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Alan E. Friedman
Researcher at State University of New York System
Publications - 86
Citations - 6211
Alan E. Friedman is an academic researcher from State University of New York System. The author has contributed to research in topics: Ruthenium & Metallacycle. The author has an hindex of 29, co-authored 85 publications receiving 5601 citations. Previous affiliations of Alan E. Friedman include University of Rochester & Eastman Kodak Company.
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Journal ArticleDOI
Molecular light switch for DNA : Ru(bpy)2(dppz)2+
Alan E. Friedman,Jean Claude Chambron,Jean-Pierre Sauvage,Nicholas J. Turro,Jacqueline K. Barton +4 more
TL;DR: In this article, a transition-metal complex was used as a molecular light switch for double-helical DNA, which showed no photoluminescence in aqueous solution at ambient temperatures.
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Transport pathways for clearance of human Alzheimer's amyloid β-peptide and apolipoproteins E and J in the mouse central nervous system
Robert D. Bell,Abhay P. Sagare,Alan E. Friedman,Gurrinder S. Bedi,David M. Holtzman,Rashid Deane,Berislav V. Zlokovic +6 more
TL;DR: Aβ, apoE, and apoJ are cleared from brain by different transport pathways, andApoE and ApoJ may critically modify Aβ clearance at the BBB.
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A multimodal RAGE-specific inhibitor reduces amyloid β–mediated brain disorder in a mouse model of Alzheimer disease
Rashid Deane,Itender Singh,Abhay P. Sagare,Robert D. Bell,Nathan T. Ross,Barbra LaRue,Rachal Love,Sheldon Perry,Nicole Paquette,Richard J. Deane,Meenakshisundaram Thiyagarajan,Troy J. Zarcone,Günter Fritz,Alan E. Friedman,Benjamin L. Miller,Berislav V. Zlokovic +15 more
TL;DR: The data suggest that FPS-ZM1 is a potent multimodal RAGE blocker that effectively controls progression of Aβ-mediated brain disorder and that it may have the potential to be a disease-modifying agent for AD.
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Characterization of dipyridophenazine complexes of ruthenium(II): the light switch effect as a function of nucleic acid sequence and conformation.
TL;DR: Spectroscopic parameters for two novel ruthenium complexes on binding to nucleic acids of varying sequences and conformations have been determined and are shown here to be unique reporters of nucleic acid structures and may become valuable in the design of new diagnostics for DNA.
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The influence of protein adsorption on nanoparticle association with cultured endothelial cells
TL;DR: It is concluded that cellular association is not dependent on the identity of adsorbed proteins and therefore unlikely to require specific binding to any particular cellular receptors.