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George T. Hanson

Researcher at University of Oregon

Publications -  11
Citations -  3057

George T. Hanson is an academic researcher from University of Oregon. The author has contributed to research in topics: Green fluorescent protein & Fluorescence. The author has an hindex of 9, co-authored 11 publications receiving 2860 citations.

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Investigating Mitochondrial Redox Potential with Redox-sensitive Green Fluorescent Protein Indicators

TL;DR: By substitution of surface-exposed residues on the Aequorea victoria green fluorescent protein with cysteines in appropriate positions to form disulfide bonds, reduction-oxidation-sensitive GFPs (roGFPs) have been created and targeted to the mitochondria in HeLa cells.
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Imaging Dynamic Redox Changes in Mammalian Cells with Green Fluorescent Protein Indicators

TL;DR: The response of the redox probes under physiological redox changes during superoxide bursts in macrophage cells, hyperoxic and hypoxic conditions, and in responses to H2O2-stimulating agents, e.g. epidermal growth factor and lysophosphatidic acid is investigated.
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Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein.

TL;DR: The observed red shift of the T203Y YFP variant is proposed to be mainly due to the additional polarizability of the pi-stacked Tyr203, which significantly extend the pH range over which GFPs may be employed as pH indicators in live cells.
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Structural and spectral response of green fluorescent protein variants to changes in pH.

TL;DR: P pH titrations of popular GFP S65T/H148D variants indicate that the chromophore pKa can be modulated over a broad range from 6 to 8, allowing for pH determination from pH 5 to pH 9.6.
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The permeability transition pore signals apoptosis by directing Bax translocation and multimerization

TL;DR: It is reported that directed repetitive gating of the PTP triggers a delayed Cyt.c efflux, which is not associated with mitochondrial swelling, and subcellular imaging shows that PTP opening signals the redistribution of the cytosolic protein Bax to the mitochondria, where it secondarily forms clusters that appear to be a prerequisite for CyT.c release.