@article{MedlinLangeBaumann1994,
  author    = {Medlin, L. K. and Lange, M. and Baumann, Marcus},
  title     = {Genetic differentiation among three colony-forming species of Phaeocystis : further evidence for the phylogeny of the Prymnesiophyta},
  series = {Phycologia},
  volume    = {Vol. 33},
  journal   = {Phycologia},
  number    = {Iss. 3},
  issn      = {0031-8884},
  pages     = {199 -- 212},
  year      = {1994},
  language  = {en}
}
@article{TuegBaumann1994,
  author    = {T{\"u}g, Helmut and Baumann, Marcus},
  title     = {Problems of UV-B radiation measurements in biological research : critical remarks on current techniques and suggestions for improvements},
  series = {Geophysical research letters},
  volume    = {Vol. 21},
  journal   = {Geophysical research letters},
  number    = {Iss. 8},
  issn      = {1944-8007 (E-Journal); 0094-8276 (Print)},
  pages     = {689 -- 692},
  year      = {1994},
  language  = {en}
}
@article{AletseeBaumann1991,
  author    = {Aletsee, Ludwig and Baumann, Marcus},
  title     = {A laboratory incubator equipped with facilities to automatically simulate natural irradiance},
  series = {Boletim do Instituto Oceanogr{\´a}fico / Universidade de S{\~a}o Paulo},
  volume    = {Vol. 39},
  journal   = {Boletim do Instituto Oceanogr{\´a}fico / Universidade de S{\~a}o Paulo},
  number    = {No. 2},
  issn      = {1982-436X; 0080-6331},
  pages     = {155 -- 159},
  year      = {1991},
  language  = {en}
}
@inproceedings{Baumann1989,
  author    = {Baumann, Marcus},
  title     = {Primary production and phytoplankton growth in the marginal ice zone of the Fram Strait and the interpretation of the field data with autecological experiments (Abstract)},
  series = {Oceanography and biology of Arctic seas : selected papers from the ICES Symposium on Marine Sciences of the Arctic and Subarctic Regions, held in Santander, 28 - 30 September 1987. (Rapports et proc{\`e}s-verbaux des r{\´e}unions / Conseil International pour l'Exploration de la Mer ; 188)},
  booktitle = {Oceanography and biology of Arctic seas : selected papers from the ICES Symposium on Marine Sciences of the Arctic and Subarctic Regions, held in Santander, 28 - 30 September 1987. (Rapports et proc{\`e}s-verbaux des r{\´e}unions / Conseil International pour l'Exploration de la Mer ; 188)},
  editor    = {Hempel, G.},
  publisher = {International Council for the Exploration of the Sea},
  address   = {Copenhagen},
  organization    = {Symposium on Marine Sciences of the Arctic and Subarctic Regions <1987, Santander>},
  pages     = {128},
  year      = {1989},
  language  = {en}
}
@article{JahnkeBaumann1987,
  author    = {Jahnke, J. and Baumann, Marcus},
  title     = {Differentiation between Phaeocystis pouchetii (Har.) Lagerheim and Phaeocystis globosa Scherffel},
  series = {Hydrobiological bulletin},
  volume    = {Vol. 21},
  journal   = {Hydrobiological bulletin},
  number    = {Iss. 2},
  issn      = {0165-1404 (Print); 1573-5125 (E-Journal)},
  pages     = {141 -- 147},
  year      = {1987},
  language  = {en}
}
@article{SmithBaumannWilsonetal.1987,
  author    = {Smith, Walker O. and Baumann, Marcus and Wilson, David L. and Aletsee, Ludwig},
  title     = {Phytoplankton biomass and productivity in the marginal ice zone of the Fram Strait during summer 1984},
  series = {Journal of geophysical research},
  volume    = {Vol. 92},
  journal   = {Journal of geophysical research},
  number    = {Iss. C7},
  issn      = {2156-2202 (E-Journal); 2169-9291 (E-Journal); 0148-0227 (Print); 2169-9275 (Print)},
