	iron responsive element binding protein 2	Homo sapiens	27-31
30760976-2	2019	IRP2 depletion results in neurodegenerative movement disorder with the loss of neurons and accumulations of iron.	Iron	108-112	iron responsive element binding protein 2	Homo sapiens	0-4
30760976-3	2019	Since oxidative stress extensively exists in several neurodegenerative diseases where iron accumulation also exists, it is important to clarify the mechanisms underlying the effects of oxidative stress on IRP2 expression and its consequence.	Iron	86-90	iron responsive element binding protein 2	Homo sapiens	205-209
30760976-7	2019	The protein levels of IRP2, but not for its mRNA levels, were observed decreased in both groups, which resulted in the lower TfR1 expression and decreased iron uptake in these cells.	Iron	155-159	iron responsive element binding protein 2	Homo sapiens	22-26
30760976-8	2019	Pretreatment with MG132, the decreased IRP2 levels caused by H2O2 treatment could be antagonized.	benzyloxycarbonylleucyl-leucyl-leucine aldehyde	18-23	iron responsive element binding protein 2	Homo sapiens	39-43
30760976-8	2019	Pretreatment with MG132, the decreased IRP2 levels caused by H2O2 treatment could be antagonized.	Hydrogen Peroxide	61-65	iron responsive element binding protein 2	Homo sapiens	39-43
30760976-10	2019	When knockdown the intracellular FBXL5 levels by si-FBXL5, the protein levels of IRP2 were found increased with H2O2 treatment.	Hydrogen Peroxide	112-116	iron responsive element binding protein 2	Homo sapiens	81-85
30449675-0	2019	Perturbation of Iron Metabolism by Cisplatin through Inhibition of Iron Regulatory Protein 2.	Iron	16-20	iron responsive element binding protein 2	Homo sapiens	67-92
30449675-0	2019	Perturbation of Iron Metabolism by Cisplatin through Inhibition of Iron Regulatory Protein 2.	Cisplatin	35-44	iron responsive element binding protein 2	Homo sapiens	67-92
30449675-3	2019	Cisplatin causes intracellular iron deficiency through direct inhibition of the master regulator of iron metabolism, iron regulatory protein 2 (IRP2) with marginal effects on IRP1.	Cisplatin	0-9	iron responsive element binding protein 2	Homo sapiens	117-142
30449675-3	2019	Cisplatin causes intracellular iron deficiency through direct inhibition of the master regulator of iron metabolism, iron regulatory protein 2 (IRP2) with marginal effects on IRP1.	Cisplatin	0-9	iron responsive element binding protein 2	Homo sapiens	144-148
30449675-3	2019	Cisplatin causes intracellular iron deficiency through direct inhibition of the master regulator of iron metabolism, iron regulatory protein 2 (IRP2) with marginal effects on IRP1.	Iron	31-35	iron responsive element binding protein 2	Homo sapiens	117-142
30449675-3	2019	Cisplatin causes intracellular iron deficiency through direct inhibition of the master regulator of iron metabolism, iron regulatory protein 2 (IRP2) with marginal effects on IRP1.	Iron	31-35	iron responsive element binding protein 2	Homo sapiens	144-148
30449675-4	2019	Cisplatin, but not carboplatin or transplatin, binds human IRP2 at Cys512 and Cys516 and impairs IRP2 binding to iron-responsive elements of ferritin and transferrin receptor-1 (TfR1) mRNAs.	Cisplatin	0-9	iron responsive element binding protein 2	Homo sapiens	59-63
30449675-4	2019	Cisplatin, but not carboplatin or transplatin, binds human IRP2 at Cys512 and Cys516 and impairs IRP2 binding to iron-responsive elements of ferritin and transferrin receptor-1 (TfR1) mRNAs.	Cisplatin	0-9	iron responsive element binding protein 2	Homo sapiens	97-101
30449675-4	2019	Cisplatin, but not carboplatin or transplatin, binds human IRP2 at Cys512 and Cys516 and impairs IRP2 binding to iron-responsive elements of ferritin and transferrin receptor-1 (TfR1) mRNAs.	Iron	113-117	iron responsive element binding protein 2	Homo sapiens	97-101
30449675-5	2019	IRP2 inhibition by cisplatin caused ferritin upregulation and TfR1 downregulation leading to sustained intracellular iron deficiency.	Cisplatin	19-28	iron responsive element binding protein 2	Homo sapiens	0-4
30449675-6	2019	Cys512/516Ala mutant IRP2 made cells more resistant to cisplatin.	Cisplatin	55-64	iron responsive element binding protein 2	Homo sapiens	21-25
29449016-2	2018	Two homologs of IRPs (IRP1 and IRP2) have a typical heme regulatory motif (HRM), a consensus sequence found in "heme-regulated proteins".	Heme	52-56	iron responsive element binding protein 2	Homo sapiens	31-35
29449016-3	2018	However, specific heme binding to HRM has been reported only for IRP2, which is essential for oxidative modification and loss of binding to target mRNAs.	Heme	18-22	iron responsive element binding protein 2	Homo sapiens	65-69
29449016-4	2018	In this paper, we confirmed that IRP1 also specifically binds two molar equivalents of heme, and found that the absorption and resonance Raman spectra of heme-bound IRP1 were quite similar to those of heme-bound IRP2.	Heme	87-91	iron responsive element binding protein 2	Homo sapiens	212-216
29449016-4	2018	In this paper, we confirmed that IRP1 also specifically binds two molar equivalents of heme, and found that the absorption and resonance Raman spectra of heme-bound IRP1 were quite similar to those of heme-bound IRP2.	Heme	154-158	iron responsive element binding protein 2	Homo sapiens	212-216
29449016-4	2018	In this paper, we confirmed that IRP1 also specifically binds two molar equivalents of heme, and found that the absorption and resonance Raman spectra of heme-bound IRP1 were quite similar to those of heme-bound IRP2.	Heme	154-158	iron responsive element binding protein 2	Homo sapiens	212-216
29449016-6	2018	Pulse radiolysis experiments, however, clearly revealed an axial ligand exchange from Cys to His immediately after the reduction of the heme iron to form a 5-coordinate His-ligated heme in heme-bound IRP2, whereas the 5-coordinate His-ligated heme was not observed after the reduction of heme-bound IRP1.	Cysteine	86-89	iron responsive element binding protein 2	Homo sapiens	200-204
29449016-6	2018	Pulse radiolysis experiments, however, clearly revealed an axial ligand exchange from Cys to His immediately after the reduction of the heme iron to form a 5-coordinate His-ligated heme in heme-bound IRP2, whereas the 5-coordinate His-ligated heme was not observed after the reduction of heme-bound IRP1.	Histidine	93-96	iron responsive element binding protein 2	Homo sapiens	200-204
29449016-6	2018	Pulse radiolysis experiments, however, clearly revealed an axial ligand exchange from Cys to His immediately after the reduction of the heme iron to form a 5-coordinate His-ligated heme in heme-bound IRP2, whereas the 5-coordinate His-ligated heme was not observed after the reduction of heme-bound IRP1.	Heme	136-140	iron responsive element binding protein 2	Homo sapiens	200-204
29449016-6	2018	Pulse radiolysis experiments, however, clearly revealed an axial ligand exchange from Cys to His immediately after the reduction of the heme iron to form a 5-coordinate His-ligated heme in heme-bound IRP2, whereas the 5-coordinate His-ligated heme was not observed after the reduction of heme-bound IRP1.	Iron	141-145	iron responsive element binding protein 2	Homo sapiens	200-204
29449016-6	2018	Pulse radiolysis experiments, however, clearly revealed an axial ligand exchange from Cys to His immediately after the reduction of the heme iron to form a 5-coordinate His-ligated heme in heme-bound IRP2, whereas the 5-coordinate His-ligated heme was not observed after the reduction of heme-bound IRP1.	Histidine	169-172	iron responsive element binding protein 2	Homo sapiens	200-204
29449016-6	2018	Pulse radiolysis experiments, however, clearly revealed an axial ligand exchange from Cys to His immediately after the reduction of the heme iron to form a 5-coordinate His-ligated heme in heme-bound IRP2, whereas the 5-coordinate His-ligated heme was not observed after the reduction of heme-bound IRP1.	Heme	181-185	iron responsive element binding protein 2	Homo sapiens	200-204
29449016-6	2018	Pulse radiolysis experiments, however, clearly revealed an axial ligand exchange from Cys to His immediately after the reduction of the heme iron to form a 5-coordinate His-ligated heme in heme-bound IRP2, whereas the 5-coordinate His-ligated heme was not observed after the reduction of heme-bound IRP1.	Heme	181-185	iron responsive element binding protein 2	Homo sapiens	200-204
29449016-6	2018	Pulse radiolysis experiments, however, clearly revealed an axial ligand exchange from Cys to His immediately after the reduction of the heme iron to form a 5-coordinate His-ligated heme in heme-bound IRP2, whereas the 5-coordinate His-ligated heme was not observed after the reduction of heme-bound IRP1.	Histidine	169-172	iron responsive element binding protein 2	Homo sapiens	200-204
29449016-6	2018	Pulse radiolysis experiments, however, clearly revealed an axial ligand exchange from Cys to His immediately after the reduction of the heme iron to form a 5-coordinate His-ligated heme in heme-bound IRP2, whereas the 5-coordinate His-ligated heme was not observed after the reduction of heme-bound IRP1.	Heme	181-185	iron responsive element binding protein 2	Homo sapiens	200-204
29449016-6	2018	Pulse radiolysis experiments, however, clearly revealed an axial ligand exchange from Cys to His immediately after the reduction of the heme iron to form a 5-coordinate His-ligated heme in heme-bound IRP2, whereas the 5-coordinate His-ligated heme was not observed after the reduction of heme-bound IRP1.	Heme	181-185	iron responsive element binding protein 2	Homo sapiens	200-204
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Heme	64-68	iron responsive element binding protein 2	Homo sapiens	75-79
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Heme	64-68	iron responsive element binding protein 2	Homo sapiens	143-147
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Heme	64-68	iron responsive element binding protein 2	Homo sapiens	143-147
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Heme	64-68	iron responsive element binding protein 2	Homo sapiens	143-147
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Histidine	192-195	iron responsive element binding protein 2	Homo sapiens	75-79
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Histidine	192-195	iron responsive element binding protein 2	Homo sapiens	143-147
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Histidine	192-195	iron responsive element binding protein 2	Homo sapiens	143-147
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Histidine	192-195	iron responsive element binding protein 2	Homo sapiens	143-147
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Heme	204-208	iron responsive element binding protein 2	Homo sapiens	75-79
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Heme	204-208	iron responsive element binding protein 2	Homo sapiens	143-147
