D
Dennis K. Stone
Researcher at University of Texas Southwestern Medical Center
Publications - 37
Citations - 2098
Dennis K. Stone is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Vesicle & ATPase. The author has an hindex of 25, co-authored 37 publications receiving 2080 citations. Previous affiliations of Dennis K. Stone include Cornell University & University of Texas Health Science Center at San Antonio.
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Journal ArticleDOI
An ATP-driven proton pump in clathrin-coated vesicles.
TL;DR: Analyses performed during the purification procedure demonstrated that the oligomycin-resistant pump was concentrated and highly purified in the fractions containing coated vesicles.
Journal ArticleDOI
Bafilomycin inhibits proton flow through the H+ channel of vacuolar proton pumps
TL;DR: Vacuolar-type proton-translocating ATPases are complex heterooligomers that are characterized by a specific inhibition by bafilomycin A1, which is termed VB.
Journal ArticleDOI
Isolation and reconstitution of the clathrin-coated vesicle proton translocating complex.
Xiao Song Xie,Dennis K. Stone +1 more
TL;DR: It is reported that the entire proton transporting complex has been solubilized and purified 200-fold and catalyzes azide-resistant, N-ethylmaleimide-sensitive H+ transport manifested as both generation of a pH gradient and an electrical gradient.
Journal ArticleDOI
Determinants of clathrin-coated vesicle acidification.
TL;DR: The proton-translocating ATPase of clathrin-coated vesicles of bovine brain is characterized by ATP specificity, and chloride transport can be observed independent of proton movements in the absence of ATP.
Journal ArticleDOI
Structure of the 116-kDa polypeptide of the clathrin-coated vesicle/synaptic vesicle proton pump.
Mark S. Perin,Victor A. Fried,Dennis K. Stone,Dennis K. Stone,Xiao Song Xie,Thomas C. Südhof,Thomas C. Südhof +6 more
TL;DR: The structural properties of the 116-kDa proton pump polypeptide agree well with its proposed function in coupling ATP hydrolysis by the cytoplasmic subunits to proton translocation by the intramembranous components of the pump.