  pages     = {6777 -- 6786},
  year      = {1987},
  language  = {en}
}
@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}
}
@misc{BerndtHoeckerKuropkaetal.1991,
  author    = {Berndt, Heinz and H{\"o}cker, Hartwig and Kuropka, Rolf and Kinkel, Joachim},
  title     = {Silane coated inorganic materials for chromatography : United States Patent},
  publisher = {[The United States Patent and Trademark Office]},
  address   = {[Alexandria, VA u.a.]},
  pages     = {9 S. : graph. Darst.},
  year      = {1991},
  language  = {en}
}
@inproceedings{KroggelBerndt1984,
  author    = {Kroggel, Matthias and Berndt, Heinz},
  title     = {The 0-hydroxiphenyloxicarbonyl-group a new base labile amine protecting group},
  series = {Peptides 1984 : Proceedings of the 18th European Peptide Symposium Djur{\"o}n{\"a}set, Sweden, June 10 - 15, 1984},
  booktitle = {Peptides 1984 : Proceedings of the 18th European Peptide Symposium Djur{\"o}n{\"a}set, Sweden, June 10 - 15, 1984},
  editor    = {Ragnarsson, Ulf},
  publisher = {Almquist \& Wiksell},
  address   = {Stockholm},
  isbn      = {91-22-00715-6},
  pages     = {81 -- 83},
  year      = {1984},
  language  = {en}
}
@inproceedings{SchnabelBerndt1973,
  author    = {Schnabel, Eberhard and Berndt, Heinz},
  title     = {Zur selektive Abspaltbarkeit der t-Butyloxycarbonylgruppe},
  series = {Peptides 1971 : proceedings of the Eleventh European Peptide Symposium, Vienna, Austria, April 1971},
  booktitle = {Peptides 1971 : proceedings of the Eleventh European Peptide Symposium, Vienna, Austria, April 1971},
  editor    = {Nesvadba, H.},
  publisher = {North-Holland Publ. [u.a.]},
  address   = {Amsterdam [u.a.]},
  isbn      = {0-7204-4120-X},
  pages     = {69 -- 70},
  year      = {1973},
  language  = {en}
}
@inproceedings{BerndtTurck1984,
  author    = {Berndt, Heinz and Turck, Christoph W.},
  title     = {Syntheses of defined peptide derivatives by aminolysis of 3-[Nα-benzyloxycarbonyl peptidyloxy] -2-hydroxy-N-methyl-benzamides at elevated temperatures II. Synthesis of the peptide derivatives Z-Ala-X-Gly-N(Et)2, X=Phe, Leu, Val, Ser (But), Glu (OBut)},
  series = {Chemistry of peptides and proteins : proceedings of the Fourth USSR-FRG Symposium, T{\"u}bingen, Federal Republic of Germany, June 8 - 12, 1982 / ed. Wolfgang Voelter ... - Vol. 2},
  booktitle = {Chemistry of peptides and proteins : proceedings of the Fourth USSR-FRG Symposium, T{\"u}bingen, Federal Republic of Germany, June 8 - 12, 1982 / ed. Wolfgang Voelter ... - Vol. 2},
  editor    = {Voelter, Wolfgang},
  publisher = {de Gruyter},
  address   = {Berlin [u.a.]},
  isbn      = {3-11009-580-7},
  pages     = {97 -- 103},
  year      = {1984},
  language  = {en}
}
@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{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{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{DanhoNaithaniSasakietal.1980,
  author    = {Danho, Waleed and Naithani, Vinod K. and Sasaki, Andr{\´e} N. and F{\"o}hles, Joseph and Berndt, Heinz and [u.a.],},
  title     = {Human proinsulin, VII : synthesis of two protected peptides corresponding to the sequences 1—45 and 46—86 of the prohormone},
  series = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  volume    = {361},
  journal   = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  number    = {1},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1980.361.1.857},
  pages     = {857 -- 863},
  year      = {1980},
  language  = {en}
}
@article{BerndtKrueger1985,
  author    = {Berndt, Heinz and Kr{\"u}ger, G{\"o}tz},
