PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32976958-7 2020 Both HFD-fed mice and PA/OA-induced HepG2 cells displayed ferroptosis-based panel of biomarkers such as iron overload with the up-regulation of TFR1 and the down-regulation of FTH1, lipid peroxidation and inhibition of Nrf2 activity, which further induced GPX4 and HO-1 levels. Iron 104-108 ferritin heavy chain 1 Homo sapiens 176-180 33061378-10 2020 The transfected cells showed higher intracellular iron accumulation and resulted in a lower MR T2-weighted imaging (T2WI) intensity, suggesting that the transfection of AFP@Fth could be a potential strategy for early diagnosis of liver cancer. Iron 50-54 ferritin heavy chain 1 Homo sapiens 173-176 31701665-0 2019 ROS-Mediated Apoptosis and Anticancer Effect Achieved by Artesunate and Auxiliary Fe(II) Released from Ferriferous Oxide-Containing Recombinant Apoferritin. Iron 82-88 ferritin heavy chain 1 Homo sapiens 144-155 32432042-3 2020 Here, we demonstrate that the alteration of iron homeostasis and the consequent increase of redox metabolism, mediated by the stable knock down of ferritin heavy chain (FtH), enhances the expression of CXCR4 in K562 erythroleukemia cells, thus promoting CXCL12-mediated motility. Iron 44-48 ferritin heavy chain 1 Homo sapiens 147-167 32432042-3 2020 Here, we demonstrate that the alteration of iron homeostasis and the consequent increase of redox metabolism, mediated by the stable knock down of ferritin heavy chain (FtH), enhances the expression of CXCR4 in K562 erythroleukemia cells, thus promoting CXCL12-mediated motility. Iron 44-48 ferritin heavy chain 1 Homo sapiens 169-172 32432042-11 2020 The effects of FtH dysregulation on CXCR4/CXCL12-mediated K562 cell motility extend the meaning of iron homeostasis in the leukemia cell microenvironment. Iron 99-103 ferritin heavy chain 1 Homo sapiens 15-18 32336023-7 2020 By 60 minutes, notable changes included phosphosites significantly changing on p53 (P04637), CAD protein (P27708), and proteins important for iron homeostasis, such as FTH1 (P02794), HMOX1 (P09601), and PCBP1 (Q15365). Iron 142-146 ferritin heavy chain 1 Homo sapiens 168-172 32810738-8 2020 FTMT and ferritin heavy chain (FTH) cooperated to protect macrophages from RSL-3-induced ferroptosis under hypoxia as this form of cell death is linked to iron metabolism. Iron 155-159 ferritin heavy chain 1 Homo sapiens 9-29 32810738-8 2020 FTMT and ferritin heavy chain (FTH) cooperated to protect macrophages from RSL-3-induced ferroptosis under hypoxia as this form of cell death is linked to iron metabolism. Iron 155-159 ferritin heavy chain 1 Homo sapiens 31-34 31701665-3 2019 To overcome this problem, a recombinant apoferritin nanocarrier containing ferriferous oxide (M-HFn) is constructed to produce auxiliary exogenous Fe(II) when delivering AS to cancer cells. Iron 147-153 ferritin heavy chain 1 Homo sapiens 40-51 31401526-7 2019 Moreover, significantly changed expression of TFRC, FTL and FTH1 hinted that dysfunction of iron uptake and storage is a major inducer of ferroptosis. Iron 92-96 ferritin heavy chain 1 Homo sapiens 60-64 31507082-10 2019 Ferritin heavy chain 1 (FTH1) and transferrin receotor protein 1 (TFR1), both of which are critical for iron metabolism, were markedly up-regulated in HCC cells treated with erastin and sorafenib, whereas knockdown of S1R inhibited these increases. Iron 104-108 ferritin heavy chain 1 Homo sapiens 0-22 31507082-10 2019 Ferritin heavy chain 1 (FTH1) and transferrin receotor protein 1 (TFR1), both of which are critical for iron metabolism, were markedly up-regulated in HCC cells treated with erastin and sorafenib, whereas knockdown of S1R inhibited these increases. Iron 104-108 ferritin heavy chain 1 Homo sapiens 24-28 31059232-1 2019 We report a method where the refractive index increments of an iron storage protein, ferritin, and apoferritin (ferritin minus iron) were measured over the wavelength range of 450-678 nm to determine the average iron content of the protein. Iron 127-131 ferritin heavy chain 1 Homo sapiens 99-110 31059232-1 2019 We report a method where the refractive index increments of an iron storage protein, ferritin, and apoferritin (ferritin minus iron) were measured over the wavelength range of 450-678 nm to determine the average iron content of the protein. Iron 127-131 ferritin heavy chain 1 Homo sapiens 99-110 32255103-0 2019 Simultaneous sensing of ferritin and apoferritin proteins using an iron-responsive dye and evaluation of physiological parameters associated with serum iron estimation. Iron 67-71 ferritin heavy chain 1 Homo sapiens 37-48 32255103-1 2019 An iron-responsive optical probe has been developed for simultaneous sensing of both ferritin and apoferritin proteins at pH 7.4 in water. Iron 3-7 ferritin heavy chain 1 Homo sapiens 98-109 32255103-3 2019 In contrast, apoferritin dissociates the preformed iron complex and revives the green colored fluorescence of the native probe (turn-on signal). Iron 51-55 ferritin heavy chain 1 Homo sapiens 13-24 30325535-7 2019 The gene signature designed from AML patients overexpressing FTH1 revealed a significant enrichment in genes of the immune and inflammatory response including Nf-KB pathway, oxidative stress, or iron pathways. Iron 195-199 ferritin heavy chain 1 Homo sapiens 61-65 30019062-2 2018 Upon iron removal, apoferritin was shown to allow the encapsulation of an artificial transfer hydrogenase (ATHase) based on the streptavidin-biotin technology. Iron 5-9 ferritin heavy chain 1 Homo sapiens 19-30 30881642-1 2019 We took advantage of the iron binding affinity of apoferritin to immobilize iron-sulfur clusters into apoferritin up to 312 moieties per protein, with a loading rate as high as 25 wt%. Iron 25-29 ferritin heavy chain 1 Homo sapiens 50-61 30881642-1 2019 We took advantage of the iron binding affinity of apoferritin to immobilize iron-sulfur clusters into apoferritin up to 312 moieties per protein, with a loading rate as high as 25 wt%. Iron 25-29 ferritin heavy chain 1 Homo sapiens 102-113 30881642-1 2019 We took advantage of the iron binding affinity of apoferritin to immobilize iron-sulfur clusters into apoferritin up to 312 moieties per protein, with a loading rate as high as 25 wt%. Iron 76-80 ferritin heavy chain 1 Homo sapiens 50-61 30881642-1 2019 We took advantage of the iron binding affinity of apoferritin to immobilize iron-sulfur clusters into apoferritin up to 312 moieties per protein, with a loading rate as high as 25 wt%. Iron 76-80 ferritin heavy chain 1 Homo sapiens 102-113 30046590-7 2018 The R2 value was significantly increased in MSCs-FTH1 and Neurons-FTH1 cells, which was consistent with the findings of Prussian blue staining, transmission electron microscopy, and intracellular iron measurements. Iron 196-200 ferritin heavy chain 1 Homo sapiens 49-53 30046590-7 2018 The R2 value was significantly increased in MSCs-FTH1 and Neurons-FTH1 cells, which was consistent with the findings of Prussian blue staining, transmission electron microscopy, and intracellular iron measurements. Iron 196-200 ferritin heavy chain 1 Homo sapiens 66-70 28622511-3 2017 Here, we demonstrate that induction of the iron-sequestering ferritin H chain (FTH) in response to polymicrobial infections is critical to establish disease tolerance to sepsis. Iron 43-47 ferritin heavy chain 1 Homo sapiens 61-77 29279245-0 2018 An optimized low-cost protocol for standardized production of iron-free apoferritin nanocages with high protein recovery and suitable conformation for nanotechnological applications. Iron 62-66 ferritin heavy chain 1 Homo sapiens 72-83 29279245-2 2018 Elimination of iron atoms to obtain the empty protein called apoferritin is the first step to use this organic shell as a nanoreactor for different nanotechnological applications. Iron 15-19 ferritin heavy chain 1 Homo sapiens 61-72 29019009-7 2018 The released FTH1 appears in the form of an oligomer with a molecular mass of approximately 480 kDa, which is able to bind iron. Iron 123-127 ferritin heavy chain 1 Homo sapiens 13-17 28583206-16 2017 Mosquitoes respond to viral infection, by inducing expression of heavy chain ferritin, which sequesters available iron, reducing its availability to virus infected cells. Iron 114-118 ferritin heavy chain 1 Homo sapiens 65-76 29580991-3 2018 Recently, ferritin heavy chain (FTH1) has been characterized to reinforce the HIF-1 signaling pathway in an indirect way through the inhibition of PHD activity by depleting the free iron pool in the cytoplasm. Iron 182-186 ferritin