The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

DNP-SG     [2-[2-[(4-amino-4-carboxy- butanoyl)amino]...

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of DNP-SG


High impact information on DNP-SG

  • Biliary secretion of the Mrp2 substrate, 2,4-dinitrophenyl-S-glutathione (GS-DNP), was studied in the presence or absence of the PKC inhibitor, bisindolylmaleimide I (BIM-I; 1 micromol/L) [2].
  • Both N-RLIP76(1-367) and C-RLIP76(410-655) had ATPase activity (K(m) for ATP, 2.5 and 2.0 mM, respectively) which was stimulated by DNP-SG, DOX, and colchicine (COL) [3].
  • In addition, the observation that both mildly cationic or neutral natural product cytotoxic drugs and anionic compounds such as DNP-SG, MK571, and arsenate are competitive inhibitors of MRP action suggests that the substrate specificity of the transporter is quite broad [4].
  • Hepatovenous lactate dehydrogenase and alanine aminotransferase efflux as markers of liver integrity and biliary secretion of 2,4-dinitrophenyl-S-glutathione (DNP-GS) were determined photometrically [5].
  • Secretion of DNP-SG was not altered in pregnant rats but increased in lactating animals by late lactation [6].

Chemical compound and disease context of DNP-SG


Anatomical context of DNP-SG


Associations of DNP-SG with other chemical compounds


Gene context of DNP-SG


  1. Novel function of human RLIP76: ATP-dependent transport of glutathione conjugates and doxorubicin. Awasthi, S., Cheng, J., Singhal, S.S., Saini, M.K., Pandya, U., Pikula, S., Bandorowicz-Pikula, J., Singh, S.V., Zimniak, P., Awasthi, Y.C. Biochemistry (2000) [Pubmed]
  2. Tauroursodeoxycholic acid inserts the apical conjugate export pump, Mrp2, into canalicular membranes and stimulates organic anion secretion by protein kinase C-dependent mechanisms in cholestatic rat liver. Beuers, U., Bilzer, M., Chittattu, A., Kullak-Ublick, G.A., Keppler, D., Paumgartner, G., Dombrowski, F. Hepatology (2001) [Pubmed]
  3. Functional reassembly of ATP-dependent xenobiotic transport by the N- and C-terminal domains of RLIP76 and identification of ATP binding sequences. Awasthi, S., Cheng, J.Z., Singhal, S.S., Pandya, U., Sharma, R., Singh, S.V., Zimniak, P., Awasthi, Y.C. Biochemistry (2001) [Pubmed]
  4. Cellular and in vitro transport of glutathione conjugates by MRP. Shen, H., Paul, S., Breuninger, L.M., Ciaccio, P.J., Laing, N.M., Helt, M., Tew, K.D., Kruh, G.D. Biochemistry (1996) [Pubmed]
  5. Phosphatidylinositol 3-kinase-dependent signaling modulates taurochenodeoxycholic acid-induced liver injury and cholestasis in perfused rat livers. Rust, C., Bauchmuller, K., Fickert, P., Fuchsbichler, A., Beuers, U. Am. J. Physiol. Gastrointest. Liver Physiol. (2005) [Pubmed]
  6. Expression of multidrug resistance-associated protein 2 in small intestine from pregnant and postpartum rats. Mottino, A.D., Hoffman, T., Jennes, L., Cao, J., Vore, M. Am. J. Physiol. Gastrointest. Liver Physiol. (2001) [Pubmed]
  7. Transport of glutathione S-conjugates in Escherichia coli. Kałuzna, A., Bartosz, G. Biochem. Mol. Biol. Int. (1997) [Pubmed]
  8. Multiple routes and regulation by tyrosine phosphorylation characterize the ATP-dependent transport of 2,4-dinitrophenyl S-glutathione in inside-out vesicles from human erythrocytes. Saxena, M., Henderson, G.B. Arch. Biochem. Biophys. (1997) [Pubmed]
  9. Impaired hepatocanalicular organic anion transport in endotoxemic rats. Roelofsen, H., Schoemaker, B., Bakker, C., Ottenhoff, R., Jansen, P.L., Elferink, R.P. Am. J. Physiol. (1995) [Pubmed]
  10. Temocaprilat, a novel angiotensin-converting enzyme inhibitor, is excreted in bile via an ATP-dependent active transporter (cMOAT) that is deficient in Eisai hyperbilirubinemic mutant rats (EHBR). Ishizuka, H., Konno, K., Naganuma, H., Sasahara, K., Kawahara, Y., Niinuma, K., Suzuki, H., Sugiyama, Y. J. Pharmacol. Exp. Ther. (1997) [Pubmed]
  11. Differences in substrate specificity among glutathione conjugates (GS-X) pump family members: comparison between multidrug resistance-associated protein and a novel transporter expressed on a cisplatin-resistant cell line (KCP-4). Ueda, K., Suzuki, H., Akiyama, S., Sugiyama, Y. Jpn. J. Cancer Res. (1999) [Pubmed]
  12. RLIP76 is the major ATP-dependent transporter of glutathione-conjugates and doxorubicin in human erythrocytes. Sharma, R., Singhal, S.S., Cheng, J., Yang, Y., Sharma, A., Zimniak, P., Awasthi, S., Awasthi, Y.C. Arch. Biochem. Biophys. (2001) [Pubmed]
  13. Do multidrug resistance-associated protein-1 and -2 play any role in the elimination of estradiol-17 beta-glucuronide and 2,4-dinitrophenyl-S-glutathione across the blood-cerebrospinal fluid barrier? Lee, Y.J., Kusuhara, H., Sugiyama, Y. Journal of pharmaceutical sciences. (2004) [Pubmed]
  14. Modulation by (iso)flavonoids of the ATPase activity of the multidrug resistance protein. Hooijberg, J.H., Broxterman, H.J., Heijn, M., Fles, D.L., Lankelma, J., Pinedo, H.M. FEBS Lett. (1997) [Pubmed]
WikiGenes - Universities