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Alexander R. Lippert

Researcher at Southern Methodist University

Publications -  63
Citations -  3798

Alexander R. Lippert is an academic researcher from Southern Methodist University. The author has contributed to research in topics: Chemiluminescence & Chemistry. The author has an hindex of 22, co-authored 53 publications receiving 3023 citations. Previous affiliations of Alexander R. Lippert include University of California, Berkeley & University of Pennsylvania.

Papers
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Journal ArticleDOI

Reaction-based fluorescent probes for selective imaging of hydrogen sulfide in living cells.

TL;DR: A pair of new reaction-based fluorescent probes for selective imaging of H(2)S in living cells that exploit the H( 2)S-mediated reduction of azides to fluorescent amines and display high selectivity over other biologically relevant reactive sulfur, oxygen, and nitrogen species are reported.
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Boronate Oxidation as a Bioorthogonal Reaction Approach for Studying the Chemistry of Hydrogen Peroxide in Living Systems

TL;DR: Studies from the laboratory are summarized using the H(2)O(2)-mediated oxidation of aryl boronates to phenols as a bioorthogonal approach to detect fluxes of this important ROS in living systems.
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A Reaction-Based Fluorescent Probe for Selective Imaging of Carbon Monoxide in Living Cells Using a Palladium-Mediated Carbonylation

TL;DR: CO Probe 1 (COP-1) is capable of detecting CO both in aqueous buffer and in live cells with high selectivity over a range of biologically relevant reactive small molecules, providing a potentially powerful approach for interrogating its chemistry in biological systems.
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Cell-trappable fluorescent probes for endogenous hydrogen sulfide signaling and imaging H2O2-dependent H2S production

TL;DR: Sulfidefluor-7 acetoxymethyl ester allows for direct, real-time visualization of endogenous H2S produced in live human umbilical vein endothelial cells upon stimulation with vascular endothelial growth factor (VEGF).
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A chemoenzymatic approach toward the rapid and sensitive detection of O-GlcNAc posttranslational modifications.

TL;DR: This approach exploits the ability of an engineered mutant of beta-1,4-galactosyltransferase to selectively transfer an unnatural ketone functionality onto O-GlcNAc glycosylated proteins, thereby enabling chemiluminescent detection of the modified protein.