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Klaus M. Hahn

Researcher at University of North Carolina at Chapel Hill

Publications -  215
Citations -  16976

Klaus M. Hahn is an academic researcher from University of North Carolina at Chapel Hill. The author has contributed to research in topics: RHOA & Proto-oncogene tyrosine-protein kinase Src. The author has an hindex of 61, co-authored 210 publications receiving 15343 citations. Previous affiliations of Klaus M. Hahn include University of California, Berkeley & University of California, San Diego.

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LOVTRAP: A Versatile Method to Control Protein Function with Light.

TL;DR: The technique relies on binding of an engineered Zdk domain to a LOV2 domain, with affinity <30 nM in the dark and >500 nM upon irradiation between 400 and 500 nm, to reversibly sequester and release proteins from cellular membranes using light.
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Multiplexed GTPase and GEF biosensor imaging enables network connectivity analysis.

TL;DR: Biosensors of guanine exchange factors (GEFs) and red-shifted GTPase biosensors are used to visualize GEF and GTPases activities in the same cells and enable correlation analysis to reveal which GEF–GTPase interactions regulate cell movement.
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Membrane-Permeant, Environment-Sensitive Dyes Generate Biosensors within Living Cells

TL;DR: This work modified a proven, environment-sensitive biosensor fluorophore so that it can pass through cell membranes without staining intracellular compartments and can be attached to proteins within living cells using unnatural amino acid (UAA) mutagenesis.
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Mineral Processing and Metallurgical Treatment of Lead Vanadate Ores

TL;DR: In this paper, the authors provide an overview of lead vanadate sources and the challenges in previous mechanical and metallurgical processing activities, but show opportunities to ensure vanadium production out of primary sources in the future.
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An oxonol dye is the most potent known inhibitor of band 3-mediated anion exchange.

TL;DR: DiBA may be useful for investigating conformational changes during anion exchange and for stopping transport without preventing substrate binding, however, when diBA and other oxonols are used to sense membrane potential, they may have undesirable side effects on anion transport processes.