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

Sort By:
Pageof 2
You have reached the last page of results.This site can display upto 20 results.
Biochemistry|July 13, 2005
The role of hydrogen bond acceptor groups in the interaction of substrates with Pdr5p, a major yeast drug transporterLeanne Hanson, Leopold May, Pamela Tuma, et al.
The Journal of Biological Chemistry|December 24, 2002
Studies with novel Pdr5p substrates demonstrate a strong size dependence for xenobiotic effluxJohn Golin, Suresh V Ambudkar, Michael M Gottesman, et al.
The Journal of Biological Chemistry|September 11, 2013
The deviant ATP-binding site of the multidrug efflux pump Pdr5 plays an active role in the transport cycleChristopher Furman, Jitender Mehla, Neeti Ananthaswamy, et al.
Biochemistry|April 30, 2010
The signaling interface of the yeast multidrug transporter Pdr5 adopts a cis conformation, and there are functional overlap and equivalence of the deviant and canonical Q-loop residuesNeeti Ananthaswamy, Robert Rutledge, Zuben E Sauna, et al.
Drug Resistance Updates : Reviews and Commentaries in Antimicrobial and Anticancer Chemotherapy|October 5, 2023
Second-site suppressor mutations reveal connection between the drug-binding pocket and nucleotide-binding domain 1 of human P-glycoprotein (ABCB1)Megumi Murakami, Andaleeb Sajid, Sabrina Lusvarghi, et al.
Antimicrobial Agents and Chemotherapy|December 21, 2012
The transmission interface of the Saccharomyces cerevisiae multidrug transporter Pdr5: Val-656 located in intracellular loop 2 plays a major role in drug resistanceMarianne T Downes, Jitender Mehla, Neeti Ananthaswamy, et al.
Biochemistry|October 25, 2007
Complete inhibition of the Pdr5p multidrug efflux pump ATPase activity by its transport substrate clotrimazole suggests that GTP as well as ATP may be used as an energy sourceJohn Golin, Zachary N Kon, Chung-Pu Wu, et al.
G3 (Bethesda, Md.)|November 24, 2019
Nonsynonymous Mutations in Linker-2 of the Pdr5 Multidrug Transporter Identify a New RNA Stability ElementHadiar Rahman, Andrew Rudrow, Joshua Carneglia, et al.
The Journal of Biological Chemistry|October 10, 2008
Mutations define cross-talk between the N-terminal nucleotide-binding domain and transmembrane helix-2 of the yeast multidrug transporter Pdr5: possible conservation of a signaling interface for coupling ATP hydrolysis to drug transportZuben E Sauna, Sherry Supernavage Bohn, Robert Rutledge, et al.
The Journal of Biological Chemistry|November 12, 2022
Residues forming the gating regions of asymmetric multidrug transporter Pdr5 also play roles in conformational switching and protein foldingMaryam Alhumaidi, Lea-Marie Nentwig, Hadiar Rahman, et al.
Pageof 2