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Heme	204-208	iron responsive element binding protein 2	Homo sapiens	143-147
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Heme	204-208	iron responsive element binding protein 2	Homo sapiens	143-147
30449675-8	2019	Collectively, cisplatin is an inhibitor of IRP2 that induces intracellular iron deficiency.	Cisplatin	14-23	iron responsive element binding protein 2	Homo sapiens	43-47
30311259-8	2019	Interestingly, we also observed reduced expression of iron regulatory protein 2 along with impaired activity of mitochondrial aconitase and reduced mitochondrial superoxide formation in restless legs syndrome subjects.	Superoxides	162-172	iron responsive element binding protein 2	Homo sapiens	54-79
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Heme	204-208	iron responsive element binding protein 2	Homo sapiens	75-79
29572489-3	2018	Irp1 or Irp2-null mutation is known to reduce the cellular iron level by decreasing transferrin receptor 1 and increasing ferritin.	Iron	59-63	iron responsive element binding protein 2	Homo sapiens	8-12
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Heme	204-208	iron responsive element binding protein 2	Homo sapiens	143-147
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Heme	204-208	iron responsive element binding protein 2	Homo sapiens	143-147
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Heme	204-208	iron responsive element binding protein 2	Homo sapiens	143-147
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Heme	204-208	iron responsive element binding protein 2	Homo sapiens	75-79
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Heme	204-208	iron responsive element binding protein 2	Homo sapiens	143-147
29449016-7	2018	Considering that the oxidative modification is only observed in heme-bound IRP2, but not IRP1, probably owing to the structural flexibility of IRP2, we propose that the transient 5-coordinate His-ligated heme is a prerequisite for oxidative modification of heme-bound IRP2, which functionally differentiates heme binding of IRP2 from that of IRP1.	Heme	204-208	iron responsive element binding protein 2	Homo sapiens	143-147
29652073-1	2018	In animal cells the specific translational control of proteins contributing to iron homeostasis is mediated by the interaction between the Iron Regulatory Proteins (IRP1 and IRP2) and the Iron Responsive Elements (IRE) located in the untranslated regions (UTR) of regulated messengers, such as those encoding ferritin or the transferrin receptor.	Iron	79-83	iron responsive element binding protein 2	Homo sapiens	174-178
29652073-1	2018	In animal cells the specific translational control of proteins contributing to iron homeostasis is mediated by the interaction between the Iron Regulatory Proteins (IRP1 and IRP2) and the Iron Responsive Elements (IRE) located in the untranslated regions (UTR) of regulated messengers, such as those encoding ferritin or the transferrin receptor.	Iron	139-143	iron responsive element binding protein 2	Homo sapiens	174-178
29652073-1	2018	In animal cells the specific translational control of proteins contributing to iron homeostasis is mediated by the interaction between the Iron Regulatory Proteins (IRP1 and IRP2) and the Iron Responsive Elements (IRE) located in the untranslated regions (UTR) of regulated messengers, such as those encoding ferritin or the transferrin receptor.	Iron	188-192	iron responsive element binding protein 2	Homo sapiens	174-178
29572489-6	2018	Overexpression of human ISCU and frataxin in Irp1 or Irp2-null cells was able to rescue the defects in iron-sulfur cluster biogenesis and mitochondrial quality.	Sulfur	108-114	iron responsive element binding protein 2	Homo sapiens	53-57
29572489-4	2018	Here, we report that Irp1 or Irp2-null mutation also causes downregulation of frataxin and IscU, two of the core components in the iron-sulfur cluster biogenesis machinery.	Iron	131-135	iron responsive element binding protein 2	Homo sapiens	29-33
29572489-4	2018	Here, we report that Irp1 or Irp2-null mutation also causes downregulation of frataxin and IscU, two of the core components in the iron-sulfur cluster biogenesis machinery.	Sulfur	136-142	iron responsive element binding protein 2	Homo sapiens	29-33
29572489-6	2018	Overexpression of human ISCU and frataxin in Irp1 or Irp2-null cells was able to rescue the defects in iron-sulfur cluster biogenesis and mitochondrial quality.	Iron	103-107	iron responsive element binding protein 2	Homo sapiens	53-57
29070551-7	2017	Cellular iron concentrations are modulated by the iron regulatory proteins (IRPs) IRP1 and IRP2.	Iron	9-13	iron responsive element binding protein 2	Homo sapiens	91-95
28768766-3	2017	Inactivation of IRP1 RNA binding by iron primarily involves insertion of a [4Fe-4S] cluster by the cytosolic iron-sulfur cluster assembly (CIA) system, converting it into cytosolic aconitase (c-acon), but can also involve iron-mediated degradation of IRP1 by the E3 ligase FBXL5 that also targets IRP2.	Iron	36-40	iron responsive element binding protein 2	Homo sapiens	297-301
29061112-2	2017	Iron homeostasis is maintained by iron regulatory proteins (IRP1 and IRP2) and the iron-responsive element (IRE) signaling pathway.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	69-73
28939752-1	2017	The RNA-binding iron regulatory proteins IRP1 and IRP2 are inactivated by either Fe-S cluster insertion or protein degradation mediated by the E3 ligase component FBXL5.	Iron	16-20	iron responsive element binding protein 2	Homo sapiens	50-54
28939752-1	2017	The RNA-binding iron regulatory proteins IRP1 and IRP2 are inactivated by either Fe-S cluster insertion or protein degradation mediated by the E3 ligase component FBXL5.	Iron	81-83	iron responsive element binding protein 2	Homo sapiens	50-54
29187867-3	2017	It has been suggested, that lower oxygen tension, may modulate the IREB2 and FAM13A activity.	Oxygen	34-40	iron responsive element binding protein 2	Homo sapiens	67-72
28775066-3	2017	At the cellular level, iron homeostasis is dependent on the iron regulatory proteins IRP1/IRP2.	Iron	23-27	iron responsive element binding protein 2	Homo sapiens	90-94
28775066-3	2017	At the cellular level, iron homeostasis is dependent on the iron regulatory proteins IRP1/IRP2.	Iron	60-64	iron responsive element binding protein 2	Homo sapiens	90-94
28768766-3	2017	Inactivation of IRP1 RNA binding by iron primarily involves insertion of a [4Fe-4S] cluster by the cytosolic iron-sulfur cluster assembly (CIA) system, converting it into cytosolic aconitase (c-acon), but can also involve iron-mediated degradation of IRP1 by the E3 ligase FBXL5 that also targets IRP2.	Iron	109-113	iron responsive element binding protein 2	Homo sapiens	297-301
28768766-3	2017	Inactivation of IRP1 RNA binding by iron primarily involves insertion of a [4Fe-4S] cluster by the cytosolic iron-sulfur cluster assembly (CIA) system, converting it into cytosolic aconitase (c-acon), but can also involve iron-mediated degradation of IRP1 by the E3 ligase FBXL5 that also targets IRP2.	Iron	109-113	iron responsive element binding protein 2	Homo sapiens	297-301
28387022-4	2017	Physiological iron balance is tightly controlled at the cellular and systemic level by iron regulatory proteins (IRP1, IRP2) and the iron regulatory hormone hepcidin, respectively.	Iron	14-18	iron responsive element binding protein 2	Homo sapiens	119-123
29137259-3	2017	Here we report that prostate cancer cells overexpress IRP2 and that overexpression of IRP2 drives the altered iron phenotype of prostate cancer cells.	Iron	110-114	iron responsive element binding protein 2	Homo sapiens	86-90
29137259-4	2017	IRP2 knockdown in prostate cancer cell lines reduces intracellular iron and causes cell cycle inhibition and apoptosis.	Iron	67-71	iron responsive element binding protein 2	Homo sapiens	0-4
29137259-8	2017	These results demonstrate that upregulation of IRP2 in prostate cancer cells co-opts normal iron regulatory mechanisms to facilitate iron retention and drive enhanced tumor growth.	Iron	92-96	iron responsive element binding protein 2	Homo sapiens	47-51
29137259-8	2017	These results demonstrate that upregulation of IRP2 in prostate cancer cells co-opts normal iron regulatory mechanisms to facilitate iron retention and drive enhanced tumor growth.	Iron	133-137	iron responsive element binding protein 2	Homo sapiens	47-51
28638917-0	2017	Influence of sodium nitroprusside on expressions of FBXL5 and IRP2 in SH-SY5Y cells.	Nitroprusside	13-33	iron responsive element binding protein 2	Homo sapiens	62-66
28638917-3	2017	Iron regulatory proteins (IRPs) including IRP1 and IRP2 are cytosolic proteins that play important roles in maintaining cellular iron homeostasis.	Iron	129-133	iron responsive element binding protein 2	Homo sapiens	51-55
28638917-4	2017	F-box and leucine-rich repeat protein 5 (FBXL5) is involved in the regulation of iron metabolism by degrading IRP2 through the ubiquitin-proteasome system.	Iron	81-85	iron responsive element binding protein 2	Homo sapiens	110-114
28638917-6	2017	Therefore, in the present study, we aim to determine whether sodium nitroprusside (SNP), a NO donor, regulates FBXL5 and IRP2 expression in cultured SH-SY5Y cells.	Nitroprusside	61-81	iron responsive element binding protein 2	Homo sapiens	121-125
28450115-9	2017	A cell-based study using Ishikawa cells revealed that IRP2 expression was decreased by an overload of Fe(II) under normoxia but remained unchanged under hypoxia even in the presence of excess Fe(II).	ammonium ferrous sulfate	102-108	iron responsive element binding protein 2	Homo sapiens	54-58
28450115-9	2017	A cell-based study using Ishikawa cells revealed that IRP2 expression was decreased by an overload of Fe(II) under normoxia but remained unchanged under hypoxia even in the presence of excess Fe(II).	ammonium ferrous sulfate	192-198	iron responsive element binding protein 2	Homo sapiens	54-58
28450115-10	2017	An increase in the expression of IRP2 caused upregulation of intracellular iron as a result of the response to iron deficiency, whereas the protein was degraded under iron-rich conditions.	Iron	75-79	iron responsive element binding protein 2	Homo sapiens	33-37
28450115-10	2017	An increase in the expression of IRP2 caused upregulation of intracellular iron as a result of the response to iron deficiency, whereas the protein was degraded under iron-rich conditions.	Iron	111-115	iron responsive element binding protein 2	Homo sapiens	33-37
28450115-10	2017	An increase in the expression of IRP2 caused upregulation of intracellular iron as a result of the response to iron deficiency, whereas the protein was degraded under iron-rich conditions.	Iron	111-115	iron responsive element binding protein 2	Homo sapiens	33-37