  title     = {Resolution of enantiomeric amino acid derivatives by high-performance liquid chromatography on chiral stationary phases},
  series = {Journal of chromatography A},
  volume    = {1985},
  journal   = {Journal of chromatography A},
  number    = {348},
  issn      = {0021-9673},
  doi       = {10.1016/S0021-9673(01)92461-6},
  pages     = {275 -- 279},
  year      = {1985},
  language  = {en}
}
@inproceedings{KalbeKuropkaMeyerStorketal.1988,
  author    = {Kalbe, Jochen and Kuropka, Rolf and Meyer-Stork, L. Sebastian and Lauter, S. L. and H{\"o}cker, Hartwig and Berndt, Heinz},
  title     = {Identification of fine animal hair via DNA analysis},
  series = {Proceedings of the 1st International Symposium on Specialty Animal Fibers : Aachen, October 26 - 27, 1987 ; [scientific, technological and economical aspects] . - (Schriftenreihe des Deutschen Wollforschungsinstitutes an der Technischen Hochschule Aachen e.V. ; 103)},
  booktitle = {Proceedings of the 1st International Symposium on Specialty Animal Fibers : Aachen, October 26 - 27, 1987 ; [scientific, technological and economical aspects] . - (Schriftenreihe des Deutschen Wollforschungsinstitutes an der Technischen Hochschule Aachen e.V. ; 103)},
  editor    = {K{\"o}rner, Andrea},
  publisher = {Dt. Wollforschungsinst.},
  address   = {Aachen},
  issn      = {0930-3723},
  pages     = {221 -- 227},
  year      = {1988},
  language  = {en}
}
@inproceedings{TakenagaHerreraWerneretal.2013,
  author    = {Takenaga, Shoko and Herrera, Cony F. and Werner, Frederik and Biselli, Manfred and Schnitzler, Thomas and Sch{\"o}ning, Michael Josef and {\"O}hlschl{\"a}ger, Peter and Wagner, Torsten},
  title     = {Detection of the metabolic activity of cells by differential measurements based on a single light-addressable potentiometric sensor chip},
  series = {11. Dresdner Sensor-Symposium : 9.-11.12.2013},
  booktitle = {11. Dresdner Sensor-Symposium : 9.-11.12.2013},
  organization    = {Dresdner Sensor-Symposium <11, 2013>},
  isbn      = {978-3-9813484-5-3},
  pages     = {63 -- 67},
  year      = {2013},
  language  = {en}
}
@article{KruegerGroetzingerBerndt1987,
  author    = {Kr{\"u}ger, G{\"o}tz and Gr{\"o}tzinger, Joachim and Berndt, Heinz},
  title     = {Enantiomeric resolution of amino acid derivatives on chiral stationary phases by high-performance liquid chromatography},
  series = {Journal of Chromatography A},
  volume    = {1987},
  journal   = {Journal of Chromatography A},
  number    = {397},
  issn      = {0021-9673},
  doi       = {10.1016/S0021-9673(01)85005-6},
  pages     = {223 -- 232},
  year      = {1987},
  language  = {en}
}
@article{DuttaHartkopfFroederWitteetal.2013,
  author    = {Dutta, Suryendu and Hartkopf-Fr{\"o}der, Christoph and Witte, Karin and Brocke, Rainer and Mann, Ulrich},
  title     = {Molecular characterization of fossil palynomorphs by transmission micro-FTIR spectroscopy: implications for hydrocarbon source evaluation},
  series = {International journal of coal geology},
  volume    = {Vol. 115},
  journal   = {International journal of coal geology},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1872-7840 (E-Journal); 0166-5162 (Print)},
  pages     = {13 -- 23},
  year      = {2013},
  language  = {en}
}
@article{HeinzeMangPeteretal.2014,
  author    = {Heinze, Daniel and Mang, Thomas and Peter, Karin and M{\"o}ller, Martin and Weichold, Oliver},
  title     = {Synthesis of low molecular weight poly(vinyl acetate) and its application as plasticizer},
  series = {Journal of applied polymer science},
