@article{KueppersSteffenHellmuthetal.2014,
  author    = {K{\"u}ppers, Tobias and Steffen, Victoria and Hellmuth, Hendrik and O'Connell, Timothy and Bongaerts, Johannes and Maurer, Karl-Heinz and Wiechert, Wolfgang},
  title     = {Developing a new production host from a blueprint: Bacillus pumilus as an industrial enzyme producer},
  series = {Microbial cell factories},
  volume    = {13},
  journal   = {Microbial cell factories},
  publisher = {BioMed Central},
  address   = {London},
  issn      = {1475-2859 (E-Journal)},
  doi       = {10.1186/1475-2859-13-46},
  pages     = {Article No. 46},
  year      = {2014},
  language  = {en}
}
@article{TakenagaBiselliSchnitzleretal.2014,
  author    = {Takenaga, Shoko and Biselli, Manfred and Schnitzler, Thomas and {\"O}hlschl{\"a}ger, Peter and Wagner, Torsten and Sch{\"o}ning, Michael Josef},
  title     = {Toward multi-analyte bioarray sensors: LAPS-based on-chip determination of a Michaelis-Menten-like kinetics for cell culturing},
  series = {Physica status solidi A : Applications and materials science},
  volume    = {211},
  journal   = {Physica status solidi A : Applications and materials science},
  number    = {6},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1521-396X (E); 1862-6319 (E-Journal); 0031-8965 (Print); 1862-6300 (Print)},
  doi       = {10.1002/pssa.201330464},
  pages     = {1410 -- 1415},
  year      = {2014},
  abstract  = {The metabolic activity of Chinese hamster ovary (CHO) cells was observed using a light-addressable potentiometric sensor (LAPS). The dependency toward different glucose concentrations (17-200 mM) follows a Michaelis-Menten kinetics trajectory with Kₘ = 32.8 mM, and the obtained Kₘ value in this experiment was compared with that found in literature. In addition, the pH shift induced by glucose metabolism of tumor cells transfected with the HPV-16 genome (C3 cells) was successfully observed. These results indicate the possibility to determine the tumor cells metabolism with a LAPS-based measurement device.},
  language  = {en}
}
@article{GuoMiyamotoWagneretal.2014,
  author    = {Guo, Yuanyuan and Miyamoto, Ko-ichiro and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Yoshinobu, Tatsuo},
  title     = {Theoretical study and simulation of light-addressable potentiometric sensors},
  series = {Physica status solidi (A) : applications and materials},
  volume    = {211},
  journal   = {Physica status solidi (A) : applications and materials},
  number    = {6},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {0031-8965},
  doi       = {10.1002/pssa.201330354},
  pages     = {1467 -- 1472},
  year      = {2014},
  abstract  = {The light-addressable potentiometric sensor (LAPS) is a semiconductor-based potentiometric sensor using a light probe with an ability of detecting the concentration of biochemical species in a spatially resolved manner. As an important biomedical sensor, research has been conducted to improve its performance, for instance, to realize high-speed measurement. In this work, the idea of facilitating the device-level simulation, instead of using an equivalent-circuit model, is presented for detailed analysis and optimization of the performance of the LAPS. Both carrier distribution and photocurrent response have been simulated to provide new insight into both amplitude-mode and phase-mode operations of the LAPS. Various device parameters can be examined to effectively design and optimize the LAPS structures and setups for enhanced performance.},
  language  = {en}
}
@article{HeineHerrmannSelmeretal.2014,
  author    = {Heine, A. and Herrmann, G. and Selmer, Thorsten and Terwesten, F. and Buckel, W. and Reuter, K.},
