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10.1016/B978-0-12-394390-3.00001-X http://scihub22266oqcxt.onion/10.1016/B978-0-12-394390-3.00001-X C4479283!4479283!23046645     free     free     free       Curr+Top+Membr 2012 ; 69 (ä): 3-35 Nephropedia Template TP {{tp|p=23046645|t=2012. Transferrin-Mediated Cellular Iron Delivery |pdf=|usr=}}{{23046645}} gab.com Text Transferrin-Mediated Cellular Iron Delivery JO: Curr Top Membr http://www.kidney.de/pget.php?&tw=1&pmid=23046645 #FOAvip Essential to iron homeostasis is the transport of iron by the bilobal protein human serum transferrin (hTF). Each lobe (N- and C-lobe) of hTF forms a deep cleft which binds a single Fe3+. Iron-bearing hTF in the blood binds tightly to the specific transferrin receptor (TFR), a homodimeric transmembrane protein. After undergoing endocytosis, acidification of the endosome initiates the release of Fe3+ from hTF in a TFR-mediated process. Iron-free hTF remains tightly bound to the TFR at acidic pH; following recycling back to the cell surface, it is released to sequester more iron. Efficient delivery of iron is critically dependent on hTF/TFR interactions. Therefore, identification of the pH-specific contacts between hTF and the TFR is crucial. Recombinant protein production has enabled deconvolution of this complex system. The studies reviewed herein support a model in which pH-induced interrelated events control receptor-stimulated iron release from each lobe of hTF. Twit Text FOAVip Transferrin-Mediated Cellular Iron Delivery ????Curr Top Membr http://www.kidney.de/pget.php?&tw=1&pmid=23046645 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=23046645 #FOAvip English Wikipedia <ref>{{Cite pmid|23046645}}</ref> Transferrin-Mediated Cellular Iron Delivery #MMPMID23046645 Luck AN; Mason AB Curr Top Membr 2012[]; 69 (ä): 3-35 PMID23046645show ga Essential to iron homeostasis is the transport of iron by the bilobal protein human serum transferrin (hTF). Each lobe (N- and C-lobe) of hTF forms a deep cleft which binds a single Fe3+. Iron-bearing hTF in the blood binds tightly to the specific transferrin receptor (TFR), a homodimeric transmembrane protein. After undergoing endocytosis, acidification of the endosome initiates the release of Fe3+ from hTF in a TFR-mediated process. Iron-free hTF remains tightly bound to the TFR at acidic pH; following recycling back to the cell surface, it is released to sequester more iron. Efficient delivery of iron is critically dependent on hTF/TFR interactions. Therefore, identification of the pH-specific contacts between hTF and the TFR is crucial. Recombinant protein production has enabled deconvolution of this complex system. The studies reviewed herein support a model in which pH-induced interrelated events control receptor-stimulated iron release from each lobe of hTF. äTransferrin-Mediated Cellular Iron Delivery (epmc).pdf DeepDyve Pubget Overpricing