Tampé

Labeling and modification of intracellular proteins remain a major challenge in life sciences, often limited by large fusion domains, high quantities of costly probes, and long reaction times. Here, we will guide protein trans-splicing by minimal high-affinity interaction pairs to trace proteins´ function and assembly in living cells. In addition, we aim at modulating cellular processes by light with high resolution in time and space. Combined with super-resolution microscopy and single-molecule analysis, these traceless approaches shall provide valuable insights into the co-operative function and suprastructures of proteins in particular at intracellular membranes.

M.F. Sánchez, S. Els-Heindl, A.G. Beck-Sickinger, R. Wieneke, R. Tampé
Science2021, 371, abb7657
Photo-induced receptor confinement drives ligand-independent GPCR signaling
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J. Brunnberg, V. Herbring, E. Günther Castillo, H. Krüger, R. Wieneke, R. Tampé
Commun Biol2021, 4, 430
Light control of the peptide-loading complex synchronizes antigen translocation and MHC I trafficking
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S. Hofmann, D. Januliene, A.R. Mehdipour, C. Thomas, E. Stefan, S. Brüchert, B.T. Kuhn, E.R. Geertsma, G. Hummer, R. Tampé
Nature 2019, 471, 580-583
Conformation space of a heterodimeric ABC exporter under turnover conditions
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M. Braner, N. Koller, J. Knauer, V. Herbring, S. Hank, R. Wieneke, R. Tampé
Chem. Sci 2018, 10, 2001-2005
Optical control of the antigen translocation by synthetic photo-conditional viral inhibitors
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A. Klein, S. Hank, A. Raulf, E.F. Joest, F. Tissen, M. Heilemann, R. Wieneke, R. Tampé
Chem Science, 2018, 9, 7835
Live-cell labeling of endogenous proteins with nanometer precision by transduced nanobodies
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A. Blees, D. Januliene, T. Hofmann, N. Koller, C. Schmidt, S. Trowitzsch, A. Moeller, R. Tampé
Nature 2017, 551, 525-528
Structure of the human MHC-I peptide-loading complex
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M. Braner, R. Wieneke, R. Tampé
Chem.Commun. 2017, 53, 545-548
Nanomolar affinity protein trans-splicing monitored in real-time by fluorophore-quencher pairs.
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A. Guesdon, F. Bazile, R.M. Buey, R. Mohan, S. Monier, R.R. Garcia, M. Angevin, C. Heichette, R. Wieneke, R. Tampé, L. Duchesne, A. Akhmanova, M.O. Steinmetz, D. Chrétien
Nature Cell Biology 2016, 8, 1102-1108
EB1 interacts with outwardly curved and straight regions of the microtubule lattice.
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V. Herbring, A. Bäucker, S. Trowitzsch, R. Tampé
Sci Rep 2016, 6, 36907
A dual inhibition mechanism of the herpesviral ICP47 arresting a conformationally thermostable TAP complex
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A. Kollmannsperger, A. Sharei, A. Raulf, M. Heilemann, R. Langer, K.F. Jensen, R. Wieneke, R. Tampé
Nature Commun. 2016, 7, 10372
Live-cell protein labelling with nanometre precision by cell squeezing
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M. Braner, A. Kollmannsperger, R. Wieneke, R. Tampé
Chem.Sci. 2016, 7, 2646-2652
'Traceless' tracing of proteins - high-affinity transsplicing directed by a minimal interaction pair.
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R. Wieneke, A. Raulf, A. Kollmannsperger, M. Heilemann, R. Tampé
Angew. Chem. Int. Ed. 2015, 54(35), 10216-10219
SLAP: Small Labeling Pair for Single-Molecule Super-Resolution Imaging
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R. Wieneke, N. Labòria, M. Rajan, A. Kollmannsperger, F. Natale, M.C. Cardoso, R. Tampé
J. Am. Chem. Soc. 2014, 136, 13975-13978
Live-cell Targeting of His-tagged Proteins by Multivalent N-Nitrilotriacetic Acid Carrier Complexe
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V. Gatterdam, R. Ramadass, T. Stoess, M.A.H. Fichte, J. Wachtveitl, A. Heckel, R. Tampé
Angew. Chem. Int. Ed.2014, 53(22) 5680-5684
Three-dimensional protein networks guided by two-photon activation
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N. Labòria, R. Wieneke, R. Tampé
Angew. Chem. Int. Ed.2013, 52, 848-853
Control of Nanomolar Interaction and In Situ Assembly of Proteins in Four Dimensions by Light
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