heavy chain 1 Homo sapiens 10-30 29580991-3 2018 Recently, ferritin heavy chain (FTH1) has been characterized to reinforce the HIF-1 signaling pathway in an indirect way through the inhibition of PHD activity by depleting the free iron pool in the cytoplasm. Iron 182-186 ferritin heavy chain 1 Homo sapiens 32-36 29368506-1 2018 Apoferritin (AF) is a natural nontoxic iron carrier and has a natural hollow structure that can be used to deliver small molecules. Iron 39-43 ferritin heavy chain 1 Homo sapiens 0-11 28476795-7 2017 Real time quantitative polymerase chain reaction showed that iron up-regulated the expression of FTH1 and iron chelator DFOM reduced FTH1 expression of MCF-7 and MDA-MB-231 cells. Iron 61-65 ferritin heavy chain 1 Homo sapiens 97-101 28476795-7 2017 Real time quantitative polymerase chain reaction showed that iron up-regulated the expression of FTH1 and iron chelator DFOM reduced FTH1 expression of MCF-7 and MDA-MB-231 cells. Iron 106-110 ferritin heavy chain 1 Homo sapiens 133-137 28622511-3 2017 Here, we demonstrate that induction of the iron-sequestering ferritin H chain (FTH) in response to polymicrobial infections is critical to establish disease tolerance to sepsis. Iron 43-47 ferritin heavy chain 1 Homo sapiens 79-82 28622511-4 2017 The protective effect of FTH is exerted via a mechanism that counters iron-driven oxidative inhibition of the liver glucose-6-phosphatase (G6Pase), and in doing so, sustains endogenous glucose production via liver gluconeogenesis. Iron 70-74 ferritin heavy chain 1 Homo sapiens 25-28 28216608-8 2017 The multivariate statistical analysis indicated an iron-related 10-protein panel effective in separating non-cancerous from cancerous lesions including STAT5, STAT5_pY694, myeloid differentiation factor 88 (MYD88), CD74, iron exporter ferroportin (FPN), high mobility group box 1 (HMGB1), STAT3_pS727, TFRC, ferritin heavy chain (FTH), and ferritin light chain (FTL). Iron 51-55 ferritin heavy chain 1 Homo sapiens 308-328 28216608-8 2017 The multivariate statistical analysis indicated an iron-related 10-protein panel effective in separating non-cancerous from cancerous lesions including STAT5, STAT5_pY694, myeloid differentiation factor 88 (MYD88), CD74, iron exporter ferroportin (FPN), high mobility group box 1 (HMGB1), STAT3_pS727, TFRC, ferritin heavy chain (FTH), and ferritin light chain (FTL). Iron 51-55 ferritin heavy chain 1 Homo sapiens 330-333 27873495-7 2017 RESULTS: Cell pellet imaging of Ad-hFTH in vitro showed a strong negatively enhanced contrast in T2w and T2*w images, presenting with darker signal intensity in high concentrations of Fe. Iron 184-186 ferritin heavy chain 1 Homo sapiens 35-39 27206843-8 2016 Overall, our data support a model of neurotoxicity where Pb enhances iron regulatory protein/IRE-mediated repression of APP and FTH translation. Iron 69-73 ferritin heavy chain 1 Homo sapiens 128-131 27671803-3 2016 METHODS AND RESULTS: We designed and developed a chimeric construct encoding for both of iron-binding human ferritin heavy chain (hFTH) controlled by the beta-catenin-responsive TCF/lymphoid-enhancer binding factor (Lef) promoter and constitutively expressed green fluorescent protein (GFP). Iron 89-93 ferritin heavy chain 1 Homo sapiens 108-128 27671803-3 2016 METHODS AND RESULTS: We designed and developed a chimeric construct encoding for both of iron-binding human ferritin heavy chain (hFTH) controlled by the beta-catenin-responsive TCF/lymphoid-enhancer binding factor (Lef) promoter and constitutively expressed green fluorescent protein (GFP). Iron 89-93 ferritin heavy chain 1 Homo sapiens 130-134 25448225-5 2015 The transduction of FTH led to a significant enhancement in cellular iron storage capacity and caused hypointensity and a significant increase in R2 * values of FTH-hMSC-collected phantoms and FTH-hMSC-transplanted sites of the brain, as shown by in vitro and in vivo MRI performed at 9.4 T, compared with control hMSCs. Iron 69-73 ferritin heavy chain 1 Homo sapiens 20-23 26625322-6 2016 In addition, iron-response protein (IRP-1) regulatory loop was overridden by DFP as reflected by resumed level of ferritin (FTH) back to basal level and the attenuated transferrin receptor (TSFR) mRNA level suppression thereby reducing further iron uptake. Iron 13-17 ferritin heavy chain 1 Homo sapiens 124-127 26774668-10 2016 These include a single base deletion mutation in the ferritin heavy chain gene (FTH1) resulting in a frame shift and protein truncation in TK6 that impairs iron metabolism. Iron 156-160 ferritin heavy chain 1 Homo sapiens 53-73 26774668-10 2016 These include a single base deletion mutation in the ferritin heavy chain gene (FTH1) resulting in a frame shift and protein truncation in TK6 that impairs iron metabolism. Iron 156-160 ferritin heavy chain 1 Homo sapiens 80-84 25993535-7 2015 FTH-DCs exhibited increased iron storage capacity, and displayed a significantly higher transverse relaxation rate (R2*) as compared to DCs in phantom. Iron 28-32 ferritin heavy chain 1 Homo sapiens 0-3 27142241-5 2016 Many nuclear processes are influenced by a spatial switch involving the proteins {KPNA2, KPNB1, PCNA, PTMA, SET} and heme/iron proteins HMOX1 and FTH1. Iron 122-126 ferritin heavy chain 1 Homo sapiens 146-150 26886577-1 2016 Ferritin is a sub-family of iron binding proteins that form multi-subunit nanotype iron storage structures and prevent oxidative stress induced apoptosis. Iron 28-32 ferritin heavy chain 1 Homo sapiens 0-8 26886577-1 2016 Ferritin is a sub-family of iron binding proteins that form multi-subunit nanotype iron storage structures and prevent oxidative stress induced apoptosis. Iron 83-87 ferritin heavy chain 1 Homo sapiens 0-8 26423448-9 2015 Our results support the role of FHC in neutralizing the iron toxicity as well as mediating the protective effect of HO-1 in response to oxidative stress. Iron 56-60 ferritin heavy chain 1 Homo sapiens 32-35 25685985-3 2015 This protein captures huge amounts of iron ions inside the apoferritin shell and isolates them from the environment. Iron 38-42 ferritin heavy chain 1 Homo sapiens 59-70 24742827-1 2014 Ferritin heavy chain (FTH1) is a 21-kDa subunit of the ferritin complex, known for its role in iron metabolism, and which has recently been identified as a favorable prognostic protein for triple negative breast cancer (TNBC) patients. Iron 95-99 ferritin heavy chain 1 Homo sapiens 0-20 25378496-9 2015 Taken together, these results suggest that PK1 prevents apoferritin from iron loading, and thus stabilizes the cellular LIP levels, and that WSSV uses this novel mechanism to counteract the host cell"s iron-withholding defense mechanism. Iron 73-77 ferritin heavy chain 1 Homo sapiens 56-67 25378496-13 2015 PK1 interacts with both ferritin and apoferritin, suppresses apoferritin"s ability to sequester free iron ions, and maintains the intracellular labile iron pool (LIP), and thus the availability of free iron is increased within cells. Iron 101-105 ferritin heavy chain 1 Homo sapiens 61-72 25370199-2 2015 Although recombinant human apoferritin (HuFtH) rapidly oxidizes Fe(II) to Fe(III) , this iron is not properly stored in the ferritin cavity, as otherwise occurs in horse-spleen H/L-apoferritin (HsFt; H=heavy subunit, L=light subunit). Iron 89-93 ferritin heavy chain 1 Homo sapiens 27-38 25265351-8 2014 Along with it, in cell of lines of basal subtype MDA-MB-231 and MDA-MB-468, high level of FTH (254 +- 2.3 and 270 +- 1.9) is being detected in consequence of increase of level of free iron, ROS (11.3 +- 1.05 and 7.27 +- 0.26) and SOD (9.4 +- 0.24 and 8.5 +- 0.18) as well as decrease of expression of microRNA 200b. Iron 184-188 ferritin heavy chain 1 Homo sapiens 90-93 24742827-1 2014 Ferritin heavy chain (FTH1) is a 21-kDa subunit of the ferritin complex, known for its role in iron metabolism, and which has recently been identified as a favorable prognostic protein for triple negative breast cancer (TNBC) patients. Iron 95-99 ferritin heavy chain 1 Homo sapiens 22-26 24124891-5 2014 While heme catabolism by heme oxygenase-1 (HO-1) prevents programmed cell death, this cytoprotective effect requires the co-expression of ferritin H (heart/heavy) chain (FTH), which controls the pro-oxidant effect of labile Fe released from the protoporphyrin IX ring of heme. Iron 224-226 ferritin heavy chain 1 Homo sapiens 170-173 24124891-6 2014 This antioxidant effect of FTH restrains JNK activation, whereas JNK activation inhibits FTH expression, a cross talk that controls metabolic adaptation to cellular Fe