@article{PrestelMoeller2016,
  author    = {Prestel, Andreas and M{\"o}ller, Heiko Michael},
  title     = {Spatio-temporal control of cellular uptake achieved by photoswitchable cell-penetrating peptides},
  series = {Chemical communications},
  volume    = {52},
  journal   = {Chemical communications},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {1359-7345},
  doi       = {10.1039/c5cc06848g},
  pages     = {701 -- 704},
  year      = {2016},
  abstract  = {The selective uptake of compounds into specific cells of interest is a major objective in cell biology and drug delivery. By incorporation of a novel, thermostable azobenzene moiety we generated peptides that can be switched optically between an inactive state and an active, cell-penetrating state with excellent spatio-temporal control.},
  language  = {en}
}
@article{PrestelMoeller2015,
  author    = {Prestel, Andreas and M{\"o}ller, Heiko Michael},
  title     = {Spatio-temporal control of cellular uptake achieved by photoswitchable cell-penetrating peptides},
  series = {Chemical communications : ChemComm},
  journal   = {Chemical communications : ChemComm},
  number    = {52},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {1364-548X},
  doi       = {10.1039/C5CC06848G},
  pages     = {701 -- 704},
  year      = {2015},
  abstract  = {The selective uptake of compounds into specific cells of interest is a major objective in cell biology and drug delivery. By incorporation of a novel, thermostable azobenzene moiety we generated peptides that can be switched optically between an inactive state and an active, cell-penetrating state with excellent spatio-temporal control.},
  language  = {en}
}
@article{VorburgerNedielkovBrosigetal.2016,
  author    = {Vorburger, Thomas and Nedielkov, Ruslan and Brosig, Alexander and Bok, Eva and Schunke, Emina and Steffen, Wojtek and Mayer, Sonja and Goetz, Friedrich and M{\"o}ller, Heiko Michael and Steuber, Julia},
  title     = {Role of the Na+-translocating NADH:quinone oxidoreductase in voltage generation and Na+ extrusion in Vibrio cholerae},
  series = {Biochimica et biophysica acta : Bioenergetics},
  volume    = {1857},
  journal   = {Biochimica et biophysica acta : Bioenergetics},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0005-2728},
  doi       = {10.1016/j.bbabio.2015.12.010},
  pages     = {473 -- 482},
  year      = {2016},
  abstract  = {For Vibrio cholerae, the coordinated import and export of Na+ is crucial for adaptation to habitats with different osmolarities. We investigated the Na+-extruding branch of the sodium cycle in this human pathogen by in vivo Na-23-NMR spectroscopy. The Na+ extrusion activity of cells was monitored after adding glucose which stimulated respiration via the Na+-translocating NADH:quinone oxidoreductase (Na+-NQR). In a V. cholerae deletion mutant devoid of the Na+-NQR encoding genes (nqrA-F), rates of respiratory Na+ extrusion were decreased by a factor of four, but the cytoplasmic Na+ concentration was essentially unchanged. Furthermore, the mutant was impaired in formation of transmembrane voltage (Delta psi, inside negative) and did not grow under hypoosmotic conditions at pH 8.2 or above. This growth defect could be complemented by transformation with the plasmid encoded nqr operon. In an alkaline environment, Na+/H+ antiporters acidify the cytoplasm at the expense of the transmembrane voltage. It is proposed that, at alkaline pH and limiting Na+ concentrations, the Na+-NQR is crucial for generation of a transmembrane voltage to drive the import of H+ by electrogenic Na+/H+ antiporters. Our study provides the basis to understand the role of the Na+-NQR in pathogenicity of V. cholerae and other pathogens relying on this primary Na+ pump for respiration. (C) 2015 Elsevier B.V. All rights reserved.},
  language  = {en}
}
@article{KastlBraunPresteletal.2015,
  author    = {Kastl, Johanna and Braun, Joachim and Prestel, Andreas and M{\"o}ller, Heiko Michael and Huhn, Thomas and Mayer, Thomas U.},
  title     = {Mad2 Inhibitor-1 (M2I-1): A Small Molecule Protein-Protein Interaction Inhibitor Targeting the Mitotic Spindle Assembly Checkpoint},
  series = {ACS chemical biology},
  volume    = {10},
  journal   = {ACS chemical biology},
  number    = {7},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {1554-8929},
  doi       = {10.1021/acschembio.5b00121},
  pages     = {1661 -- 1666},
  year      = {2015},
