Pub. Date : 2014 Oct 1
PMID : 25074810
9 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Moonlighting cell-surface GAPDH recruits apotransferrin to effect iron egress from mammalian cells. | Iron | glyceraldehyde-3-phosphate dehydrogenase | Homo sapiens |
| 2 | 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 | glyceraldehyde-3-phosphate dehydrogenase | Homo sapiens |
| 3 | 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 | glyceraldehyde-3-phosphate dehydrogenase | Homo sapiens |
| 4 | 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 | glyceraldehyde-3-phosphate dehydrogenase | Homo sapiens |
| 5 | 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 | glyceraldehyde-3-phosphate dehydrogenase | Homo sapiens |
| 6 | 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 | glyceraldehyde-3-phosphate dehydrogenase | Homo sapiens |
| 7 | 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 | glyceraldehyde-3-phosphate dehydrogenase | Homo sapiens |
| 8 | 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 | glyceraldehyde-3-phosphate dehydrogenase | Homo sapiens |
| 9 | Increased expression of surface GAPDH correlated with increased apotransferrin binding and enhanced iron export from cells, a capability lost in GAPDH-knockdown cells. | Iron | glyceraldehyde-3-phosphate dehydrogenase | Homo sapiens |