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Markus Axmann

Researcher at Max Planck Society

Publications -  11
Citations -  884

Markus Axmann is an academic researcher from Max Planck Society. The author has contributed to research in topics: T-cell receptor & Major histocompatibility complex. The author has an hindex of 9, co-authored 10 publications receiving 786 citations. Previous affiliations of Markus Axmann include Johannes Kepler University of Linz & Vienna University of Technology.

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TCR–peptide–MHC interactions in situ show accelerated kinetics and increased affinity

TL;DR: It is shown that synaptic TCR–pMHC binding dynamics differ significantly from TCR’s binding in solution, and TCR affinity for pMHC was significantly elevated as the result of a large (about 100-fold) increase in the association rate, a likely consequence of complementary molecular orientation and clustering.
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Bax monomers form dimer units in the membrane that further self-assemble into multiple oligomeric species.

TL;DR: By analysing the stoichiometry of Bax oligomers at the single-molecule level, it is found that Bax binds to the membrane in a monomersic state and then self-assembles in <1 min, and active Bax does not exist in a unique oligomeric state, but as several different species based on dimer units.
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T Cell Activation is Determined by the Number of Presented Antigens

TL;DR: N nanopatterned antigen arrays that mimic the antigen presenting cell surface during T cell activation are introduced and it is demonstrated that these substrates induce T cell responses in a pMHC dose-dependent manner and that the number of presented p MHCs dominates over local pM HC density.
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Versatile Analysis of Single-Molecule Tracking Data by Comprehensive Testing against Monte Carlo Simulations

TL;DR: An approach for the analysis of single-molecule trajectories which is based on a comprehensive comparison of an experimental data set with multiple Monte Carlo simulations of the diffusion process allows quantitative data analysis, particularly whenever analytical treatment of a model is infeasible.
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Determination of Interaction Kinetics between the T Cell Receptor and Peptide-Loaded MHC Class II via Single-Molecule Diffusion Measurements

TL;DR: A single-molecule approach is presented to determine pMHC-TCR interaction kinetics in situ based on diffusion analysis of dye-labeled pM HC and finds synaptic off-rates >10-fold accelerated when compared to the dissociation of purified proteins measured in vitro.