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Human glucose transporters

Mueckler, M., et al. Sequence and structure of a human glucose transporter. Science 1985, 229, 941-945. [Pg.282]

Fukumoto, H., et al. Sequence, tissue distribution, and chromosomal localization of mRNA encoding a human glucose transporter-like protein. Proc. Natl. Acad. Sci. U. S. A. 1988, 85, 5434-5438. [Pg.282]

Doege, H., et al. Activity and genomic organization of human glucose transporter 9 (GLUT9), a novel member of the family of sugar-transport facilitators predominantly expressed in brain and leucocytes. Biochem. J. 2000, 350, 771-776. [Pg.282]

Figure 8-23 Predicted topology of the human glucose transporter GLUT1. The 12 predicted helices are numbered and the single external N-linked oligosaccharide is marked CHO. The sequence RXGRR (marked) is found in many 12-helix transporters. Its occurrence in these two positions suggests that the transporters may have evolved by duplication of a 6-helix motif. However, the human glucose transporters otherwise show no sequence similarity to other 12-helix transporters. After Bell et al.398... Figure 8-23 Predicted topology of the human glucose transporter GLUT1. The 12 predicted helices are numbered and the single external N-linked oligosaccharide is marked CHO. The sequence RXGRR (marked) is found in many 12-helix transporters. Its occurrence in these two positions suggests that the transporters may have evolved by duplication of a 6-helix motif. However, the human glucose transporters otherwise show no sequence similarity to other 12-helix transporters. After Bell et al.398...
HPLC. See High performance liquid chromatography HSQC 144 Huber, Robert 84 Human body, elements in 31 Human genome 12, 201 Human glucose transporters 416 figure 416... [Pg.920]

Gould GW, Thomas HM, Jess TJ, Bell GI (1991), Expression of human glucose transporters in Xenopus oocytes. Kinetic characterization and substrate specificities of the erythrocyte, liver, and brain isoforms, Biochemistry 30 5139-5145. [Pg.107]

Kayano T, Fukumoto H, Eddy RL, Fan YS, Byers MG, Shows TB, Bell GI (1988), Evidence for a family of human glucose transporter-like proteins. Sequence and gene localization of a protein expressed in fetal skeletal muscle and other tissues, J. Biol. Chem. 263 15245-15248. [Pg.107]

GGM. Several missense mutations in human sodium-dependent glucose transporters (SGLT1) have been described that cause GGM. [Pg.552]

By far the most complete study of the kinetics of mammalian passive glucose transporters has been done on the GLUT-1 isoform in the human erythrocyte. The transport of glucose in this cell type is a classic example of facilitated diffusion, the... [Pg.174]

The structure of the human erythrocyte glucose transport protein... [Pg.185]

The amino acid sequence of the human erythrocyte glucose transporter was deduced from the nucleotide sequence of a cDNA clone in 1985 [106]. Polyclonal antibodies raised against the protein were used to screen a Xgtl I cDNA library prepared from the human hepatocellular carcinoma cell line HepG2. (Like many other transformed... [Pg.185]

Fig. 3. Model for the two-dimensional arrangement of the human erythrocyte glucose transporter in the membrane. Amino acid residues are identified by their single letter code. Solid bars indicate the location of introns in the transporter gene. The regions coloured black are released from the membrane upon tryptic digestion. Shaded segments indicate the probable regions photolabelled by ATB-BMPA (helix 8) and by cytochalasin B (helix 11 and the loop connecting it to helix 10). The circles with heavy outlines indicate the region labelled by lAPS-forskolin (helix 10). Fig. 3. Model for the two-dimensional arrangement of the human erythrocyte glucose transporter in the membrane. Amino acid residues are identified by their single letter code. Solid bars indicate the location of introns in the transporter gene. The regions coloured black are released from the membrane upon tryptic digestion. Shaded segments indicate the probable regions photolabelled by ATB-BMPA (helix 8) and by cytochalasin B (helix 11 and the loop connecting it to helix 10). The circles with heavy outlines indicate the region labelled by lAPS-forskolin (helix 10).
In summary, studies on the human erythrocyte glucose transporter and other members of a large family of prokaryotic and eukaryotic sugar transporters have yielded... [Pg.210]


See other pages where Human glucose transporters is mentioned: [Pg.390]    [Pg.449]    [Pg.40]    [Pg.847]    [Pg.148]    [Pg.226]    [Pg.340]    [Pg.194]    [Pg.251]    [Pg.390]    [Pg.449]    [Pg.40]    [Pg.847]    [Pg.148]    [Pg.226]    [Pg.340]    [Pg.194]    [Pg.251]    [Pg.1014]    [Pg.550]    [Pg.551]    [Pg.341]    [Pg.169]    [Pg.170]    [Pg.172]    [Pg.174]    [Pg.182]    [Pg.186]    [Pg.197]    [Pg.198]    [Pg.198]    [Pg.199]    [Pg.199]    [Pg.200]    [Pg.201]    [Pg.202]    [Pg.203]    [Pg.231]    [Pg.232]    [Pg.411]   
See also in sourсe #XX -- [ Pg.416 ]

See also in sourсe #XX -- [ Pg.416 ]

See also in sourсe #XX -- [ Pg.416 ]

See also in sourсe #XX -- [ Pg.416 ]




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