PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25163484-6 2014 Overexpression of GAPDH results in increased transferrin binding to M.tb cells and iron uptake. Iron 83-87 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 18-23 25399609-0 2014 Protein moonlighting in iron metabolism: glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Iron 24-28 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 41-81 25399609-0 2014 Protein moonlighting in iron metabolism: glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Iron 24-28 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 83-88 10024547-4 1999 Analysis of staphylococcal cell wall fractions for GAPDH activity confirmed the presence of a functional enzyme which, like Tpn, is regulated by the availability of iron in the growth medium. Iron 165-169 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 51-56 22388977-2 2012 Apart from glycolysis, GAPDH participates in iron metabolism, membrane trafficking, histone biosynthesis, the maintenance of DNA integrity and receptor mediated cell signaling. Iron 45-49 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 23-28 22292499-9 2012 This suggests that upon iron depletion, cells prefer to use GAPDH to acquire lactoferrin. Iron 24-28 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 60-65 17121833-5 2007 The expression of this surface GAPDH is regulated by the availability of iron in the medium. Iron 73-77 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 31-36 25074810-0 2014 Moonlighting cell-surface GAPDH recruits apotransferrin to effect iron egress from mammalian cells. Iron 66-70 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 26-31 25074810-4 2014 Previous studies have revealed that iron-depleted cells recruit glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a multitasking, "moonlighting" protein, to their surface for internalization of the iron carrier holotransferrin. Iron 36-40 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 64-104 25074810-4 2014 Previous studies have revealed that iron-depleted cells recruit glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a multitasking, "moonlighting" protein, to their surface for internalization of the iron carrier holotransferrin. Iron 36-40 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 106-111 25074810-4 2014 Previous studies have revealed that iron-depleted cells recruit glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a multitasking, "moonlighting" protein, to their surface for internalization of the iron carrier holotransferrin. Iron 198-202 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 64-104 25074810-4 2014 Previous studies have revealed that iron-depleted cells recruit glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a multitasking, "moonlighting" protein, to their surface for internalization of the iron carrier holotransferrin. Iron 198-202 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 106-111 25074810-5 2014 Here, we report that under the converse condition of intracellular iron excess, cells switch the isoform of GAPDH on their surface to one that now recruits iron-free apotransferrin in close association with ferroportin to facilitate the efflux of iron. Iron 67-71 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 108-113 25074810-5 2014 Here, we report that under the converse condition of intracellular iron excess, cells switch the isoform of GAPDH on their surface to one that now recruits iron-free apotransferrin in close association with ferroportin to facilitate the efflux of iron. Iron 156-160 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 108-113 25074810-5 2014 Here, we report that under the converse condition of intracellular iron excess, cells switch the isoform of GAPDH on their surface to one that now recruits iron-free apotransferrin in close association with ferroportin to facilitate the efflux of iron. Iron 156-160 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 108-113 25074810-6 2014 Increased expression of surface GAPDH correlated with increased apotransferrin binding and enhanced iron export from cells, a capability lost in GAPDH-knockdown cells. Iron 100-104 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 32-37 23541988-2 2013 Here we report that, during increased iron demand, cells secrete the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) which enhances cellular uptake of Tf and iron. Iron 38-42 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 129-134 23541988-2 2013 Here we report that, during increased iron demand, cells secrete the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) which enhances cellular uptake of Tf and iron. Iron 177-181 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 129-134 30897319-0 2019 Moonlighting Protein Glyceraldehyde-3-Phosphate Dehydrogenase: A Cellular Rapid-Response Molecule for Maintenance of Iron Homeostasis in Hypoxia. Iron 117-121 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 21-61 30640524-4 2019 We present evidence that both pathways of GAPDH membrane trafficking are up-regulated upon iron starvation, potentially by mobilization of intracellular calcium. Iron 91-95 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 42-47 1438570-1 1992 We have studied the damage of alcohol dehydrogenase (ADH) and glyceraldehyde 3-phosphate dehydrogenase (GAPD) induced by Fe++/EDTA + H2O2 in combination with UV-A (main output at 365 nm). Iron 121-125 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 62-102 1438570-1 1992 We have studied the damage of alcohol dehydrogenase (ADH) and glyceraldehyde 3-phosphate dehydrogenase (GAPD) induced by Fe++/EDTA + H2O2 in combination with UV-A (main output at 365 nm). Iron 121-125 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 104-108 30897319-6 2019 RESULTS: In the current study, we demonstrated that hypoxia induces K562 cells to translocate the cytosolic moonlighting protein glyceraldehyde-3-phosphate dehydrogenase (GAPDH) onto cell surfaces and into the extracellular milieu to acquire transferrin-bound iron, even while levels of the classical transferrin receptor TfR1 (CD71) remain suppressed. Iron 260-264 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 129-169 30897319-6 2019 RESULTS: In the current study, we demonstrated that hypoxia induces K562 cells to translocate the cytosolic moonlighting protein glyceraldehyde-3-phosphate dehydrogenase (GAPDH) onto cell surfaces and into the extracellular milieu to acquire transferrin-bound iron, even while levels of the classical transferrin receptor TfR1 (CD71) remain suppressed. Iron 260-264 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 171-176 30897319-9 2019 CONCLUSION: Our results suggest the role of GAPDH-mediated Tf uptake as a rapid response mechanism by which cells acquire iron during the early stages of hypoxia. Iron 122-126 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 44-49 30209795-3 2018 As such, apart from its classical role in energy production, membrane-bound GAPDH is required for membrane fusion, endocytosis and, intriguingly, for iron transport. Iron 150-154 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 76-81 26743084-3 2016 Utilizing primary cells and cell lines (including those with no discernible expression of ferroportin on their surface), we demonstrate that upon Fe loading, the multifunctional enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH), which is recruited to the cell surface, "treadmills" apotransferrin in and out of the cell. Iron 146-148 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 185-225 26743084-3 2016 Utilizing primary cells and cell lines (including those with no discernible expression of ferroportin on their surface), we demonstrate that upon Fe loading, the multifunctional enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH), which is recruited to the cell surface, "treadmills" apotransferrin in and out of the cell. Iron 146-148 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 227-232 26743084-4 2016 Kinetic analysis utilizing labeled ligand, GAPDH-knockdown cells, (55)Fe-labeled cells and pharmacological inhibitors of endocytosis confirmed GAPDH-dependent apotransferrin internalization as a prerequisite for cellular Fe export. Iron 70-72 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 143-148 26672975-0 2015 Secreted multifunctional Glyceraldehyde-3-phosphate dehydrogenase sequesters lactoferrin and iron into cells via a non-canonical pathway. Iron 93-97 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 25-65 26672975-6 2015 We also demonstrate the operation of this phenomenon during inflammation, as an arm of the innate immune response where lactoferrin denies iron to invading microorganisms by chelating it and then itself being sequestered into surrounding host cells by GAPDH. Iron 139-143 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 252-257