  volume    = {131},
  journal   = {Journal of applied polymer science},
  number    = {9},
  publisher = {Wiley},
  address   = {New York},
  issn      = {1097-4628 (E-Journal); 0021-8995 (Print)},
  doi       = {10.1002/app.40226},
  pages     = {Article No. 40226},
  year      = {2014},
  abstract  = {Poly(vinyl acetate), PVAc, with a degree of polymerization Xn = 10 was prepared by chain-transfer radical polymerization using carbon tetrachloride and used as oligomeric plasticizer for commercial PVAc. However, the chlorinated chain ends cause a low thermal stability requiring mild Cl/H substitution. The product exhibits high thermal stability and excellent melt-compounding properties. Blends of oligomeric and commercial PVAc show single glass transition temperatures which decrease with higher oligomer content and exhibit small negative deviations from Fox' linear additivity rule. This indicates plasticization and miscibility being mainly due to entropic effects. Injection-moulded thick specimens show ductile behaviour at oligomer contents >10 wt \%, while sheets with a thickness of 0.2-0.5 mm appear flexible already at 7.5 wt \%. The oxygen permeability coefficients are an order of magnitude lower than those of low-density polyethylene. Due to the sum of their properties, the plasticized sheets present a promising alternative in the preparation of barrier materials.},
  language  = {en}
}
@article{KalbeKuropkaMeyerStorketal.1988,
  author    = {Kalbe, Jochen and Kuropka, Rolf and Meyer-Stork, L. Sebastian and Berndt, Heinz and [u.a.],},
  title     = {Isolation and characterization of high-molecular mass DNA from hair shafts},
  series = {Biological chemistry},
  volume    = {369},
  journal   = {Biological chemistry},
  number    = {1},
  isbn      = {0177-3593},
  doi       = {10.1515/bchm3.1988.369.1.413},
  pages     = {413 -- 416},
  year      = {1988},
  language  = {en}
}
@article{KuropkaMuellerHoeckeretal.1989,
  author    = {Kuropka, Rolf and M{\"u}ller, Bettina and H{\"o}cker, Hartwig and Berndt, Heinz},
  title     = {Chiral stationary phases via hydrosilylation reaction of N-acryloylamino acids : I. Stationary phase with one chiral centre for high-performance liquid chromatography and development of a new derivatization pattern for amino acid enantiomers},
  series = {Journal of chromatography A},
  journal   = {Journal of chromatography A},
  number    = {481},
  isbn      = {0021-9673},
  pages     = {380 -- 386},
  year      = {1989},
  language  = {en}
}
@article{KalbeHoeckerBerndt1989,
  author    = {Kalbe, Jochen and H{\"o}cker, Hartwig and Berndt, Heinz},
  title     = {Design of enzyme reactors as chromatographic columns for racemic resolution of amino acid esters},
  series = {Chromatographia},
  volume    = {28},
  journal   = {Chromatographia},
  number    = {3-4},
  isbn      = {0009-5893},
  doi       = {10.1007/BF02319646},
  pages     = {193 -- 196},
  year      = {1989},
  language  = {en}
}
@inproceedings{BerndtKalbeKuropkaetal.1990,
  author    = {Berndt, Heinz and Kalbe, Jochen and Kuropka, Rolf and Meyer-Stork, L. Sebastian and H{\"o}cker, Hartwig},
  title     = {Progress and limitations of the DNA analysis in fine animal fiber identification},
  series = {Proceedings of the 2nd International Symposium on Specialty Animal Fibers : Aachen, October 19 - 20, 1989. - (Schriftenreihe des Deutschen Wollforschungsinstituts an der Technischen Hochschule Aachen e. V. ; 106)},