overload associated with systemic infections. Iron 165-167 ferritin heavy chain 1 Homo sapiens 27-30 24124891-7 2014 CRITICAL ISSUES AND FUTURE DIRECTIONS: Identification and characterization of the mechanisms via which FTH provides metabolic adaptation to tissue Fe overload should provide valuable information to our current understanding of the pathogenesis of systemic infections as well as other immune-mediated inflammatory diseases. Iron 147-149 ferritin heavy chain 1 Homo sapiens 103-106 24007662-8 2013 The elevation of ferritin (FTL, FTH1) may indicate an iron-mediated oxidative imbalance aggravating the mitochondrial failure and neurotoxicity. Iron 54-58 ferritin heavy chain 1 Homo sapiens 32-36 24734754-5 2014 In addition, we applied a ferritin/apoferritin blended monolayer to the study of iron mineralization and revealed that biomineralization in this system is spatially selective. Iron 81-85 ferritin heavy chain 1 Homo sapiens 35-46 24401274-6 2014 Transfection of a CXCR4-expressing human cell line with an iron-deficient FHC mutant confirmed that increased FHC expression deregulated CXCR4 signaling and that this function of FHC was independent of iron binding. Iron 59-63 ferritin heavy chain 1 Homo sapiens 74-77 24401274-6 2014 Transfection of a CXCR4-expressing human cell line with an iron-deficient FHC mutant confirmed that increased FHC expression deregulated CXCR4 signaling and that this function of FHC was independent of iron binding. Iron 59-63 ferritin heavy chain 1 Homo sapiens 110-113 23940258-6 2013 Increased iron incorporation into the FtH homopolymer leads to reduced cellular iron availability, diminished levels of cytosolic catalase, SOD1 protein levels, enhanced ROS production and higher levels of oxidized proteins. Iron 80-84 ferritin heavy chain 1 Homo sapiens 38-41 23940258-6 2013 Increased iron incorporation into the FtH homopolymer leads to reduced cellular iron availability, diminished levels of cytosolic catalase, SOD1 protein levels, enhanced ROS production and higher levels of oxidized proteins. Iron 10-14 ferritin heavy chain 1 Homo sapiens 38-41 22975354-3 2012 Real-time PCR analyses of the human PDL revealed abundant expression of ferritin light polypeptide (FTL) and ferritin heavy polypeptide (FTH), which encode the highly-conserved iron storage protein, ferritin. Iron 177-181 ferritin heavy chain 1 Homo sapiens 109-135 23801774-9 2013 RESULTS: CV1-FHC fibroblasts (vs CV1 fibroblasts) showed enhanced iron uptake (1.8 mmol +- 0.5 x 10(-8) vs 0.9 mmol +- 0.5 x 10(-8); P < .05), retention (1.6 mmol +- 0.5 x 10(-8) vs 0.5 mmol +- 0.5 x 10(-8), P < .05), and cell density-dependent R2 contrast. Iron 66-70 ferritin heavy chain 1 Homo sapiens 13-16 22975354-3 2012 Real-time PCR analyses of the human PDL revealed abundant expression of ferritin light polypeptide (FTL) and ferritin heavy polypeptide (FTH), which encode the highly-conserved iron storage protein, ferritin. Iron 177-181 ferritin heavy chain 1 Homo sapiens 137-140 21029774-5 2011 We show here the facile assembly of Mt-FTL and FTH1 subunits into soluble ferritin heteropolymers, but their ability to incorporate iron was significantly reduced relative to Wt-FTL/FTH1 heteropolymers. Iron 132-136 ferritin heavy chain 1 Homo sapiens 47-51 21029774-6 2011 In addition, Mt-FTL/FTH1 heteropolymers formed aggregates during iron loading, contrasting Wt-FTL/FTH1 heteropolymers and similar to what was seen for Mt-FTL homopolymers. Iron 65-69 ferritin heavy chain 1 Homo sapiens 20-24 19818853-3 2010 Here, we tested potential neuroprotection via genetic expression of the iron chelator human ferritin heavy chain (H-ferritin). Iron 72-76 ferritin heavy chain 1 Homo sapiens 92-112 20390345-7 2011 The up-regulation of ferritin light chain and ferritin heavy chain in MDA-MB-231 cells was accompanied by alterations in the subcellular distribution of these proteins as characterized by an increased level of nuclear ferritin and a lower level of the cellular labile iron pool as compared to MCF-7 cells. Iron 268-272 ferritin heavy chain 1 Homo sapiens 46-66 20823165-6 2010 Iron accumulation was observed in myc-hFTH cells and tumors by Prussian blue staining and iron binding assays. Iron 0-4 ferritin heavy chain 1 Homo sapiens 38-42 20823165-6 2010 Iron accumulation was observed in myc-hFTH cells and tumors by Prussian blue staining and iron binding assays. Iron 90-94 ferritin heavy chain 1 Homo sapiens 38-42 20586408-4 2010 In this work, the processes of accumulation and incorporation of organometallic palladium complexes within the cage of the iron storage protein apo-ferritin (apo-Fr) are elucidated by analysis of X-ray crystal structures of apo-Fr and selected mutants thereof, in the presence of the metal complexes. Iron 123-127 ferritin heavy chain 1 Homo sapiens 144-156 19258503-5 2009 We show that inhibition of constitutively active NF-kappaB causes down-regulation of ferritin heavy chain (FHC) that leads to an increase of free intracellular iron, which, in turn, induces massive generation of ROS. Iron 160-164 ferritin heavy chain 1 Homo sapiens 85-105 19855093-9 2009 In addition to its well known iron storage role, FTH1 has been shown to protect the nucleus from oxidative damage. Iron 30-34 ferritin heavy chain 1 Homo sapiens 49-53 19290800-4 2009 FTH generated MRI contrast through compensatory upregulation of transferrin receptor (Tfrc) that led to increased cellular iron stored in ferritin-bound form. Iron 123-127 ferritin heavy chain 1 Homo sapiens 0-3 21314673-5 2009 The iron exporter ferroportin is downregulated within 1-6 h, followed by downregulation of transferrin receptor-1 (TfR1) and ferritin heavy chain (H-ferritin) mainly after 24-48 h. The hemochromatosis protein-1, a ligand of TfR1, peaked after 24 h. All effects were independent of iron supply with the exception of H-ferritin, which was restored by excess iron. Iron 4-8 ferritin heavy chain 1 Homo sapiens 125-145 19258503-5 2009 We show that inhibition of constitutively active NF-kappaB causes down-regulation of ferritin heavy chain (FHC) that leads to an increase of free intracellular iron, which, in turn, induces massive generation of ROS. Iron 160-164 ferritin heavy chain 1 Homo sapiens 107-110 18160403-4 2008 FTL and FTH are regulated primarily at a post-transcriptional level in response to cellular iron concentrations. Iron 92-96 ferritin heavy chain 1 Homo sapiens 8-11 19317403-4 2009 In this Article, we report on the detailed processes of accumulation of Pd(II) ions demonstrated by a series of X-ray crystal structural analyses of apo-ferritin (apo-Fr), an iron storage protein, containing different amounts of Pd(II) ions in the protein cage. Iron 175-179 ferritin heavy chain 1 Homo sapiens 149-161 18270695-3 2008 In this article, a systematic study of diffusive dynamics of ferritin and apoferritin (=ferritin without iron core) is presented. Iron 105-109 ferritin heavy chain 1 Homo sapiens 74-85 18160403-7 2008 We have designed a quantitative assay system sensitive enough to detect differences between FTL and FTH iron regulatory elements (IREs) that a standard electrophoretic mobility shift assay does not. Iron 104-108 ferritin heavy chain 1 Homo sapiens 100-103 18160403-9 2008 These results provide evidence that FTL and FTH subunits respond independently to cellular iron concentrations and underscore the importance of evaluating FTL and FTH IREs separately. Iron 91-95 ferritin heavy chain 1 Homo sapiens 44-47 17434931-4 2007 Here, we demonstrate that ferritin heavy chain (FHC), a core subunit of iron-binding protein ferritin, works as an anti-apoptotic protein against toxic asbestos and oxidative stress in human mesothelial cells and MM cells. Iron 72-76 ferritin heavy chain 1 Homo sapiens 26-46 17434931-4 2007 Here, we demonstrate that ferritin heavy chain (FHC), a core subunit of iron-binding protein ferritin, works as an anti-apoptotic protein against toxic asbestos and oxidative stress in human mesothelial cells and MM cells. Iron 72-76 ferritin heavy chain 1 Homo sapiens 48-51 15901240-7 2005 However, by 24 h, both iron import and iron export were significantly inhibited, coinciding with an induction of ferritin heavy chain (P<0.05) and a decrease in DMT-1 and IREG-1 to baseline levels. Iron 23-27 ferritin heavy chain 1 Homo sapiens 113-133 15901240-7 2005 However, by 24 h, both iron import and iron export were significantly inhibited, coinciding with an induction of ferritin heavy chain (P<0.05) and a decrease in DMT-1 and IREG-1 to baseline levels. Iron 39-43 ferritin heavy chain 1 Homo