TY - JOUR A1 - Zimmermann, Andreas A1 - Herrmann, Franziska T1 - 70 Jahre Genfer Flüchtlingskonvention BT - Versuch einer Bilanz JF - Informationsbrief Ausländerrecht Y1 - 2021 UR - https://research.wolterskluwer-online.de/document/2c925f57-8d47-351f-87f5-26bc36668bb7 SN - 0174-2108 SN - 2366-195X IS - 6 SP - 221 EP - 227 PB - Luchterhand CY - Köln ; Neuwied ER - TY - JOUR A1 - Hofmann, Markus J. A1 - Dambacher, Michael A1 - Jacobs, Arthur M. A1 - Kliegl, Reinhold A1 - Radach, Ralph A1 - Kuchinke, Lars A1 - Plichta, Michael M. A1 - Fallgatter, Andreas J. A1 - Herrmann, Martin J. T1 - Occipital and orbitofrontal hemodynamics during naturally paced reading: An fNIRS study JF - NeuroImage : a journal of brain function N2 - Humans typically read at incredibly fast rates, because they predict likely occurring words from a given context. Here, we used functional near-infrared spectroscopy (fNIRS) to track the ultra-rapid hemodynamic responses of words presented every 280 ms in a naturally paced sentence context. We found a lower occipital deoxygenation to unpredictable than to predictable words. The greater hemodynamic responses to unexpected words suggest that the visual features of expected words have been pre-activated previous to stimulus presentation. Second, we tested opposing theoretical proposals about the role of the medial orbitofrontal cortex (OFC): Either OFC may respond to the breach of expectation; or OFC is activated when the present stimulus matches the prediction. A significant interaction between word frequency and predictability indicated OFC responses to breaches of expectation for low- but not for high-frequency words: OFC is sensitive to both, bottom-up processing as mediated by word frequency, as well as top-down predictions. Particularly, when a rare word is unpredictable, OFC becomes active. Finally, we discuss how a high temporal resolution can help future studies to disentangle the hemodynamic responses of single trials in such an ultra-rapid event succession as naturally paced reading. (C) 2014 Elsevier Inc. All rights reserved. KW - Frontopolar KW - Orbitofrontal KW - Bayesian brain KW - Predictive coding KW - Cloze probability Y1 - 2014 U6 - https://doi.org/10.1016/j.neuroimage.2014.03.014 SN - 1053-8119 SN - 1095-9572 VL - 94 SP - 193 EP - 202 PB - Elsevier CY - San Diego ER - TY - JOUR A1 - Bobone, Sara A1 - Hilsch, Malte A1 - Storm, Julian A1 - Dunsing, Valentin A1 - Herrmann, Andreas A1 - Chiantia, Salvatore T1 - Phosphatidylserine Lateral Organization Influences the Interaction of Influenza Virus Matrix Protein 1 with Lipid Membranes JF - Journal of virology N2 - Influenza A virus matrix protein 1 (M1) is an essential component involved in the structural stability of the virus and in the budding of new virions from infected cells. A deeper understanding of the molecular basis of virion formation and the budding process is required in order to devise new therapeutic approaches. We performed a detailed investigation of the interaction between M1 and phosphatidylserine (PS) (i.e., its main binding target at the plasma membrane [PM]), as well as the distribution of PS itself, both in model membranes and in living cells. To this end, we used a combination of techniques, including Forster resonance energy transfer (FRET), confocal microscopy imaging, raster image correlation spectroscopy, and number and brightness (N&B) analysis. Our results show that PS can cluster in segregated regions in the plane of the lipid bilayer, both in model bilayers constituted of PS and phosphatidylcholine and in living cells. The viral protein M1 interacts specifically with PS-enriched domains, and such interaction in turn affects its oligomerization process. Furthermore, M1 can stabilize PS domains, as observed in model membranes. For living cells, the presence of PS clusters is suggested by N&B experiments monitoring the clustering of the PS sensor lactadherin. Also, colocalization between M1 and a fluorescent PS probe suggest that, in infected cells, the matrix protein can specifically bind to the regions of PM in which PS is clustered. Taken together, our observations provide novel evidence regarding the role of PS-rich domains in tuning M1-lipid and M1-M1 interactions at the PM of infected cells. IMPORTANCE Influenza virus particles assemble at the plasma membranes (PM) of infected cells. This process is orchestrated by the matrix protein M1, which interacts with membrane lipids while binding to the other proteins and genetic material of the virus. Despite its importance, the initial step in virus assembly (i.e., M1-lipid interaction) is still not well understood. In this work, we show that phosphatidylserine can form lipid domains in physical models of the inner leaflet of the PM. Furthermore, the spatial organization of PS in the plane of the bilayer modulates M1-M1 interactions. Finally, we show that PS domains appear to be present in the PM of living cells and that M1 seems to display a high affinity