  booktitle = {Proceedings of the 2nd International Symposium on Specialty Animal Fibers : Aachen, October 19 - 20, 1989. - (Schriftenreihe des Deutschen Wollforschungsinstituts an der Technischen Hochschule Aachen e. V. ; 106)},
  editor    = {K{\"o}rner, Andrea},
  publisher = {Dt. Wollforschungsinst.},
  address   = {Aachen},
  pages     = {259 -- 265},
  year      = {1990},
  language  = {en}
}
@article{WiegandDietrichHerteletal.2013,
  author    = {Wiegand, Sandra and Dietrich, Sascha and Hertel, Robert and Bongaerts, Johannes and Evers, Stefan and Volland, Sonja and Daniel, Rolf and Liesegang, Heiko},
  title     = {RNA-Seq of Bacillus licheniformis: active regulatory RNA features expressed within a productive fermentation},
  series = {BMC genomics},
  volume    = {Vol. 14},
  journal   = {BMC genomics},
  publisher = {BioMed Central},
  address   = {London},
  issn      = {1471-2164},
  pages     = {667},
  year      = {2013},
  language  = {en}
}
@article{RachingerBauchStrittmatteretal.2013,
  author    = {Rachinger, Michael and Bauch, Melanie and Strittmatter, Axel and Bongaerts, Johannes and Evers, Stefan and Maurer, Karl-Heinz and Daniel, Rolf and Liebl, Wolfgang and Liesegang, Heiko and Ehrenreich, Armin},
  title     = {Size unlimited markerless deletions by a transconjugative plasmid-system in Bacillus licheniformis},
  series = {Journal of biotechnology},
  volume    = {Vol. 164},
  journal   = {Journal of biotechnology},
  number    = {Iss. 4},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1873-4863 (E-Journal); 0168-1656 (Print)},
  pages     = {365 -- 369},
  year      = {2013},
  language  = {en}
}
@article{VoigtSchroeterJuergenetal.2013,
  author    = {Voigt, Birgit and Schroeter, Rebecca and J{\"u}rgen, Britta and Albrecht, Dirk and Evers, Stefan and Bongaerts, Johannes and Maurer, Karl-Heinz and Schweder, Thomas and Hecker, Michael},
  title     = {The response of Bacillus licheniformis to heat and ethanol stress and the role of the SigB regulon},
  series = {Proteomics},
  volume    = {Vol. 13},
  journal   = {Proteomics},
  number    = {Iss. 14},
  publisher = {Wiley},
  address   = {Weinheim},
  issn      = {1615-9861 (E-Journal); 1615-9853 (Print)},
  pages     = {2140 -- 2146},
  year      = {2013},
  language  = {en}
}
@article{WilmingBegemannKuhneetal.2013,
  author    = {Wilming, Anja and Begemann, Jens and Kuhne, Stefan and Regestein, Lars and Bongaerts, Johannes and Evers, Stefan and Maurer, Karl-Heinz and B{\"u}chs, Jochen},
  title     = {Metabolic studies of γ-polyglutamic acid production in Bacillus licheniformis by small-scale continuous cultivations},
  series = {Biochemical engineering journal},
  volume    = {Vol. 73},
  journal   = {Biochemical engineering journal},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1873-295X (E-Journal); 1369-703X (Print)},
  pages     = {29 -- 37},
  year      = {2013},
  language  = {en}
}
@article{ScheeleOertelBongaertsetal.2013,
  author    = {Scheele, Sandra and Oertel, Dan and Bongaerts, Johannes and Evers, Stefan and Hellmuth, Hendrik and Maurer, Karl-Heinz and Bott, Michael and Freudl, Roland},
  title     = {Secretory production of an FAD cofactor-containing cytosolic enzyme (sorbitol-xylitol oxidase from Streptomyces coelicolor) using the twin-arginine translocation (Tat) pathway of Corynebacterium glutamicum},
  series = {Microbial biotechnology},
  journal   = {Microbial biotechnology},
  publisher = {Wiley-Blackwell},
  address   = {Oxford},
  issn      = {1751-7915},
  pages     = {202 -- 206},
  year      = {2013},
  language  = {en}
}
@article{BorgmeierBongaertsMeinhardt2012,
  author    = {Borgmeier, Claudia and Bongaerts, Johannes and Meinhardt, Friedhelm},