sapiens 113-133 15611622-6 2004 Suppression of ROS by NF-kappaB is mediated by Ferritin heavy chain (FHC)--the primary iron-storage mechanism in cells--and possibly, by the mitochondrial enzyme Mn++ superoxide dismutase (Mn-SOD). Iron 87-91 ferritin heavy chain 1 Homo sapiens 47-67 15611622-6 2004 Suppression of ROS by NF-kappaB is mediated by Ferritin heavy chain (FHC)--the primary iron-storage mechanism in cells--and possibly, by the mitochondrial enzyme Mn++ superoxide dismutase (Mn-SOD). Iron 87-91 ferritin heavy chain 1 Homo sapiens 69-72 12504902-5 2003 Incubation of apoferritin with 1-10mM ALA produced dose-dependent decreases in tryptophan fluorescence (11-35% after 5h), and a partial depletion of protein thiols (18% after 24h) despite substantial removal of catalytic iron. Iron 221-225 ferritin heavy chain 1 Homo sapiens 14-25 15537542-6 2004 FHC-mediated inhibition of JNK signaling depends on suppressing ROS accumulation and is achieved through iron sequestration. Iron 105-109 ferritin heavy chain 1 Homo sapiens 0-3 12504902-7 2003 The damage to apoferritin had no effect on ferroxidase activity, but produced a 61% decrease in iron uptake ability. Iron 96-100 ferritin heavy chain 1 Homo sapiens 14-25 11333118-10 2001 This notion was further supported by the finding that endocytosis of apoferritin, added to the medium, stabilized lysosomes (P <0.001 versus P <0.01) and increased survival (P <0.01 versus P <0.05) of iron-loaded A549 and BEAS-2B cells. Iron 213-217 ferritin heavy chain 1 Homo sapiens 69-80 11595385-4 2001 The stoichiometry of Fe(II) oxidation by apoferritin in an unbuffered solution of 50 mM NaCl, pH 7.0, was approximately 3.1 Fe(II)/O(2) at all iron-to-protein ratios tested. Iron 143-147 ferritin heavy chain 1 Homo sapiens 41-52 11595385-0 2001 The consequences of hydroxyl radical formation on the stoichiometry and kinetics of ferrous iron oxidation by human apoferritin. Iron 84-96 ferritin heavy chain 1 Homo sapiens 116-127 11415455-5 2001 Ferritin is a 24 subunit protein composed of two subunit types, termed H and L. The ferritin H subunit has a potent ferroxidase activity that catalyses the oxidation of ferrous iron, whereas ferritin L plays a role in iron nucleation and protein stability. Iron 177-181 ferritin heavy chain 1 Homo sapiens 84-102 11415455-5 2001 Ferritin is a 24 subunit protein composed of two subunit types, termed H and L. The ferritin H subunit has a potent ferroxidase activity that catalyses the oxidation of ferrous iron, whereas ferritin L plays a role in iron nucleation and protein stability. Iron 218-222 ferritin heavy chain 1 Homo sapiens 84-102 11333118-11 2001 Assuming that primary cell lines of the alveolar and bronchial epithelium behave in a similar manner as these respiratory cell lines, intrabronchial instillation of apoferritin-containing liposomes may in the future be a treatment for iron-dependent airway inflammatory processes. Iron 235-239 ferritin heavy chain 1 Homo sapiens 165-176 9931300-1 1999 The polypeptide chain that assembles into the unusual dodecameric shell of Listeria innocua apoferritin lacks the ferroxidase centre characteristic of H-type mammalian chains, but is able to catalyse both Fe(II) oxidation and nucleation of the iron core. Iron 244-248 ferritin heavy chain 1 Homo sapiens 92-103 11128746-2 2000 Although the synthesis of iron-free ferritin (apoferritin) provides antioxidant protection, the secretion of iron-containing ferritin by AMs could increase the availability of catalytic iron in the lungs. Iron 26-30 ferritin heavy chain 1 Homo sapiens 46-57 10964660-2 2000 In primary avian erythroblasts undergoing short-term proliferation, however, ferritin heavy chain (ferH) mRNA is repressed at all iron levels. Iron 130-134 ferritin heavy chain 1 Homo sapiens 77-97 10964660-2 2000 In primary avian erythroblasts undergoing short-term proliferation, however, ferritin heavy chain (ferH) mRNA is repressed at all iron levels. Iron 130-134 ferritin heavy chain 1 Homo sapiens 99-103 10964660-3 2000 Yet, expression of v-ErbA oncoprotein is sufficient to reinduce ferH mRNA utilization at physiological iron concentrations. Iron 103-107 ferritin heavy chain 1 Homo sapiens 64-68 10964660-5 2000 Whereas endogenous c-Kit in combination with exogenous EpoR had no significant effect, ectopic overexpression of both receptors abolished translational repression of ferH mRNA upon iron administration. Iron 181-185 ferritin heavy chain 1 Homo sapiens 166-170 9931300-7 1999 The marked inhibitory effect of Tb(III) on the kinetics of iron incorporation confirms that carboxylates provide the iron ligands in L. innocua apoferritin. Iron 117-121 ferritin heavy chain 1 Homo sapiens 144-155 9931300-8 1999 Iron uptake followed in steady-state fluorescence experiments allows one to distinguish Fe(II) binding and oxidation from the subsequent movement of Fe(III) into the apoferritin cavity as in mammalian ferritins despite the different localization of the tryptophan residues. Iron 0-4 ferritin heavy chain 1 Homo sapiens 166-177 9931300-7 1999 The marked inhibitory effect of Tb(III) on the kinetics of iron incorporation confirms that carboxylates provide the iron ligands in L. innocua apoferritin. Iron 59-63 ferritin heavy chain 1 Homo sapiens 144-155 9518065-2 1997 Following autophagocytosis of endogenous ferritin/apoferritin, these compounds may serve as chelators of such lysosomal iron and counteract the occurrence of iron-mediated intralysosomal oxidative reactions. Iron 120-124 ferritin heavy chain 1 Homo sapiens 50-61 9367531-5 1997 The magnitude of this stimulatory effect increased as the molar ratio of ceruloplasmin to apoferritin approached 1.0, shown previously to be the optimum ratio for loading iron into ferritin. Iron 171-175 ferritin heavy chain 1 Homo sapiens 90-101 9367531-6 1997 The rate of ferrous iron oxidation by ceruloplasmin was significantly stimulated by the presence of apoferritin; however, apotransferrin had no effect. Iron 20-24 ferritin heavy chain 1 Homo sapiens 100-111 9518065-2 1997 Following autophagocytosis of endogenous ferritin/apoferritin, these compounds may serve as chelators of such lysosomal iron and counteract the occurrence of iron-mediated intralysosomal oxidative reactions. Iron 158-162 ferritin heavy chain 1 Homo sapiens 50-61 9518065-4 1997 In this study we have shown: (i) human monocyte-derived macrophages to accumulate ferritin in response to iron exposure; (ii) iron to destabilise macrophage secondary lysosomes when the cells are exposed to H2O2; and (iii) endocytosed apoferritin to act as a stabiliser of the acidic vacuolar compartment of iron-loaded macrophages. Iron 126-130 ferritin heavy chain 1 Homo sapiens 235-246 9518065-4 1997 In this study we have shown: (i) human monocyte-derived macrophages to accumulate ferritin in response to iron exposure; (ii) iron to destabilise macrophage secondary lysosomes when the cells are exposed to H2O2; and (iii) endocytosed apoferritin to act as a stabiliser of the acidic vacuolar compartment of iron-loaded macrophages. Iron 126-130 ferritin heavy chain 1 Homo sapiens 235-246 7794895-0 1995 Tyrosyl radical formation during the oxidative deposition of iron in human apoferritin. Iron 61-65 ferritin heavy chain 1 Homo sapiens 75-86 8075594-0 1994 Most free-radical injury is iron-related: it is promoted by iron, hemin, holoferritin and vitamin C, and inhibited by desferoxamine and apoferritin. Iron 28-32 ferritin heavy chain 1 Homo sapiens 136-147 7951057-0 1994 Xanthine oxidase: an efficient promoter of the iron loading of apoferritin. Iron 47-51 ferritin heavy chain 1 Homo sapiens 63-74 7951057-2 1994 These studies demonstrate that xanthine oxidase also efficiently promotes the oxidative incorporation of iron into apoferritin, the major iron storage protein of vertebrates, and that the ferroxidase activity of intestinal xanthine oxidase could be important in determining the fraction of iron within the intestinal mucosa cell partitioned to ferritin versus the iron that remains in a transient pool for rapid transport to plasma. Iron 105-109 ferritin heavy chain 1 Homo sapiens 115-126 7951057-2 1994 These studies demonstrate that xanthine oxidase also efficiently promotes the oxidative incorporation of iron into apoferritin, the major iron storage protein of vertebrates, and that the ferroxidase activity of intestinal xanthine oxidase could be important in determining the fraction of iron within the intestinal mucosa cell partitioned to ferritin versus the iron that remains in a transient pool for rapid