@article{HerrmannKauppGeueetal.1997,
  author    = {Herrmann, A. and Kaupp, G. and Geue, Thomas and Pietsch, Ullrich},
  title     = {AFM and GID investigations of the gas-solid diazotation of 4-sulfanil-acid-monohydrat single crystals},
  year      = {1997},
  language  = {en}
}
@article{SchweighoeferMorenoBoboneetal.2017,
  author    = {Schweigh{\"o}fer, F. and Moreno, J. and Bobone, Sara and Chiantia, Salvatore and Herrmann, A. and Hecht, S. and Wachtveitl, Josef},
  title     = {Connectivity pattern modifies excited state relaxation dynamics of fluorophore-photoswitch molecular dyads},
  series = {Physical chemistry, chemical physics : a journal of European Chemical Societies},
  volume    = {19},
  journal   = {Physical chemistry, chemical physics : a journal of European Chemical Societies},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {1463-9076},
  doi       = {10.1039/c6cp07112k},
  pages     = {4010 -- 4018},
  year      = {2017},
  abstract  = {In order to modulate the emission of BODIPY fluorophores, they were connected to a diarylethene (DAE) photoswitch via phenylene-ethynylene linkers of different lengths and orientations. The latter allowed for modulation of the electronic coupling in the prepared four BODIPY-DAE dyads, which were compared also to appropriate BODIPY and DAE model compounds by steady state as well as time-resolved spectroscopies. In their open isomers, all dyads show comparable luminescence behavior indicative of an unperturbed BODIPY fluorophore. In strong contrast, in the closed isomers the BODIPY emission is efficiently quenched but the deactivation mechanism depends on the nature of the linker. The most promising dyad was rendered water-soluble by means of micellar encapsulation and aqueous suspensions were investigated by fluorescence spectroscopy and microscopy. Our results (i) illustrate that the electronic communication between the BODIPY and DAE units can indeed be fine-tuned by the nature of the linker to achieve fluorescence modulation while maintaining photoswitchability and (ii) highlight potential applications to image and control biological processes with high spatio-temporal resolution.},
  language  = {en}
}
@misc{HoeferDiLellaDahmanietal.2019,
  author    = {H{\"o}fer, Chris Tina and Di Lella, Santiago and Dahmani, Ismail and Jungnick, Nadine and Bordag, Natalie and Bobone, Sara and Huan, Q. and Keller, S. and Herrmann, A. and Chiantia, Salvatore},
  title     = {Corrigendum to: Structural determinants of the interaction between influenza A virus matrix protein M1 and lipid membranes (Biochimica et Biophysica Acta (BBA) - Biomembranes. - 1861, (2019), pg 1123-1134)},
  series = {Biochimica et biophysica acta : Biomembranes},
  volume    = {1861},
  journal   = {Biochimica et biophysica acta : Biomembranes},
  number    = {10},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0005-2736},
  doi       = {10.1016/j.bbamem.2019.07.002},
  pages     = {1},
  year      = {2019},
  language  = {en}
}
@article{HoeferDiLellaDahmanietal.2019,
  author    = {H{\"o}fer, C. T. and Di Lella, S. and Dahmani, Ismail and Jungnick, N. and Bordag, N. and Bobone, Sara and Huang, Q. and Keller, S. and Herrmann, A. and Chiantia, Salvatore},
  title     = {Structural determinants of the interaction between influenza A virus matrix protein M1 and lipid membranes},
  series = {Biochimica et biophysica acta : Biomembranes},
  volume    = {1861},
  journal   = {Biochimica et biophysica acta : Biomembranes},
  number    = {6},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0005-2736},
  doi       = {10.1016/j.bbamem.2019.03.013},
  pages     = {1123 -- 1134},
  year      = {2019},
  abstract  = {Influenza A virus is a pathogen responsible for severe seasonal epidemics threatening human and animal populations every year. One of the ten major proteins encoded by the viral genome, the matrix protein M1, is abundantly produced in infected cells and plays a structural role in determining the morphology of the virus. During assembly of new viral particles, M1 is recruited to the host cell membrane where it associates with lipids and other viral proteins. The structure of M1 is only partially known. In particular, structural details of M1 interactions with the cellular plasma membrane as well as M1 protein interactions and multimerization have not been clarified, yet. In this work, we employed a set of complementary experimental and theoretical tools to tackle these issues. Using raster image correlation, surface plasmon resonance and circular dichroism spectroscopies, we quantified membrane association and oligomerization of full-length M1 and of different genetically engineered M1 constructs (i.e., N- and C-terminally truncated constructs and a mutant of the polybasic region, residues 95-105). Furthermore, we report novel information on structural changes in M1 occurring upon binding to membranes. Our experimental results are corroborated by an all-atom model of the full-length M1 protein bound to a negatively charged lipid bilayer.},
  language  = {en}
}
@misc{LucknerDunsingDruekeetal.2019,
  author    = {Luckner, Madlen and Dunsing, Valentin and Dr{\"u}ke, Markus and Zuehlke, B. and Petazzi, Roberto Arturo and Chiantia, Salvatore and Herrmann, A.},
  title     = {Quantifying protein oligomerization directly in living cells},
  series = {European biophysics journal : with biophysics letters ; an international journal of biophysics},
  volume    = {48},
  journal   = {European biophysics journal : with biophysics letters ; an international journal of biophysics},
  publisher = {Springer},
  address   = {New York},
  issn      = {0175-7571},
  pages     = {S183 -- S183},
  year      = {2019},
  language  = {en}
}