  title     = {High resolution crystal structure of clostridium propionicum β-Alanyl-CoA:Ammonia Lyase, a new member of the "Hot Dog Fold" protein superfamily},
  series = {Proteins},
  volume    = {82},
  journal   = {Proteins},
  number    = {9},
  publisher = {Wiley-Liss},
  address   = {New York},
  issn      = {1097-0134 (E-Journal); 0887-3585 (Print)},
  doi       = {10.1002/prot.24557},
  pages     = {2041 -- 2053},
  year      = {2014},
  abstract  = {Clostridium propionicum is the only organism known to ferment β-alanine, a constituent of coenzyme A (CoA) and the phosphopantetheinyl prosthetic group of holo-acyl carrier protein. The first step in the fermentation is a CoA-transfer to β-alanine. Subsequently, the resulting β-alanyl-CoA is deaminated by the enzyme β-alanyl-CoA:ammonia lyase (Acl) to reversibly form ammonia and acrylyl-CoA. We have determined the crystal structure of Acl in its apo-form at a resolution of 0.97 {\AA} as well as in complex with CoA at a resolution of 1.59 {\AA}. The structures reveal that the enyzme belongs to a superfamily of proteins exhibiting a so called "hot dog fold" which is characterized by a five-stranded antiparallel β-sheet with a long α-helix packed against it. The functional unit of all "hot dog fold" proteins is a homodimer containing two equivalent substrate binding sites which are established by the dimer interface. In the case of Acl, three functional dimers combine to a homohexamer strongly resembling the homohexamer formed by YciA-like acyl-CoA thioesterases. Here, we propose an enzymatic mechanism based on the crystal structure of the Acl·CoA complex and molecular docking. Proteins 2014; 82:2041-2053. © 2014 Wiley Periodicals, Inc.},
  language  = {en}
}
@article{SchroeterHoffmannVoigtetal.2014,
  author    = {Schroeter, Rebecca and Hoffmann, Tamara and Voigt, Birgit and Meyer, Hanna and Bleisteiner, Monika and Muntel, Jan and J{\"u}rgen, Britta and Albrecht, Dirk and Becher, D{\"o}rte and Lalk, Michael and Evers, Stefan and Bongaerts, Johannes and Maurer, Karl-Heinz and Putzer, Harald and Hecker, Michael and Schweder, Thomas and Bremer, Erhard},
  title     = {Stress responses of the industrial workhorse Bacillus licheniformis to osmotic challenges},
  series = {PLoS ONE},
  volume    = {8},
  journal   = {PLoS ONE},
  number    = {11},
  publisher = {PLOS},
  address   = {San Francisco},
  issn      = {1932-6203},
  doi       = {10.1371/journal.pone.0080956},
  pages     = {e80956},
  year      = {2014},
  abstract  = {The Gram-positive endospore-forming bacterium Bacillus licheniformis can be found widely in nature and it is exploited in industrial processes for the manufacturing of antibiotics, specialty chemicals, and enzymes. Both in its varied natural habitats and in industrial settings, B. licheniformis cells will be exposed to increases in the external osmolarity, conditions that trigger water efflux, impair turgor, cause the cessation of growth, and negatively affect the productivity of cell factories in biotechnological processes. We have taken here both systems-wide and targeted physiological approaches to unravel the core of the osmostress responses of B. licheniformis. Cells were suddenly subjected to an osmotic upshift of considerable magnitude (with 1 M NaCl), and their transcriptional profile was then recorded in a time-resolved fashion on a genome-wide scale. A bioinformatics cluster analysis was used to group the osmotically up-regulated genes into categories that are functionally associated with the synthesis and import of osmostress-relieving compounds (compatible solutes), the SigB-controlled general stress response, and genes whose functional annotation suggests that salt stress triggers secondary oxidative stress responses in B. licheniformis. The data