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Wade D. Van Horn

Researcher at Arizona State University

Publications -  50
Citations -  1808

Wade D. Van Horn is an academic researcher from Arizona State University. The author has contributed to research in topics: Transient receptor potential channel & Medicine. The author has an hindex of 20, co-authored 43 publications receiving 1533 citations. Previous affiliations of Wade D. Van Horn include University of Utah & Arizona's Public Universities.

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The Amyloid Precursor Protein Has a Flexible Transmembrane Domain and Binds Cholesterol

TL;DR: NMR titration of C99 reveals a binding site for cholesterol, providing mechanistic insight into how cholesterol promotes amyloidogenesis and may aid in the design of Alzheimer’s therapeutics.
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Solution Nuclear Magnetic Resonance Structure of Membrane-Integral Diacylglycerol Kinase

TL;DR: The three-dimensional structure of the DAGK homotrimer is determined with the use of solution nuclear magnetic resonance, providing insight into the determinants of lipid substrate specificity and phosphotransferase activity.
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Recent Advances in the Application of Solution NMR Spectroscopy to Multi-Span Integral Membrane Proteins.

TL;DR: Recent progress in the application of solution NMR of IMPs is highlighted to outline sample preparative and spectroscopic advances that have led to this breakthrough and there is reason to believe that this recent progress reflects only the beginning of a phase of exponential growth in the use of solutions NMR methods to solve important problems in membrane protein structural biology.
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The structural diversity of artificial genetic polymers

TL;DR: This review provides a structural perspective on known antiparallel duplex structures in which at least one strand of the Watson–Crick duplex is composed entirely of XNA.
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Reverse micelle encapsulation as a model for intracellular crowding.

TL;DR: The data presented here provide an important bridge between commonly employed dilute in vitro studies and studies of the effects of a crowded environment, as found in vivo, and reconcile alternative interpretations of protein cold denaturation within reverse micelles.