28450115-11	2017	We found that iron-rich regions existed in ovarian endometrial cysts concomitantly with the high level of IRP2 expression, which should generally be decomposed upon an overload of iron.	Iron	14-18	iron responsive element binding protein 2	Homo sapiens	106-110
28450115-12	2017	We revealed that an insufficient level of oxygen in the cysts is the main factor for the unusual stabilization of IRP2 against iron-mediated degradation, which provides aberrant uptake of iron in ovarian endometrial stromal cells and can potentially lead to carcinogenesis.	Oxygen	42-48	iron responsive element binding protein 2	Homo sapiens	114-118
28450115-12	2017	We revealed that an insufficient level of oxygen in the cysts is the main factor for the unusual stabilization of IRP2 against iron-mediated degradation, which provides aberrant uptake of iron in ovarian endometrial stromal cells and can potentially lead to carcinogenesis.	Iron	127-131	iron responsive element binding protein 2	Homo sapiens	114-118
28450115-12	2017	We revealed that an insufficient level of oxygen in the cysts is the main factor for the unusual stabilization of IRP2 against iron-mediated degradation, which provides aberrant uptake of iron in ovarian endometrial stromal cells and can potentially lead to carcinogenesis.	Iron	188-192	iron responsive element binding protein 2	Homo sapiens	114-118
28281325-2	2017	To date, however, the expression of iron regulatory protein-2 (IRP2), which is known to regulate several iron metabolism proteins, has not been assessed in colorectal cancer.	Iron	36-40	iron responsive element binding protein 2	Homo sapiens	63-67
28281325-5	2017	The impact of suppressing IRP2 on cellular iron metabolism was also determined by using siRNA and by using the MEK inhibitor trametinib.	Iron	43-47	iron responsive element binding protein 2	Homo sapiens	26-30
28281325-8	2017	The MEK inhibitor trametinib suppressed IRP2 and this was associated with a suppression in TfR1 and the labile iron pool (LIP).	trametinib	18-28	iron responsive element binding protein 2	Homo sapiens	40-44
28289076-5	2017	Specifically, fumarate covalently modifies cysteine residues on iron regulatory protein 2 (IRP2), rendering it unable to repress ferritin mRNA translation.	Fumarates	14-22	iron responsive element binding protein 2	Homo sapiens	64-89
28289076-5	2017	Specifically, fumarate covalently modifies cysteine residues on iron regulatory protein 2 (IRP2), rendering it unable to repress ferritin mRNA translation.	Fumarates	14-22	iron responsive element binding protein 2	Homo sapiens	91-95
28289076-5	2017	Specifically, fumarate covalently modifies cysteine residues on iron regulatory protein 2 (IRP2), rendering it unable to repress ferritin mRNA translation.	Cysteine	43-51	iron responsive element binding protein 2	Homo sapiens	64-89
28289076-5	2017	Specifically, fumarate covalently modifies cysteine residues on iron regulatory protein 2 (IRP2), rendering it unable to repress ferritin mRNA translation.	Cysteine	43-51	iron responsive element binding protein 2	Homo sapiens	91-95
28404645-1	2017	IREB2 is a gene that produces iron regulatory protein 2 (IRP2), which is critical to intracellular iron homeostasis and which relates to the rate of cellular proliferation.	Iron	30-34	iron responsive element binding protein 2	Homo sapiens	0-5
28453699-13	2017	Conclusion: The miRNA binding site SNP rs1062980 in iron regulatory pathway, which may alter the expression of IREB2 potentially through modulating the binding of miR-29a, together with dietary iron intake may modify risk of LC both individually and jointly.	Iron	52-56	iron responsive element binding protein 2	Homo sapiens	111-116
28453699-13	2017	Conclusion: The miRNA binding site SNP rs1062980 in iron regulatory pathway, which may alter the expression of IREB2 potentially through modulating the binding of miR-29a, together with dietary iron intake may modify risk of LC both individually and jointly.	Iron	194-198	iron responsive element binding protein 2	Homo sapiens	111-116
28404645-1	2017	IREB2 is a gene that produces iron regulatory protein 2 (IRP2), which is critical to intracellular iron homeostasis and which relates to the rate of cellular proliferation.	Iron	30-34	iron responsive element binding protein 2	Homo sapiens	57-61
28404645-6	2017	A cohort of operated NSCLC patients was studied for markers of systemic iron status, tumour IRP2 staining and survival.Iron loading caused cell proliferation in cancer cell lines, which were less able to regulate IREB2 expression than PBECs.	Iron	119-123	iron responsive element binding protein 2	Homo sapiens	92-96
28404645-6	2017	A cohort of operated NSCLC patients was studied for markers of systemic iron status, tumour IRP2 staining and survival.Iron loading caused cell proliferation in cancer cell lines, which were less able to regulate IREB2 expression than PBECs.	Iron	119-123	iron responsive element binding protein 2	Homo sapiens	213-218
28404645-8	2017	IRP2-positive tumours were larger (p=0.045) and higher percentage staining related to poorer survival (p=0.079).Loss of iron regulation represents a poor prognostic marker in lung cancer.	Iron	120-124	iron responsive element binding protein 2	Homo sapiens	0-4
27794191-6	2017	This increased intracellular iron complexed to quercetin does not associate with the labile iron pool and cells behave as though they are iron deficient (increased transferrin receptor-1 and iron regulatory protein-2 expression and low ferritin expression).	Quercetin	47-56	iron responsive element binding protein 2	Homo sapiens	191-216
27794191-6	2017	This increased intracellular iron complexed to quercetin does not associate with the labile iron pool and cells behave as though they are iron deficient (increased transferrin receptor-1 and iron regulatory protein-2 expression and low ferritin expression).	Iron	29-33	iron responsive element binding protein 2	Homo sapiens	191-216
28131773-1	2017	FBXL5 is a subunit of the SCFFBXL5 ubiquitin ligase complex that targets the proteasomal degradation of iron regulatory protein IRP2, which is an important regulator in iron metabolism.	Iron	104-108	iron responsive element binding protein 2	Homo sapiens	128-132
26629341-3	2015	IREB2 is a gene that produces iron regulatory protein 2 (IRP2), which has a key role in iron homeostasis.	Iron	30-34	iron responsive element binding protein 2	Homo sapiens	0-5
28166223-4	2017	The first is that overexpression of iron regulatory protein 2 (IRP2) recapitulates many aspects of the alterations in free iron and iron-related proteins in cancer cells without affecting the oxidative stress response or the oncogenic pathways included in the model.	Iron	36-40	iron responsive element binding protein 2	Homo sapiens	63-67
28166223-4	2017	The first is that overexpression of iron regulatory protein 2 (IRP2) recapitulates many aspects of the alterations in free iron and iron-related proteins in cancer cells without affecting the oxidative stress response or the oncogenic pathways included in the model.	Iron	123-127	iron responsive element binding protein 2	Homo sapiens	36-61
28166223-4	2017	The first is that overexpression of iron regulatory protein 2 (IRP2) recapitulates many aspects of the alterations in free iron and iron-related proteins in cancer cells without affecting the oxidative stress response or the oncogenic pathways included in the model.	Iron	123-127	iron responsive element binding protein 2	Homo sapiens	63-67
28031527-5	2017	Importantly, we have identified specific gene signature related to iron metabolism consisting of genes regulating iron uptake, mitochondrial FeS cluster biogenesis and hypoxic response (ABCB10, ACO1, CYBRD1, EPAS1, GLRX5, HEPH, HFE, IREB2, QSOX1 and TFRC).	Iron	67-71	iron responsive element binding protein 2	Homo sapiens	233-238
26629341-3	2015	IREB2 is a gene that produces iron regulatory protein 2 (IRP2), which has a key role in iron homeostasis.	Iron	30-34	iron responsive element binding protein 2	Homo sapiens	57-61
26629341-4	2015	This review addresses pathways involved in iron metabolism, particularly focusing on the role of IREB2.	Iron	43-47	iron responsive element binding protein 2	Homo sapiens	97-102
23505071-8	2013	In agreement with this possibility, we found that pharmacological inhibitors (ferrostatin-1) and genetic procedures (RNA interference against IREB-2) previously reported to modulate ferroptosis, readily block the cytotoxic effects of sorafenib in HCC cells.	Sorafenib	234-243	iron responsive element binding protein 2	Homo sapiens	142-148
24778179-2	2014	IRP2 plays a central role in the maintenance of cellular iron homeostasis in mammals through posttranscriptional regulation of proteins that contribute to control of the intracellular iron concentration.	Iron	57-61	iron responsive element binding protein 2	Homo sapiens	0-4
24778179-2	2014	IRP2 plays a central role in the maintenance of cellular iron homeostasis in mammals through posttranscriptional regulation of proteins that contribute to control of the intracellular iron concentration.	Iron	184-188	iron responsive element binding protein 2	Homo sapiens	0-4
25101718-11	2015	Both meta-analyses revealed a genome-wide significant locus on chromosome 15q25.1 in IREB2 (COPD with versus without PAE, rs7181486; odds ratio [OR] = 1.32; P = 2.10 x 10(-8); versus smoking control subjects, rs2009746; OR = 1.42; P = 1.32 x 10(-9)).	phenyl-2-aminoethyl sulfide	117-120	iron responsive element binding protein 2	Homo sapiens	85-90
25117307-9	2014	IRP2 can regulate the expression of TfR and Fn by changing its own protein expression and thereby regulate iron metabolism.	Iron	107-111	iron responsive element binding protein 2	Homo sapiens	0-4
24285726-3	2014	Here, we demonstrate that iron regulatory protein 2 (IRP2) plays a key role in iron accumulation in breast cancer.	Iron	26-30	iron responsive element binding protein 2	Homo sapiens	53-57
24285726-5	2014	Knockdown of IRP2 in triple-negative MDA-MB-231 human breast cancer cells increases ferritin H expression and decreases TfR1 expression, resulting in a decrease in the labile iron pool.	Iron	175-179	iron responsive element binding protein 2	Homo sapiens	13-17
24285726-9	2014	These results suggest that dysregulation of IRP2 is an early nodal point underlying altered iron metabolism in breast cancer and may contribute to poor outcome of some patients with breast cancer.	Iron	92-96	iron responsive element binding protein 2	Homo sapiens	44-48
24394537-0	2014	Iron transport through ferroportin is induced by intracellular ascorbate and involves IRP2 and HIF2alpha.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	86-90
24394537-7	2014	Ascorbate-induced up-regulation of cellular ferroportin levels (no added iron) was associated with increased levels of the iron regulatory protein IRP2 (230%, p=0.0009), and the hypoxia-inducible factor HIF2alpha (69%, p=0.03).	Ascorbic Acid	0-9	iron responsive element binding protein 2	Homo sapiens	147-151