  title     = {Genetic analysis of the Bacillus licheniformis degSU operon and the impact of regulatory mutations on protease production},
  series = {Journal of biotechnology},
  volume    = {159},
  journal   = {Journal of biotechnology},
  number    = {1-2},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1873-4863 (E-Journal); 0168-1656 (Print)},
  doi       = {10.1016/j.jbiotec.2012.02.011},
  pages     = {12 -- 20},
  year      = {2012},
  abstract  = {Disruption experiments targeted at the Bacillus licheniformis degSU operon and GFP-reporter analysis provided evidence for promoter activity immediately upstream of degU. pMutin mediated concomitant introduction of the degU32 allele - known to cause hypersecretion in Bacillus subtilis - resulted in a marked increase in protease activity. Application of 5-fluorouracil based counterselection through establishment of a phosphoribosyltransferase deficient Δupp strain eventually facilitated the marker-free introduction of degU32 leading to further protease enhancement achieving levels as for hypersecreting wild strains in which degU was overexpressed. Surprisingly, deletion of rapG - known to interfere with DegU DNA-binding in B. subtilis - did not enhance protease production neither in the wild type nor in the degU32 strain. The combination of degU32 and Δupp counterselection in the type strain is not only equally effective as in hypersecreting wild strains with respect to protease production but furthermore facilitates genetic strain improvement aiming at biological containment and effectiveness of biotechnological processes.},
  language  = {en}
}
@article{BongaertsEsserLorbachetal.2011,
  author    = {Bongaerts, Johannes and Esser, Simon and Lorbach, Volker and Al-Momani, L{\´o}ay and M{\"u}ller, Michael A. and Franke, Dirk and Grondal, Christoph and Kurutsch, Anja and Bujnicki, Robert and Takors, Ralf and Raeven, Leon and Wubbolts, Marcel and Bovenberg, Roel and Nieger, Martin and Sch{\"u}rmann, Melanie and Trachtmann, Natalie and Kozak, Stefan and Sprenger, Georg A. and M{\"u}ller, Michael},
  title     = {Diversity-oriented production of metabolites derived from chorismate and their use in organic synthesis},
  series = {Angewandte Chemie International Edition},
  volume    = {Vol. 50},
  journal   = {Angewandte Chemie International Edition},
  number    = {Iss. 34},
  publisher = {Wiley},
  address   = {Weinheim},
  issn      = {1521-3773 (E-Journal); 0570-0833 (Print); 1433-7851 (Print)},
  pages     = {7781 -- 7786},
  year      = {2011},
  language  = {en}
}
@article{DeppeKlatteBongaertsetal.2011,
  author    = {Deppe, Veronika Maria and Klatte, Stephanie and Bongaerts, Johannes and Maurer, Karl-Heinz and O'Connell, Timothy and Meinhardt, Friedhelm},
  title     = {Genetic control of Amadori product degradation in Bacillus subtilis via regulation of frlBONMD expression by FrlR},
  series = {Applied and environmental microbiology},
  volume    = {Vol. 77},
  journal   = {Applied and environmental microbiology},
  number    = {No. 9},
  publisher = {American Society of Mechanical Engineers (ASME)},
  address   = {New York},
  issn      = {1098-5336 (E-Journal); 0003-6919 (Print); 0099-2240 (Print)},
  pages     = {2839 -- 2846},
  year      = {2011},
  language  = {en}
}
@article{DeppeBongaertsO'Connelletal.2011,
  author    = {Deppe, Veronika Maria and Bongaerts, Johannes and O'Connell, Timothy and Maurer, Karl-Heinz and Meinhardt, Friedhelm},
  title     = {Enzymatic deglycation of Amadori products in bacteria},
