Publikationen von Thomas R. Weikl

Chakrabarti, K. S.; Olsson, S.; Pratihar, S.; Giller, K.; Overkamp, K.; Lee, K. O.; Gapsys, V.; Ryu, K.-S.; de Groot, B. L.; Noé, F. et al.; Becker, S.; Lee, D.; Weikl, T. R.; Griesinger, C.: A litmus test for classifying recognition mechanisms of transiently binding proteins. Nature Communications 13, 3792 (2022)

Bonazzi, F.; Hall, C.; Weikl, T. R.: Membrane morphologies induced by mixtures of arc-shaped particles with opposite curvature. Soft Matter 17 (2), S. 268 - 275 (2021)

Kav, B.; Demé, B.; Gege, C.; Tanaka, M.; Schneck, E.; Weikl, T. R.: Interplay of trans- and cis-interactions of glycolipids in membrane adhesion. Frontiers in Molecular Biosciences 8 (1047), 754654 (2021)

Pandey, P. R.; Różycki, B.; Lipowsky, R.; Weikl, T. R.: Structural variability and concerted motions of the T cell receptor - CD3 complex. eLife 10, e67195 (2021)

Różycki, B.; Weikl, T. R.: Cooperative stabilization of close-contact zones leads to sensitivity and selectivity in T-cell recognition. Cells 10 (5), 1023 (2021)

Kav, B.; Grafmüller, A.; Schneck, E.; Weikl, T. R.: Weak carbohydrate-carbohydrate interactions in membrane adhesion are fuzzy and generic. Nanoscale 12 (33), S. 17342 - 17353 (2020)

Weikl, T. R.; Hemmateenejad, B.: Accessory mutations balance the marginal stability of the HIV-1 protease in drug resistance. Proteins: Structure, Function, and Bioinformatics 88 (3), S. 476 - 484 (2020)

Bonazzi, F.; Weikl, T. R.: Membrane morphologies induced by arc-shaped scaffolds are determined by arc angle and coverage. Biophysical Journal 116 (7), S. 1239 - 1247 (2019)

Mobaraki, N.; Hemmateenejad, B.; Weikl, T. R.; Sakhteman, A.: On the relationship between docking scores and protein conformational changes in HIV-1 protease. Journal of molecular graphics and modelling 91, S. 186 - 193 (2019)

Steinkühler, J.; Różycki, B.; Alvey, C.; Lipowsky, R.; Weikl, T. R.; Dimova, R.; Discher, D. E.: Membrane fluctuations and acidosis regulate cooperative binding of “marker of self” CD47 with macrophage checkpoint receptor SIRPα. Journal of Cell Science 132 (4), JCS216770 (2019)

Weikl, T. R.; Hu, J.; Kav, B.; Różycki, B.: Binding and segregation of proteins in membrane adhesion: theory, modeling, and simulations. Advances in Biomembranes and Lipid Self-Assembly 30, S. 159 - 194 (2019)

Bahrami, A. H.; Weikl, T. R.: Curvature-mediated assembly of Janus nanoparticles on membrane vesicles. Nano Letters 18 (2), S. 1259 - 1263 (2018)

Bassereau, P.; Jin, R.; Baumgart, T.; Deserno, M.; Dimova, R.; Frolov, V. A.; Bashkirov, P. V.; Grubmüller, H.; Jahn, R.; Risselada, H. J. et al.; Johannes, L.; Kozlov, M. M.; Lipowsky, R.; Pucadyil, T. J.; Zeno, W. F.; Stachowiak, J. C.; Stamou, D.; Breuer, A.; Lauritsen, L.; Simon, C.; Sykes, C.; Voth, G. A.; Weikl, T. R.: The 2018 biomembrane curvature and remodeling roadmap. Journal of Physics D: Applied Physics 51 (34), 343001 (2018)

Paul, F.; Noé, F.; Weikl, T. R.: Identifying conformational-selection and induced-fit aspects in the binding-induced folding of PMI from Markov state modeling of atomistic simulations. Journal of Physical Chemistry B 122 (21), S. 5649 - 5656 (2018)

Sadeghi, M.; Weikl, T. R.; Noe, F.: Particle-based membrane model for mesoscopic simulation of cellular dynamics. The Journal of Chemical Physics 148 (4), 044901 (2018)

Weikl, T. R.: Membrane-mediated cooperativity of proteins. Annual Review of Physical Chemistry 69, S. 521 - 539 (2018)

Paul, F.; Wehmeyer, C.; Abualrous, E. T.; Wu, H.; Crabtree, M. D.; Schöneberg, J.; Clarke, J.; Freund, C.; Weikl, T. R.; Noé, F.: Protein-peptide association kinetics beyond the seconds timescale from atomistic simulations. Nature Communications 8, 1095 (2017)

Raatz, M.; Weikl, T. R.: Membrane tubulation by elongated and patchy nanoparticles. Advanced Materials Interfaces 4 (1), 1600325 (2017)

Bahrami, A. H.; Lipowsky, R.; Weikl, T. R.: The role of membrane curvature for the wrapping of nanoparticles. Soft Matter 12 (2), S. 581 - 587 (2016)

Paul, F.; Weikl, T. R.: How to distinguish conformational selection and induced fit based on chemical relaxation rates. PLoS Computational Biology 12 (9), e1005067 (2016)