24394537-7	2014	Ascorbate-induced up-regulation of cellular ferroportin levels (no added iron) was associated with increased levels of the iron regulatory protein IRP2 (230%, p=0.0009), and the hypoxia-inducible factor HIF2alpha (69%, p=0.03).	Iron	123-127	iron responsive element binding protein 2	Homo sapiens	147-151
24394537-8	2014	Thus, iron transport across the basal border via ferroportin is influenced by the intracellular status of ascorbate and IRP2 and HIF2alpha are involved.	Iron	6-10	iron responsive element binding protein 2	Homo sapiens	120-124
23520538-2	2013	Cellular iron metabolism is coordinately controlled by the Iron Regulatory Proteins (IRP1 and IRP2), whose activity is affected by 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), a current and persistent environmental contaminant.	Iron	9-13	iron responsive element binding protein 2	Homo sapiens	94-98
23891004-6	2013	Surprisingly, a second layer of iron regulation involves the stabilization of IRP2 by CIA2A binding or upon depletion of CIA2B or MMS19, even though IRP2 lacks an Fe/S cluster.	Iron	32-36	iron responsive element binding protein 2	Homo sapiens	78-82
23891004-6	2013	Surprisingly, a second layer of iron regulation involves the stabilization of IRP2 by CIA2A binding or upon depletion of CIA2B or MMS19, even though IRP2 lacks an Fe/S cluster.	Iron	32-36	iron responsive element binding protein 2	Homo sapiens	149-153
23891004-7	2013	In summary, CIA2B-CIA1-MMS19 and CIA2A-CIA1 assist different branches of Fe/S protein assembly and intimately link this process to cellular iron regulation via IRP1 Fe/S cluster maturation and IRP2 stabilization.	Iron	140-144	iron responsive element binding protein 2	Homo sapiens	193-197
23520538-2	2013	Cellular iron metabolism is coordinately controlled by the Iron Regulatory Proteins (IRP1 and IRP2), whose activity is affected by 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), a current and persistent environmental contaminant.	Polychlorinated Dibenzodioxins	168-172	iron responsive element binding protein 2	Homo sapiens	94-98
23520538-2	2013	Cellular iron metabolism is coordinately controlled by the Iron Regulatory Proteins (IRP1 and IRP2), whose activity is affected by 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), a current and persistent environmental contaminant.	Iron	59-63	iron responsive element binding protein 2	Homo sapiens	94-98
23520538-2	2013	Cellular iron metabolism is coordinately controlled by the Iron Regulatory Proteins (IRP1 and IRP2), whose activity is affected by 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), a current and persistent environmental contaminant.	Polychlorinated Dibenzodioxins	131-166	iron responsive element binding protein 2	Homo sapiens	94-98
22609301-10	2012	In mammalian cells, the iron regulatory proteins IRP1, an Fe/S protein, and IRP2 act in a post-transcriptional fashion to adjust the cellular needs for iron.	Iron	24-28	iron responsive element binding protein 2	Homo sapiens	76-80
22609301-10	2012	In mammalian cells, the iron regulatory proteins IRP1, an Fe/S protein, and IRP2 act in a post-transcriptional fashion to adjust the cellular needs for iron.	Iron	152-156	iron responsive element binding protein 2	Homo sapiens	76-80
22610083-1	2012	Cellular iron homeostasis is maintained by iron regulatory proteins 1 and 2 (IRP1 and IRP2).	Iron	9-13	iron responsive element binding protein 2	Homo sapiens	86-90
22610083-1	2012	Cellular iron homeostasis is maintained by iron regulatory proteins 1 and 2 (IRP1 and IRP2).	Iron	43-47	iron responsive element binding protein 2	Homo sapiens	86-90
22093897-1	2011	OBJECTIVE: To discuss the regulating mechanism of iron regulatory protein-2 (IRP2) in the iron metabolism of lung cancer.	Iron	50-54	iron responsive element binding protein 2	Homo sapiens	77-81
22648410-2	2012	An E3 ubiquitin ligase complex containing FBXL5 targets IRP2 for proteasomal degradation under iron- and oxygen-replete conditions, whereas FBXL5 itself is degraded when iron and oxygen availability decreases.	Iron	95-99	iron responsive element binding protein 2	Homo sapiens	56-60
22648410-2	2012	An E3 ubiquitin ligase complex containing FBXL5 targets IRP2 for proteasomal degradation under iron- and oxygen-replete conditions, whereas FBXL5 itself is degraded when iron and oxygen availability decreases.	Oxygen	105-111	iron responsive element binding protein 2	Homo sapiens	56-60
22648410-2	2012	An E3 ubiquitin ligase complex containing FBXL5 targets IRP2 for proteasomal degradation under iron- and oxygen-replete conditions, whereas FBXL5 itself is degraded when iron and oxygen availability decreases.	Iron	170-174	iron responsive element binding protein 2	Homo sapiens	56-60
22648410-2	2012	An E3 ubiquitin ligase complex containing FBXL5 targets IRP2 for proteasomal degradation under iron- and oxygen-replete conditions, whereas FBXL5 itself is degraded when iron and oxygen availability decreases.	Oxygen	179-185	iron responsive element binding protein 2	Homo sapiens	56-60
22658601-6	2012	We further show that BTBD9 regulates brain dopamine levels in flies and controls iron homeostasis through the iron regulatory protein-2 in human cell lines.	Iron	81-85	iron responsive element binding protein 2	Homo sapiens	110-135
21907923-2	2011	Reduced AMPK levels lead to diminished expression of the DMT1 iron transporter, and the resulting cytosolic iron deficiency activates the iron regulatory proteins, IRP1 and IRP2, and increases expression of the hypoxia inducible factor HIF-1alpha, but not HIF-2alpha.	Iron	108-112	iron responsive element binding protein 2	Homo sapiens	173-177
22093897-11	2011	CONCLUSION: IRP2 may affect the expressions of TfR and Fn in lung adenocarcinoma A549 cells by changing the amount of protein and regulating the iron metabolism.	Iron	145-149	iron responsive element binding protein 2	Homo sapiens	12-16
21188590-7	2011	A sorbitol positive, streptomycin resistant STEC strain was isolated from the drinking water, and belonged to the serotype O100:H(-), produced Stx2 toxin (titre 1:8 by reversed-passive latex agglutination method), and carried the genes stx(2e), estIa and irp2.	Sorbitol	2-10	iron responsive element binding protein 2	Homo sapiens	255-259
21333694-1	2011	Cellular iron metabolism is essentially controlled by the binding of cytosolic iron regulatory proteins (IRP1 or IRP2) to iron-responsive elements (IREs) located on mRNAs coding for proteins involved in iron acquisition, utilization and storage.	Iron	79-83	iron responsive element binding protein 2	Homo sapiens	113-117
21333694-1	2011	Cellular iron metabolism is essentially controlled by the binding of cytosolic iron regulatory proteins (IRP1 or IRP2) to iron-responsive elements (IREs) located on mRNAs coding for proteins involved in iron acquisition, utilization and storage.	Iron	79-83	iron responsive element binding protein 2	Homo sapiens	113-117
21333694-1	2011	Cellular iron metabolism is essentially controlled by the binding of cytosolic iron regulatory proteins (IRP1 or IRP2) to iron-responsive elements (IREs) located on mRNAs coding for proteins involved in iron acquisition, utilization and storage.	Iron	79-83	iron responsive element binding protein 2	Homo sapiens	113-117
21333694-5	2011	We found that exposure of Madin-Darby Bovine Kidney cell to TCDD caused a divergent modulation of IRP1 and IRP2 RNA-binding capacity.	Polychlorinated Dibenzodioxins	60-64	iron responsive element binding protein 2	Homo sapiens	107-111
21558272-1	2011	Iron regulatory protein 2 (IRP2) controls the synthesis of many proteins involved in iron metabolism, and the level of IRP2 itself is regulated by varying the rate of its degradation.	Iron	85-89	iron responsive element binding protein 2	Homo sapiens	0-25
21558272-1	2011	Iron regulatory protein 2 (IRP2) controls the synthesis of many proteins involved in iron metabolism, and the level of IRP2 itself is regulated by varying the rate of its degradation.	Iron	85-89	iron responsive element binding protein 2	Homo sapiens	27-31
21558272-1	2011	Iron regulatory protein 2 (IRP2) controls the synthesis of many proteins involved in iron metabolism, and the level of IRP2 itself is regulated by varying the rate of its degradation.	Iron	85-89	iron responsive element binding protein 2	Homo sapiens	119-123
21558272-3	2011	Most studies on the degradation of IRP2 have employed cells overexpressing IRP2 and also rendered iron deficient to further increase IRP2 levels.	Iron	98-102	iron responsive element binding protein 2	Homo sapiens	35-39
21558272-8	2011	We conclude that under physiological, iron-sufficient conditions, the steady-state level of IRP2 in HEK293A cells is regulated by the nonproteasomal pathway.	Iron	38-42	iron responsive element binding protein 2	Homo sapiens	92-96
21333694-1	2011	Cellular iron metabolism is essentially controlled by the binding of cytosolic iron regulatory proteins (IRP1 or IRP2) to iron-responsive elements (IREs) located on mRNAs coding for proteins involved in iron acquisition, utilization and storage.	Iron	9-13	iron responsive element binding protein 2	Homo sapiens	113-117
21188590-7	2011	A sorbitol positive, streptomycin resistant STEC strain was isolated from the drinking water, and belonged to the serotype O100:H(-), produced Stx2 toxin (titre 1:8 by reversed-passive latex agglutination method), and carried the genes stx(2e), estIa and irp2.	Streptomycin	21-33	iron responsive element binding protein 2	Homo sapiens	255-259
20214491-3	2010	IRP1 and IRP2 are similar (but not identical) proteins with partially overlapping and complementary functions, and control cell iron metabolism by binding to IREs (i.e., conserved RNA stem-loops located in the untranslated regions of a dozen mRNAs directly or indirectly related to iron metabolism).	Iron	128-132	iron responsive element binding protein 2	Homo sapiens	9-13
21360641-2	2011	Iron regulatory proteins (IRPs, IRP1 and IRP2) are master regulators of cellular iron metabolism.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	41-45
21360641-2	2011	Iron regulatory proteins (IRPs, IRP1 and IRP2) are master regulators of cellular iron metabolism.	Iron	81-85	iron responsive element binding protein 2	Homo sapiens	41-45
21185934-4	2011	Iron-response proteins (IRP1 and IRP2) and "cap-n-collar" bZIP transcriptional factors (NE-F2 p45; Nrf1, 2, and 3; Bach1 and 2) also control gene and protein expression of the key iron homeostasis proteins.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	33-37
21185934-4	2011	Iron-response proteins (IRP1 and IRP2) and "cap-n-collar" bZIP transcriptional factors (NE-F2 p45; Nrf1, 2, and 3; Bach1 and 2) also control gene and protein expression of the key iron homeostasis proteins.	Iron	180-184	iron responsive element binding protein 2	Homo sapiens	33-37
