P
Pamela L. Tuma
Researcher at The Catholic University of America
Publications - 54
Citations - 2648
Pamela L. Tuma is an academic researcher from The Catholic University of America. The author has contributed to research in topics: Membrane protein & Acetylation. The author has an hindex of 22, co-authored 48 publications receiving 2302 citations. Previous affiliations of Pamela L. Tuma include Northwestern University & Johns Hopkins University School of Medicine.
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Journal ArticleDOI
Transcytosis: Crossing Cellular Barriers
Pamela L. Tuma,Ann L. Hubbard +1 more
TL;DR: The authors' knowledge of the different cell types using transcytosis in vivo, the variety of cargo moved, and the diverse pathways for delivering that cargo are summarized.
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ABCG5 and ABCG8 are obligate heterodimers for protein trafficking and biliary cholesterol excretion.
Gregory A. Graf,Liqing Yu,Wei Ping Li,Robert D. Gerard,Pamela L. Tuma,Jonathan Cohen,Helen H. Hobbs +6 more
TL;DR: It is confirmed, in vivo, that G5 is localized to the apical membranes of mouse enterocytes and hepatocytes and that adenoviral expression of G2 in the presence or absence of G5 or G8 failed to promote sterol excretion into bile.
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Activation of dynamin GTPase by acidic phospholipids and endogenous rat brain vesicles.
TL;DR: An analysis of the enzymatic and membrane binding properties of dynamin has found that the acidic phospholipids, phosph atidylserine, phosphatidylglycerol, and phosphAtidylinositol, are able to stimulate GTP hydrolysis in a manner similar to activation previously shown with microtubules.
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VAP-33 localizes to both an intracellular vesicle population and with occludin at the tight junction.
TL;DR: The results suggest that tight junctions may participate in vesicle targeting at the plasma membrane or alternatively VAP-33 may regulate the localization of occludin.
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Activation of dynamin GTPase is a result of positive cooperativity.
TL;DR: Analysis of dynamin enzymatic properties suggests that cooperative interactions between dynamin molecules are responsible for the apparent activation of GTPase observed and are likely involved in dynamin function in vivo.