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Tip W Loo

Showing results (11-20 of 70) with videos related to

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Methods in Molecular Biology (Clifton, N.J.)|July 4, 2003
Application of chemical chaperones to the rescue of folding defectsTip W Loo, David M Clarke
Biochemical and Biophysical Research Communications|March 2, 2005
Do drug substrates enter the common drug-binding pocket of P-glycoprotein through "gates"?Tip W Loo, David M Clarke
Biochemical and Biophysical Research Communications|May 24, 2017
Thiol-reactive drug substrates of human P-glycoprotein label the same sites to activate ATPase activity in membranes or dodecyl maltoside detergent micellesTip W Loo, David M Clarke
Methods in Molecular Biology (Clifton, N.J.)|May 20, 2011
Repair of CFTR folding defects with correctors that function as pharmacological chaperonesTip W Loo, David M Clarke
The Journal of Biological Chemistry|October 29, 2015
Mapping the Binding Site of the Inhibitor Tariquidar That Stabilizes the First Transmembrane Domain of P-glycoproteinTip W Loo, David M Clarke
Biochemical Pharmacology|December 3, 2014
Tariquidar inhibits P-glycoprotein drug efflux but activates ATPase activity by blocking transition to an open conformationTip W Loo, David M Clarke
Biochemical Pharmacology|January 14, 2014
The cystic fibrosis V232D mutation inhibits CFTR maturation by disrupting a hydrophobic pocket rather than formation of aberrant interhelical hydrogen bondsTip W Loo, David M Clarke
The Journal of Biological Chemistry|February 14, 2014
Identification of the distance between the homologous halves of P-glycoprotein that triggers the high/low ATPase activity switchTip W Loo, David M Clarke
Biochemical and Biophysical Research Communications|December 28, 2016
Attachment of a 'molecular spring' restores drug-stimulated ATPase activity to P-glycoprotein lacking both Q loop glutaminesTip W Loo, David M Clarke
The Journal of Physiology|February 25, 2006
Using a cysteine-less mutant to provide insight into the structure and mechanism of CFTRTip W Loo, David M Clarke
Pageof 7

Showing results (11-20 of 70) with videos related to

Sort By:
Pageof 7
Methods in Molecular Biology (Clifton, N.J.)|July 4, 2003
Application of chemical chaperones to the rescue of folding defectsTip W Loo, David M Clarke
Biochemical and Biophysical Research Communications|March 2, 2005
Do drug substrates enter the common drug-binding pocket of P-glycoprotein through "gates"?Tip W Loo, David M Clarke
Biochemical and Biophysical Research Communications|May 24, 2017
Thiol-reactive drug substrates of human P-glycoprotein label the same sites to activate ATPase activity in membranes or dodecyl maltoside detergent micellesTip W Loo, David M Clarke
Methods in Molecular Biology (Clifton, N.J.)|May 20, 2011
Repair of CFTR folding defects with correctors that function as pharmacological chaperonesTip W Loo, David M Clarke
The Journal of Biological Chemistry|October 29, 2015
Mapping the Binding Site of the Inhibitor Tariquidar That Stabilizes the First Transmembrane Domain of P-glycoproteinTip W Loo, David M Clarke
Biochemical Pharmacology|December 3, 2014
Tariquidar inhibits P-glycoprotein drug efflux but activates ATPase activity by blocking transition to an open conformationTip W Loo, David M Clarke
Biochemical Pharmacology|January 14, 2014
The cystic fibrosis V232D mutation inhibits CFTR maturation by disrupting a hydrophobic pocket rather than formation of aberrant interhelical hydrogen bondsTip W Loo, David M Clarke
The Journal of Biological Chemistry|February 14, 2014
Identification of the distance between the homologous halves of P-glycoprotein that triggers the high/low ATPase activity switchTip W Loo, David M Clarke
Biochemical and Biophysical Research Communications|December 28, 2016
Attachment of a 'molecular spring' restores drug-stimulated ATPase activity to P-glycoprotein lacking both Q loop glutaminesTip W Loo, David M Clarke
The Journal of Physiology|February 25, 2006
Using a cysteine-less mutant to provide insight into the structure and mechanism of CFTRTip W Loo, David M Clarke
Pageof 7