  abstract  = {The genetic integrity of each organism depends on the faithful segregation of its genome during mitosis. To meet this challenge, a cellular surveillance mechanism, termed the spindle assembly checkpoint (SAC), evolved that monitors the correct attachment of chromosomes and blocks progression through mitosis if corrections are needed. While the central role of the SAC for genome integrity is well established, its functional dissection has been hampered by the limited availability of appropriate small molecule inhibitors. Using a fluorescence polarization-based screen, we identify Mad2 inhibitor-1 (M2I-1), the first small molecule inhibitor targeting the binding of Mad2 to Cdc20, an essential protein-protein interaction (PPI) within the SAC. Based on computational and biochemical analyses, we propose that M2I-1 disturbs conformational dynamics of Mad2 critical for complex formation with Cdc20. Cellular studies revealed that M2I-1 weakens the SAC response, indicating that the compound might be active in cells. Thus, our study identifies the SAC specific complex formation between Mad2 and Cdc20 as a protein-protein interaction that can be targeted by small molecules.},
  language  = {en}
}
@article{AbbasVranicHoffmannetal.2018,
  author    = {Abbas, Ioana M. and Vranic, Marija and Hoffmann, Holger and El-Khatib, Ahmed H. and Montes-Bay{\´o}n, Mar{\´i}a and M{\"o}ller, Heiko Michael and Weller, Michael G.},
  title     = {Investigations of the Copper Peptide Hepcidin-25 by LC-MS/MS and NMR⁺},
  series = {International Journal of Molecular Sciences},
  volume    = {19},
  journal   = {International Journal of Molecular Sciences},
  number    = {8},
  publisher = {Molecular Diversity Preservation International},
  address   = {Basel},
  issn      = {1422-0067},
  doi       = {10.3390/ijms19082271},
  pages     = {16},
  year      = {2018},
  abstract  = {Hepcidin-25 was identified as themain iron regulator in the human body, and it by binds to the sole iron-exporter ferroportin. Studies showed that the N-terminus of hepcidin is responsible for this interaction, the same N-terminus that encompasses a small copper(II) binding site known as the ATCUN (amino-terminal Cu(II)- and Ni(II)-binding) motif. Interestingly, this copper-binding property is largely ignored in most papers dealing with hepcidin-25. In this context, detailed investigations of the complex formed between hepcidin-25 and copper could reveal insight into its biological role. The present work focuses on metal-bound hepcidin-25 that can be considered the biologically active form. The first part is devoted to the reversed-phase chromatographic separation of copper-bound and copper-free hepcidin-25 achieved by applying basic mobile phases containing 0.1\% ammonia. Further, mass spectrometry (tandemmass spectrometry (MS/MS), high-resolutionmass spectrometry (HRMS)) and nuclear magnetic resonance (NMR) spectroscopy were employed to characterize the copper-peptide. Lastly, a three-dimensional (3D)model of hepcidin-25with bound copper(II) is presented. The identification of metal complexes and potential isoforms and isomers, from which the latter usually are left undetected by mass spectrometry, led to the conclusion that complementary analytical methods are needed to characterize a peptide calibrant or referencematerial comprehensively. Quantitative nuclear magnetic resonance (qNMR), inductively-coupled plasma mass spectrometry (ICP-MS), ion-mobility spectrometry (IMS) and chiral amino acid analysis (AAA) should be considered among others.},
  language  = {en}
}
@article{HolertYuecelJagmannetal.2016,
  author    = {Holert, Johannes and Y{\"u}cel, Onur and Jagmann, Nina and Prestel, Andreas and M{\"o}ller, Heiko Michael and Philipp, Bodo},
  title     = {Identification of bypass reactions leading to the formation of one central steroid degradation intermediate in metabolism of different bile salts in Pseudomonas sp strain Chol1},
  series = {Environmental microbiology},
  volume    = {18},
  journal   = {Environmental microbiology},
  publisher = {Wiley-Blackwell},
  address   = {Hoboken},
  issn      = {1462-2912},
  doi       = {10.1111/1462-2920.13192},
  pages     = {3373 -- 3389},
  year      = {2016},
  language  = {en}
}
@article{MaierPoluektovJesteretal.2016,
  author    = {Maier, Stefan K. and Poluektov, Georgiy and Jester, Stefan-S. and M{\"o}ller, Heiko Michael and Hoeger, Sigurd},
  title     = {Fast Oxidative Cyclooligomerization towards Low- and High-Symmetry Thiophene Macrocycles},
  series = {Chemistry - a European journal},
  volume    = {22},
  journal   = {Chemistry - a European journal},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {0947-6539},
  doi       = {10.1002/chem.201503211},
  pages     = {1379 -- 1384},
  year      = {2016},
  abstract  = {Macrocycles with quaterthiophene subunits were obtained by cyclooligomerization by direct oxidative coupling of unsubstituted dithiophene moieties. The rings were closed with high selectivity by an \&\#945;,\&\#946;\&\#8242;-connection of the thiophenes as proven by NMR spectroscopy. The reaction of the precursor with terthiophene moieties yielded the symmetric \&\#945;,\&\#945;\&\#8242;-linked macrocycle in low yield together with various differently connected isomers. Blocking of the \&\#946;-position of the half-rings yielded selectively the \&\#945;,\&\#945;\&\#8242;-linked macrocycle. Selected cyclothiophenes were investigated by scanning tunneling microscopy, which displayed the formation of highly ordered 2D crystalline monolayers.},
