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1 cMOAT mediates hepatobiliary clearance of many organic a
2 y expressed in tissues, including liver, and cMOAT, the expression of which is largely restricted to
3 protein cluster formed by PDZK1, MAP17, and cMOAT is upregulated in a significant number of human ca
4 ansporter that is closely related to MRP and cMOAT and raise the possibility that it may be an organi
5 ophobic extension that is present in MRP and cMOAT and which is predicted to encode several transmemb
7 transport taurocholate, MRP3, like MRP1 and cMOAT, is concluded to be competent in the transport of
8 amino acids in length, similar to mammalian cMOAT/cMRP1 and MRP1 transporters, yeast Ycf1p, and two
9 known to interact with PDZK1, such as MAP17, cMOAT, and the type IIa Na/Pi cotransporter, was observe
10 aled that it is most closely related to MRP, cMOAT, and the yeast organic anion transporter YCF1.
11 complete coding sequences of four human MRP/cMOAT subfamily members and found that, among these prot
13 ort of arsenic into bile depends on the MRP2/cMOAT transporter and that glutathione is obligatory for
14 a small 17-kDa membrane-associated protein; cMOAT, an organic anion transporter implicated in multid
15 ecent evidence suggests the possibility that cMOAT may contribute to cytotoxic drug resistance as wel
16 he urine in TR- Wistar rats, suggesting that cMOAT is important in the clearance of the compounds fro
17 lar multispecific organic anion transporter (cMOAT or MRP2) are ATP-binding cassette transporters tha
18 lar multispecific organic anion transporter (cMOAT) are closely related mammalian ATP-binding cassett
20 lar multispecific organic anion transporter (cMOAT)/MRP2 are ATP-binding cassette (ABC) transporters
22 such as the multispecific anion transporter, cMOAT, bile acid transporters, ion-motive ATPases, gluta
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