PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23146871-2 2013 Mn(2+) is transported into cells via a number of mechanisms, while Mn(3+) is believed to be transported similarly to iron (Fe) via the transferrin (Tf) mechanism. manganese(III) acetate dihydrate 67-73 transferrin Homo sapiens 135-146 23146871-2 2013 Mn(2+) is transported into cells via a number of mechanisms, while Mn(3+) is believed to be transported similarly to iron (Fe) via the transferrin (Tf) mechanism. manganese(III) acetate dihydrate 67-73 transferrin Homo sapiens 148-150 23146871-6 2013 Using purified and labeled Mn(3+)Tf and biophysical tools, we have developed a novel approach to study Mn(3+)Tf transport independently of other Mn transport mechanisms. manganese(III) acetate dihydrate 27-33 transferrin Homo sapiens 109-111 1406294-3 1992 The 54Mn content of the Tf peak increased with increasing incubation time in vitro, suggesting the oxidation of Mn+2 to Mn+3 before its association with Tf. manganese(III) acetate dihydrate 120-124 transferrin Homo sapiens 24-26 10385881-8 1999 Accordingly, the distribution and membrane transport of Mn emphasizes the importance of: 1) the oxidation state of Mn, as it governs the affinity of Mn to endogenous ligands, and 2) the reaction of Mn3+ with transferrin, the plasma iron-carrying protein. manganese(III) acetate dihydrate 198-202 transferrin Homo sapiens 208-219 23146871-8 2013 Results confirm that in these cell lines significant Mn(3+) is transported by the Tf mechanism similarly to Fe(3+)Tf transport; although Mn(3+)Tf transport is markedly slower than other Mn transport mechanisms. manganese(III) acetate dihydrate 53-59 transferrin Homo sapiens 82-84 3995083-9 1985 The amount of 54Mn radioactivity recovered with transferrin increased as incubation time was increased, probably due to oxidation of Mn2+ to Mn3+. manganese(III) acetate dihydrate 141-145 transferrin Homo sapiens 48-59 6250582-2 1980 As in the case of Fe(III)- and Cu(II)-transferrin, a significant quenching of apolactoferrin"s intrinsic fluorescence is caused by the interaction of Fe(III), Cu(II), Cr(III), Mn(III), and Co(III) with specific metal binding sites. manganese(III) acetate dihydrate 176-183 transferrin Homo sapiens 38-49