  series = {Applied microbiology and biotechnology},
  volume    = {Vol. 90},
  journal   = {Applied microbiology and biotechnology},
  number    = {Iss. 2},
  publisher = {Springer},
  address   = {Berlin},
  issn      = {1432-0614 (E-Journal); 0171-1741 (Print); 0175-7598 (Print); 0340-2118 (Print)},
  pages     = {399 -- 406},
  year      = {2011},
  language  = {en}
}
@article{DegeringEggertPulsetal.2010,
  author    = {Degering, Christian and Eggert, Thorsten and Puls, Michael and Bongaerts, Johannes and Evers, Stefan and Maurer, Karl-Heinz and Jaeger, Karl-Erich},
  title     = {Optimization of protease secretion in Bacillus subtilis and Bacillus licheniformis by screening of homologous and herologous signal peptides},
  series = {Applied and environmental microbiology},
  volume    = {76},
  journal   = {Applied and environmental microbiology},
  number    = {19},
  publisher = {American Society for Microbiology},
  address   = {Washington, DC},
  issn      = {1098-5336 (E-Journal); 0003-6919 (Print); 0099-2240 (Print)},
  doi       = {10.1128/AEM.01146-10},
  pages     = {6370 -- 6378},
  year      = {2010},
  abstract  = {Bacillus subtilis and Bacillus licheniformis are widely used for the large-scale industrial production of proteins. These strains can efficiently secrete proteins into the culture medium using the general secretion (Sec) pathway. A characteristic feature of all secreted proteins is their N-terminal signal peptides, which are recognized by the secretion machinery. Here, we have studied the production of an industrially important secreted protease, namely, subtilisin BPN′ from Bacillus amyloliquefaciens. One hundred seventy-three signal peptides originating from B. subtilis and 220 signal peptides from the B. licheniformis type strain were fused to this secretion target and expressed in B. subtilis, and the resulting library was analyzed by high-throughput screening for extracellular proteolytic activity. We have identified a number of signal peptides originating from both organisms which produced significantly increased yield of the secreted protease. Interestingly, we observed that levels of extracellular protease were improved not only in B. subtilis, which was used as the screening host, but also in two different B. licheniformis strains. To date, it is impossible to predict which signal peptide will result in better secretion and thus an improved yield of a given extracellular target protein. Our data show that screening a library consisting of homologous and heterologous signal peptides fused to a target protein can identify more-effective signal peptides, resulting in improved protein export not only in the original screening host but also in different production strains.},
  language  = {en}
}
@article{PolenKraemerBongaertsetal.2005,
  author    = {Polen, T. and Kr{\"a}mer, Marco and Bongaerts, Johannes and Wubbolts, Marcel and Wendisch, V. F.},
  title     = {The global gene expression response of Escherichia coli to L-phenylalanine},
  series = {Journal of biotechnology},
  volume    = {Vol. 115},
  journal   = {Journal of biotechnology},
  number    = {Iss. 3},
  issn      = {1873-4863 (E-Journal); 0168-1656 (Print)},
  pages     = {221 -- 237},
  year      = {2005},
  language  = {en}
}
@article{KraemerBongaertsBovenbergetal.2003,
  author    = {Kr{\"a}mer, Marco and Bongaerts, Johannes and Bovenberg, Roel and Kremer, Susanne and M{\"u}ller, Ulrike and Orf, Sonja and Wubbolts, Marcel and Raeven, Leon},
  title     = {Metabolic engineering for microbial production of shikimic acid},
