Hoernke Publications
20. Pourmasoumi, F.; Hengoju, S.; Beck, K.; Stephan, P.; Klopfleisch, L.; Hoernke, M.; Rosenbaum, M. A.; Kries, H. Analysing Megasynthetase Mutants at High Throughput Using Droplet Microfluidics. ChemBioChem 2023, 24 (24), e202300680.
https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cbic.202300680
19. Nimmrich, A.; Panman, M. R.; Berntsson, O.; Biasin, E.; Niebling, S.; Petersson, J.; Hoernke, M.; Björling, A.; Gustavsson, E.; van Driel, T. B.; Dohn, A. O.; Laursen, M.; Zederkof, D. B.; Tono, K.; Katayama, T.; Owada, S.; Nielsen, M. M.; Davidsson, J.; Uhlig, J.; Hub, J. S.; Haldrup, K.; Westenhoff, S. Solvent-Dependent Structural Dynamics in the Ultrafast Photodissociation Reaction of Triiodide Observed with Time-Resolved X-Ray Solution Scattering. J. Am. Chem. Soc. 2023, 145, 29, 15754–15765.
https://doi.org/10.1021/jacs.3c00484
18. Beck, K.; Nandy, J. & Hoernke, M*: Membrane permeabilization can be crucially biased by a fusogenic lipid composition – leaky fusion caused by antimicrobial peptides in model membranes, Soft Matter, 2023, 19, 2919-2931
http://dx.doi.org/10.1039/D2SM01691E
17. Shi, S.; Fan, H. & Hoernke, M.*: Leaky membrane fusion: an ambivalent effect induced by antimicrobial polycations, Nanoscale Advances, 2022, 4, 5109 – 5122
https://pubs.rsc.org/en/content/articlehtml/2022/NA/D2NA00464J
16. Hausig-Punke, F.; Richter, F.; Hoernke, M.; Brendel, J. C. & Traeger, A.: Tracking the Endosomal Escape: A Closer Look at Calcein and Related Reporters Bioscience Macromolecular Bioscience, 2022, n/a, 2200167 https://onlinelibrary.wiley.com/doi/full/10.1002/mabi.202200167
15. Shi, S.; Markl, A.M.; Lu, Z.; Liu, R. & Hoernke, M.*: Interplay of fusion, leakage, and electrostatic lipid clustering: membrane perturbations by a hydrophobic antimicrobial polycation Langmuir, 2022, 38, 2379-2391 https://pubs.acs.org/doi/10.1021/acs.langmuir.1c03445
14. Shi, S.; Quarta, N.; Zhang, H.; Lu, Z.; Hof, M.; Šachl, R.; Liu, R. & Hoernke, M.*: Hidden complexity in membrane permeabilization behavior of antimicrobial polycations Phys. Chem. Chem. Phys., 2021, 23, 1475-1488
https://pubs.rsc.org/en/content/articlelanding/2021/cp/d0cp05651k
13. Stulz, A.; Vogt, A.; Saar, J. S.; Akil, L.; Lienkamp, K.; & Hoernke, M.*: Quantified membrane permeabilization indicates the lipid selectivity of membrane-active antimicrobials Langmuir, 2019, 35, 16366
https://pubs.acs.org/doi/abs/10.1021/acs.langmuir.9b01849
12. Braun, S.; Pokorna, S.; Sachl, R.; Hof, M.; Heerklotz, H. & Hoernke, M.*: Biomembrane permeabilization: statistics of individual leakage events harmonize interpretation of vesicle leakage ACS nano, 2018, 12, 813
https://pubs.acs.org/doi/abs/10.1021/acsnano.7b08184
11. Berntsson, O.; Diensthuber, R.P.; Panman, M.; Björling, A.; Gustavsson, E. ; Hoernke, M.; Hughes, A.J.; Henry, L.; Niebling, S.; Takala, H.; Ihalainen, J.A.; Newby, G.; Kerruth, S.; Heberle, J.; Liebi, M.; Menzel, A.; Henning, R. ; Kosheleva, I; Möglich, A. & Westenhoff, S.: Sequential conformational transitions and alpha-helical supercoiling regulate a sensor histidine kinase, Nature communications, 2017, 8: 284
https://www.nature.com/articles/s41467-017-00300-5
