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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Solute carrier family 44, member 3

Top mentioned proteins: CTL1, CTL2, Histone, RANK, OCT
Papers on CTL-3
Membrane transport mechanisms of choline in human intestinal epithelial LS180 cells.
Hashimoto et al., Toyama, Japan. In Biopharm Drug Dispos, 2014
The mRNA of choline transporter-like proteins (CTLs) was expressed significantly in LS180 cells, and the rank order was CTL1 > CTL4 > CTL3 > CTL2 > CTL5.
Enhanced choline metabolism in a rodent rhabdomyosarcoma model: correlation between RT-PCR and translational 3 T H-MRS.
Duprez et al., Brussels, Belgium. In Magn Reson Imaging, 2012
Choline kinase α and β gene expression as well as genes of the transmembrane transporters OCT1, OCT2, OCT3, CTL1, CTL3, CTL4 and CHT1 were studied using reverse transcriptase polymerase chain reaction.
Na(+)-independent choline transport in rat retinal capillary endothelial cells.
Hosoya et al., Toyama, Japan. In Neurochem Res, 2007
The transcript level of CTL1 in a conditionally immortalized rat retinal capillary endothelial cell line (TR-iBRB2) is more than 100-fold greater than that of CTL3 and CTL4, and no expression of organic cation transporter (OCT) mRNA was detected.
Suppression of human immunodeficiency virus type 1 replication by arginine deiminase of Mycoplasma arginini.
Kannagi et al., Tokyo, Japan. In J Gen Virol, 2006
However, one of these CTL lines (CTL-3) also significantly suppressed HIV-1 replication through its supernatant.
Dengue virus-specific, human CD4+ cytotoxic T lymphocytes generated in short-term culture.
Ennis et al., Worcester, United States. In Viral Immunol, 1992
In the present experiments we tried to determine whether dengue virus-specific CD4+ CD8- CTL3 are present in short-term bulk cultures.
Possible role of histones in the organization of rat liver thyroid hormone receptors in chromatin.
Yamada et al., Matsumoto, Japan. In J Endocrinol, 1989
H1 histone subfractions (calf thymus lysine-rich histone (CTL)-1, CTL-2 and CTL-3) showed potent inhibition of receptor-DNA binding indistinguishable from each other.
Does high-mobility-group non-histone protein HMG 1 interact specifically with histone H1 subfractions?
Bradbury et al., In Biochem J, 1980
In contrast with a previous report [Smerdon & Isenberg (1976) Biochemistry 15, 4242--4247], it was found, by using equilibrium-sedimentation analysis, that protein HMG 1 binds to all three histone H1 subfractions CTL1, CTL2, and CTL3, arguing against there being a specific interaction between protein HMG 1 and only two of the subfractions, CTL1 and CTL2.
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