set focusing on the transcriptional profile of B. licheniformis was enriched by proteomics aimed at identifying those proteins that were accumulated by the cells through increased biosynthesis in response to osmotic stress. Furthermore, these global approaches were augmented by a set of experiments that addressed the synthesis of the compatible solutes proline and glycine betaine and assessed the growth-enhancing effects of various osmoprotectants. Combined, our data provide a blueprint of the cellular adjustment processes of B. licheniformis to both sudden and sustained osmotic stress.},
  language  = {en}
}
@article{WangDruckenmuellerElbersetal.2014,
  author    = {Wang, Ren-Qi and Druckenm{\"u}ller, Katharina and Elbers, Gereon and Guenther, Klaus and Crou{\´e}, Jean-Philippe},
  title     = {Analysis of aquatic-phase natural organic matter by optimized LDI-MS method},
  series = {Journal of mass spectrometry},
  volume    = {49},
  journal   = {Journal of mass spectrometry},
  number    = {2},
  publisher = {Wiley},
  address   = {Bognor Regis},
  issn      = {1096-9888},
  doi       = {10.1002/jms.3321},
  pages     = {154 -- 160},
  year      = {2014},
  abstract  = {The composition and physiochemical properties of aquatic-phase natural organic matter (NOM) are most important problems for both environmental studies and water industry. Laser desorption/ionization (LDI) mass spectrometry facilitated successful examinations of NOM, as humic and fulvic acids in NOM are readily ionized by the nitrogen laser. In this study, hydrophobic NOMs (HPO NOMs) from river, reservoir and waste water were characterized by this technique. The effect of analytical variables like concentration, solvent composition and laser energy was investigated. The exact masses of small molecular NOM moieties in the range of 200-1200 m/z were determined in reflectron mode. In addition, spectra of post-source-decay experiments in this range showed that some compounds from different natural NOMs had the same fragmental ions. In the large mass range of 1200-15 000 Da, macromolecules and their aggregates were found in HPO NOMs from natural waters. Highly humic HPO exhibited mass peaks larger than 8000 Da. On the other hand, the waste water and reservoir water mainly had relatively smaller molecules of about 2000 Da. The LDI-MS measurements indicated that highly humic river waters were able to form large aggregates and membrane foulants, while the HPO NOMs from waste water and reservoir water were unlikely to form large aggregates. Copyright © 2014 John Wiley \& Sons, Ltd.},
  language  = {en}
}
@article{HandtkeSchroeterJuergenetal.2014,
  author    = {Handtke, Stefan and Schroeter, Rebecca and J{\"u}rgen, Britta and Methling, Karen and Schl{\"u}ter, Rabea and Albrecht, Dirk and Hijum, Sacha A. F. T. van and Bongaerts, Johannes and Maurer, Karl-Heinz and Lalk, Michael and Schweder, Thomas and Hecker, Michael and Voigt, Birgit},
  title     = {Bacillus pumilus reveals a remarkably high resistance to hydrogen peroxide provoked oxidative stress},
  series = {PLOS one},
  volume    = {9},
  journal   = {PLOS one},
  number    = {1},
  publisher = {PLOS},
  address   = {San Francisco},
  issn      = {1932-6203},
  doi       = {10.1371/journal.pone.0085625},
  pages     = {e85625},
  year      = {2014},