21281640-1	2011	Iron regulatory protein 2 (IRP2) is a critical switch for cellular and systemic iron homeostasis.	Iron	80-84	iron responsive element binding protein 2	Homo sapiens	0-25
21281640-1	2011	Iron regulatory protein 2 (IRP2) is a critical switch for cellular and systemic iron homeostasis.	Iron	80-84	iron responsive element binding protein 2	Homo sapiens	27-31
21281640-2	2011	In iron-deficient or hypoxic cells, IRP2 binds to mRNAs containing iron responsive elements (IREs) and regulates their expression.	Iron	3-7	iron responsive element binding protein 2	Homo sapiens	36-40
21281640-3	2011	Iron promotes proteasomal degradation of IRP2 via the F-box protein FBXL5.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	41-45
21281640-5	2011	We show that iron-dependent decay of tetracycline-inducible IRP2 proceeds efficiently under mild hypoxic conditions (3% oxygen) but is compromised in severe hypoxia (0.1% oxygen).	Iron	13-17	iron responsive element binding protein 2	Homo sapiens	60-64
21281640-5	2011	We show that iron-dependent decay of tetracycline-inducible IRP2 proceeds efficiently under mild hypoxic conditions (3% oxygen) but is compromised in severe hypoxia (0.1% oxygen).	Tetracycline	37-49	iron responsive element binding protein 2	Homo sapiens	60-64
21281640-5	2011	We show that iron-dependent decay of tetracycline-inducible IRP2 proceeds efficiently under mild hypoxic conditions (3% oxygen) but is compromised in severe hypoxia (0.1% oxygen).	Oxygen	120-126	iron responsive element binding protein 2	Homo sapiens	60-64
21281640-5	2011	We show that iron-dependent decay of tetracycline-inducible IRP2 proceeds efficiently under mild hypoxic conditions (3% oxygen) but is compromised in severe hypoxia (0.1% oxygen).	Oxygen	171-177	iron responsive element binding protein 2	Homo sapiens	60-64
21281640-6	2011	A treatment of cells with exogenous H(2)O(2) protects IRP2 against iron and increases its IRE-binding activity.	Iron	67-71	iron responsive element binding protein 2	Homo sapiens	54-58
21281640-7	2011	IRP2 is also stabilized during menadione-induced oxidative stress.	Vitamin K 3	31-40	iron responsive element binding protein 2	Homo sapiens	0-4
21281640-8	2011	These data demonstrate that the degradation of IRP2 in iron-replete cells is not only oxygen-dependent but also sensitive to redox perturbations.	Iron	55-59	iron responsive element binding protein 2	Homo sapiens	47-51
21281640-8	2011	These data demonstrate that the degradation of IRP2 in iron-replete cells is not only oxygen-dependent but also sensitive to redox perturbations.	Oxygen	86-92	iron responsive element binding protein 2	Homo sapiens	47-51
21320324-11	2011	CONCLUSIONS: These studies have therefore confirmed that the IREB2 locus is a contributor to COPD susceptibility and suggests a new pathway in COPD pathogenesis invoking iron homeostasis.	Iron	170-174	iron responsive element binding protein 2	Homo sapiens	61-66
20214491-3	2010	IRP1 and IRP2 are similar (but not identical) proteins with partially overlapping and complementary functions, and control cell iron metabolism by binding to IREs (i.e., conserved RNA stem-loops located in the untranslated regions of a dozen mRNAs directly or indirectly related to iron metabolism).	Iron	282-286	iron responsive element binding protein 2	Homo sapiens	9-13
19762597-2	2009	However, the manner in which iron levels are sensed to affect IRP2 activity is poorly understood.	Iron	29-33	iron responsive element binding protein 2	Homo sapiens	62-66
20558735-2	2010	Equal modulated interaction of the iron regulatory proteins (IRP1 and IRP2) with canonical IREs controls iron-dependent translation of the ferritin subunits.	Iron	35-39	iron responsive element binding protein 2	Homo sapiens	70-74
20558735-2	2010	Equal modulated interaction of the iron regulatory proteins (IRP1 and IRP2) with canonical IREs controls iron-dependent translation of the ferritin subunits.	Iron	105-109	iron responsive element binding protein 2	Homo sapiens	70-74
20405006-1	2010	Iron regulatory proteins, IRP1 and IRP2, bind to mRNAs harboring iron responsive elements and control their expression.	Iron	65-69	iron responsive element binding protein 2	Homo sapiens	35-39
20405006-5	2010	Human H1299 lung cancer cells or clones engineered for tetracycline-inducible expression of wild type IRP2, or the deletion mutant IRP2(Delta73) (lacking a specific insert of 73 amino acids), were injected subcutaneously into nude mice.	Tetracycline	55-67	iron responsive element binding protein 2	Homo sapiens	102-106
20405006-6	2010	The induction of IRP2 profoundly stimulated the growth of tumor xenografts, and this response was blunted by addition of tetracycline in the drinking water of the animals, to turnoff the IRP2 transgene.	Tetracycline	121-133	iron responsive element binding protein 2	Homo sapiens	17-21
20405006-6	2010	The induction of IRP2 profoundly stimulated the growth of tumor xenografts, and this response was blunted by addition of tetracycline in the drinking water of the animals, to turnoff the IRP2 transgene.	Tetracycline	121-133	iron responsive element binding protein 2	Homo sapiens	187-191
20405006-6	2010	The induction of IRP2 profoundly stimulated the growth of tumor xenografts, and this response was blunted by addition of tetracycline in the drinking water of the animals, to turnoff the IRP2 transgene.	Drinking Water	141-155	iron responsive element binding protein 2	Homo sapiens	17-21
20405006-6	2010	The induction of IRP2 profoundly stimulated the growth of tumor xenografts, and this response was blunted by addition of tetracycline in the drinking water of the animals, to turnoff the IRP2 transgene.	Drinking Water	141-155	iron responsive element binding protein 2	Homo sapiens	187-191
19800271-3	2010	The mutation results in a loss of post-transcriptional negative feedback exerted by the interaction between iron regulatory proteins 1, 2 (IRP1 and IRP2) and IRE, which leads to uncontrolled expression of L-ferritin.	Iron	108-112	iron responsive element binding protein 2	Homo sapiens	148-152
26190951-0	2009	On the mechanism of iron sensing by IRP2: new players, new paradigms.	Iron	20-24	iron responsive element binding protein 2	Homo sapiens	36-40
26190951-1	2009	Two iron regulatory proteins (IRP1 and IRP2) regulate translation and/or stability of mRNAs encoding proteins required for iron storage, acquisition and utilization.	Iron	4-8	iron responsive element binding protein 2	Homo sapiens	39-43
26190951-1	2009	Two iron regulatory proteins (IRP1 and IRP2) regulate translation and/or stability of mRNAs encoding proteins required for iron storage, acquisition and utilization.	Iron	123-127	iron responsive element binding protein 2	Homo sapiens	39-43
26190951-2	2009	Rather than IRP2 directly sensing iron concentrations, iron has been shown to regulate the level of the SKP1-CUL1-FBXL5 E3 ubiquitin ligase protein complex, which is responsible for IRP2 degradation.	Iron	55-59	iron responsive element binding protein 2	Homo sapiens	182-186
19762596-2	2009	The degradation of iron regulatory protein 2 (IRP2) in iron-replete cells is a key event in this pathway, but the E3 ubiquitin ligase responsible for its proteolysis has remained elusive.	Iron	19-23	iron responsive element binding protein 2	Homo sapiens	46-50
19762596-3	2009	We found that a SKP1-CUL1-FBXL5 ubiquitin ligase protein complex associates with and promotes the iron-dependent ubiquitination and degradation of IRP2.	Iron	98-102	iron responsive element binding protein 2	Homo sapiens	147-151
19762596-5	2009	Thus, iron homeostasis is regulated by a proteolytic pathway that couples IRP2 degradation to intracellular iron levels through the stability and activity of FBXL5.	Iron	6-10	iron responsive element binding protein 2	Homo sapiens	74-78
19762597-1	2009	Cellular iron homeostasis is maintained by the coordinate posttranscriptional regulation of genes responsible for iron uptake, release, use, and storage through the actions of the iron regulatory proteins IRP1 and IRP2.	Iron	9-13	iron responsive element binding protein 2	Homo sapiens	214-218
19762597-1	2009	Cellular iron homeostasis is maintained by the coordinate posttranscriptional regulation of genes responsible for iron uptake, release, use, and storage through the actions of the iron regulatory proteins IRP1 and IRP2.	Iron	114-118	iron responsive element binding protein 2	Homo sapiens	214-218
19762597-1	2009	Cellular iron homeostasis is maintained by the coordinate posttranscriptional regulation of genes responsible for iron uptake, release, use, and storage through the actions of the iron regulatory proteins IRP1 and IRP2.	Iron	114-118	iron responsive element binding protein 2	Homo sapiens	214-218
19762597-6	2009	These observations suggest a mechanistic link between iron sensing via the FBXL5 hemerythrin domain, IRP2 regulation, and cellular responses to maintain mammalian iron homeostasis.	Iron	54-58	iron responsive element binding protein 2	Homo sapiens	101-105
19762597-6	2009	These observations suggest a mechanistic link between iron sensing via the FBXL5 hemerythrin domain, IRP2 regulation, and cellular responses to maintain mammalian iron homeostasis.	Iron	163-167	iron responsive element binding protein 2	Homo sapiens	101-105
19021541-7	2008	The APP IRE is homologous with the canonical IRE RNA stem-loop that binds the iron regulatory proteins (IRP1 and IRP2) to control intracellular iron homoeostasis by modulating ferritin mRNA translation and transferrin receptor mRNA stability.	Iron	78-82	iron responsive element binding protein 2	Homo sapiens	113-117
19223469-7	2009	These studies provide insight into the structural basis for IRP2-RNA interactions and reveal an iron-independent mechanism for regulating iron homeostasis through the redox regulation of IRP2 cysteines.	Iron	96-100	iron responsive element binding protein 2	Homo sapiens	187-191
19223469-7	2009	These studies provide insight into the structural basis for IRP2-RNA interactions and reveal an iron-independent mechanism for regulating iron homeostasis through the redox regulation of IRP2 cysteines.	Cysteine	192-201	iron responsive element binding protein 2	Homo sapiens	187-191
19223469-0	2009	Cysteine oxidation regulates the RNA-binding activity of iron regulatory protein 2.	Cysteine	0-8	iron responsive element binding protein 2	Homo sapiens	57-82
19223469-1	2009	Iron regulatory protein 2 (IRP2) is an RNA-binding protein that regulates the posttranscriptional expression of proteins required for iron homeostasis such as ferritin and transferrin receptor 1.	Iron	134-138	iron responsive element binding protein 2	Homo sapiens	0-25
