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The Journal of Biological Chemistry|November 1, 1996
The minimum functional unit of human P-glycoprotein appears to be a monomerT W Loo, D M ClarkeThe Journal of Membrane Biology|February 4, 2006
Recent progress in understanding the mechanism of P-glycoprotein-mediated drug effluxT W Loo, D M ClarkeThe Journal of Biological Chemistry|August 24, 2001
Determining the dimensions of the drug-binding domain of human P-glycoprotein using thiol cross-linking compounds as molecular rulersT W Loo, D M ClarkeThe American Journal of Physiology|July 1, 1994
Functional expression of human renal Na+/Ca2+ exchanger in insect cellsT W Loo, D M ClarkeBiochemistry|November 29, 1994
Mutations to amino acids located in predicted transmembrane segment 6 (TM6) modulate the activity and substrate specificity of human P-glycoproteinT W Loo, D M ClarkeThe Journal of Biological Chemistry|January 24, 1998
Identification of residues in the drug-binding site of human P-glycoprotein using a thiol-reactive substrateT W Loo, D M ClarkeThe Journal of Biological Chemistry|February 22, 2000
The packing of the transmembrane segments of human multidrug resistance P-glycoprotein is revealed by disulfide cross-linking analysisT W Loo, D M ClarkeBiochemistry and Cell Biology = Biochimie Et Biologie Cellulaire|July 30, 1999
Merck Frosst Award Lecture 1998. Molecular dissection of the human multidrug resistance P-glycoproteinT W Loo, D M ClarkeThe Journal of Biological Chemistry|June 29, 2001
Cross-linking of human multidrug resistance P-glycoprotein by the substrate, tris-(2-maleimidoethyl)amine, is altered by ATP hydrolysis. Evidence for rotation of a transmembrane helixT W Loo, D M ClarkeThe Journal of Biological Chemistry|May 12, 2000
Drug-stimulated ATPase activity of human P-glycoprotein is blocked by disulfide cross-linking between the nucleotide-binding sitesT W Loo, D M ClarkePageof 11