  abstract  = {Bacillus pumilus is characterized by a higher oxidative stress resistance than other comparable industrially relevant Bacilli such as B. subtilis or B. licheniformis. In this study the response of B. pumilus to oxidative stress was investigated during a treatment with high concentrations of hydrogen peroxide at the proteome, transcriptome and metabolome level. Genes/proteins belonging to regulons, which are known to have important functions in the oxidative stress response of other organisms, were found to be upregulated, such as the Fur, Spx, SOS or CtsR regulon. Strikingly, parts of the fundamental PerR regulon responding to peroxide stress in B. subtilis are not encoded in the B. pumilus genome. Thus, B. pumilus misses the catalase KatA, the DNA-protection protein MrgA or the alkyl hydroperoxide reductase AhpCF. Data of this study suggests that the catalase KatX2 takes over the function of the missing KatA in the oxidative stress response of B. pumilus. The genome-wide expression analysis revealed an induction of bacillithiol (Cys-GlcN-malate, BSH) relevant genes. An analysis of the intracellular metabolites detected high intracellular levels of this protective metabolite, which indicates the importance of bacillithiol in the peroxide stress resistance of B. pumilus.},
  language  = {en}
}
@article{BerndtGattnerZahn1975,
  author    = {Berndt, Heinz and Gattner, Hans-Gregor and Zahn, Helmut},
  title     = {Semisynthetisches Des-A1-glycin-Schafinsulin},
  series = {Biological Chemistry},
  volume    = {356},
  journal   = {Biological Chemistry},
  number    = {2},
  publisher = {De Gruyter},
  address   = {Berlin},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1975.356.2.1455},
  pages     = {1469 -- 1472},
  year      = {1975},
  language  = {de}
}
@article{NokiharaBerndt1978,
  author    = {Nokihara, Kiyoshi and Berndt, Heinz},
  title     = {Synthesis of hapten-polypeptide conjugates as antigen models for the N-terminal region of the α-2-chain of rabbit skin collagen},
  series = {Journal of the Royal Society of Chemistry: Perkin Transactions 1},
  volume    = {1978},
  journal   = {Journal of the Royal Society of Chemistry: Perkin Transactions 1},
  number    = {3},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {1364-5463},
  doi       = {10.1039/P19780000260},
  pages     = {260 -- 263},
  year      = {1978},
  abstract  = {Synthesis of derivatives of the peptide sequence L-pyroglutamyl-L-phenylalanyl-L-aspartyl-glycyl-L-lysyl-glycyl-glycyl-glycine as the antigenic determinant representing the N-terminal non-helical region of the α-2-chain of rabbit skin collagen, and conjugation to two different polypeptide carriers, are described.},
  language  = {en}
}
@article{SchnabelSchnabelBerndt1971,
  author    = {Schnabel, Eugen and Schnabel, Henning and Berndt, Heinz},
  title     = {Zur selektiven acidolytischen Abspaltbarkeit der tert.-Butyloxycarbonyl-Gruppe},
  series = {Justus Liebigs Annalen der Chemie},
  volume    = {749},
  journal   = {Justus Liebigs Annalen der Chemie},
  number    = {1},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1099-0690},
  doi       = {10.1002/jlac.19717490111},
  pages     = {90 -- 108},
  year      = {1971},
  abstract  = {Die tert.-Butyloxycarbonyl-Gruppe (Boc) l{\"a}ßt sich mittels reiner Trifluoressigs{\"a}ure nicht selektiv neben dem Benzyloxycarbonyl-Rest (Z) abspalten. Das gelingt auch nicht mit L{\"o}sungen von Trifluoressigs{\"a}ure bzw. Chlorwasserstoff in organischen L{\"o}sungsmitteln. Kern-substituierte Z-Gruppen wie Z(pCl), Z(mCl) oder Z(pNO₂) sind zwar stabiler, werden aber von den obengenannten Reagenzien ebenfalls angegriffen bzw. sind nicht mehr acidolytisch abspaltbar. - Mit 70proz. w{\"a}ßriger Trifluoressigs{\"a}ure gelingt die Abspaltung von Boc neben Z dagegen fast selektiv; dabei werden aber Benzylester, besonders Glutamins{\"a}ure-γ-benzylester, teilweise hydrolysiert, w{\"a}hrend Methyl- sowie {\"A}thylester nahezu best{\"a}ndig sind. Die Brauchbarkeit des Abspaltungsverfahrens wird anhand der schrittweise durchgef{\"u}hrten Synthese zweier Heptapeptid-Derivate gezeigt. - {\"A}hnlich spezifisch gelingt