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ATP binding to the first nucleotide-binding domain of multidrug resistance protein MRP1 increases binding and hydrolysis of ATP and trapping of ADP at the second domain.
Hou YX, Cui L, Riordan JR, Chang XB. Hou YX, et al. J Biol Chem. 2002 Feb 15;277(7):5110-9. doi: 10.1074/jbc.M107133200. Epub 2001 Dec 7. J Biol Chem. 2002. PMID: 11741902 Free article.
P., and Deeley, R. G. (2000) J. Biol. Chem. 275, 13098-13108; Hou, Y., Cui, L., Riordan, J. R., and Chang, X. (2000) J. Biol. ...Mutations of Walker A or B motifs in either NBD greatly reduced their ability to be labeled by [alpha-(32)P]8-N(3)ADP as well as by eithe …
P., and Deeley, R. G. (2000) J. Biol. Chem. 275, 13098-13108; Hou, Y., Cui, L., Riordan, J. R., and Chang, X. (2000) J. Biol. …
ATP binding, not hydrolysis, at the first nucleotide-binding domain of multidrug resistance-associated protein MRP1 enhances ADP.Vi trapping at the second domain.
Hou YX, Riordan JR, Chang XB. Hou YX, et al. J Biol Chem. 2003 Feb 7;278(6):3599-605. doi: 10.1074/jbc.M210480200. Epub 2002 Nov 27. J Biol Chem. 2003. PMID: 12458196 Free article.
We found that ATP binding to the first NBD of MRP1 increases binding and trapping of ADP at the second domain (Hou, Y., Cui, L., Riordan, J. R., and Chang, X. (2002) J. Biol. ...
We found that ATP binding to the first NBD of MRP1 increases binding and trapping of ADP at the second domain (Hou, Y., Cui, L …
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