transport to plasma. Iron 138-142 ferritin heavy chain 1 Homo sapiens 115-126 7951057-2 1994 These studies demonstrate that xanthine oxidase also efficiently promotes the oxidative incorporation of iron into apoferritin, the major iron storage protein of vertebrates, and that the ferroxidase activity of intestinal xanthine oxidase could be important in determining the fraction of iron within the intestinal mucosa cell partitioned to ferritin versus the iron that remains in a transient pool for rapid transport to plasma. Iron 138-142 ferritin heavy chain 1 Homo sapiens 115-126 7951057-2 1994 These studies demonstrate that xanthine oxidase also efficiently promotes the oxidative incorporation of iron into apoferritin, the major iron storage protein of vertebrates, and that the ferroxidase activity of intestinal xanthine oxidase could be important in determining the fraction of iron within the intestinal mucosa cell partitioned to ferritin versus the iron that remains in a transient pool for rapid transport to plasma. Iron 138-142 ferritin heavy chain 1 Homo sapiens 115-126 1536576-2 1992 It was shown that loading of apoferritin with ferrous ammonium sulfate was dependent on buffer and pH, and was directly related to the rate of iron autoxidation. Iron 143-147 ferritin heavy chain 1 Homo sapiens 29-40 1463463-6 1992 Competition experiments at pH 5.5 demonstrated that L-chain apoferritin is able to incorporate iron only when in the presence of H-chain variants with ferroxidase activity. Iron 95-99 ferritin heavy chain 1 Homo sapiens 60-71 1463463-7 1992 The results indicate that L-chain apoferritin has a higher capacity than the H-chain apoferritin to induce iron-core nucleation, whereas H-chain ferritin is superior in promoting Fe(II) oxidation. Iron 107-111 ferritin heavy chain 1 Homo sapiens 34-45 1463463-7 1992 The results indicate that L-chain apoferritin has a higher capacity than the H-chain apoferritin to induce iron-core nucleation, whereas H-chain ferritin is superior in promoting Fe(II) oxidation. Iron 107-111 ferritin heavy chain 1 Homo sapiens 85-96 1353023-5 1992 Modelling of Fe(III) dimer binding to human H chain apoferritin shows a solvent-accessible site, which resembles that of ribonucleotide reductase in its ligands. Iron 13-15 ferritin heavy chain 1 Homo sapiens 52-63 8338887-7 1993 The affinity of the monoclonal antibody for the ferritin deprived of iron (apoferritin) was higher than that for native ferritin due to the greater conformational flexibility of the apoferritin molecule. Iron 69-73 ferritin heavy chain 1 Homo sapiens 75-86 8338887-7 1993 The affinity of the monoclonal antibody for the ferritin deprived of iron (apoferritin) was higher than that for native ferritin due to the greater conformational flexibility of the apoferritin molecule. Iron 69-73 ferritin heavy chain 1 Homo sapiens 182-193 1536576-7 1992 We suggest that the loading of apoferritin with ferrous ammonium sulfate occurred as a result of iron autoxidation and may result in oxidation of amino acids and loss of integrity of the protein, and that ceruloplasmin may act as a catalyst for the incorporation of iron into apoferritin in a manner more closely related to that occurring in vivo. Iron 97-101 ferritin heavy chain 1 Homo sapiens 31-42 1536576-7 1992 We suggest that the loading of apoferritin with ferrous ammonium sulfate occurred as a result of iron autoxidation and may result in oxidation of amino acids and loss of integrity of the protein, and that ceruloplasmin may act as a catalyst for the incorporation of iron into apoferritin in a manner more closely related to that occurring in vivo. Iron 266-270 ferritin heavy chain 1 Homo sapiens 31-42 1679940-2 1991 The iron-core is gradually built up when FeII is added to apoferritin and allowed to oxidize. Iron 4-8 ferritin heavy chain 1 Homo sapiens 58-69 1581551-5 1992 Defensive mechanisms against iron overload are exhibited by most cell lines and include: (1) the capacity of synthesis of the protein apoferritin by most cells whenever the concentration of ambient iron increases, (2) the capacity to bind toxic inorganic iron within the hollow shell of apoferritin; the transfer of the assembled iron-rich ferritin molecules into siderosomes and (3) the capability of further iron segregation within siderosomes by degradation of ferritin to hemosiderin. Iron 29-33 ferritin heavy chain 1 Homo sapiens 134-145 1581551-5 1992 Defensive mechanisms against iron overload are exhibited by most cell lines and include: (1) the capacity of synthesis of the protein apoferritin by most cells whenever the concentration of ambient iron increases, (2) the capacity to bind toxic inorganic iron within the hollow shell of apoferritin; the transfer of the assembled iron-rich ferritin molecules into siderosomes and (3) the capability of further iron segregation within siderosomes by degradation of ferritin to hemosiderin. Iron 29-33 ferritin heavy chain 1 Homo sapiens 287-298 1581551-5 1992 Defensive mechanisms against iron overload are exhibited by most cell lines and include: (1) the capacity of synthesis of the protein apoferritin by most cells whenever the concentration of ambient iron increases, (2) the capacity to bind toxic inorganic iron within the hollow shell of apoferritin; the transfer of the assembled iron-rich ferritin molecules into siderosomes and (3) the capability of further iron segregation within siderosomes by degradation of ferritin to hemosiderin. Iron 198-202 ferritin heavy chain 1 Homo sapiens 134-145 1581551-5 1992 Defensive mechanisms against iron overload are exhibited by most cell lines and include: (1) the capacity of synthesis of the protein apoferritin by most cells whenever the concentration of ambient iron increases, (2) the capacity to bind toxic inorganic iron within the hollow shell of apoferritin; the transfer of the assembled iron-rich ferritin molecules into siderosomes and (3) the capability of further iron segregation within siderosomes by degradation of ferritin to hemosiderin. Iron 198-202 ferritin heavy chain 1 Homo sapiens 134-145 1581551-5 1992 Defensive mechanisms against iron overload are exhibited by most cell lines and include: (1) the capacity of synthesis of the protein apoferritin by most cells whenever the concentration of ambient iron increases, (2) the capacity to bind toxic inorganic iron within the hollow shell of apoferritin; the transfer of the assembled iron-rich ferritin molecules into siderosomes and (3) the capability of further iron segregation within siderosomes by degradation of ferritin to hemosiderin. Iron 198-202 ferritin heavy chain 1 Homo sapiens 134-145 1581551-5 1992 Defensive mechanisms against iron overload are exhibited by most cell lines and include: (1) the capacity of synthesis of the protein apoferritin by most cells whenever the concentration of ambient iron increases, (2) the capacity to bind toxic inorganic iron within the hollow shell of apoferritin; the transfer of the assembled iron-rich ferritin molecules into siderosomes and (3) the capability of further iron segregation within siderosomes by degradation of ferritin to hemosiderin. Iron 198-202 ferritin heavy chain 1 Homo sapiens 134-145 2065674-0 1991 Uptake of iron by apoferritin from a ferric dihydrolipoate complex. Iron 10-14 ferritin heavy chain 1 Homo sapiens 18-29 2065674-2 1991 The ferric dihydrolipoate complex was chemically synthesized and used as an iron donor to apoferritin. Iron 76-80 ferritin heavy chain 1 Homo sapiens 90-101 2065674-3 1991 Iron uptake was studied, at slightly alkaline pH and in anaerobic conditions, as a function of the concentration of both the iron donor and apoferritin. Iron 0-4 ferritin heavy chain 1 Homo sapiens 140-151 2310509-6 1990 The analytical technique of immobilized metal ion affinity chromatography also shows great promise in the purification of apoferritin, ferritin, and other iron-binding proteins. Iron 155-159 ferritin heavy chain 1 Homo sapiens 122-133 2007131-0 1991 Role of phosphate in initial iron deposition in apoferritin. Iron 29-33 ferritin heavy chain 1 Homo sapiens 48-59 2007131-3 1991 The influence of phosphate on the initial deposition of iron in apoferritin (12 Fe/protein) was investigated by EPR, 57Fe Mossbauer spectroscopy, and equilibrium dialysis. Iron 56-60 ferritin heavy chain 1 Homo sapiens 64-75 2007131-5 1991 The presence of 1 mM phosphate during reconstitution of ferritin from apoferritin, Fe(II), and O2 accelerates the rate of oxidation of the iron 2-fold at pH 7.5. Iron 139-143 ferritin heavy chain 1 Homo sapiens 