die Abspaltung von Boc mit Bortrifluorid-{\"a}therat in Eisessig; Benzylester sind gegen{\"u}ber diesem Reagenz stabiler als gegen w{\"a}ßrige Trifluoressigs{\"a}ure. Das Bortrifluorid-Verfahren eignet sich besonders f{\"u}r die Abspaltung von Boc-Gruppen neben s{\"a}urelabilen Thiol-Schutzgruppen (Tetrahydropyranyl- bzw. Trityl-Rest) sowie neben dem Cyclocystinyl-Rest. Die Leistungsf{\"a}higkeit der Methode wird durch die Synthese zweier Peptid-Derivate mit S-Trityl-Schutzgruppen belegt. Als Nebenreaktion ist die Acetylierung von aliphatischen Hydroxylgruppen m{\"o}glich. Sie l{\"a}ßt sich vermeiden, wenn man die Spaltung in anderen L{\"o}sungsmitteln durchf{\"u}hrt. Die als Modellverbindungen f{\"u}r Stabilit{\"a}tsuntersuchungen verwendeten Nε-acylierten Lysin-Derivate werden mit dem Aminos{\"a}ureanalysator quantitativ neben Lysin bestimmt.},
  language  = {de}
}
@article{BerndtKlostermeyerZahn1972,
  author    = {Berndt, Heinz and Klostermeyer, Henning and Zahn, Helmut},
  title     = {Zur Synthese monomerer cyclischer Cystinpeptidderivate, I : Synthese der Sequenz A 6-9 des Schafinsulins als Cyclocystinylderivat},
  series = {Justus Liebigs Annalen der Chemie},
  volume    = {759},
  journal   = {Justus Liebigs Annalen der Chemie},
  number    = {1},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1099-0690},
  doi       = {10.1002/jlac.19727590109},
  pages     = {114 -- 120},
  year      = {1972},
  abstract  = {Es wird die Synthese der Sequenz A 6-9 des Schafinsulins in der gesch{\"u}tzten Form Boc-Cys-Cys-Ala-Gly-OBuᵗ (5) sowie das Verhalten dieses monomeren cyclischen Cystinpeptidderivates gegen{\"u}ber den in der Peptidchemie gebr{\"a}uchlichen Reagenzien Bortrifluorid/Eisessig, Tri{\"a}thylamin und Hydrazinhydrat beschrieben.},
  language  = {de}
}
@article{SchwertnerBerndtGielenetal.1975,
  author    = {Schwertner, Eberhard and Berndt, Heinz and Gielen, Hans-G{\"u}nter and Zahn, Helmut},
  title     = {Peptide 96 : Synthese einiger [2-(p-Biphenylyl)isopropyloxycarbonyl]-Aminos{\"a}urederivate},
  series = {Justus Liebigs Annalen der Chemie},
  volume    = {75},
  journal   = {Justus Liebigs Annalen der Chemie},
  number    = {3},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1099-0690},
  doi       = {10.1002/jlac.197519750318},
  pages     = {581 -- 585},
  year      = {1975},
  abstract  = {Die Darstellung der N-[2-(p-Biphenylyl)isopropyloxycarbonyl]-Derivate (Bpoc-Derivate) des Cysteins unter Verwendung der Thiolschutzgruppen Tetrahydropyranyl (Thp) f{\"u}r 1, Diphenylmethyl (Dpm) f{\"u}r 2, Trityl (Trt) f{\"u}r 3 und S-tert.-Butyl (SBut) f{\"u}r 4 sowie die Synthese von aktivierten Estern der Bpoc-Derivate des Glycins (5), Isoleucins (6) und Prolins (7) werden beschrieben. An einem Beispiel wird die M{\"o}glichkeit aufgezeigt, die Bpoc-Gruppe {\"u}ber das Bpoc-Azid nachtr{\"a}glich in den Peptidverband einzuf{\"u}hren.},
  language  = {de}
}
@article{BerndtZahn1975,
  author    = {Berndt, Heinz and Zahn, Helmut},
  title     = {Peptide, 99 : Monomere cyclische Cystinpeptidderivate, III ; Synthese der Schafinsulin-A-Kettensequenzen A2-21 und A1-21 als monomere cyclische Dicystinpeptidderivate},
  series = {Justus Liebigs Annalen der Chemie},
  volume    = {1975},
  journal   = {Justus Liebigs Annalen der Chemie},
  number    = {9},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1099-0690},
  doi       = {10.1002/jlac.197519750908},
  pages     = {1601 -- 1612},
  year      = {1975},
  abstract  = {Die Synthese der Sequenzen A2—21 (13) und A1—21 (15) der Schafinsulin-A-Kette als monomere cyclische Dicystinpeptidderivate wird beschrieben. Die intrachenaren Cystinbr{\"u}cken A6—7 und A 11 —20 vermitteln die L{\"o}slichkeit dieser Derivate in Dimethylformamid und erm{\"o}glichen erstmalig die Reindarstellung vollgesch{\"u}tzter Insulin-A-Kettenderivate. Die w{\"a}hrend der Synthese eingesetzten Schutzgruppen lassen sich mittels Trifluoressigs{\"a}ure und 2-Mercapto{\"a}thanol quantitativ entfernen.},