19223469-1	2009	Iron regulatory protein 2 (IRP2) is an RNA-binding protein that regulates the posttranscriptional expression of proteins required for iron homeostasis such as ferritin and transferrin receptor 1.	Iron	134-138	iron responsive element binding protein 2	Homo sapiens	27-31
19223469-2	2009	IRP2 RNA-binding activity is primarily regulated by iron-mediated proteasomal degradation, but studies have suggested that IRP2 RNA binding is also regulated by thiol oxidation.	Iron	52-56	iron responsive element binding protein 2	Homo sapiens	0-4
19223469-2	2009	IRP2 RNA-binding activity is primarily regulated by iron-mediated proteasomal degradation, but studies have suggested that IRP2 RNA binding is also regulated by thiol oxidation.	Sulfhydryl Compounds	161-166	iron responsive element binding protein 2	Homo sapiens	123-127
19223469-3	2009	We generated a model of IRP2 bound to RNA and found that two cysteines (C512 and C516) are predicted to lie in the RNA-binding cleft.	Cysteine	61-70	iron responsive element binding protein 2	Homo sapiens	24-28
19223469-5	2009	Oxidative stress induced by cellular glucose deprivation reduces the RNA-binding activity of IRP2 but not IRP2-C512S or IRP2-C516S, consistent with the formation of a disulfide bond between IRP2 C512 and C516 during oxidative stress.	Disulfides	167-176	iron responsive element binding protein 2	Homo sapiens	93-97
18574241-0	2008	Iron-independent phosphorylation of iron regulatory protein 2 regulates ferritin during the cell cycle.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	36-61
18655771-1	2008	Iron regulatory protein (IRP)-1 and IRP2 inhibit ferritin synthesis by binding to an iron responsive element in the 5"-untranslated region of its mRNA.	Iron	85-89	iron responsive element binding protein 2	Homo sapiens	36-40
18655771-6	2008	Ferritin expression after H(2)O(2) treatment was increased 1.9- and 6.7-fold in IRP1 and IRP2 knockout cultures, respectively, compared with wild-type.	Hydrogen Peroxide	26-34	iron responsive element binding protein 2	Homo sapiens	89-93
18655771-7	2008	These results suggest that iron regulatory proteins, particularly IRP2, increase neuronal vulnerability to oxidative injury.	Iron	27-31	iron responsive element binding protein 2	Homo sapiens	66-70
18574241-1	2008	Iron regulatory protein 2 (IRP2) is a key iron sensor that post-transcriptionally regulates mammalian iron homeostasis by binding to iron-responsive elements (IREs) in mRNAs that encode proteins involved in iron metabolism (e.g. ferritin and transferrin receptor 1).	Iron	42-46	iron responsive element binding protein 2	Homo sapiens	0-25
18574241-1	2008	Iron regulatory protein 2 (IRP2) is a key iron sensor that post-transcriptionally regulates mammalian iron homeostasis by binding to iron-responsive elements (IREs) in mRNAs that encode proteins involved in iron metabolism (e.g. ferritin and transferrin receptor 1).	Iron	42-46	iron responsive element binding protein 2	Homo sapiens	27-31
18574241-1	2008	Iron regulatory protein 2 (IRP2) is a key iron sensor that post-transcriptionally regulates mammalian iron homeostasis by binding to iron-responsive elements (IREs) in mRNAs that encode proteins involved in iron metabolism (e.g. ferritin and transferrin receptor 1).	Iron	102-106	iron responsive element binding protein 2	Homo sapiens	0-25
18574241-1	2008	Iron regulatory protein 2 (IRP2) is a key iron sensor that post-transcriptionally regulates mammalian iron homeostasis by binding to iron-responsive elements (IREs) in mRNAs that encode proteins involved in iron metabolism (e.g. ferritin and transferrin receptor 1).	Iron	102-106	iron responsive element binding protein 2	Homo sapiens	27-31
18574241-1	2008	Iron regulatory protein 2 (IRP2) is a key iron sensor that post-transcriptionally regulates mammalian iron homeostasis by binding to iron-responsive elements (IREs) in mRNAs that encode proteins involved in iron metabolism (e.g. ferritin and transferrin receptor 1).	Iron	102-106	iron responsive element binding protein 2	Homo sapiens	0-25
18574241-1	2008	Iron regulatory protein 2 (IRP2) is a key iron sensor that post-transcriptionally regulates mammalian iron homeostasis by binding to iron-responsive elements (IREs) in mRNAs that encode proteins involved in iron metabolism (e.g. ferritin and transferrin receptor 1).	Iron	102-106	iron responsive element binding protein 2	Homo sapiens	27-31
18574241-1	2008	Iron regulatory protein 2 (IRP2) is a key iron sensor that post-transcriptionally regulates mammalian iron homeostasis by binding to iron-responsive elements (IREs) in mRNAs that encode proteins involved in iron metabolism (e.g. ferritin and transferrin receptor 1).	Iron	102-106	iron responsive element binding protein 2	Homo sapiens	0-25
18574241-1	2008	Iron regulatory protein 2 (IRP2) is a key iron sensor that post-transcriptionally regulates mammalian iron homeostasis by binding to iron-responsive elements (IREs) in mRNAs that encode proteins involved in iron metabolism (e.g. ferritin and transferrin receptor 1).	Iron	102-106	iron responsive element binding protein 2	Homo sapiens	27-31
18574241-2	2008	During iron deficiency, IRP2 binds IREs to regulate mRNA translation or stability, whereas during iron sufficiency IRP2 is degraded by the proteasome.	Iron	7-11	iron responsive element binding protein 2	Homo sapiens	24-28
18574241-3	2008	Here, we identify an iron-independent IRP2 phosphorylation site that is regulated by the cell cycle.	Iron	21-25	iron responsive element binding protein 2	Homo sapiens	38-42
18574241-4	2008	IRP2 Ser-157 is phosphorylated by Cdk1/cyclin B1 during G(2)/M and is dephosphorylated during mitotic exit by the phosphatase Cdc14A.	Serine	5-8	iron responsive element binding protein 2	Homo sapiens	0-4
18574241-5	2008	Ser-157 phosphorylation during G(2)/M reduces IRP2 RNA-binding activity and increases ferritin synthesis, whereas Ser-157 dephosphorylation during mitotic exit restores IRP2 RNA-binding activity and represses ferritin synthesis.	Serine	0-3	iron responsive element binding protein 2	Homo sapiens	46-50
18574241-6	2008	These data show that reversible phosphorylation of IRP2 during G(2)/M has a role in modulating the iron-independent expression of ferritin and other IRE-containing mRNAs during the cell cycle.	Iron	99-103	iron responsive element binding protein 2	Homo sapiens	51-55
18424449-4	2008	Lymphoblasts and fibroblasts of FA patients have evidence of cytosolic iron depletion, as indicated by increased levels of iron regulatory protein 2 (IRP2) and/or increased IRE-binding activity of IRP1.	Iron	71-75	iron responsive element binding protein 2	Homo sapiens	123-148
18424449-4	2008	Lymphoblasts and fibroblasts of FA patients have evidence of cytosolic iron depletion, as indicated by increased levels of iron regulatory protein 2 (IRP2) and/or increased IRE-binding activity of IRP1.	Iron	71-75	iron responsive element binding protein 2	Homo sapiens	150-154
18549630-5	2008	It is concluded that IRP(2) protein serves as an important regulator of iron metabolism in the human body, and regulates iron uptake from the intestine by controlling the expression of fn mRNA at the post transcriptional level.	Iron	72-76	iron responsive element binding protein 2	Homo sapiens	21-26
18549630-5	2008	It is concluded that IRP(2) protein serves as an important regulator of iron metabolism in the human body, and regulates iron uptake from the intestine by controlling the expression of fn mRNA at the post transcriptional level.	Iron	121-125	iron responsive element binding protein 2	Homo sapiens	21-26
17546407-6	2008	The bioavailability of the released iron was confirmed by a 100% increase in L-ferritin protein as well as a 60% decrease of the IRP2 protein levels.	Iron	36-40	iron responsive element binding protein 2	Homo sapiens	129-133
17822790-1	2008	Iron regulatory protein 2 (IRP2) binds to iron-responsive elements (IREs) to regulate the translation and stability of mRNAs encoding several proteins involved in mammalian iron homeostasis.	Iron	42-46	iron responsive element binding protein 2	Homo sapiens	0-25
17822790-1	2008	Iron regulatory protein 2 (IRP2) binds to iron-responsive elements (IREs) to regulate the translation and stability of mRNAs encoding several proteins involved in mammalian iron homeostasis.	Iron	42-46	iron responsive element binding protein 2	Homo sapiens	27-31
17822790-1	2008	Iron regulatory protein 2 (IRP2) binds to iron-responsive elements (IREs) to regulate the translation and stability of mRNAs encoding several proteins involved in mammalian iron homeostasis.	Iron	173-177	iron responsive element binding protein 2	Homo sapiens	0-25
17822790-1	2008	Iron regulatory protein 2 (IRP2) binds to iron-responsive elements (IREs) to regulate the translation and stability of mRNAs encoding several proteins involved in mammalian iron homeostasis.	Iron	173-177	iron responsive element binding protein 2	Homo sapiens	27-31
17822790-2	2008	Increases in cellular iron stimulate the polyubiquitylation and proteasomal degradation of IRP2.	Iron	22-26	iron responsive element binding protein 2	Homo sapiens	91-95
17822790-3	2008	One study has suggested that haem-oxidized IRP2 ubiquitin ligase-1 (HOIL-1) binds to a unique 73-amino acid (aa) domain in IRP2 in an iron-dependent manner to regulate IRP2 polyubiquitylation and degradation.	Iron	134-138	iron responsive element binding protein 2	Homo sapiens	43-47
17822790-3	2008	One study has suggested that haem-oxidized IRP2 ubiquitin ligase-1 (HOIL-1) binds to a unique 73-amino acid (aa) domain in IRP2 in an iron-dependent manner to regulate IRP2 polyubiquitylation and degradation.	Iron	134-138	iron responsive element binding protein 2	Homo sapiens	123-127
17822790-4	2008	Other studies have questioned the role of the 73-aa domain in iron-dependent IRP2 degradation.	Iron	62-66	iron responsive element binding protein 2	Homo sapiens	77-81
17822790-5	2008	We investigated the potential role of HOIL-1 in the iron-mediated degradation of IRP2 in human embryonic kidney 293 (HEK293) cells.	Iron	52-56	iron responsive element binding protein 2	Homo sapiens	81-85
17822790-6	2008	We found that transiently expressed HOIL-1 and IRP2 interact via the 73-aa domain, but this interaction is not iron-dependent, nor does it enhance the rate of IRP2 degradation by iron.	Iron	179-183	iron responsive element binding protein 2	Homo sapiens	47-51
18261896-1	2008	Iron homeostasis in animal cells is controlled post-transcriptionally by the iron regulatory proteins IRP1 and IRP2.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	111-115
18261896-1	2008	Iron homeostasis in animal cells is controlled post-transcriptionally by the iron regulatory proteins IRP1 and IRP2.	Iron	77-81	iron responsive element binding protein 2	Homo sapiens	111-115
18226225-5	2008	Truncated versions of IRP2 were expressed in H1299 cells and analyzed for their response to iron.	Iron	92-96	iron responsive element binding protein 2	Homo sapiens	22-26