10. Hoernke, M.; Larsson, E.; Mohan, J.; Blomberg, J.; Kahra, D.; Westenhoff, S.; Schwieger, C. & Lundmark, R.: EHD2 restrains dynamics of caveolae by an ATP‑dependent, membrane-bound, open conformation, PNAS, 2017, 114 (22), E4360
http://www.pnas.org/content/early/2017/02/14/1614066114
9. Björling, A.; Berntsson, O.; Lehtivuori, H.; Takala, H.; Hughes, A.J.; Panman, M.; Hoernke, M.; Niebling, St.; Henry, L.; Henning, R.; Kosheleva, I.; Chukharev, V.; Tkachenko, N.V.; Menzel, A.; Newby, G.; Khakulin, D.; Wulff, M.; Ihalainen, J. & Westenhoff, S.: Structural photoactivation of a full-length bacterial phytochrome, Science Advances, 2016, 2 (8), e1600920
http://advances.sciencemag.org/content/2/8/e1600920
8. Takala, H.; Niebling, St.; Berntsson, O.; Björling, A.; Lehtivuori, H.; Hakkanen, H.; Panman, M.; Gustavsson, E.; Hoernke, M.; Newby, G.; Zotone, F.; Wulff, M.; Menzel, A.; Ihalainen, J. & Westenhoff, S.: Light-induced Structural Changes in a Monomeric Bacteriophytochrome, Struct. Dyn. 2016, 3, 054701
https://aca.scitation.org/doi/pdf/10.1063/1.4961911
7. Hoernke, M.*; Tassler, S.; Koksch, B. & Brezesinski, G.*: Membrane Binding of Peptide Models for Early Stages of Amyloid Formation: Lipid Packing Counts more than Charge, ChemPhysLipids, 2016, 198, 28-38
https://www.sciencedirect.com/science/article/pii/S0009308416300329?via%3Dihub
6. Björling, A.; Berntsson, O.; Takala, H.; Gallagher, K.; Patel, H.; Gustavsson, E.; St. Peter, R.; Duong, P.; Nugent, A.; Zhang, F.; Berntsen, P.; Appio, R.; Rajkovic, I.; Lehtivuori, H.; Panman, M.; Hoernke, M.; Niebling, St.; Harimoorthy, R.; Lamparter, T.; Stojkovic, E.; Ihalainen, J. & Westenhoff, S.: Ubiquitous Structural Signaling in Bacterial Phytochromes, J Phys Chem Lett. 2015, 6 (17), 3379–3383
https://pubs.acs.org/doi/abs/10.1021/acs.jpclett.5b01629
5. Takala, H.; Björling, A.; Berntsson, O.; Lehtivuori, H.; Niebling, S.; Hoernke; M.; Kosheleva, I.; Henning, R.; Menzel, A.; Ihalainen, J.A. & Westenhoff,S.: Signal Amplification and Transduction in Phytochrome Photosensors, Nature, 2014, 509, 245–248
https://www.nature.com/articles/nature13310
4. Hoernke, M.; Schwieger, C.; Kerth, A. & Blume, A.: The Binding of Pentapeptides with Modified Side Chains to Negatively Charged Lipid Membranes: Complex Interplay of Electrostatic and Hydrophobic Interactions, BBA-Biomembranes, 2012, 1818 (7), 1663-1672
https://www.sciencedirect.com/science/article/pii/S0005273612000818
3. Hoernke, M.; Falenski, J.A.; Schwieger, C.; Koksch, B. & Brezesinski, G.: Triggers for beta-Sheet Formation at the Hydrophobic-Hydrophilic Interface: High Concentration, In-Plane Orientational Order, and Metal Ion Complexation, Langmuir, 2011, 27 (23), 14218 – 14231
https://pubs.acs.org/doi/abs/10.1021/la203016z
2. Hoernke, M.*; Koksch, B. & Brezesinski, G.*: Amyloidogenic Peptides at Hydrophobic-Hydrophilic Interfaces: Coordination Affinities and the Chelate Effect Dictate the Competitive Binding of Cu2+ and Zn2+, ChemPhysChem, 2011, 12, 2225-2229
https://onlinelibrary.wiley.com/doi/abs/10.1002/cphc.201100215
1. Hoernke, M.; Koksch, B. & Brezesinski, G.: Influence of the Hydrophobic Interface and Transition Metal Ions on the Conformation of Amyloidogenic Model Peptides, Biophys. Chem., 2010, 150, 64-72
https://www.sciencedirect.com/science/article/pii/S0301462210000426?via%3Dihub