70-81 34826424-7 2022 In addition, we demonstrated significant FTH1 expression in normal lung cells when compared to lung cancer cells, which prevented iron from playing a role in increasing IR-induced cell death. Iron 130-134 ferritin heavy chain 1 Homo sapiens 41-45 26560363-4 2015 Knockdown of ISCU enhanced the binding of iron regulatory protein 1 (IRP1), a cytosolic Fe-S protein, to an iron-responsive element in the 5" UTR of ferritin heavy polypeptide 1 (FTH1) mRNA and subsequently reduced the translation of FTH1, a major iron storage protein. Iron 42-46 ferritin heavy chain 1 Homo sapiens 149-177 26560363-4 2015 Knockdown of ISCU enhanced the binding of iron regulatory protein 1 (IRP1), a cytosolic Fe-S protein, to an iron-responsive element in the 5" UTR of ferritin heavy polypeptide 1 (FTH1) mRNA and subsequently reduced the translation of FTH1, a major iron storage protein. Iron 42-46 ferritin heavy chain 1 Homo sapiens 179-183 26560363-4 2015 Knockdown of ISCU enhanced the binding of iron regulatory protein 1 (IRP1), a cytosolic Fe-S protein, to an iron-responsive element in the 5" UTR of ferritin heavy polypeptide 1 (FTH1) mRNA and subsequently reduced the translation of FTH1, a major iron storage protein. Iron 42-46 ferritin heavy chain 1 Homo sapiens 234-238 26560363-4 2015 Knockdown of ISCU enhanced the binding of iron regulatory protein 1 (IRP1), a cytosolic Fe-S protein, to an iron-responsive element in the 5" UTR of ferritin heavy polypeptide 1 (FTH1) mRNA and subsequently reduced the translation of FTH1, a major iron storage protein. Iron 108-112 ferritin heavy chain 1 Homo sapiens 149-177 26560363-4 2015 Knockdown of ISCU enhanced the binding of iron regulatory protein 1 (IRP1), a cytosolic Fe-S protein, to an iron-responsive element in the 5" UTR of ferritin heavy polypeptide 1 (FTH1) mRNA and subsequently reduced the translation of FTH1, a major iron storage protein. Iron 108-112 ferritin heavy chain 1 Homo sapiens 179-183 26560363-4 2015 Knockdown of ISCU enhanced the binding of iron regulatory protein 1 (IRP1), a cytosolic Fe-S protein, to an iron-responsive element in the 5" UTR of ferritin heavy polypeptide 1 (FTH1) mRNA and subsequently reduced the translation of FTH1, a major iron storage protein. Iron 108-112 ferritin heavy chain 1 Homo sapiens 234-238 26560363-5 2015 In addition, in response to DNA damage, p53 induced FTH1 and suppressed transferrin receptor, which regulates iron entry into cells. Iron 110-114 ferritin heavy chain 1 Homo sapiens 52-56 34896255-4 2022 When iron atoms are removed apoferritin (AFt) is formed which consists of a hollow shell where it can be used to load guest molecules. Iron 5-9 ferritin heavy chain 1 Homo sapiens 28-39 34896255-4 2022 When iron atoms are removed apoferritin (AFt) is formed which consists of a hollow shell where it can be used to load guest molecules. Iron 5-9 ferritin heavy chain 1 Homo sapiens 41-44 34460113-11 2021 These results indicate that Fth iron storage in astrocytes is vital for early oligodendrocyte development as well as for the remyelination of the CNS. Iron 32-36 ferritin heavy chain 1 Homo sapiens 28-31 34939417-4 2021 These nanoprobes utilize apoferritin (an intracellular protein for iron stores and release) to encase appropriate molecular organic dyes to produce on-demand fluorescence in aqueous solution. Iron 67-71 ferritin heavy chain 1 Homo sapiens 25-36 34965856-0 2021 FTH promotes the proliferation and renders the HCC cells specifically resist to ferroptosis by maintaining iron homeostasis. Iron 107-111 ferritin heavy chain 1 Homo sapiens 0-3 34965856-2 2021 Ferritin heavy chain (FTH) is a major iron storing nanocage to store redox-inactive iron, and harbors ferroxidase activity to prevent the iron-mediated production of ROS. Iron 38-42 ferritin heavy chain 1 Homo sapiens 0-20 34965856-2 2021 Ferritin heavy chain (FTH) is a major iron storing nanocage to store redox-inactive iron, and harbors ferroxidase activity to prevent the iron-mediated production of ROS. Iron 38-42 ferritin heavy chain 1 Homo sapiens 22-25 34965856-2 2021 Ferritin heavy chain (FTH) is a major iron storing nanocage to store redox-inactive iron, and harbors ferroxidase activity to prevent the iron-mediated production of ROS. Iron 84-88 ferritin heavy chain 1 Homo sapiens 0-20 34965856-2 2021 Ferritin heavy chain (FTH) is a major iron storing nanocage to store redox-inactive iron, and harbors ferroxidase activity to prevent the iron-mediated production of ROS. Iron 84-88 ferritin heavy chain 1 Homo sapiens 22-25 34965856-2 2021 Ferritin heavy chain (FTH) is a major iron storing nanocage to store redox-inactive iron, and harbors ferroxidase activity to prevent the iron-mediated production of ROS. Iron 138-142 ferritin heavy chain 1 Homo sapiens 0-20 34965856-2 2021 Ferritin heavy chain (FTH) is a major iron storing nanocage to store redox-inactive iron, and harbors ferroxidase activity to prevent the iron-mediated production of ROS. Iron 138-142 ferritin heavy chain 1 Homo sapiens 22-25 34965856-12 2021 Importantly, the proteins interaction network elucidated that FTH is involved in iron homeostasis maintenance and lysosomal-dependent degradation. Iron 81-85 ferritin heavy chain 1 Homo sapiens 62-65 34731167-10 2021 The apoferritin hydrogel also adsorbed Co2+ and Cu2+ ions and released them in the presence of EDTA, while it adsorbed less Ni2+ ions; more Fe3+ ions adsorbed to the apoferritin hydrogel than other metal ions, indicating that the hydrogel keeps the iron storage characteristic of ferritin. Iron 249-253 ferritin heavy chain 1 Homo sapiens 4-15 34732689-6 2021 GSK-3beta KD antagonizes the expression of iron metabolic components including DMT1, FTH1, and FTL, leading to the disruption of iron homeostasis and decline in intracellular labile free iron level. Iron 43-47 ferritin heavy chain 1 Homo sapiens 85-89 34765600-3 2021 Yes-associated protein (YAP) controls intracellular iron levels by affecting the transcription of ferritin heavy chain (FTH) and transferrin receptor (TFRC). Iron 52-56 ferritin heavy chain 1 Homo sapiens 98-118 34765600-3 2021 Yes-associated protein (YAP) controls intracellular iron levels by affecting the transcription of ferritin heavy chain (FTH) and transferrin receptor (TFRC). Iron 52-56 ferritin heavy chain 1 Homo sapiens 120-123 34572080-3 2021 In this study, we investigated different aspects involved in ESCs" response to iron accumulation following stable knockdown of the ferritin heavy chain (FTH1) gene, which encodes for a major iron storage protein with ferroxidase activity. Iron 79-83 ferritin heavy chain 1 Homo sapiens 131-151 34265052-9 2021 Cellular iron-loading caused a marked increase in CD63 expression and the secretion from cells of CD63 positive (i.e., CD63(+)) EVs, which were shown to contain ferritin-H (FtH) and -L (FtL). Iron 9-13 ferritin heavy chain 1 Homo sapiens 161-171 34265052-9 2021 Cellular iron-loading caused a marked increase in CD63 expression and the secretion from cells of CD63 positive (i.e., CD63(+)) EVs, which were shown to contain ferritin-H (FtH) and -L (FtL). Iron 9-13 ferritin heavy chain 1 Homo sapiens 173-176 34722507-6 2021 Furthermore, we found that iron accumulation and iron regulatory proteins, including transferrin (Tf), transferrin receptor (CD71), and Ferritin (FTH), increased after radiation treatment, and the silencing of transferrin decreased radiation-induced cell death. Iron 27-31 ferritin heavy chain 1 Homo sapiens 146-149 34722507-6 2021 Furthermore, we found that iron accumulation and iron regulatory proteins, including transferrin (Tf), transferrin receptor (CD71), and Ferritin (FTH), increased after radiation treatment, and the silencing of transferrin decreased radiation-induced cell death. Iron 49-53 ferritin heavy chain 1 Homo sapiens 146-149 34572080-3 2021 In this study, we investigated different aspects involved in ESCs" response to iron accumulation following stable knockdown of the ferritin heavy chain (FTH1) gene, which encodes for a major iron storage protein with ferroxidase activity. Iron 79-83 ferritin heavy chain 1 Homo sapiens 153-157 34572080-3 2021 In this study, we investigated different aspects involved in ESCs" response to iron accumulation following stable knockdown of the ferritin heavy chain (FTH1) gene, which encodes for a major iron storage protein with ferroxidase activity. Iron 191-195 ferritin heavy chain 1 Homo sapiens 131-151 34572080-3 2021 In this study, we investigated different aspects involved in ESCs" response to iron accumulation following stable