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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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Engineering proteins for allosteric control by light or ligands.

TL;DR: A detailed protocol to generate genetically encoded analogs of proteins that can be allosterically controlled by either rapamycin or blue light is described, as well as how to identify sites for insertion of engineered regulatory domains and test the analogs biochemically and in living cells.
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STEF/TIAM2-mediated Rac1 activity at the nuclear envelope regulates the perinuclear actin cap.

TL;DR: It is demonstrated that STEF/TIAM2, a Rac1 selective guanine nucleotide exchange factor, localises at the nuclear envelope, co-localising with the key perinuclear proteins Nesprin-2G and Non-muscle myosin IIB (NMMIIB), where it regulates perin nuclear Rac1 activity.
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RhoA GTPase Activation by TLR2 and TLR3 Ligands: Connecting via Src to NF-κB

TL;DR: The results suggest that RhoA plays a role downstream of MyD88-dependent and -independent TLR signaling and acts as a molecular switch downstream of TLR-Src-initiated pathways.
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An optogenetic tool for the activation of endogenous diaphanous-related formins induces thickening of stress fibers without an increase in contractility

TL;DR: A decoupling between F‐actin accumulation and contractility in stress fibers is suggested and the utility of photoactivatable diaphanous autoregulatory domain is demonstrated for the study of diaphAnous‐related formin function in cells.
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Visualizing and quantifying adhesive signals

TL;DR: Computational multiplexing is outlined as a framework for the integration of data from high-resolution live cell imaging approaches to measure forces, assembly, and interaction ofAdhesion components, and the activation of adhesion-mediated signals.