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研究领域

My research interests lie in elucidating the mechanistic, functional details of proteins that do important jobs in the cell, both in health and disease. To date these have included membrane transporter proteins of the ABC superfamily (ATP Binding Casette) involved in drug resistance in cancer, and the chaperone proteins involved in removing the clathrin coat from endocytosed vesicles, both of which use ATP hydrolysis to drive their function, and are closely associated with cell membranes.

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Rothnie A., Clarke A.R., Kuzmic P., Cameron A. & Smith C.J. (2011) A sequential mechanism for clathrin cage disassembly by Hsc70 and auxilin.Proc. Natl. Acad. Sci USA108; 6927-32 Maeno K., Nakajima A., Conseil G., Rothnie A., Deeley R.G. & Cole S.P.C (2009) Molecular basis for reduced estrone sulphate transport & altered modulator sensitivity of TM6 and TM17 mutants of MRP1 (ABCC1). Drug Metab. & Dispos. 37; 1411-20. Conseil G., Rothnie A., Deeley R.G. & Cole S.P.C. (2009). Multiple roles of charged amino acids in cytoplasmic loop 7 for the expression and function of the multidrug and organic anion transporter MRP1 (ABCC1). Mol. Pharmacol. 75; 397-406. Heikal A., Box K., Rothnie A., Storm J., Callaghan R. & Allen M. (2009) The stabilisation of purified, reconstituted, P-glycoprotein by freeze drying with disaccharides. Cryobiology 58; 37-44. Rothnie A., Conseil G., Lau A.Y.T., Deeley R.G. & Cole S.P.C. (2008) Mechanistic differences between GSH transport by MRP1 (ABCC1) and GSH modulation of MRP1-mediated transport. Mol. Pharmacol. 74; 1630-40. Rothnie A., Callaghan R., Deeley R.G. & Cole S.P.C. (2006). Role of GSH in estrone sulphate binding and translocation by the multidrug resistance protein 1 (MRP1, ABCC1). J. Biol. Chem. 281; 13906-14. Rothnie A., Storm J., McMahon R., Taylor A., Kerr I.D. & Callaghan R. (2005). The coupling mechanism of P-glycoprotein involves residue L339 in the sixth membrane spanning segment. FEBS Letts. 579; 3984-90. Rothnie A., Storm J., Campbell J., Linton K.J., Kerr I.D. & Callaghan R. (2004). The topography of transmembrane segment six is altered during the catalytic cycle of P-glycoprotein. J. Biol. Chem. 279; 34913-21. Martin C., Walker J., Rothnie A. & Callaghan R. (2003). The expression of P-glycoprotein does influence the distribution of novel fluorescent compounds in solid tumour models. Brit. J. Cancer 89; 1581-9. Gabriel M.P., Storm J., Rothnie A., Taylor A.M., Linton K.J., Kerr I.D. & Callaghan R. (2003). Communication between the nucleotide binding domains of P-glycoprotein occurs via conformational changes that involve residue 508. Biochemistry 42; 7780-9. Rothnie A., Theron D., Soceneantu L., Martin C., Traikia M., Berridge G., Higgins C.F., Devaux P.P. & Callaghan R. (2001). The importance of cholesterol in maintenance of P-glycoprotein activity and its membrane perturbing influence. Eur. Biophys. J. 30; 30-42.

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