knockdown of the ferritin heavy chain (FTH1) gene, which encodes for a major iron storage protein with ferroxidase activity. Iron 191-195 ferritin heavy chain 1 Homo sapiens 153-157 34474835-5 2021 Magnetoferritin is synthesized by loading iron in apoferritin in anaerobic condition at 65 C. The loading method results in one order of magnitude enhancement of r1 and r2 relaxivities compared to standard ferritin synthesized by aerobic loading of iron at room temperature. Iron 42-46 ferritin heavy chain 1 Homo sapiens 50-61 34188614-8 2021 The data were subsequently used to determine the spatial distribution of either iron or cobalt atoms incorporated into the ferritin/apoferritin protein cages. Iron 80-84 ferritin heavy chain 1 Homo sapiens 132-143 34386079-9 2021 Further, erastin and RSL3 promoted the transition of aconitase 1 to IRP1, which regulated downstream iron metabolism proteins, including transferrin receptor (TFRC), ferroportin (FPN) and ferritin heavy chain 1 (FTH1). Iron 101-105 ferritin heavy chain 1 Homo sapiens 212-216 34140491-3 2021 We apply the presented concept to ferritin, an iron storage protein, and its iron-free analog, apoferritin, in order to form single-layers, double-layers, as well as several types of 3D protein lattices. Iron 77-81 ferritin heavy chain 1 Homo sapiens 95-106 34140491-6 2021 The framework design of the arrays then allows small molecules to access the ferritins and their iron cores and convert them into apoferritin arrays through the release of iron ions. Iron 172-176 ferritin heavy chain 1 Homo sapiens 130-141 2660938-2 1989 At the molecular level, the main features are: the increased capacity of cells to bind toxic, inorganic iron to a specific storage protein, apoferritin, which becomes visible due to its iron-containing, electron-opaque core; since iron itself is involved in the de-repression of apoferritin synthesis, the number of assembled ferritin molecules depends on the amount of unbound iron present in the cell; there is a maximal, cell line-specific concentration of cytosolic ferritin; ferritin particles have a variable iron content, with richer molecules having a tendency to form clusters. Iron 104-108 ferritin heavy chain 1 Homo sapiens 140-151 35378780-1 2022 Purpose: Ferritin is a protein that plays an important role in iron metabolism, it consists of two subunits: heavy chain (FTH) and light chain (FTL). Iron 63-67 ferritin heavy chain 1 Homo sapiens 122-125 35417944-6 2022 Excessive accumulation of the ferritin heavy chain in neuroglia can increase the concentration of reactive forms of iron and increase neurotoxicity. Iron 116-120 ferritin heavy chain 1 Homo sapiens 30-50 35598199-4 2022 METHODS AND RESULTS: Proteomic analyses found that ATO can affect the signaling pathway associated with ferroptosis, including the upregulation of iron absorption (FTL, FTH1, HO-1), ferritinophagy (LC3, P62, ATG7, NCOA4) and modifier of glutathione synthesis (GCLM); downregulation of glutamine synthetase (GS) and GPX4, which was the critical inhibitor of ferroptosis. Iron 147-151 ferritin heavy chain 1 Homo sapiens 169-173 35504898-8 2022 Mechanistically, we found that de-O-GlcNAcylation of the ferritin heavy chain at S179 promoted its interaction with NCOA4, the ferritinophagy receptor, thereby accumulating labile iron for ferroptosis. Iron 180-184 ferritin heavy chain 1 Homo sapiens 57-77 2601708-1 1989 The 5" untranslated region of the ferritin heavy-chain mRNA contains a stem-loop structure called an iron-responsive element (IRE), that is solely responsible for the iron-mediated control of ferritin translation. Iron 101-105 ferritin heavy chain 1 Homo sapiens 34-54 2601708-1 1989 The 5" untranslated region of the ferritin heavy-chain mRNA contains a stem-loop structure called an iron-responsive element (IRE), that is solely responsible for the iron-mediated control of ferritin translation. Iron 167-171 ferritin heavy chain 1 Homo sapiens 34-54 2660938-2 1989 At the molecular level, the main features are: the increased capacity of cells to bind toxic, inorganic iron to a specific storage protein, apoferritin, which becomes visible due to its iron-containing, electron-opaque core; since iron itself is involved in the de-repression of apoferritin synthesis, the number of assembled ferritin molecules depends on the amount of unbound iron present in the cell; there is a maximal, cell line-specific concentration of cytosolic ferritin; ferritin particles have a variable iron content, with richer molecules having a tendency to form clusters. Iron 186-190 ferritin heavy chain 1 Homo sapiens 140-151 2660938-2 1989 At the molecular level, the main features are: the increased capacity of cells to bind toxic, inorganic iron to a specific storage protein, apoferritin, which becomes visible due to its iron-containing, electron-opaque core; since iron itself is involved in the de-repression of apoferritin synthesis, the number of assembled ferritin molecules depends on the amount of unbound iron present in the cell; there is a maximal, cell line-specific concentration of cytosolic ferritin; ferritin particles have a variable iron content, with richer molecules having a tendency to form clusters. Iron 186-190 ferritin heavy chain 1 Homo sapiens 140-151 2660938-2 1989 At the molecular level, the main features are: the increased capacity of cells to bind toxic, inorganic iron to a specific storage protein, apoferritin, which becomes visible due to its iron-containing, electron-opaque core; since iron itself is involved in the de-repression of apoferritin synthesis, the number of assembled ferritin molecules depends on the amount of unbound iron present in the cell; there is a maximal, cell line-specific concentration of cytosolic ferritin; ferritin particles have a variable iron content, with richer molecules having a tendency to form clusters. Iron 186-190 ferritin heavy chain 1 Homo sapiens 140-151 2660938-2 1989 At the molecular level, the main features are: the increased capacity of cells to bind toxic, inorganic iron to a specific storage protein, apoferritin, which becomes visible due to its iron-containing, electron-opaque core; since iron itself is involved in the de-repression of apoferritin synthesis, the number of assembled ferritin molecules depends on the amount of unbound iron present in the cell; there is a maximal, cell line-specific concentration of cytosolic ferritin; ferritin particles have a variable iron content, with richer molecules having a tendency to form clusters. Iron 186-190 ferritin heavy chain 1 Homo sapiens 140-151 2660938-2 1989 At the molecular level, the main features are: the increased capacity of cells to bind toxic, inorganic iron to a specific storage protein, apoferritin, which becomes visible due to its iron-containing, electron-opaque core; since iron itself is involved in the de-repression of apoferritin synthesis, the number of assembled ferritin molecules depends on the amount of unbound iron present in the cell; there is a maximal, cell line-specific concentration of cytosolic ferritin; ferritin particles have a variable iron content, with richer molecules having a tendency to form clusters. Iron 104-108 ferritin heavy chain 1 Homo sapiens 279-290 2535839-8 1989 However, CP-dependent, iron-catalyzed lipid peroxidation was inhibited by the addition of apoferritin. Iron 23-27 ferritin heavy chain 1 Homo sapiens 90-101 2539862-2 1989 The knowledge of the route through which iron can enter and leave the apoferritin shell is a prerequisite for the understanding of ferritin"s function. Iron 41-45 ferritin heavy chain 1 Homo sapiens 70-81 2539862-6 1989 In particular, the introduction of the additional carboxylate carried by p-(chloromercuri)benzoate near Asp-127 and Glu-130 increases the initial rate of iron uptake and affects the coordination geometry of the metal in the Fe(III)-apoferritin complex as indicated by optical absorption and EPR data. Iron 154-158 ferritin heavy chain 1 Homo sapiens 232-243 2535839-9 1989 Apoferritin did not function as a peroxyl radical-scavenging antioxidant but was shown to incorporate iron in the presence of CP. Iron 102-106 ferritin heavy chain 1 Homo sapiens 0-11 2982843-0 1985 Iron deposition in apoferritin. Iron 0-4 ferritin heavy chain 1 Homo sapiens 19-30 2458347-4 1988 The molecular basis of these findings is discussed and a possible mechanism suggested where one of the molecular forms of concanavalin A has the structure of an apoferritin into which iron is deposited in the form of ferrihydrite. Iron 184-188 ferritin heavy