  language  = {de}
}
@article{NokiharaBerndt1978,
  author    = {Nokihara, Kiyoshi and Berndt, Heinz},
  title     = {Studies on sulfur-containing peptides : tert-butyloxycarbonylsulfenyl and benzyloxycarbonylsulfenyl derivatives as protecting groups for cysteine},
  series = {The journal of organic chemistry},
  volume    = {43},
  journal   = {The journal of organic chemistry},
  number    = {25},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {0022-3263},
  doi       = {10.1021/jo00419a046},
  pages     = {4893 -- 4895},
  year      = {1978},
  language  = {en}
}
@article{MatoniBerndt1980,
  author    = {Matoni, Georg and Berndt, Heinz},
  title     = {Thermal synthesis of the optical pure pentapeptide derivative Z-(L)-Ala-(L)-Phe-Gly-(L)-Phe-Gly-OMe},
  series = {Tetrahedron letters},
  volume    = {21},
  journal   = {Tetrahedron letters},
  number    = {1},
  issn      = {0040-4039},
  doi       = {10.1016/S0040-4039(00)93618-9},
  pages     = {37 -- 40},
  year      = {1980},
  language  = {en}
}
@article{Berndt1980,
  author    = {Berndt, Heinz},
  title     = {Zur Reaktion von Iminodithiocarbonaten mit Carbons{\"a}uren. I : Synthese des Modellpeptid-Derivates Z-(L)-Ala-(L/D)-Phe-(L)-Val-OMe},
  series = {Tetrahedron letters},
  volume    = {21},
  journal   = {Tetrahedron letters},
  number    = {34},
  issn      = {0040-4039},
  doi       = {10.1016/S0040-4039(00)78663-1},
  pages     = {3265 -- 3268},
  year      = {1980},
  language  = {de}
}
@article{NaithaniKlostermeyerLangeetal.1971,
  author    = {Naithani, V. K and Klostermeyer, Henning and Lange, H. R. and [u.a.], and Berndt, Heinz and [u.a.],},
  title     = {Preparation of peptide derivatives for porcine proinsulin-synthesis},
  series = {Biological Chemistry},
  volume    = {352},
  journal   = {Biological Chemistry},
  number    = {1},
  publisher = {De Gruyter},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1971.352.1.1},
  pages     = {2 -- 3},
  year      = {1971},
  language  = {en}
}
@article{Berndt1979,
  author    = {Berndt, Heinz},
  title     = {Synthese der Sequenz 71—86 des Humanproinsulins, I : Synthese der Sequenz 71—86 als monomeres cyclisches Biscystinpeptidderivat und als Tetra-S-tritylderivat},
  series = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  volume    = {360},
  journal   = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  number    = {1},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1979.360.1.747},
  pages     = {747 -- 760},
  year      = {1979},
  language  = {de}
}
@article{Berndt1979,
  author    = {Berndt, Heinz},
  title     = {Synthese der Sequenz 71—86 des Humanproinsulins, III : Synthese {\"u}ber die Fragmente 71—78 und 79—86},
  series = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  volume    = {360},
  journal   = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  number    = {1},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1979.360.1.765},
  pages     = {765 -- 772},
  year      = {1979},
  language  = {de}
}
@article{NokiharaBerndt1979,
  author    = {Nokihara, Kiyoshi and Berndt, Heinz},
  title     = {Darstellung von Bis(S-methoxycarbonylthio)-B-Kette des Rinderinsulins},
  series = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  volume    = {360},
  journal   = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  number    = {1},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1979.360.1.773},
  pages     = {773 -- 776},
  year      = {1979},
  language  = {de}
}