M
Mario M. Moronne
Researcher at Lawrence Berkeley National Laboratory
Publications - 9
Citations - 9326
Mario M. Moronne is an academic researcher from Lawrence Berkeley National Laboratory. The author has contributed to research in topics: Voltage clamp & Molecular beacon. The author has an hindex of 7, co-authored 9 publications receiving 9063 citations.
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Journal ArticleDOI
Semiconductor Nanocrystals as Fluorescent Biological Labels
TL;DR: Semiconductor nanocrystals prepared for use as fluorescent probes in biological staining and diagnostics have a narrow, tunable, symmetric emission spectrum and are photochemically stable.
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Direct Physical Measure of Conformational Rearrangement Underlying Potassium Channel Gating
TL;DR: During channel activation, a stretch of at least seven amino acids of the putative transmembrane segment S4 moved from a buried position into the extracellular environment, providing physical evidence in support of the hypothesis that S4 is the voltage sensor of voltage-gated ion channels.
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Role of the Plasmodium falciparum mature-parasite-infected erythrocyte surface antigen (MESA/PfEMP-2) in malarial infection of erythrocytes
Cathleen Magowan,Ross L. Coppel,Audrey O.T. Lau,Mario M. Moronne,Gil Tchernia,Narla Mohandas +5 more
TL;DR: Findings suggest that MESA binding to protein 4.1 plays a major role in intraerythrocytic parasite viability, similar to that played in cytoadherence of infected ERYthrocytes.
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Detection of functional groups and antibodies on microfabricated surfaces by confocal microscopy.
TL;DR: Fluorescence confocal microscopy was used to characterize micron-sized microfabricated silicon particles and planar oxide surfaces after silanization and immobilization of IgG antibody and estimates of the surface density were consistent with 8.3% of a monolayer of covalent antibody.
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Estimate of the number of urea transport sites in erythrocyte ghosts using a hydrophobic mercurial.
TL;DR: It is concluded that a significant hydrophobic barrier limits access to the urea inhibition site, suggesting that the Urea site is buried in the bilayer or in ahydrophobic region of the transporter.