18226225-6	2008	Deletion mutants lacking the entire C-terminal domain 4 (amino acids 719-963) of IRP2 remained stable following iron treatments.	Iron	112-116	iron responsive element binding protein 2	Homo sapiens	81-85
18226225-0	2008	Iron-dependent degradation of IRP2 requires its C-terminal region and IRP structural integrity.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	30-34
18226225-7	2008	Moreover, the replacement of domain 4 of IRP1 with the corresponding region of IRP2 sensitized the chimerical IRP11-3/IRP24 protein to iron-dependent degradation, while the reverse manipulation gave rise to a stable chimerical IRP21-3/IRP14 protein.	Iron	135-139	iron responsive element binding protein 2	Homo sapiens	79-83
18226225-1	2008	BACKGROUND: Iron regulatory protein 2 (IRP2), a post-transcriptional regulator of cellular iron metabolism, undergoes iron-dependent degradation via the ubiquitin-proteasome pathway.	Iron	91-95	iron responsive element binding protein 2	Homo sapiens	12-37
18226225-8	2008	The deletion of just 26 or 34 C-terminal amino acids stabilized IRP2 against iron.	Iron	77-81	iron responsive element binding protein 2	Homo sapiens	64-68
18226225-1	2008	BACKGROUND: Iron regulatory protein 2 (IRP2), a post-transcriptional regulator of cellular iron metabolism, undergoes iron-dependent degradation via the ubiquitin-proteasome pathway.	Iron	91-95	iron responsive element binding protein 2	Homo sapiens	39-43
18226225-1	2008	BACKGROUND: Iron regulatory protein 2 (IRP2), a post-transcriptional regulator of cellular iron metabolism, undergoes iron-dependent degradation via the ubiquitin-proteasome pathway.	Iron	118-122	iron responsive element binding protein 2	Homo sapiens	12-37
18226225-10	2008	CONCLUSION: Our data suggest that the C-terminus of IRP2 contains elements that are necessary but not sufficient for iron-dependent degradation.	Iron	117-121	iron responsive element binding protein 2	Homo sapiens	52-56
18226225-1	2008	BACKGROUND: Iron regulatory protein 2 (IRP2), a post-transcriptional regulator of cellular iron metabolism, undergoes iron-dependent degradation via the ubiquitin-proteasome pathway.	Iron	118-122	iron responsive element binding protein 2	Homo sapiens	39-43
18582596-1	2008	The two mammalian iron regulatory proteins, IRP1 and IRP2, are post-transcriptional regulators of cellular iron homeostasis.	Iron	18-22	iron responsive element binding protein 2	Homo sapiens	53-57
18195524-3	2008	We have studied the iron-mediated regulatory mechanism of a regulator of the iron metabolism, IRP2, and found that IRP2 is regulated by an oxidation-induced degradation, which is triggered by heme and molecular oxygen.	Iron	20-24	iron responsive element binding protein 2	Homo sapiens	94-98
18195524-3	2008	We have studied the iron-mediated regulatory mechanism of a regulator of the iron metabolism, IRP2, and found that IRP2 is regulated by an oxidation-induced degradation, which is triggered by heme and molecular oxygen.	Iron	20-24	iron responsive element binding protein 2	Homo sapiens	115-119
18195524-3	2008	We have studied the iron-mediated regulatory mechanism of a regulator of the iron metabolism, IRP2, and found that IRP2 is regulated by an oxidation-induced degradation, which is triggered by heme and molecular oxygen.	Iron	77-81	iron responsive element binding protein 2	Homo sapiens	94-98
18195524-3	2008	We have studied the iron-mediated regulatory mechanism of a regulator of the iron metabolism, IRP2, and found that IRP2 is regulated by an oxidation-induced degradation, which is triggered by heme and molecular oxygen.	Iron	77-81	iron responsive element binding protein 2	Homo sapiens	115-119
18195524-3	2008	We have studied the iron-mediated regulatory mechanism of a regulator of the iron metabolism, IRP2, and found that IRP2 is regulated by an oxidation-induced degradation, which is triggered by heme and molecular oxygen.	Heme	192-196	iron responsive element binding protein 2	Homo sapiens	115-119
18195524-3	2008	We have studied the iron-mediated regulatory mechanism of a regulator of the iron metabolism, IRP2, and found that IRP2 is regulated by an oxidation-induced degradation, which is triggered by heme and molecular oxygen.	Oxygen	211-217	iron responsive element binding protein 2	Homo sapiens	115-119
18195524-5	2008	Considering that heme is generated in the matrix of mitochondria, our observation that IRP2 is regulated by the protein degradation pathway triggered by the heme-mediated oxidation indicates the involvement and importance of mitochondria in cellular iron sensing as well as the regulation of the iron metabolism.	Heme	17-21	iron responsive element binding protein 2	Homo sapiens	87-91
18195524-5	2008	Considering that heme is generated in the matrix of mitochondria, our observation that IRP2 is regulated by the protein degradation pathway triggered by the heme-mediated oxidation indicates the involvement and importance of mitochondria in cellular iron sensing as well as the regulation of the iron metabolism.	Heme	157-161	iron responsive element binding protein 2	Homo sapiens	87-91
18195524-5	2008	Considering that heme is generated in the matrix of mitochondria, our observation that IRP2 is regulated by the protein degradation pathway triggered by the heme-mediated oxidation indicates the involvement and importance of mitochondria in cellular iron sensing as well as the regulation of the iron metabolism.	Iron	250-254	iron responsive element binding protein 2	Homo sapiens	87-91
18195524-5	2008	Considering that heme is generated in the matrix of mitochondria, our observation that IRP2 is regulated by the protein degradation pathway triggered by the heme-mediated oxidation indicates the involvement and importance of mitochondria in cellular iron sensing as well as the regulation of the iron metabolism.	Iron	296-300	iron responsive element binding protein 2	Homo sapiens	87-91
18582596-1	2008	The two mammalian iron regulatory proteins, IRP1 and IRP2, are post-transcriptional regulators of cellular iron homeostasis.	Iron	107-111	iron responsive element binding protein 2	Homo sapiens	53-57
18582596-3	2008	Whereas IRP1 levels remain nearly constant, IRP2 is rapidly degraded by the proteasome in iron-replete cells.	Iron	90-94	iron responsive element binding protein 2	Homo sapiens	44-48
18582596-4	2008	In non iron-loaded H1299 human lung cancer cells, the decay of transfected hemagglutinin-tagged IRP2 was significantly antagonized by addition of not only proteasomal, but also lysosomal inhibitors.	Iron	7-11	iron responsive element binding protein 2	Homo sapiens	96-100
18582596-6	2008	These data uncover an alternative, iron independent, mechanism of IRP2 degradation via the lysosomal pathway.	Iron	35-39	iron responsive element binding protein 2	Homo sapiens	66-70
18582596-9	2008	Together with previous data obtained in the presence of iron excess, these results show that the parallel degradation pathways through lysosomes and the proteasome that are active on IRP2 under normal growth conditions are preferentially shifted to the proteasome when iron becomes plentiful.	Iron	56-60	iron responsive element binding protein 2	Homo sapiens	183-187
18582596-9	2008	Together with previous data obtained in the presence of iron excess, these results show that the parallel degradation pathways through lysosomes and the proteasome that are active on IRP2 under normal growth conditions are preferentially shifted to the proteasome when iron becomes plentiful.	Iron	269-273	iron responsive element binding protein 2	Homo sapiens	183-187
17604281-1	2007	Iron regulatory proteins (IRP1 and IRP2) are master regulators of cellular iron metabolism.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	35-39
17785948-4	2007	Iron concentration in the cell is sensed and regulated by the heme-mediated oxidization and subsequent degradation of iron regulatory protein 2 (IRP2).	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	118-143
17785948-4	2007	Iron concentration in the cell is sensed and regulated by the heme-mediated oxidization and subsequent degradation of iron regulatory protein 2 (IRP2).	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	145-149
17785948-4	2007	Iron concentration in the cell is sensed and regulated by the heme-mediated oxidization and subsequent degradation of iron regulatory protein 2 (IRP2).	Heme	62-66	iron responsive element binding protein 2	Homo sapiens	118-143
17785948-4	2007	Iron concentration in the cell is sensed and regulated by the heme-mediated oxidization and subsequent degradation of iron regulatory protein 2 (IRP2).	Heme	62-66	iron responsive element binding protein 2	Homo sapiens	145-149
17760563-1	2007	Mammalian IRPs (iron regulatory proteins), IRP1 and IRP2, are cytosolic RNA-binding proteins that post-transcriptionally control the mRNA of proteins involved in storage, transport, and utilization of iron.	Iron	16-20	iron responsive element binding protein 2	Homo sapiens	52-56
17760563-2	2007	In iron-replete cells, IRP2 undergoes degradation by the ubiquitin/proteasome pathway.	Iron	3-7	iron responsive element binding protein 2	Homo sapiens	23-27
17760563-3	2007	Binding of haem to a 73aa-Domain (73-amino-acid domain) that is unique in IRP2 has been previously proposed as the initial iron-sensing mechanism.	Iron	123-127	iron responsive element binding protein 2	Homo sapiens	74-78
17760563-6	2007	Iron-independent cleavage of IRP2 within the 73aa-Domain also occurs in lung cancer (H1299) cells.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	29-33
17485548-8	2007	Based on the biochemical and clinical phenotype, we hypothesize that IRP2, less degraded by low heme, contributes to the repression of the erythroblasts ferritin and ALAS2, increasing mitochondrial iron.	Heme	96-100	iron responsive element binding protein 2	Homo sapiens	69-73
17485548-8	2007	Based on the biochemical and clinical phenotype, we hypothesize that IRP2, less degraded by low heme, contributes to the repression of the erythroblasts ferritin and ALAS2, increasing mitochondrial iron.	Iron	198-202	iron responsive element binding protein 2	Homo sapiens	69-73
17485548-9	2007	Iron chelation, redistributing iron to the cytosol, might relieve IRP2 excess, improving heme synthesis and anemia.	Iron	0-4	iron responsive element binding protein 2	Homo sapiens	66-70
17485548-9	2007	Iron chelation, redistributing iron to the cytosol, might relieve IRP2 excess, improving heme synthesis and anemia.	Iron	31-35	iron responsive element binding protein 2	Homo sapiens	66-70
17604281-1	2007	Iron regulatory proteins (IRP1 and IRP2) are master regulators of cellular iron metabolism.	Iron	75-79	iron responsive element binding protein 2	Homo sapiens	35-39
