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1 4F2hc increases the stability of the light subunit LAT2
2 n obtained by co-expression of b(0, +)AT and 4F2hc or b(0,+)AT and rBAT in human retinal pigment epit
4 is different from that of b(0,+)AT mRNA and 4F2hc mRNA, but there are regions in the kidney where b(
8 fication of the LAT1 with its chaperon CD98 (4F2hc,SLC3A2) and that this stabilised complex retained
10 (-) (the light chain xCT and the heavy chain 4F2hc) as is evident from functional and molecular studi
11 (b(0, +)AT) interacts with 4F2 heavy chain (4F2hc) as well as with the protein related to b(0,+) ami
12 , when coexpressed with the 4F2 heavy chain (4F2hc) in mammalian cells, induces a b(0,+)-like amino a
13 d with bovine BBB LAT1 mRNA and the mRNA for 4F2hc, which encodes the heavy chain of the heterodimer.
16 d single-particle analysis of purified human 4F2hc/L-type amino acid transporter 2 (LAT2) heterodimer
19 nts, reveal that the extracellular domain of 4F2hc interacts with LAT2, almost completely covering th
27 higher than that of transcripts such as the 4F2hc antigen, actin, or the Glut1 glucose transporter.
29 ics of the transport process mediated by the 4F2hc/4F2-lc6 complex and the expression pattern of 4F2-
32 essed in COS-7 cells with rBAT, but not with 4F2hc, BAT1 exhibited a Na(+)-independent transport of c
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