David M. Clarke
Toronto, ON M5S1A8, Canada
Last Updated: 09/26/2026
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Found 26 publications
A short cross-linker activates human P-glycoprotein missing a catalytic carboxylate.
Journal: Biochemical pharmacology
Published: July 21, 2017
Thiol-reactive drug substrates of human P-glycoprotein label the same sites to activate ATPase activity in membranes or dodecyl maltoside detergent micelles.
Journal: Biochemical and biophysical research communications
Published: May 10, 2017
Inflammatory Cell Findings in the Female Rabbit Heart and Stress-associated Exacerbation with Handling and Procedures Used in Nonclinical Studies.
Journal: Toxicologic pathology
Published: March 29, 2017
Corrector VX-809 promotes interactions between cytoplasmic loop one and the first nucleotide-binding domain of CFTR.
Journal: Biochemical pharmacology
Published: January 30, 2017
Attachment of a 'molecular spring' restores drug-stimulated ATPase activity to P-glycoprotein lacking both Q loop glutamines.
Journal: Biochemical and biophysical research communications
Published: December 07, 2016
Drugs Modulate Interactions between the First Nucleotide-Binding Domain and the Fourth Cytoplasmic Loop of Human P-Glycoprotein.
Journal: Biochemistry
Published: May 10, 2016
P-glycoprotein ATPase activity requires lipids to activate a switch at the first transmission interface.
Journal: Biochemical and biophysical research communications
Published: February 23, 2016
Mapping the Binding Site of the Inhibitor Tariquidar That Stabilizes the First Transmembrane Domain of P-glycoprotein.
Journal: The Journal of biological chemistry
Published: September 28, 2015
The Transmission Interfaces Contribute Asymmetrically to the Assembly and Activity of Human P-glycoprotein.
Journal: The Journal of biological chemistry
Published: March 16, 2015
Tariquidar inhibits P-glycoprotein drug efflux but activates ATPase activity by blocking transition to an open conformation.
Journal: Biochemical pharmacology
Published: September 03, 2014
Cysteines introduced into extracellular loops 1 and 4 of human P-glycoprotein that are close only in the open conformation spontaneously form a disulfide bond that inhibits drug efflux and ATPase activity.
Journal: The Journal of biological chemistry
Published: July 24, 2014
Identification of the distance between the homologous halves of P-glycoprotein that triggers the high/low ATPase activity switch.
Journal: The Journal of biological chemistry
Published: February 14, 2014
Last Updated: 09/26/2026