20020877-11	2007	In the cytosol, iron regulatory proteins 1 and 2 (IRP1 and IRP2) play a prominent role in sensing the presence of iron in order to posttranscriptionally regulate the expression of TfR1 and ferritin, two important participants in iron metabolism.	Iron	16-20	iron responsive element binding protein 2	Homo sapiens	59-63
17200797-1	2007	Iron regulatory proteins 1 and 2 (IRP1, IRP2) are key determinants of uptake and storage of iron by the liver, and are responsive to oxidative stress and hypoxia potentially at the level of both protein concentration and mRNA-binding activity.	Iron	92-96	iron responsive element binding protein 2	Homo sapiens	40-44
20020877-11	2007	In the cytosol, iron regulatory proteins 1 and 2 (IRP1 and IRP2) play a prominent role in sensing the presence of iron in order to posttranscriptionally regulate the expression of TfR1 and ferritin, two important participants in iron metabolism.	Iron	114-118	iron responsive element binding protein 2	Homo sapiens	59-63
16911529-1	2006	The discovery of iron-responsive elements (IREs), along with the identification of iron regulatory proteins (IRP1, IRP2), has provided a molecular basis for our current understanding of the remarkable post-transcriptional regulation of intracellular iron homeostasis.	Iron	17-21	iron responsive element binding protein 2	Homo sapiens	115-119
16911529-1	2006	The discovery of iron-responsive elements (IREs), along with the identification of iron regulatory proteins (IRP1, IRP2), has provided a molecular basis for our current understanding of the remarkable post-transcriptional regulation of intracellular iron homeostasis.	Iron	83-87	iron responsive element binding protein 2	Homo sapiens	115-119
16911529-1	2006	The discovery of iron-responsive elements (IREs), along with the identification of iron regulatory proteins (IRP1, IRP2), has provided a molecular basis for our current understanding of the remarkable post-transcriptional regulation of intracellular iron homeostasis.	Iron	83-87	iron responsive element binding protein 2	Homo sapiens	115-119
16914832-2	2006	Regulation of the proteins that maintain cellular iron metabolism is mediated by two cytoplasmic RNA-binding proteins, the Iron Regulatory Proteins (IRP1 and IRP2), that function through post-transcriptional interactions with RNA stem loop structures called iron-responsive elements.	Iron	50-54	iron responsive element binding protein 2	Homo sapiens	158-162
16914832-2	2006	Regulation of the proteins that maintain cellular iron metabolism is mediated by two cytoplasmic RNA-binding proteins, the Iron Regulatory Proteins (IRP1 and IRP2), that function through post-transcriptional interactions with RNA stem loop structures called iron-responsive elements.	Iron	123-127	iron responsive element binding protein 2	Homo sapiens	158-162
16914832-2	2006	Regulation of the proteins that maintain cellular iron metabolism is mediated by two cytoplasmic RNA-binding proteins, the Iron Regulatory Proteins (IRP1 and IRP2), that function through post-transcriptional interactions with RNA stem loop structures called iron-responsive elements.	Iron	258-262	iron responsive element binding protein 2	Homo sapiens	158-162
16914832-3	2006	As the primary mediator of iron homeostasis in neuronal cells, IRP2 is a strong candidate for polymorphisms that could impact AD pathogenesis.	Iron	27-31	iron responsive element binding protein 2	Homo sapiens	63-67
16460831-7	2006	Importantly, hepcidin expression from Huh7 cells elicited a decrease in the levels of the iron-sensitive post-transcriptional regulator IRP2 in THP1 cells, accompanied by de novo synthesis of the iron storage protein ferritin.	Iron	90-94	iron responsive element binding protein 2	Homo sapiens	136-140
16850017-1	2006	Iron regulatory proteins 1 and 2 (IRP1 and IRP2) are mammalian proteins that register cytosolic iron concentrations and post-transcriptionally regulate expression of iron metabolism genes to optimize cellular iron availability.	Iron	96-100	iron responsive element binding protein 2	Homo sapiens	43-47
16850017-1	2006	Iron regulatory proteins 1 and 2 (IRP1 and IRP2) are mammalian proteins that register cytosolic iron concentrations and post-transcriptionally regulate expression of iron metabolism genes to optimize cellular iron availability.	Iron	166-170	iron responsive element binding protein 2	Homo sapiens	43-47
16850017-1	2006	Iron regulatory proteins 1 and 2 (IRP1 and IRP2) are mammalian proteins that register cytosolic iron concentrations and post-transcriptionally regulate expression of iron metabolism genes to optimize cellular iron availability.	Iron	166-170	iron responsive element binding protein 2	Homo sapiens	43-47
16850017-4	2006	Although IRP2 is homologous to IRP1, IRP2 activity is regulated primarily by iron-dependent degradation through the ubiquitin-proteasomal system in iron-replete cells.	Iron	77-81	iron responsive element binding protein 2	Homo sapiens	37-41
16850017-4	2006	Although IRP2 is homologous to IRP1, IRP2 activity is regulated primarily by iron-dependent degradation through the ubiquitin-proteasomal system in iron-replete cells.	Iron	148-152	iron responsive element binding protein 2	Homo sapiens	37-41
16850017-5	2006	Targeted deletions of IRP1 and IRP2 in animals have demonstrated that IRP2 is the chief physiologic iron sensor.	Iron	100-104	iron responsive element binding protein 2	Homo sapiens	31-35
16850017-5	2006	Targeted deletions of IRP1 and IRP2 in animals have demonstrated that IRP2 is the chief physiologic iron sensor.	Iron	100-104	iron responsive element binding protein 2	Homo sapiens	70-74
16679315-1	2006	In mammalian cells, iron homeostasis is largely regulated by post-transcriptional control of gene expression through the binding of iron-regulatory proteins (IRP1 and IRP2) to iron-responsive elements (IREs) contained in the untranslated regions of target mRNAs.	Iron	20-24	iron responsive element binding protein 2	Homo sapiens	167-171
16679315-1	2006	In mammalian cells, iron homeostasis is largely regulated by post-transcriptional control of gene expression through the binding of iron-regulatory proteins (IRP1 and IRP2) to iron-responsive elements (IREs) contained in the untranslated regions of target mRNAs.	Iron	132-136	iron responsive element binding protein 2	Homo sapiens	167-171
16679315-2	2006	IRP2 is the dominant iron sensor in mammalian cells under normoxia, but IRP1 is the more ancient protein in evolutionary terms and has an additional function as a cytosolic aconitase.	Iron	21-25	iron responsive element binding protein 2	Homo sapiens	0-4
16503547-1	2006	BACKGROUND AND OBJECTIVES: The functions of the iron regulatory proteins (IRP1 and IRP2), which control cellular iron homeostasis are similar but not identical.	Iron	48-52	iron responsive element binding protein 2	Homo sapiens	83-87
16503547-1	2006	BACKGROUND AND OBJECTIVES: The functions of the iron regulatory proteins (IRP1 and IRP2), which control cellular iron homeostasis are similar but not identical.	Iron	113-117	iron responsive element binding protein 2	Homo sapiens	83-87
16503547-10	2006	INTERPRETATION AND CONCLUSIONS: These findings of the first extensive investigation of the comparative expression of the two IRP in human tissues and blood cells indicate that IRP2 is the major regulator of intracellular iron homeostasis in humans.	Iron	221-225	iron responsive element binding protein 2	Homo sapiens	176-180
16479012-0	2006	Sodium nitroprusside promotes IRP2 degradation via an increase in intracellular iron and in the absence of S nitrosylation at C178.	Nitroprusside	0-20	iron responsive element binding protein 2	Homo sapiens	30-34
16479012-1	2006	In iron-replete cells the posttranscriptional regulator IRP2 undergoes ubiquitination and proteasomal degradation.	Iron	3-7	iron responsive element binding protein 2	Homo sapiens	56-60
16479012-5	2006	Surprisingly, we show that IRP2 bearing a C178S mutation or a Delta73 deletion is sensitive to degradation not only by ferric ammonium citrate (FAC) but also by SNP.	ferric ammonium citrate	119-142	iron responsive element binding protein 2	Homo sapiens	27-31
16479012-7	2006	Actinomycin D, cycloheximide, succinylacetone, and dimethyl-oxalylglycine antagonize IRP2 degradation in response to both FAC and SNP, suggesting a common mechanistic basis.	Dactinomycin	0-13	iron responsive element binding protein 2	Homo sapiens	85-89
16479012-7	2006	Actinomycin D, cycloheximide, succinylacetone, and dimethyl-oxalylglycine antagonize IRP2 degradation in response to both FAC and SNP, suggesting a common mechanistic basis.	Cycloheximide	15-28	iron responsive element binding protein 2	Homo sapiens	85-89
16479012-7	2006	Actinomycin D, cycloheximide, succinylacetone, and dimethyl-oxalylglycine antagonize IRP2 degradation in response to both FAC and SNP, suggesting a common mechanistic basis.	succinylacetone	30-45	iron responsive element binding protein 2	Homo sapiens	85-89
16479012-7	2006	Actinomycin D, cycloheximide, succinylacetone, and dimethyl-oxalylglycine antagonize IRP2 degradation in response to both FAC and SNP, suggesting a common mechanistic basis.	oxalylglycine	51-73	iron responsive element binding protein 2	Homo sapiens	85-89
16479012-10	2006	Collectively, these results suggest that IRP2 degradation by SNP does not require S nitrosylation but rather represents a response to iron loading.	Iron	134-138	iron responsive element binding protein 2	Homo sapiens	41-45
16819431-1	2006	The iron regulatory proteins (IRP1 and IRP2) are two cytoplasmic RNA-binding proteins that control iron metabolism in mammalian cells.	Iron	4-8	iron responsive element binding protein 2	Homo sapiens	39-43
16819431-1	2006	The iron regulatory proteins (IRP1 and IRP2) are two cytoplasmic RNA-binding proteins that control iron metabolism in mammalian cells.	Iron	99-103	iron responsive element binding protein 2	Homo sapiens	39-43
15831703-9	2005	We postulate that IRP2 mutations or deletions may be a cause of refractory microcytic anemia and bone marrow iron depletion in patients with normal transferrin saturations, elevated serum ferritins, elevated red cell protoporphyrin IX levels, and adult-onset neurodegeneration.	Iron	109-113	iron responsive element binding protein 2	Homo sapiens	18-22
15831703-9	2005	We postulate that IRP2 mutations or deletions may be a cause of refractory microcytic anemia and bone marrow iron depletion in patients with normal transferrin saturations, elevated serum ferritins, elevated red cell protoporphyrin IX levels, and adult-onset neurodegeneration.	protoporphyrin IX	217-234	iron responsive element binding protein 2	Homo sapiens	18-22
16464747-6	2006	Consequently performed mutation analyses in genes involved in brain iron metabolism lead to the discovery of specific mutations in the ferritin-H, IRP2 and HFE gene in single PD patients.	Iron	68-72	iron responsive element binding protein 2	Homo sapiens	147-151