for them. KW - influenza KW - assembly KW - confocal microscopy KW - fluorescence image analysis KW - lipid rafts KW - matrix protein KW - model membranes KW - phosphatidylserine KW - plasma membrane Y1 - 2017 U6 - https://doi.org/10.1128/JVI.00267-17 SN - 0022-538X SN - 1098-5514 VL - 91 PB - American Society for Microbiology CY - Washington ER - TY - JOUR A1 - Welke, Robert-William A1 - Sperber, Hannah Sabeth A1 - Bergmann, Ronny A1 - Koikkarah, Amit A1 - Menke, Laura A1 - Sieben, Christian A1 - Krüger, Detlev H. A1 - Chiantia, Salvatore A1 - Herrmann, Andreas A1 - Schwarzer, Roland T1 - Characterization of hantavirus N protein intracellular dynamics and localization JF - Viruses N2 - Hantaviruses are enveloped viruses that possess a tri-segmented, negative-sense RNA genome. The viral S-segment encodes the multifunctional nucleocapsid protein (N), which is involved in genome packaging, intracellular protein transport, immunoregulation, and several other crucial processes during hantavirus infection. In this study, we generated fluorescently tagged N protein constructs derived from Puumalavirus (PUUV), the dominant hantavirus species in Central, Northern, and Eastern Europe. We comprehensively characterized this protein in the rodent cell line CHO-K1, monitoring the dynamics of N protein complex formation and investigating co-localization with host proteins as well as the viral glycoproteins Gc and Gn. We observed formation of large, fibrillar PUUV N protein aggregates, rapidly coalescing from early punctate and spike-like assemblies. Moreover, we found significant spatial correlation of N with vimentin, actin, and P-bodies but not with microtubules. N constructs also co-localized with Gn and Gc albeit not as strongly as the glycoproteins associated with each other. Finally, we assessed oligomerization of N constructs, observing efficient and concentration-dependent multimerization, with complexes comprising more than 10 individual proteins. KW - hantavirus KW - N protein KW - oligomerization KW - actin KW - P-bodies KW - vimentin KW - Number and Brightness KW - Puumalavirus KW - macromolecular assemblies Y1 - 2022 U6 - https://doi.org/10.3390/v14030457 SN - 1999-4915 VL - 14 IS - 3 PB - MDPI CY - Basel ER - TY - JOUR A1 - Klose, Tim A1 - Guillemoteau, Julien A1 - Vignoli, Giulio A1 - Walter, Judith A1 - Herrmann, Andreas A1 - Tronicke, Jens T1 - Structurally constrained inversion by means of a Minimum Gradient Support regularizer: examples of FD-EMI data inversion constrained by GPR reflection data JF - Geophysical journal international N2 - Many geophysical inverse problems are known to be ill-posed and, thus, requiring some kind of regularization in order to provide a unique and stable solution. A possible approach to overcome the inversion ill-posedness consists in constraining the position of the model interfaces. For a grid-based parameterization, such a structurally constrained inversion can be implemented by adopting the usual smooth regularization scheme in which the local weight of the regularization is reduced where an interface is expected. By doing so, sharp contrasts are promoted at interface locations while standard smoothness constraints keep affecting the other regions of the model. In this work, we present a structurally constrained approach and test it on the inversion of frequency-domain electromagnetic induction (FD-EMI) data using a regularization approach based on the Minimum Gradient Support stabilizer, which is capable to promote sharp transitions everywhere in the model, i.e., also in areas where no structural a prioriinformation is available. Using 1D and 2D synthetic data examples, we compare the proposed approach to a structurally constrained smooth inversion as well as to more standard (i.e., not structurally constrained) smooth and sharp inversions. Our results demonstrate that the proposed approach helps in finding a better and more reliable reconstruction of the subsurface electrical conductivity distribution, including its structural characteristics. Furthermore, we demonstrate that it allows to promote sharp parameter variations in areas where no structural information are available. Lastly, we apply our structurally constrained scheme to FD-EMI field data collected at a field site in Eastern Germany to image the thickness of peat deposits along two selected profiles. In this field example, we use collocated constant offset ground-penetrating radar (GPR) data to derive structural a priori information to constrain the inversion of the FD-EMI data. The results of this case study demonstrate the effectiveness and flexibility of the proposed approach. KW - Controlled source electromagnetics (CSEM) KW - Inverse theory KW - Electrical properties KW - Ground penetrating radar KW - Frequency Domain Electromagnetics KW - Inversion Y1 - 2023 U6 - https://doi.org/10.1093/gji/ggad041 SN - 0956-540X SN - 1365-246X VL - 233 IS - 3 SP - 1938 EP - 1949 PB - Oxford Univ. Press CY - Oxford ER -