  series = {Metabolic engineering},
  volume    = {Vol. 5},
  journal   = {Metabolic engineering},
  number    = {Iss. 4},
  issn      = {1096-7184 (E-Journal); 1096-7176 (Print)},
  pages     = {277 -- 283},
  year      = {2003},
  language  = {en}
}
@article{GerigkMaassKreutzeretal.2002,
  author    = {Gerigk, M. and Maaß, D. and Kreutzer, A. and Sprenger, G. and Bongaerts, Johannes and Wubbolts, Marcel and Takors, Ralf},
  title     = {Enhanced pilot-scale fed-batch L-phenylalanine production with recombinant Escherichia coli by fully integrated reactive extraction},
  series = {Bioprocess and biosystems engineering},
  volume    = {Vol. 25},
  journal   = {Bioprocess and biosystems engineering},
  number    = {Iss. 1},
  issn      = {1432-0797 (E-Journal); 1615-7605 (E-Journal); 0178-515X (Print); 1615-7591 (Print)},
  pages     = {43 -- 52},
  year      = {2002},
  language  = {en}
}
@article{GerigkBujnickiGanpoNkwenkwaetal.2002,
  author    = {Gerigk, M. and Bujnicki, R. and Ganpo-Nkwenkwa, E. and Bongaerts, Johannes and Sprenger, G. and Takors, Ralf},
  title     = {Process control for enhanced L-phenylalanine production using different recombinant Escherichia coli strains},
  series = {Biotechnology and bioengineering},
  volume    = {Vol. 80},
  journal   = {Biotechnology and bioengineering},
  number    = {Iss. 7},
  issn      = {1097-0290 (E-Journal); 0006-3592 (Print)},
  pages     = {746 -- 754},
  year      = {2002},
  language  = {en}
}
@article{BongaertsBovenbergKraemeretal.2002,
  author    = {Bongaerts, Johannes and Bovenberg, Roel and Kr{\"a}mer, Marco and M{\"u}ller, Ulrike and Raeven, Leon and Wubbolts, Marcel},
  title     = {Metabolic engineering to produce fine chemicals in Escherichia coli},
  series = {Chemie - Ingenieur - Technik (CIT)},
  volume    = {Vol. 74},
  journal   = {Chemie - Ingenieur - Technik (CIT)},
  number    = {Iss. 5},
  issn      = {1522-2640 (E-Journal); 0009-286X (Print)},
  pages     = {694},
  year      = {2002},
  language  = {en}
}
@article{SchmitzHirschBongaertsetal.2002,
  author    = {Schmitz, M. and Hirsch, E. and Bongaerts, Johannes and Takors, Ralf},
  title     = {Pulse experiments as a prerequisite for the quantification of in vivo enzyme kinetics in aromatic amino acid pathway of Eschericia coli},
  series = {Biotechnology progress},
  volume    = {Vol. 18},
  journal   = {Biotechnology progress},
  number    = {Iss. 5},
  issn      = {1520-6033 (E-Journal); 8756-7938 (Print)},
  pages     = {935 -- 941},
  year      = {2002},
  language  = {en}
}
@article{BongaertsKraemerMuelleretal.2001,
  author    = {Bongaerts, Johannes and Kr{\"a}mer, Marco and M{\"u}ller, Ulrike and Raeven, Leon and Wubbolts, Marcel},
  title     = {Metabolic engineering for microbial production of aromatic amino acids and derived compounds},
  series = {Metabolic engineering},
  volume    = {Vol. 3},
  journal   = {Metabolic engineering},
  number    = {Iss. 4},
  issn      = {1096-7184 (E-Journal); 1096-7176 (Print)},
  pages     = {289 -- 300},
  year      = {2001},
  language  = {en}
}
@article{JossekBongaertsSprenger2001,
  author    = {Jossek, Ralf and Bongaerts, Johannes and Sprenger, Georg A.},
  title     = {Characterization of a new feedback-resistant 3-deoxy-D-arabinoheptulosonate 7-phosphate synthase AroF of Escherichia coli},
  series = {FEMS microbiology letters},
  volume    = {Vol. 202},
  journal   = {FEMS microbiology letters},
  number    = {Iss. 1},
  issn      = {1574-6968},
  pages     = {145 -- 148},
  year      = {2001},
  language  = {en}
}