Author

A. Karner

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 2 Cell Biology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 3 Approach:experimental assay· 2 Approach:microscopy & imaging analysis· 2 Organism:bacteria (other)· 1 Assay:fluorescence / live-cell microscopy· 1 Organism:human· 1 Approach:mechanistic / dynamical model· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

j. preiner· 3 shared A. Horner· 1 shared A. R. Harders· 1 shared A. S. Eklund· 1 shared C. Dirscherl· 1 shared C. Hannesschlaeger· 1 shared C. Siligan· 1 shared C. Uetrecht· 1 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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3 shared papersBiophysics

j. preiner

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Dissociation of β2m from MHC Class I Triggers Formation of Noncovalent, Transient Heavy Chain Dimers

C. Dirscherl, S. Loechte, Z. Hein, J.-D. Kopicki, A. R. Harders, N. Linden, a. Karner, j. preiner, J. Weghuber, M. Garcia-Alai, C. Uetrecht, M. Zacharias, J. Piehler, P. Lanzerstorfer, S. Springer

This study investigates the formation of non-covalent MHC-I heavy chain dimers after dissociation of β2m and peptide, revealing a dimerization interface mediated by the 3 domain.

bioRxiv · Jul 2, 2021Cell Biology

DNA origami demonstrate the unique stimulatory power of single pMHCs as T-cell antigens

J. Hellmeier, R. Platzer, A. S. Eklund, T. Schlichthaerle, A. Karner, V. Motsch, E. Kurz, V. Bamieh, M. Brameshuber, J. Preiner, R. Jungmann, H. Stockinger, G. J. Schuetz, J. B. Huppa, E. Sevcsik

The paper demonstrates that single pMHCs can robustly stimulate T-cells as isolated entities, identifying the minimal requirements for effective TCR-triggering.

Proceedings of the National Academy of Sciences · Jan 19, 2021Peer-reviewedBiophysics

Binding of the motor protein SecA to the bacterial protein translocation channel SecYEG in the absence of ATP

K. Winkler, A. Karner, A. Horner, C. Hannesschlaeger, D. Knyazev, C. Siligan, M. Zimmermann, R. Kuttner, P. Pohl, J. Preiner

The paper investigates how SecA remains bound to SecYEG without ATP, showing stable interactions and conformational changes that support protein translocation.

Nanoscale Advances · Jan 1, 2020Peer-reviewedBiophysics