@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}
}
@inproceedings{ZahnBerndtFehrenbach1973,
  author    = {Zahn, Helmut and Berndt, Heinz and Fehrenbach, P.},
  title     = {Synthese cyclischer Cystinpeptide mit Insulin A-und B-Kettensequenzen},
  series = {Peptides 1972 : proceedings of the Twelfth European Peptide Symposium, Reinhardsbrunn Castle, German Democratic Republic, September 1972},
  booktitle = {Peptides 1972 : proceedings of the Twelfth European Peptide Symposium, Reinhardsbrunn Castle, German Democratic Republic, September 1972},
  editor    = {Hanson, Horst},
  publisher = {North-Holland Publ. [u.a.],},
  address   = {Amsterdam [u.a.]},
  isbn      = {0-7204-4132-3},
  pages     = {101 -- 102},
  year      = {1973},
  language  = {de}
}
@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{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}
}
@phdthesis{Berndt1972,
  author    = {Berndt, Heinz},
  title     = {Zur Synthese der Sequenz 60-84[Ala71, Gly72, Val73] des Schweineproinsulins als monomeres cyclisches Bis-Cystinpeptidderivat},
  address   = {Aachen},
  pages     = {115 S.},
  year      = {1972},
  language  = {de}
}
@book{Berndt2014,
  author    = {Berndt, Heinz},
  title     = {Neue Kondensations-Methoden zur Synthese definierter Peptid-Derivate},
  address   = {Aachen},
  pages     = {XII, VI, 207 S. : graph. Darst.},
  year      = {2014},
  language  = {de}
}
@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{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{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{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}
}