M
Moritz Bünemann
Researcher at University of Marburg
Publications - 97
Citations - 6625
Moritz Bünemann is an academic researcher from University of Marburg. The author has contributed to research in topics: Receptor & G protein-coupled receptor. The author has an hindex of 37, co-authored 93 publications receiving 6053 citations. Previous affiliations of Moritz Bünemann include University of Würzburg & Northwestern University.
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Journal ArticleDOI
Novel single chain cAMP sensors for receptor-induced signal propagation.
TL;DR: The development of novel fluorescent indicators for cAMP based on the cAMP-binding domains of Epac and PKA, comprised of only a single binding site lacking cooperativity, catalytic properties, and interactions with other proteins, allow us to easily image free intracellular cAMP and rapid signaling events.
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A FlAsH-based FRET approach to determine G protein-coupled receptor activation in living cells.
Carsten Hoffmann,Guido M. Gaietta,Moritz Bünemann,Stephen R. Adams,Silke Oberdorff-Maass,Björn Behr,Jean-Pierre Vilardaga,Roger Y. Tsien,Mark H. Ellisman,Martin J. Lohse +9 more
TL;DR: FRET from CFP to FlAsH reports GPCR activation in living cells without disturbing receptor function and shows that the small size of the tetracysteine-biarsenical tag can be decisively advantageous.
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Measurement of the millisecond activation switch of G protein-coupled receptors in living cells.
TL;DR: A generally applicable fluorescence-based technique is developed that allows the comparison of agonist and partial agonist intrinsic activities at the receptor level and provides evidence for millisecond activation times of GPCRs.
Journal ArticleDOI
Gi protein activation in intact cells involves subunit rearrangement rather than dissociation
TL;DR: It is found that Gi proteins activate within 1-2 s, which is considerably slower than activation kinetics of the receptors themselves, which will be of particular interest for unraveling Gβγ-induced signaling pathways.
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Cyclic AMP imaging in adult cardiac myocytes reveals far-reaching beta1-adrenergic but locally confined beta2-adrenergic receptor-mediated signaling.
Viacheslav O. Nikolaev,Moritz Bünemann,Eva M. Schmitteckert,Martin J. Lohse,Stefan Engelhardt +4 more
TL;DR: New cAMP-FRET sensor based on a single cAMP binding domain of the hyperpolarization activated cyclic nucleotide-gated potassium channel 2 (HCN2) makes HCN2-camps particularly well suited to monitor subcellular localization of cardiomyocyte cAMP.