chain 1 Homo sapiens 161-172 3667586-6 1987 The binding of the first 100 irons to apoferritin quenches the intrinsic fluorescence without affecting the lifetimes in a proportional way. Iron 29-34 ferritin heavy chain 1 Homo sapiens 38-49 3600643-5 1987 We have identified a sequence of 22 highly conserved nucleotides in the 5" untranslated sequences of chicken, human, and tadpole ferritin H-subunit genes and propose that this conserved sequence may regulate iron-modulated translation of ferritin H-subunit mRNAs. Iron 208-212 ferritin heavy chain 1 Homo sapiens 129-147 3600643-5 1987 We have identified a sequence of 22 highly conserved nucleotides in the 5" untranslated sequences of chicken, human, and tadpole ferritin H-subunit genes and propose that this conserved sequence may regulate iron-modulated translation of ferritin H-subunit mRNAs. Iron 208-212 ferritin heavy chain 1 Homo sapiens 238-256 3759957-0 1986 Iron incorporation into apoferritin. Iron 0-4 ferritin heavy chain 1 Homo sapiens 24-35 3759957-7 1986 It is suggested that the described oxidation process represents the initial step of iron deposition in apoferritin. Iron 84-88 ferritin heavy chain 1 Homo sapiens 103-114 3943278-6 1986 It seems likely that apoferritin is synthesized in response to the amount of iron taken into the cell and this iron is incorporated within the protein shell to form ferritin. Iron 77-81 ferritin heavy chain 1 Homo sapiens 21-32 3943278-6 1986 It seems likely that apoferritin is synthesized in response to the amount of iron taken into the cell and this iron is incorporated within the protein shell to form ferritin. Iron 111-115 ferritin heavy chain 1 Homo sapiens 21-32 2982843-2 1985 A preliminary EPR investigation of iron accumulation in apoferritin has identified paramagnetic species generated during the early stage of iron deposition within the apoprotein shell. Iron 35-39 ferritin heavy chain 1 Homo sapiens 56-67 2982843-2 1985 A preliminary EPR investigation of iron accumulation in apoferritin has identified paramagnetic species generated during the early stage of iron deposition within the apoprotein shell. Iron 140-144 ferritin heavy chain 1 Homo sapiens 56-67 6249590-7 1980 We conclude that the unprotonated form of imidazole inhibits iron deposition, possibly by binding to the active site of the apoferritin molecule. Iron 61-65 ferritin heavy chain 1 Homo sapiens 124-135 6847196-3 1983 This competition may be the molecular basis for the inhibition of iron incorporation into apoferritin brought about by Tb(III). Iron 66-70 ferritin heavy chain 1 Homo sapiens 90-101 6726222-0 1984 Spectroscopic studies on the binding of iron, terbium, and zinc by apoferritin. Iron 40-44 ferritin heavy chain 1 Homo sapiens 67-78 6653779-1 1983 The protein component of the iron storage molecule, ferritin, contains 24 subunits in form of a hollow shell known as apoferritin. Iron 29-33 ferritin heavy chain 1 Homo sapiens 118-129 6416253-0 1983 The incorporation of iron into apoferritin as mediated by ceruloplasmin. Iron 21-25 ferritin heavy chain 1 Homo sapiens 31-42 6416253-1 1983 Ceruloplasmin, a copper ferroxidase, promotes the incorporation of Fe(III) into the iron storage protein, apoferritin. Iron 84-88 ferritin heavy chain 1 Homo sapiens 106-117 4798313-2 1973 Inhibition by Zn(2+) of iron uptake by apoferritin at very low substrate concentrations is shown to be competitive. Iron 24-28 ferritin heavy chain 1 Homo sapiens 39-50 1144955-2 1975 Iron induction of apoferritin biosynthesis. Iron 0-4 ferritin heavy chain 1 Homo sapiens 18-29 620821-0 1978 Stoichiometry of iron oxidation by apoferritin. Iron 17-21 ferritin heavy chain 1 Homo sapiens 35-46 186315-0 1976 Iron binding to apoferritin: a fluorescence spectroscopy study. Iron 0-4 ferritin heavy chain 1 Homo sapiens 16-27 4855331-2 1974 The uptake and subsequent release of iron by apoferritin and ferritin was studied by using labelled iron ((59)Fe). Iron 37-41 ferritin heavy chain 1 Homo sapiens 45-56 4855331-2 1974 The uptake and subsequent release of iron by apoferritin and ferritin was studied by using labelled iron ((59)Fe). Iron 100-104 ferritin heavy chain 1 Homo sapiens 45-56 4855331-2 1974 The uptake and subsequent release of iron by apoferritin and ferritin was studied by using labelled iron ((59)Fe). Iron 110-112 ferritin heavy chain 1 Homo sapiens 45-56 5075227-3 1972 Starting from apoferritin, or ferritin of low iron content, Fe(2+) and an oxidizing agent, the uptake of iron can be recorded spectrophotometrically. Iron 46-50 ferritin heavy chain 1 Homo sapiens 14-25 4797166-3 1973 A study was made of the uptake of ferrous iron by apoferritin in the presence of an oxidizing agent at very low iron:protein ratios. Iron 42-46 ferritin heavy chain 1 Homo sapiens 50-61 4797166-3 1973 A study was made of the uptake of ferrous iron by apoferritin in the presence of an oxidizing agent at very low iron:protein ratios. Iron 112-116 ferritin heavy chain 1 Homo sapiens 50-61 4797166-4 1973 At ratios of less than about 150 iron atoms per apoferritin molecule hyperbolic progress curves were obtained, whereas at higher ratios the curves became sigmoidal under the conditions used. Iron 33-37 ferritin heavy chain 1 Homo sapiens 48-59 4797166-6 1973 The experimental evidence indicates that apoferritin binds ferrous iron and catalyses the initial stage in the formation of the ferric oxide hydrate inside the protein shell. Iron 59-71 ferritin heavy chain 1 Homo sapiens 41-52 5075227-3 1972 Starting from apoferritin, or ferritin of low iron content, Fe(2+) and an oxidizing agent, the uptake of iron can be recorded spectrophotometrically. Iron 105-109 ferritin heavy chain 1 Homo sapiens 14-25 5075227-5 1972 The progress curves of iron uptake by apoferritin are sigmoidal; those for ferritins of low iron content are hyperbolic. Iron 23-27 ferritin heavy chain 1 Homo sapiens 38-49 5805400-0 1969 On the mechanism of iron-induced synthesis of apoferritin in HeLa cells. Iron 20-24 ferritin heavy chain 1 Homo sapiens 46-57 6011202-0 1966 [Synthesis of apoferritin-iron complex in a test tube and its properties]. Iron 26-30 ferritin heavy chain 1 Homo sapiens 14-25 14336439-0 1965 FAILURE OF ACTINOMYCIN D TO PREVENT INDUCTION OF LIVER APOFERRITIN AFTER IRON ADMINISTRATION. Iron 73-77 ferritin heavy chain 1 Homo sapiens 55-66 13614978-0 1958 [Electron-microscopic aspect of apoferritin more or less saturated with iron; comparison of images observed in the cells with those of chemically prepared substances]. Iron 72-76 ferritin heavy chain 1 Homo sapiens 32-43 14217510-0 1964 "FREE" APOFERRITIN AND APOFERRITIN OBTAINED BY REDUCTION OF IRON-CONTAINING FERRITIN. Iron 60-64 ferritin heavy chain 1 Homo sapiens 7-18 14217510-0 1964 "FREE" APOFERRITIN AND APOFERRITIN OBTAINED BY REDUCTION OF IRON-CONTAINING FERRITIN. Iron 60-64 ferritin heavy chain 1 Homo sapiens 23-34 13499392-0 1957 The incorporation of iron by apoferritin. Iron 21-25 ferritin heavy chain 1 Homo sapiens 29-40 14367535-0 1955 Effect of iron on the biosynthesis of hepatic apoferritin. Iron 10-14 ferritin heavy chain 1 Homo sapiens 46-57 21001168-0 1946 Ferritin; increase of the protein apoferritin in the gastrointestinal mucosa as a direct response to iron feeding; the function of ferritin in the regulation of iron absorption. Iron 101-105 ferritin heavy chain 1 Homo sapiens 34-45 33507490-2 2021 Ferritin is a hollow iron storage protein composed of 24 subunits of two types, ferritin heavy chain (FTH) and ferritin light chain (FTL), which plays an important role in maintaining iron homeostasis. Iron 184-188 ferritin heavy chain 1 Homo sapiens 80-100 17795255-0 1946 Protein Apoferritin and Ferritin in Iron Feeding and Absorption. Iron 36-40 ferritin heavy chain 1 Homo sapiens 8-19 21010560-0 1946 Protein apoferritin and ferritin in iron feeding and absorption. Iron 36-40 ferritin heavy chain 1 Homo sapiens 8-19 33649797-9 2021 Mechanistically, miR-335 enhanced ferroptosis through the degradation of FTH1 to increase iron release, lipid peroxidation and reactive oxygen species (ROS) accumulation, and to decrease mitochondrial membrane potential (MMP). Iron 90-94 ferritin heavy chain 1 Homo sapiens 73-77 33844625-3 2021 Finally, we propose how the application for cancer drug repurposing delivery within apoferritin could expand cancer treatment in the future.Expert opinion: Being a ubiquitous iron storage protein that exists in many living organisms, apoferritin is promising as a cancer tumor-targeting nanocarrier. Iron 175-179 ferritin heavy chain 1 Homo sapiens 234-245