  language  = {en}
}
@article{StarkeKochKammeretal.2018,
  author    = {Starke, Ines and Koch, Andreas and Kammer, Stefan and Holdt, Hans-J{\"u}rgen and M{\"o}ller, Heiko Michael},
  title     = {Electrospray mass spectrometry and molecular modeling study of formation and stability of silver complexes with diazaperylene and bisisoquinoline},
  series = {Journal of mass spectrometry},
  volume    = {53},
  journal   = {Journal of mass spectrometry},
  number    = {5},
  publisher = {Wiley},
  address   = {Hoboken},
  issn      = {1076-5174},
  doi       = {10.1002/jms.4071},
  pages     = {408 -- 418},
  year      = {2018},
  abstract  = {The complex formation of the following diazaperylene ligands (L) 1,12-diazaperylene 1, 1,1-bisisoquinoline 2, 2,11-disubstituted 1,12-diazaperylenes (alkyl=methyl, ethyl, isopropyl, 3, 5, 7), 3,3-disubstituted 1,1-bisisoquinoline (alkyl=methyl, ethyl, isopropyl, 4, 6, 8 and with R=phenyl, 11 and with pyridine 12), and the 5,8-dimethoxy-substituted diazaperylene 9, 6,6-dimethoxy-substituted bisisoquinoline 10 with AgBF4 was investigated. Collision-induced dissociation measurements were used to evaluate the relative stabilities of the ligands themselves and for the [1:1](+) complexes as well as for the homoleptic and heteroleptic silver [1:2](+) complexes in the gas phase. This method is very useful in rapid screening of the stabilities of new complexes in the gas phase. The influence of the spatial arrangement of the ligands and the type of substituents employed for the complexation were examined. The effect of the preorganization of the diazaperylene on the threshold activation voltages and thus of the relative binding energies of the different complexes are discussed. Density functional theory calculations were used to calculate the optimized structures of the silver complexes and compared with the stabilities of the complexes in the gas phase for the first time.},
  language  = {en}
}
@article{MadaniAnghileriHeydenreichetal.2022,
  author    = {Madani, Amiera and Anghileri, Lucia and Heydenreich, Matthias and M{\"o}ller, Heiko Michael and Pieber, Bartholom{\"a}us},
  title     = {Benzylic fluorination induced by a charge-transfer complex with a solvent-dependent selectivity switch},
  series = {Organic letters / publ. by the American Chemical Society},
  volume    = {24},
  journal   = {Organic letters / publ. by the American Chemical Society},
  number    = {29},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {1523-7060},
  doi       = {10.1021/acs.orglett.2c02050},
  pages     = {5376 -- 5380},
  year      = {2022},
  abstract  = {We present a divergent strategy for the fluorination of phenylacetic acid derivatives that is induced by a charge-transfer complex between Selectfluor and 4-(dimethylamino)pyridine. A comprehensive investigation of the conditions revealed a critical role of the solvent on the reaction outcome. In the presence of water, decarboxylative fluorination through a single-electron oxidation is dominant. Non-aqueous conditions result in the clean formation of alpha-fluoro-alpha-arylcarboxylic acids.},
  language  = {en}
}
@article{TrautweinFredrikssonMoelleretal.2016,
  author    = {Trautwein, Matthias and Fredriksson, Kai and M{\"o}ller, Heiko Michael and Exner, Thomas E.},
  title     = {Automated assignment of NMR chemical shifts based on a known structure and 4D spectra},
  series = {Journal of biomolecular NMR},
  volume    = {65},
  journal   = {Journal of biomolecular NMR},
  publisher = {Springer},
  address   = {Dordrecht},
  issn      = {0925-2738},
  doi       = {10.1007/s10858-016-0050-0},
  pages     = {217 -- 236},
  year      = {2016},
  abstract  = {Apart from their central role during 3D structure determination of proteins the backbone chemical shift assignment is the basis for a number of applications, like chemical shift perturbation mapping and studies on the dynamics of proteins. This assignment is not a trivial task even if a 3D protein structure is known and needs almost as much effort as the assignment for structure prediction if performed manually. We present here a new algorithm based solely on 4D [H-1, N-15]-HSQC-NOESY-[H-1, N-15]-HSQC spectra which is able to assign a large percentage of chemical shifts (73-82 \%) unambiguously, demonstrated with proteins up to a size of 250 residues. For the remaining residues, a small number of possible assignments is filtered out. This is done by comparing distances in the 3D structure to restraints obtained from the peak volumes in the 4D spectrum. Using dead-end elimination, assignments are removed in which at least one of the restraints is violated. Including additional information from chemical shift predictions, a complete unambiguous assignment was obtained for Ubiquitin and 95 \% of the residues were correctly assigned in the 251 residue-long N-terminal domain of enzyme I. The program including source code is available at https://github.com/thomasexner/4Dassign.},
  language  = {en}
}