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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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Light-mediated activation reveals a key role for Rac in collective guidance of cell movement in vivo

TL;DR: It is shown that focal activation of Rac is also sufficient to polarize an entire group of cells in vivo, specifically the border cells of the Drosophila ovary, and further shows that photoactivatable proteins are effective tools in vivo.
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Vinculin modulation of paxillin–FAK interactions regulates ERK to control survival and motility

TL;DR: Vinculin regulates survival and motility via ERK by controlling the accessibility of paxillin for FAK interaction, which results in increased survival due to up-regulated activity of extracellular signal–regulated kinase (ERK).
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Rho Family Proteins Modulate Rapid Apoptosis Induced by Cytotoxic T Lymphocytes and Fas

TL;DR: It is demonstrated that all three Rho family members are involved in CTL- and Fas-induced killing and the ability of Rac to enhance apoptosis was decreased by point mutations reported to block Rac induction of actin polymerization.
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LOVTRAP: an optogenetic system for photoinduced protein dissociation

TL;DR: By reversibly sequestering proteins at mitochondria, LOVTRAP precisely modulated the proteins' access to the cell edge, demonstrating a naturally occurring 3-mHz cell-edge oscillation driven by interactions of Vav2, Rac1, and PI3K proteins.
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Effects of cell tension on the small GTPase Rac

TL;DR: It is demonstrated that equibiaxial stretch inhibited lamellipodia formation through deactivation of Rac, and GAP-resistant, constitutively active V12Rac reversed this inhibition, supporting a critical role for Rac inhibition in the response to stretch.